Development of neuraminidase inhibitors as anti‐influenza virus drugs
Identifieur interne : 001674 ( Istex/Corpus ); précédent : 001673; suivant : 001675Development of neuraminidase inhibitors as anti‐influenza virus drugs
Auteurs : Joseph N. VargheseSource :
- Drug Development Research [ 0272-4391 ] ; 1999-03.
Abstract
Structure‐based design and synthesis of potent influenza virus neuraminidase inhibitors are now being evaluated in human trials as anti‐influenza virus drugs. The first drug of this class, Relenza™ (Zanamivir/GG167), is now awaiting pharmaceutical evaluation and registration in Australia, Europe, and North America for both treatment and prophylaxis of influenza. The target for the drug is the active site of neuraminidase, which is a pocket that has been totally conserved in both Type A and B influenza in all known subtypes of influenza (animal and human). Mutations in residues that surround this conserved pocket allow the virus to escape binding to circulating antibodies that recognise the molecular surface around the active site of the wild‐type virus. High‐affinity neuraminidase inhibitors have been designed that interact only with the conserved active site residues. The design of these sialic acid analogues was based on the crystal structure of influenza virus neuraminidase and its complex with N‐acetyl neuraminic acid (sialic acid) and 2‐deoxy‐2,3‐dehydro‐N‐acetyl neuraminic acid. These novel inhibitors are highly specific for influenza neuraminidase, and have been shown to inhibit influenza virus replication in both cell culture and animal models. The development of drugs against a rapidly mutating organism like influenza has to address to the possibility of emerging drug resistance. This is examined in the light of drug resistant mutants selected after in vitro passaging of virus in the presence of neuraminidase inhibitors. Drug Dev. Res. 46:176–196, 1999. © 1999 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/(SICI)1098-2299(199903/04)46:3/4<176::AID-DDR4>3.0.CO;2-6
Links to Exploration step
ISTEX:D278CB41B6488D1E899E112332E3EB59889CA5FFLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Development of neuraminidase inhibitors as anti‐influenza virus drugs</title><author><name sortKey="Varghese, Joseph N" sort="Varghese, Joseph N" uniqKey="Varghese J" first="Joseph N." last="Varghese">Joseph N. Varghese</name><affiliation><mods:affiliation>Biomolecular Research Institute, Parkville, Victoria, Australia</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: jose@bioresi.com.au</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:D278CB41B6488D1E899E112332E3EB59889CA5FF</idno><date when="1999" year="1999">1999</date><idno type="doi">10.1002/(SICI)1098-2299(199903/04)46:3/4<176::AID-DDR4>3.0.CO;2-6</idno><idno type="url">https://api.istex.fr/ark:/67375/WNG-VV4CKQ2F-F/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001674</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001674</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Development of neuraminidase inhibitors as anti‐influenza virus drugs</title><author><name sortKey="Varghese, Joseph N" sort="Varghese, Joseph N" uniqKey="Varghese J" first="Joseph N." last="Varghese">Joseph N. Varghese</name><affiliation><mods:affiliation>Biomolecular Research Institute, Parkville, Victoria, Australia</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: jose@bioresi.com.au</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Drug Development Research</title><title level="j" type="sub">Biotechnology and Pharmacology in Australia</title><title level="j" type="alt">DRUG DEVELOPMENT RESEARCH</title><idno type="ISSN">0272-4391</idno><idno type="eISSN">1098-2299</idno><imprint><biblScope unit="vol">46</biblScope><biblScope unit="issue">3‐4</biblScope><biblScope unit="page" from="176">176</biblScope><biblScope unit="page" to="196">196</biblScope><biblScope unit="page-count">21</biblScope><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="1999-03">1999-03</date></imprint><idno type="ISSN">0272-4391</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0272-4391</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Structure‐based design and synthesis of potent influenza virus neuraminidase inhibitors are now being evaluated in human trials as anti‐influenza virus drugs. The first drug of this class, Relenza™ (Zanamivir/GG167), is now awaiting pharmaceutical evaluation and registration in Australia, Europe, and North America for both treatment and prophylaxis of influenza. The target for the drug is the active site of neuraminidase, which is a pocket that has been totally conserved in both Type A and B influenza in all known subtypes of influenza (animal and human). Mutations in residues that surround this conserved pocket allow the virus to escape binding to circulating antibodies that recognise the molecular surface around the active site of the wild‐type virus. High‐affinity neuraminidase inhibitors have been designed that interact only with the conserved active site residues. The design of these sialic acid analogues was based on the crystal structure of influenza virus neuraminidase and its complex with N‐acetyl neuraminic acid (sialic acid) and 2‐deoxy‐2,3‐dehydro‐N‐acetyl neuraminic acid. These novel inhibitors are highly specific for influenza neuraminidase, and have been shown to inhibit influenza virus replication in both cell culture and animal models. The development of drugs against a rapidly mutating organism like influenza has to address to the possibility of emerging drug resistance. This is examined in the light of drug resistant mutants selected after in vitro passaging of virus in the presence of neuraminidase inhibitors. Drug Dev. Res. 46:176–196, 1999. © 1999 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>neuraminidase</json:string><json:string>varghese</json:string><json:string>influenza</json:string><json:string>sialic</json:string><json:string>influenza virus</json:string><json:string>viral</json:string><json:string>active site</json:string><json:string>laver</json:string><json:string>sialic acid</json:string><json:string>zanamivir</json:string><json:string>mutant</json:string><json:string>influenza virus neuraminidase</json:string><json:string>avian</json:string><json:string>antigenic</json:string><json:string>mutation</json:string><json:string>inhibitor</json:string><json:string>carboxylate</json:string><json:string>virology</json:string><json:string>hayden</json:string><json:string>antiviral</json:string><json:string>itzstein</json:string><json:string>palese</json:string><json:string>receptor</json:string><json:string>virol</json:string><json:string>sialidase</json:string><json:string>glycoprotein</json:string><json:string>chem</json:string><json:string>replication</json:string><json:string>prophylaxis</json:string><json:string>compans</json:string><json:string>bethell</json:string><json:string>guanidinyl</json:string><json:string>burmeister</json:string><json:string>chemother</json:string><json:string>neuraminidase inhibitor</json:string><json:string>drug resistance</json:string><json:string>water molecule</json:string><json:string>virion</json:string><json:string>immune</json:string><json:string>biochem</json:string><json:string>neu5ac</json:string><json:string>biol</json:string><json:string>blick</json:string><json:string>neuraminidases</json:string><json:string>amantadine</json:string><json:string>schulman</json:string><json:string>hemagglutinin</json:string><json:string>antimicrob</json:string><json:string>antigenic drift</json:string><json:string>virus</json:string><json:string>colman</json:string><json:string>carboxylate oxygen</json:string><json:string>influenza virus replication</json:string><json:string>similar result</json:string><json:string>analogue</json:string><json:string>subtypes</json:string><json:string>vaccine</json:string><json:string>influenza virus infection</json:string><json:string>avian influenza</json:string><json:string>viral replication</json:string><json:string>active site residue</json:string><json:string>icaac sept</json:string><json:string>cell surface</json:string><json:string>carbohydrate</json:string><json:string>amino</json:string><json:string>structural basis</json:string><json:string>crystal structure</json:string><json:string>carboxylate group</json:string><json:string>guanidinyl group</json:string><json:string>virus replication</json:string><json:string>neuraminidase activity</json:string><json:string>mdck cell</json:string><json:string>molecular structure</json:string><json:string>terminal sialic acid</json:string><json:string>influenza type</json:string><json:string>blood cell</json:string><json:string>neuraminic acid</json:string><json:string>enzyme mechanism</json:string><json:string>plenum press</json:string><json:string>derivative</json:string><json:string>ligand</json:string><json:string>hydrophobic pocket</json:string><json:string>nuclear protein</json:string><json:string>amino acid</json:string><json:string>thin line</json:string><json:string>viral neuraminidase</json:string><json:string>virology laver</json:string><json:string>potent inhibitor</json:string><json:string>novel inhibitor</json:string><json:string>influenza neuraminidase</json:string><json:string>transition state analogue</json:string><json:string>pyranose ring</json:string><json:string>acid group</json:string><json:string>antigenic variation</json:string><json:string>catalytic mechanism</json:string><json:string>excerpta medica</json:string><json:string>favourable binding site</json:string><json:string>salt link</json:string><json:string>conformational change</json:string><json:string>amino acid sequence</json:string><json:string>carboxamide derivative</json:string><json:string>selection pressure</json:string><json:string>enzyme activity</json:string><json:string>progeny virion</json:string><json:string>antimicrob agent chemother</json:string><json:string>oral administration</json:string><json:string>field strain</json:string><json:string>up respiratory tract</json:string><json:string>natural ligand</json:string><json:string>clinical trial</json:string><json:string>drug design</json:string><json:string>proc natl acad</json:string><json:string>avian strain</json:string><json:string>different subtypes</json:string><json:string>enzyme active site</json:string><json:string>cell culture</json:string><json:string>influenza strain</json:string><json:string>animal model</json:string><json:string>acid</json:string><json:string>residue</json:string><json:string>catalytic</json:string><json:string>variant</json:string><json:string>hydrophobic</json:string><json:string>enzyme</json:string><json:string>subtype</json:string></teeft></keywords><author><json:item><name>Joseph N. Varghese</name><affiliations><json:string>Biomolecular Research Institute, Parkville, Victoria, Australia</json:string><json:string>E-mail: jose@bioresi.com.au</json:string><json:string>Correspondence address: Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>sialidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Zanamivir</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Relenza™</value></json:item></subject><articleId><json:string>DDR4</json:string></articleId><arkIstex>ark:/67375/WNG-VV4CKQ2F-F</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Structure‐based design and synthesis of potent influenza virus neuraminidase inhibitors are now being evaluated in human trials as anti‐influenza virus drugs. The first drug of this class, Relenza™ (Zanamivir/GG167), is now awaiting pharmaceutical evaluation and registration in Australia, Europe, and North America for both treatment and prophylaxis of influenza. The target for the drug is the active site of neuraminidase, which is a pocket that has been totally conserved in both Type A and B influenza in all known subtypes of influenza (animal and human). Mutations in residues that surround this conserved pocket allow the virus to escape binding to circulating antibodies that recognise the molecular surface around the active site of the wild‐type virus. High‐affinity neuraminidase inhibitors have been designed that interact only with the conserved active site residues. The design of these sialic acid analogues was based on the crystal structure of influenza virus neuraminidase and its complex with N‐acetyl neuraminic acid (sialic acid) and 2‐deoxy‐2,3‐dehydro‐N‐acetyl neuraminic acid. These novel inhibitors are highly specific for influenza neuraminidase, and have been shown to inhibit influenza virus replication in both cell culture and animal models. The development of drugs against a rapidly mutating organism like influenza has to address to the possibility of emerging drug resistance. This is examined in the light of drug resistant mutants selected after in vitro passaging of virus in the presence of neuraminidase inhibitors. Drug Dev. Res. 46:176–196, 1999. © 1999 Wiley‐Liss, Inc.</abstract><qualityIndicators><score>9.856</score><pdfWordCount>12467</pdfWordCount><pdfCharCount>76550</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>21</pdfPageCount><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><pdfWordsPerPage>594</pdfWordsPerPage><pdfText>true</pdfText><refBibsNative>true</refBibsNative><abstractWordCount>238</abstractWordCount><abstractCharCount>1612</abstractCharCount><keywordCount>3</keywordCount></qualityIndicators><title>Development of neuraminidase inhibitors as anti‐influenza virus drugs</title><genre><json:string>article</json:string></genre><host><title>Drug Development Research</title><language><json:string>unknown</json:string></language><doi><json:string>10.1002/(ISSN)1098-2299</json:string></doi><issn><json:string>0272-4391</json:string></issn><eissn><json:string>1098-2299</json:string></eissn><publisherId><json:string>DDR</json:string></publisherId><volume>46</volume><issue>3‐4</issue><pages><first>176</first><last>196</last><total>21</total></pages><genre><json:string>journal</json:string></genre><author><json:item><name>Christopher R. Triggle PhD</name><affiliations><json:string>Department of Pharmacology & Therapeutics, University of Calgary, Alberta, Canada</json:string></affiliations></json:item><json:item><name>Evert Vos PhD, MD</name><affiliations><json:string>Metabolic Pharmaceuticals Ltd., Toorak, Victoria, Australia</json:string></affiliations></json:item></author><subject><json:item><value>Research Overview</value></json:item><json:item><value>Research Overviews</value></json:item></subject></host><namedEntities><unitex><date><json:string>1968</json:string><json:string>1917</json:string><json:string>1997</json:string><json:string>1918</json:string><json:string>1987</json:string><json:string>1994</json:string><json:string>1999</json:string><json:string>1933</json:string><json:string>1978</json:string><json:string>1980s</json:string></date><geogName></geogName><orgName><json:string>Biomolecular Research Institute</json:string><json:string>Australia, Europe, and North America</json:string><json:string>Wiley-Liss, Inc.</json:string><json:string>Biomolecular Research Institute, Parkville, Victoria, Australia Strategy, Management and Health</json:string><json:string>Wiley-Liss, Inc</json:string><json:string>Canada, Europe, and China</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Peter Colman</json:string><json:string>Vitro von Izstein</json:string><json:string>Kawkaoka</json:string><json:string>Zanamivir</json:string><json:string>Taylor</json:string><json:string>Joseph N. Varghese</json:string><json:string>Jenny McKimm-Breschkin</json:string><json:string>Brian Smith</json:string><json:string>Goto</json:string><json:string>Varghese</json:string></persName><placeName><json:string>Singapore</json:string><json:string>Australia</json:string><json:string>Beijing</json:string><json:string>US</json:string><json:string>Hong Kong</json:string><json:string>Georgia</json:string><json:string>Europe</json:string><json:string>America</json:string><json:string>Leningrad</json:string><json:string>Tokyo</json:string><json:string>Rostock</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Madren et al., 1995</json:string><json:string>Meindl et al., 1974</json:string><json:string>Palase and Compans, 1976</json:string><json:string>Hay et al., 1993</json:string><json:string>Varghese et al., 1992</json:string><json:string>Osterhaus et al., 1998</json:string><json:string>Air and Laver, 1995</json:string><json:string>Liu and Air, 1993</json:string><json:string>Weis et al., 1998</json:string><json:string>Hinshaw et al., 1980</json:string><json:string>Oxford et al., 1998</json:string><json:string>Woods et al., 1993</json:string><json:string>Pearlman et al., 1990</json:string><json:string>Mendel et al., 1998</json:string><json:string>Varghese et al., 1997</json:string><json:string>[1997]</json:string><json:string>Gubereva et al., 1998</json:string><json:string>Kim et al., 1997</json:string><json:string>Malby et al., 1994</json:string><json:string>Sprenger et al., 1993</json:string><json:string>Slemons et al., 1974</json:string><json:string>Webster et al., 1993</json:string><json:string>Yeun et al., 1998</json:string><json:string>Calfee et al., 1998</json:string><json:string>Laver and Valentine, 1969</json:string><json:string>Colman et al., 1987, 1989</json:string><json:string>McKimm-Breschkin et al., 1998</json:string><json:string>Crennell et al., 1993, 1994</json:string><json:string>Srange et al., 1991</json:string><json:string>Varghese and Colman, 1991</json:string><json:string>[1985]</json:string><json:string>Silagy et al., 1998</json:string><json:string>Palese and Schulman, 1977</json:string><json:string>Pinto et al., 1992</json:string><json:string>Nicholls et al., 1991</json:string><json:string>Fox et al., 1982</json:string><json:string>Both et al., 1983</json:string><json:string>Chong et al., 1992</json:string><json:string>Ryan et al., 1994</json:string><json:string>Li et al., 1993</json:string><json:string>Webster et al., 1992</json:string><json:string>Friebolin et al., 1980</json:string><json:string>von Itzstein et al., 1994</json:string><json:string>Sollis et al., 1996</json:string><json:string>Burmeister et al., 1994</json:string><json:string>Colman et al., 1983</json:string><json:string>Gubareva et al., 1997</json:string><json:string>Li et al., 1998</json:string><json:string>Varghese and Colman 1991</json:string><json:string>Varghese et al., 1995</json:string><json:string>Rogers and Paulson, 1983</json:string><json:string>Blok et al., 1982</json:string><json:string>Murphy and Webster, 1990</json:string><json:string>Nagai et al., 1990</json:string><json:string>Crennell et al., 1994</json:string><json:string>Hitte and Nayak, 1982</json:string><json:string>Nuss and Air, 1991</json:string><json:string>Monto et al., 1995</json:string><json:string>Compans and Dimmons, 1969</json:string><json:string>Treanor et al., 1998</json:string><json:string>Aoki et al., 1998</json:string><json:string>Taylor and von Itzstein, 1994</json:string><json:string>Chong et al., 1991</json:string><json:string>Bucher and Palese, 1975</json:string><json:string>Baker and Gandhi, 1976</json:string><json:string>Janakiraman et al., 1994</json:string><json:string>Smith et al., 1996</json:string><json:string>Wintermeyer and Nahata, 1995</json:string><json:string>Lentz et al., 1987</json:string><json:string>Hausmann et al., 1995</json:string><json:string>Hayden et al., 1998</json:string><json:string>von Itzstein et al., 1993</json:string><json:string>Thomas et al., 1994</json:string><json:string>Burmeister et al., 1993</json:string><json:string>Edmond et al., 1966</json:string><json:string>Sahasrabudhe et al., 1998</json:string><json:string>Kunkel et al., 1987</json:string><json:string>BossartWhitaker et al., 1993</json:string><json:string>Blick et al., 1995</json:string><json:string>McKimm-Breschkin et al., 1996</json:string><json:string>Meindl and Tuppy, 1969</json:string><json:string>Daniels et al., 1985</json:string><json:string>Kimberlin et al., 1995</json:string><json:string>Nagai and Yamada, 1994</json:string><json:string>[1977]</json:string><json:string>Crennell et al., 1993</json:string><json:string>Miller et al., 1978</json:string><json:string>Nohle et al., 1982</json:string><json:string>Drzenick et al., 1968</json:string><json:string>Klenk et al., 1955</json:string><json:string>Eisenberg et al., 1997</json:string><json:string>Chakraverty et al., 1993</json:string><json:string>[1994]</json:string><json:string>Palese and Compans, 1976</json:string><json:string>Hayden et al., 1997</json:string><json:string>Subbaroa et al., 1998</json:string><json:string>Baker et al., 1987</json:string><json:string>Gubareva et al., 1995</json:string><json:string>Ward et al., 1982</json:string><json:string>Griffin and Compans, 1979</json:string><json:string>Smith et al., 1933</json:string><json:string>Varghese et al., 1993</json:string><json:string>Luo et al., 1995</json:string><json:string>[1998]</json:string><json:string>Donnelly et al., 1995</json:string><json:string>Tulip et al., 1992b</json:string><json:string>McKimmBreschkin et al., 1994</json:string><json:string>Liu et al., 1995</json:string><json:string>Varghese et al., 1998</json:string><json:string>Smith and Palase, 1989</json:string><json:string>Suzuki et al., 1990</json:string><json:string>Monto et al., 1998</json:string><json:string>Hayden et al., 1996</json:string><json:string>Goto and Kawaoka, 1998</json:string><json:string>Burmeister et al., 1991</json:string><json:string>[1993]</json:string><json:string>Taylor et al., 1998</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/WNG-VV4CKQ2F-F</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - pharmacology & pharmacy</json:string><json:string>2 - chemistry, medicinal</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - clinical medicine</json:string><json:string>3 - pharmacology & pharmacy</json:string></scienceMetrix><scopus></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences medicales</json:string></inist></categories><publicationDate>1999</publicationDate><copyrightDate>1999</copyrightDate><doi><json:string>10.1002/(SICI)1098-2299(199903/04)46:3/4>176::AID-DDR4>3.0.CO;2-6</json:string></doi><id>D278CB41B6488D1E899E112332E3EB59889CA5FF</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-VV4CKQ2F-F/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-VV4CKQ2F-F/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/WNG-VV4CKQ2F-F/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main">Development of neuraminidase inhibitors as anti‐influenza virus drugs</title><title level="a" type="short" xml:lang="en">Anti‐Viral Drugs for Influenza</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><availability><licence>Copyright © 1999 Wiley‐Liss, Inc.</licence></availability><date type="published" when="1999-03"></date></publicationStmt><notesStmt><note type="content-type" subtype="article" source="article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main">Development of neuraminidase inhibitors as anti‐influenza virus drugs</title><title level="a" type="short" xml:lang="en">Anti‐Viral Drugs for Influenza</title><author xml:id="author-0000" role="corresp"><persName><forename type="first">Joseph N.</forename><surname>Varghese</surname></persName><email>jose@bioresi.com.au</email><affiliation><orgName type="institution">Biomolecular Research Institute</orgName><address><addrLine>Parkville</addrLine><addrLine>Victoria, Australia</addrLine><country key="AU" xml:lang="en">AUSTRALIA</country></address></affiliation></author><idno type="istex">D278CB41B6488D1E899E112332E3EB59889CA5FF</idno><idno type="ark">ark:/67375/WNG-VV4CKQ2F-F</idno><idno type="DOI">10.1002/(SICI)1098-2299(199903/04)46:3/4<176::AID-DDR4>3.0.CO;2-6</idno><idno type="unit">DDR4</idno><idno type="toTypesetVersion">file:DDR.DDR4.pdf</idno></analytic><monogr><editor xml:id="editor-0000"><persName><forename type="first">Christopher R.</forename><surname>Triggle</surname><roleName type="degree">PhD</roleName></persName><affiliation><orgName type="division">Department of Pharmacology & Therapeutics</orgName><orgName type="institution">University of Calgary</orgName><address><addrLine>Alberta</addrLine><addrLine>Canada</addrLine><country key="CA" xml:lang="en">CANADA</country></address></affiliation></editor><editor xml:id="editor-0001"><persName><forename type="first">Evert</forename><surname>Vos</surname><roleName type="degree">PhD, MD</roleName></persName><affiliation><address><addrLine>Metabolic Pharmaceuticals Ltd.</addrLine><addrLine>Toorak, Victoria, Australia</addrLine><country key="AU" xml:lang="en">AUSTRALIA</country></address></affiliation></editor><title level="j" type="main">Drug Development Research</title><title level="j" type="sub">Biotechnology and Pharmacology in Australia</title><title level="j" type="alt">DRUG DEVELOPMENT RESEARCH</title><idno type="pISSN">0272-4391</idno><idno type="eISSN">1098-2299</idno><idno type="book-DOI">10.1002/(ISSN)1098-2299</idno><idno type="book-part-DOI">10.1002/(SICI)1098-2299(199903/04)46:3/4<>1.0.CO;2-D</idno><idno type="product">DDR</idno><imprint><biblScope unit="vol">46</biblScope><biblScope unit="issue">3‐4</biblScope><biblScope unit="page" from="176">176</biblScope><biblScope unit="page" to="196">196</biblScope><biblScope unit="page-count">21</biblScope><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="1999-03"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><encodingDesc><schemaRef type="ODD" url="https://xml-schema.delivery.istex.fr/tei-istex.odd"></schemaRef><appInfo><application ident="pub2tei" version="1.0.10" when="2019-12-20"><label>pub2TEI-ISTEX</label><desc>A set of style sheets for converting XML documents encoded in various scientific publisher formats into a common TEI format.
<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>Structure‐based design and synthesis of potent influenza virus neuraminidase inhibitors are now being evaluated in human trials as anti‐influenza virus drugs. The first drug of this class, Relenza™ (Zanamivir/GG167), is now awaiting pharmaceutical evaluation and registration in Australia, Europe, and North America for both treatment and prophylaxis of influenza. The target for the drug is the active site of neuraminidase, which is a pocket that has been totally conserved in both Type A and B influenza in all known subtypes of influenza (animal and human). Mutations in residues that surround this conserved pocket allow the virus to escape binding to circulating antibodies that recognise the molecular surface around the active site of the wild‐type virus. High‐affinity neuraminidase inhibitors have been designed that interact only with the conserved active site residues. The design of these sialic acid analogues was based on the crystal structure of influenza virus neuraminidase and its complex with N‐acetyl neuraminic acid (sialic acid) and 2‐deoxy‐2,3‐dehydro‐N‐acetyl neuraminic acid. These novel inhibitors are highly specific for influenza neuraminidase, and have been shown to inhibit influenza virus replication in both cell culture and animal models. The development of drugs against a rapidly mutating organism like influenza has to address to the possibility of emerging drug resistance. This is examined in the light of drug resistant mutants selected after in vitro passaging of virus in the presence of neuraminidase inhibitors. Drug Dev. Res. 46:176–196, 1999. © 1999 Wiley‐Liss, Inc.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="kwd1">sialidase</term><term xml:id="kwd2">Zanamivir</term><term xml:id="kwd3">Relenza™</term></keywords><keywords rend="articleCategory"><term>Research Overview</term></keywords><keywords rend="tocHeading1"><term>Research Overviews</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-VV4CKQ2F-F/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>John Wiley & Sons, Inc.</publisherName><publisherLoc>New York</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1098-2299</doi><issn type="print">0272-4391</issn><issn type="electronic">1098-2299</issn><idGroup><id type="product" value="DDR"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="DRUG DEVELOPMENT RESEARCH">Drug Development Research</title><title type="short">Drug Dev. Res.</title></titleGroup></publicationMeta><publicationMeta level="part" position="30"><doi origin="wiley" registered="yes">10.1002/(SICI)1098-2299(199903/04)46:3/4<>1.0.CO;2-D</doi><titleGroup><title type="specialIssueTitle">Biotechnology and Pharmacology in Australia</title></titleGroup><numberingGroup><numbering type="journalVolume" number="46">46</numbering><numbering type="includedIssue">3</numbering><numbering type="includedIssue">4</numbering><numbering type="journalIssue">3‐4</numbering></numberingGroup><creators><creator xml:id="sped1" creatorRole="sponsoringEditor" affiliationRef="#sp1"><personName><givenNames>Christopher R.</givenNames><familyName>Triggle</familyName><degrees>PhD</degrees></personName></creator><creator xml:id="sped2" creatorRole="sponsoringEditor" affiliationRef="#sp2"><personName><givenNames>Evert</givenNames><familyName>Vos</familyName><degrees>PhD, MD</degrees></personName></creator></creators><affiliationGroup><affiliation xml:id="sp1" countryCode="CA" type="organization"><unparsedAffiliation>Department of Pharmacology & Therapeutics, University of Calgary, Alberta, Canada</unparsedAffiliation></affiliation><affiliation xml:id="sp2" countryCode="AU" type="organization"><unparsedAffiliation>Metabolic Pharmaceuticals Ltd., Toorak, Victoria, Australia</unparsedAffiliation></affiliation></affiliationGroup><coverDate startDate="1999-03">March ‐ April 1999</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="4" status="forIssue"><doi origin="wiley" registered="yes">10.1002/(SICI)1098-2299(199903/04)46:3/4<176::AID-DDR4>3.0.CO;2-6</doi><idGroup><id type="unit" value="DDR4"></id></idGroup><countGroup><count type="pageTotal" number="21"></count></countGroup><titleGroup><title type="articleCategory">Research Overview</title><title type="tocHeading1">Research Overviews</title></titleGroup><copyright ownership="publisher">Copyright © 1999 Wiley‐Liss, Inc.</copyright><eventGroup><event type="firstOnline" date="1999-05-25"></event><event type="publishedOnlineFinalForm" date="1999-05-25"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:HeaderRef result:HeaderRef" date="2010-03-06"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-17"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-16"></event></eventGroup><numberingGroup><numbering type="pageFirst">176</numbering><numbering type="pageLast">196</numbering></numberingGroup><correspondenceTo>Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:DDR.DDR4.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="8"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="146"></count><count type="wordTotal" number="13705"></count></countGroup><titleGroup><title type="main" xml:lang="en">Development of neuraminidase inhibitors as anti‐influenza virus drugs</title><title type="short" xml:lang="en">Anti‐Viral Drugs for Influenza</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Joseph N.</givenNames><familyName>Varghese</familyName></personName><contactDetails><email>jose@bioresi.com.au</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="AU" type="organization"><unparsedAffiliation>Biomolecular Research Institute, Parkville, Victoria, Australia</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">sialidase</keyword><keyword xml:id="kwd2">Zanamivir</keyword><keyword xml:id="kwd3">Relenza™</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Structure‐based design and synthesis of potent influenza virus neuraminidase inhibitors are now being evaluated in human trials as anti‐influenza virus drugs. The first drug of this class, Relenza™ (Zanamivir/GG167), is now awaiting pharmaceutical evaluation and registration in Australia, Europe, and North America for both treatment and prophylaxis of influenza. The target for the drug is the active site of neuraminidase, which is a pocket that has been totally conserved in both Type A and B influenza in all known subtypes of influenza (animal and human). Mutations in residues that surround this conserved pocket allow the virus to escape binding to circulating antibodies that recognise the molecular surface around the active site of the wild‐type virus. High‐affinity neuraminidase inhibitors have been designed that interact only with the conserved active site residues. The design of these sialic acid analogues was based on the crystal structure of influenza virus neuraminidase and its complex with N‐acetyl neuraminic acid (sialic acid) and 2‐deoxy‐2,3‐dehydro‐N‐acetyl neuraminic acid. These novel inhibitors are highly specific for influenza neuraminidase, and have been shown to inhibit influenza virus replication in both cell culture and animal models. The development of drugs against a rapidly mutating organism like influenza has to address to the possibility of emerging drug resistance. This is examined in the light of drug resistant mutants selected after in vitro passaging of virus in the presence of neuraminidase inhibitors. Drug Dev. Res. 46:176–196, 1999. © 1999 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Development of neuraminidase inhibitors as anti‐influenza virus drugs</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Anti‐Viral Drugs for Influenza</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Development of neuraminidase inhibitors as anti‐influenza virus drugs</title></titleInfo><name type="personal"><namePart type="given">Joseph N.</namePart><namePart type="family">Varghese</namePart><affiliation>Biomolecular Research Institute, Parkville, Victoria, Australia</affiliation><affiliation>E-mail: jose@bioresi.com.au</affiliation><affiliation>Correspondence address: Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>John Wiley & Sons, Inc.</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">1999-03</dateIssued><copyrightDate encoding="w3cdtf">1999</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">8</extent><extent unit="tables">0</extent><extent unit="references">146</extent><extent unit="words">13705</extent></physicalDescription><abstract lang="en">Structure‐based design and synthesis of potent influenza virus neuraminidase inhibitors are now being evaluated in human trials as anti‐influenza virus drugs. The first drug of this class, Relenza™ (Zanamivir/GG167), is now awaiting pharmaceutical evaluation and registration in Australia, Europe, and North America for both treatment and prophylaxis of influenza. The target for the drug is the active site of neuraminidase, which is a pocket that has been totally conserved in both Type A and B influenza in all known subtypes of influenza (animal and human). Mutations in residues that surround this conserved pocket allow the virus to escape binding to circulating antibodies that recognise the molecular surface around the active site of the wild‐type virus. High‐affinity neuraminidase inhibitors have been designed that interact only with the conserved active site residues. The design of these sialic acid analogues was based on the crystal structure of influenza virus neuraminidase and its complex with N‐acetyl neuraminic acid (sialic acid) and 2‐deoxy‐2,3‐dehydro‐N‐acetyl neuraminic acid. These novel inhibitors are highly specific for influenza neuraminidase, and have been shown to inhibit influenza virus replication in both cell culture and animal models. The development of drugs against a rapidly mutating organism like influenza has to address to the possibility of emerging drug resistance. This is examined in the light of drug resistant mutants selected after in vitro passaging of virus in the presence of neuraminidase inhibitors. Drug Dev. Res. 46:176–196, 1999. © 1999 Wiley‐Liss, Inc.</abstract><subject lang="en"><genre>keywords</genre><topic>sialidase</topic><topic>Zanamivir</topic><topic>Relenza™</topic></subject><relatedItem type="host"><titleInfo><title>Drug Development Research</title></titleInfo><titleInfo type="abbreviated"><title>Drug Dev. Res.</title></titleInfo><name type="personal"><namePart type="given">Christopher R.</namePart><namePart type="family">Triggle</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>Department of Pharmacology & Therapeutics, University of Calgary, Alberta, Canada</affiliation></name><name type="personal"><namePart type="given">Evert</namePart><namePart type="family">Vos</namePart><namePart type="termsOfAddress">PhD, MD</namePart><affiliation>Metabolic Pharmaceuticals Ltd., Toorak, Victoria, Australia</affiliation></name><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><subject><genre>article-category</genre><topic>Research Overview</topic><topic>Research Overviews</topic></subject><identifier type="ISSN">0272-4391</identifier><identifier type="eISSN">1098-2299</identifier><identifier type="DOI">10.1002/(ISSN)1098-2299</identifier><identifier type="PublisherID">DDR</identifier><part><date>1999</date><detail type="title"><title>Biotechnology and Pharmacology in Australia</title></detail><detail type="volume"><caption>vol.</caption><number>46</number></detail><detail type="issue"><caption>no.</caption><number>3‐4</number></detail><extent unit="pages"><start>176</start><end>196</end><total>21</total></extent></part></relatedItem><relatedItem type="references" displayLabel="cit1"><titleInfo><title>Red cells bound to influenza virus N9 neuraminidase are not released by the N9 neuraminidase activity</title></titleInfo><name type="personal"><namePart type="given">GM</namePart><namePart type="family">Air</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Air GM, Laver WG. 1995. Red cells bound to influenza virus N9 neuraminidase are not released by the N9 neuraminidase activity. Virology 211:278–284.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>211</number></detail><extent unit="pages"><start>278</start><end>284</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>211</number></detail><extent unit="pages"><start>278</start><end>284</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit2"><titleInfo><title>Avian diseases—historical aspects</title></titleInfo><name type="personal"><namePart type="given">DJ</namePart><namePart type="family">Alexander</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Proceedings of the 2nd International Symposium on Avian Influenza</title></titleInfo><originInfo><publisher>U.S. Animal Heath Assosiation</publisher><place><placeTerm type="text">Richmond, VA</placeTerm></place></originInfo><part><date>1986</date><extent unit="pages"><start>4</start><end>13</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit3"><titleInfo><title>Oral GS4104 successfully reduces duration and severity of naturally acquired influenza</title></titleInfo><name type="personal"><namePart type="given">F</namePart><namePart type="family">Aoki</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1998</date></part></relatedItem><relatedItem type="references" displayLabel="cit4"><titleInfo><title>Effect of Ca++ on the stability of influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">NJ</namePart><namePart type="family">Baker</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Baker NJ, Gandhi SS. 1976. Effect of Ca++ on the stability of influenza virus neuraminidase. Arch Virol 52:7–18.Medline</note><part><date>1976</date><detail type="volume"><caption>vol.</caption><number>52</number></detail><extent unit="pages"><start>7</start><end>18</end></extent></part><relatedItem type="host"><titleInfo><title>Arch Virol</title></titleInfo><part><date>1976</date><detail type="volume"><caption>vol.</caption><number>52</number></detail><extent unit="pages"><start>7</start><end>18</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit5"><titleInfo><title>The three‐dimensional structure of neuraminidase of subtype N9 from an avian influenza virus</title></titleInfo><name type="personal"><namePart type="given">AT</namePart><namePart type="family">Baker</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Baker AT, Varghese JN, Laver WG, Air GM, Colman PM. 1987. The three‐dimensional structure of neuraminidase of subtype N9 from an avian influenza virus. Proteins 1:111–117.</note><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>1</number></detail><extent unit="pages"><start>111</start><end>117</end></extent></part><relatedItem type="host"><titleInfo><title>Proteins</title></titleInfo><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>1</number></detail><extent unit="pages"><start>111</start><end>117</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit6"><titleInfo><title>Influenza: the last great plague</title></titleInfo><name type="personal"><namePart type="given">WI</namePart><namePart type="family">Beveridge</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><genre>book</genre><originInfo><publisher>Heinemann</publisher></originInfo><part><date>1977</date></part></relatedItem><relatedItem type="references" displayLabel="cit7"><titleInfo><title>Generation and characterization of an influenza virus variant with decreased sensitivity to the neuraminidase specific inhibitor 4‐guanidino‐Neu5Ac2en</title></titleInfo><name type="personal"><namePart type="given">TJ</namePart><namePart type="family">Blick</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Blick TJ, Tiong T, Sahasrabudhe A, Varghese JN, Colman PM, Hart GJ, Bethell RC, McKimm‐Breschkin JL. 1995. Generation and characterization of an influenza virus variant with decreased sensitivity to the neuraminidase specific inhibitor 4‐guanidino‐Neu5Ac2en. Virology 214:475–484.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>214</number></detail><extent unit="pages"><start>475</start><end>484</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>214</number></detail><extent unit="pages"><start>475</start><end>484</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit8"><titleInfo><title>Studies on the size, chemical composition and partial sequence of the neuraminidase (NA) from type A influenza virus show that the N‐terminal region of the NA is not processed and serves to anchor the NA in the viral membrane</title></titleInfo><name type="personal"><namePart type="given">J</namePart><namePart type="family">Blok</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Blok J, Air GM, Laver WG, Ward CW, Lilley GG, Woods EF, Roxburgh CM, Inglis AS. 1982. Studies on the size, chemical composition and partial sequence of the neuraminidase (NA) from type A influenza virus show that the N‐terminal region of the NA is not processed and serves to anchor the NA in the viral membrane. Virology 119:109–121.Medline</note><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>119</number></detail><extent unit="pages"><start>109</start><end>121</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>119</number></detail><extent unit="pages"><start>109</start><end>121</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit9"><titleInfo><title>Three dimensional structure of influenza A N 9 neuraminidase and its complex with 9 neuraminidase and its complex with the inhibitor 2‐deoxy 2,3‐dehydro‐N‐acetyl neuraminic acid</title></titleInfo><name type="personal"><namePart type="given">P</namePart><namePart type="family">Bossart‐Whitaker</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Bossart‐Whitaker P, Carson M, Babu YS, Smith CD, Laver WG, Air GM. 1993. Three dimensional structure of influenza A N 9 neuraminidase and its complex with 9 neuraminidase and its complex with the inhibitor 2‐deoxy 2,3‐dehydro‐N‐acetyl neuraminic acid J Mol Biol 232:1069–1083.Medline</note><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>232</number></detail><extent unit="pages"><start>1069</start><end>1083</end></extent></part><relatedItem type="host"><titleInfo><title>J Mol Biol</title></titleInfo><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>232</number></detail><extent unit="pages"><start>1069</start><end>1083</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit10"><titleInfo><title>Antigenic drift in influenza virus H3 haemagglutinin from 1968 to 1980: multiple evolutionary pathways and sequential amino acid changes at key antigenic sites</title></titleInfo><name type="personal"><namePart type="given">GW</namePart><namePart type="family">Both</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Both GW, Sleigh MJ, Cox NJ, Kendal AP. 1983. Antigenic drift in influenza virus H3 haemagglutinin from 1968 to 1980: multiple evolutionary pathways and sequential amino acid changes at key antigenic sites. J Virol 48:52–60.Medline</note><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>48</number></detail><extent unit="pages"><start>52</start><end>60</end></extent></part><relatedItem type="host"><titleInfo><title>J Virol</title></titleInfo><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>48</number></detail><extent unit="pages"><start>52</start><end>60</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit11"><titleInfo><title>The biologically active proteins of influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">DJ</namePart><namePart type="family">Bucher</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Influenza virus and influenza</title></titleInfo><originInfo><publisher>Academic Press</publisher><place><placeTerm type="text">New York</placeTerm></place></originInfo><part><date>1975</date><extent unit="pages"><start>83</start><end>123</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit12"><titleInfo><title>The 2. 2Å resolution crystal structure of influenza B neuraminidase and its complex to sialic acid</title></titleInfo><name type="personal"><namePart type="given">WP</namePart><namePart type="family">Burmeister</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Burmeister WP, Ruigrok RWH, Cusack S. 1991. The 2. 2Å resolution crystal structure of influenza B neuraminidase and its complex to sialic acid. EMBO J 11:49–56.</note><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>11</number></detail><extent unit="pages"><start>49</start><end>56</end></extent></part><relatedItem type="host"><titleInfo><title>EMBO J</title></titleInfo><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>11</number></detail><extent unit="pages"><start>49</start><end>56</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit13"><titleInfo><title>Influenza B virus neuraminidase can synthesize its own inhibitor</title></titleInfo><name type="personal"><namePart type="given">WP</namePart><namePart type="family">Burmeister</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Burmeister WP, Henrissat B, Bosso C, Cusack S, Ruigrok RWH. 1993. Influenza B virus neuraminidase can synthesize its own inhibitor. Structure 1:19–26.Medline</note><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>1</number></detail><extent unit="pages"><start>19</start><end>26</end></extent></part><relatedItem type="host"><titleInfo><title>Structure</title></titleInfo><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>1</number></detail><extent unit="pages"><start>19</start><end>26</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit14"><titleInfo><title>Calcium is needed for the thermostability of influeza B virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">WP</namePart><namePart type="family">Burmeister</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1994</date></part></relatedItem><relatedItem type="references" displayLabel="cit15"><titleInfo><title>Mucins and mucoids in relation to influenza virus action. IV. Inhibition by purified mucoid of infection and haemagglutinin with the virus strain WSE</title></titleInfo><name type="personal"><namePart type="given">FM</namePart><namePart type="family">Burnett</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Burnett FM. 1947. Mucins and mucoids in relation to influenza virus action. IV. Inhibition by purified mucoid of infection and haemagglutinin with the virus strain WSE. Aust J Exp Biol Med Sci 26:381–387.</note><part><date>1947</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><extent unit="pages"><start>381</start><end>387</end></extent></part><relatedItem type="host"><titleInfo><title>Aust J Exp Biol Med Sci</title></titleInfo><part><date>1947</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><extent unit="pages"><start>381</start><end>387</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit16"><titleInfo><title>Protective efficacy of reduced frequency dosing of intranasal zanamivir in experimental human influenza.</title></titleInfo><name type="personal"><namePart type="given">DP</namePart><namePart type="family">Calfee</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1998</date></part></relatedItem><relatedItem type="references" displayLabel="cit17"><titleInfo><title>Influenza activity — United States and worldwide, and composition of the 1993–94 influenza vaccine</title></titleInfo><name type="personal"><namePart type="given">al</namePart><namePart type="family">Chakraverty et</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Chakraverty et al. 1993. Influenza activity — United States and worldwide, and composition of the 1993–94 influenza vaccine. JAMA 269:1778–1779.Medline</note><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>269</number></detail><extent unit="pages"><start>1778</start><end>1779</end></extent></part><relatedItem type="host"><titleInfo><title>JAMA</title></titleInfo><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>269</number></detail><extent unit="pages"><start>1778</start><end>1779</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit18"><titleInfo><title>Characterisation of an ionisable group involved in the binding and catalysis by sialidase from influenza virus</title></titleInfo><name type="personal"><namePart type="given">AKJ</namePart><namePart type="family">Chong</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Chong AKJ, Pegg MS, von Itzstein M. 1991. Characterisation of an ionisable group involved in the binding and catalysis by sialidase from influenza virus. Biochem Int 24:165–171.Medline</note><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>24</number></detail><extent unit="pages"><start>165</start><end>171</end></extent></part><relatedItem type="host"><titleInfo><title>Biochem Int</title></titleInfo><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>24</number></detail><extent unit="pages"><start>165</start><end>171</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit19"><titleInfo><title>Evidence for a sialyl cation transition state complex in the reaction of sialidase from influenza</title></titleInfo><name type="personal"><namePart type="given">AKJ</namePart><namePart type="family">Chong</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Chong AKJ, Pegg MS, Taylor NR, von Itzstein M. 1992. Evidence for a sialyl cation transition state complex in the reaction of sialidase from influenza. Eur J Biochem 207:335–343.Medline</note><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>207</number></detail><extent unit="pages"><start>335</start><end>343</end></extent></part><relatedItem type="host"><titleInfo><title>Eur J Biochem</title></titleInfo><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>207</number></detail><extent unit="pages"><start>335</start><end>343</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit20"><titleInfo><title>Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus</title></titleInfo><name type="personal"><namePart type="given">EC</namePart><namePart type="family">Claas</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Claas EC, Osterhaus AD, van Beek R, De Jong JC, Rimmelzwaan GF, Krauss S, Shortridge KF, Webster RG. 1998. Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus. Lancet 351:472–477.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>351</number></detail><extent unit="pages"><start>472</start><end>477</end></extent></part><relatedItem type="host"><titleInfo><title>Lancet</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>351</number></detail><extent unit="pages"><start>472</start><end>477</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit21"><titleInfo><title>Influenza virus neuraminidase: Enzyme and antigen</title></titleInfo><name type="personal"><namePart type="given">PM</namePart><namePart type="family">Colman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>The influenza viruses</title></titleInfo><originInfo><publisher>Plenum Press</publisher><place><placeTerm type="text">New York</placeTerm></place></originInfo><part><date>1989</date><extent unit="pages"><start>175</start><end>218</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit22"><titleInfo><title>Influenza virus neuraminidase: structure, antibodies, and inhibitors</title></titleInfo><name type="personal"><namePart type="given">PM</namePart><namePart type="family">Colman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Colman PM. 1994. Influenza virus neuraminidase: structure, antibodies, and inhibitors. Protein Sci 3:1687–1696.Medline</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>3</number></detail><extent unit="pages"><start>1687</start><end>1696</end></extent></part><relatedItem type="host"><titleInfo><title>Protein Sci</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>3</number></detail><extent unit="pages"><start>1687</start><end>1696</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit23"><titleInfo><title>Virus versus antibody</title></titleInfo><name type="personal"><namePart type="given">PM</namePart><namePart type="family">Colman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Colman PM. 1997. Virus versus antibody. Structure 5:591–593.Medline</note><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>5</number></detail><extent unit="pages"><start>591</start><end>593</end></extent></part><relatedItem type="host"><titleInfo><title>Structure</title></titleInfo><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>5</number></detail><extent unit="pages"><start>591</start><end>593</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit24"><titleInfo><title>The structure of influenza virus neuraminidase at 5A resolution</title></titleInfo><name type="personal"><namePart type="given">PM</namePart><namePart type="family">Colman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Structural aspects of recognition and assembly in biological macromolecules</title></titleInfo><originInfo><publisher>I.S.S.</publisher><place><placeTerm type="text">Rehovot, Israel</placeTerm></place></originInfo><part><date>1981</date><extent unit="pages"><start>869</start><end>872</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit25"><titleInfo><title>Structure of the catalytic and antigenic sites in influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">PM</namePart><namePart type="family">Colman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Colman PM, Varghese JN, Laver WG. 1983. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303:41–44.Medline</note><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>303</number></detail><extent unit="pages"><start>41</start><end>44</end></extent></part><relatedItem type="host"><titleInfo><title>Nature</title></titleInfo><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>303</number></detail><extent unit="pages"><start>41</start><end>44</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit26"><titleInfo><title>Three‐dimensional structure of a complex of antibody with influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">PM</namePart><namePart type="family">Colman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Colman PM, Laver WG, Varghese JN, Baker AT, Tullock PA, Air GM, Webster RG. 1987. Three‐dimensional structure of a complex of antibody with influenza virus neuraminidase. Nature 326:358–363.Medline</note><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>326</number></detail><extent unit="pages"><start>358</start><end>363</end></extent></part><relatedItem type="host"><titleInfo><title>Nature</title></titleInfo><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>326</number></detail><extent unit="pages"><start>358</start><end>363</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit27"><titleInfo><title>3‐D structures of influenza virus neuraminidase‐antibody complexes</title></titleInfo><name type="personal"><namePart type="given">PM</namePart><namePart type="family">Colman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Colman PM, Tulip WR, Varghese JN, Tulloch PA, Baker AT, Laver WG, Air GM. 1989. 3‐D structures of influenza virus neuraminidase‐antibody complexes. Proc R Soc Lond B 323:511–518.</note><part><date>1989</date><detail type="volume"><caption>vol.</caption><number>323</number></detail><extent unit="pages"><start>511</start><end>518</end></extent></part><relatedItem type="host"><titleInfo><title>Proc R Soc Lond B</title></titleInfo><part><date>1989</date><detail type="volume"><caption>vol.</caption><number>323</number></detail><extent unit="pages"><start>511</start><end>518</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit28"><titleInfo><title>An electron microscopic study of single‐cycle infection of chick embryo fibroblasts by influenza virus</title></titleInfo><name type="personal"><namePart type="given">RW</namePart><namePart type="family">Compans</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Compans RW, Dimmock NJ. 1969. An electron microscopic study of single‐cycle infection of chick embryo fibroblasts by influenza virus. Virology 39:499Medline</note><part><date>1969</date><detail type="volume"><caption>vol.</caption><number>39</number></detail><extent unit="pages"><start>499</start></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1969</date><detail type="volume"><caption>vol.</caption><number>39</number></detail><extent unit="pages"><start>499</start></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit29"><titleInfo><title>Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">SJ</namePart><namePart type="family">Crennell</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Crennell SJ, Garman EF, Laver WG, Vimr ER, Taylor GL. 1993. Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase. Proc Natl Acad Sci USA 90:9852–9856.</note><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>90</number></detail><extent unit="pages"><start>9852</start><end>9856</end></extent></part><relatedItem type="host"><titleInfo><title>Proc Natl Acad Sci USA</title></titleInfo><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>90</number></detail><extent unit="pages"><start>9852</start><end>9856</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit30"><titleInfo><title>Crystal structure of Vibro Cholerae neuraminidase reveals dual lectin‐like domains in addition to the catalytic domain</title></titleInfo><name type="personal"><namePart type="given">SJ</namePart><namePart type="family">Crennell</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Crennell SJ, Garman E, Laver G, Vimr E, Taylor GL. 1994. Crystal structure of Vibro Cholerae neuraminidase reveals dual lectin‐like domains in addition to the catalytic domain. Structure 2:535–544.Medline</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>2</number></detail><extent unit="pages"><start>535</start><end>544</end></extent></part><relatedItem type="host"><titleInfo><title>Structure</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>2</number></detail><extent unit="pages"><start>535</start><end>544</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit31"><titleInfo><title>Fusion mutants of the influenza virus haemagglutinin glycoprotein</title></titleInfo><name type="personal"><namePart type="given">RS</namePart><namePart type="family">Daniels</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Daniels RS, Downie JC, Hay AJ, Knossow M, Skehel JJ, Wang ML, Wiley DC. 1985. Fusion mutants of the influenza virus haemagglutinin glycoprotein. Cell 40:431–439.Medline</note><part><date>1985</date><detail type="volume"><caption>vol.</caption><number>40</number></detail><extent unit="pages"><start>431</start><end>439</end></extent></part><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><part><date>1985</date><detail type="volume"><caption>vol.</caption><number>40</number></detail><extent unit="pages"><start>431</start><end>439</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit32"><titleInfo><title>Preclinical efficacy of a prototype DNA vaccine: enhanced protection against antigenic drift in influenza virus</title></titleInfo><name type="personal"><namePart type="given">JJ</namePart><namePart type="family">Donnelly</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Donnelly JJ, Friedman A, Martinez D, Montgomery DL, Shiver JW, Motzel SL, Ulmer JB, Liu MA. 1995. Preclinical efficacy of a prototype DNA vaccine: enhanced protection against antigenic drift in influenza virus. Nat Med 1:583–586.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>1</number></detail><extent unit="pages"><start>583</start><end>586</end></extent></part><relatedItem type="host"><titleInfo><title>Nat Med</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>1</number></detail><extent unit="pages"><start>583</start><end>586</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit33"><titleInfo><title>Drug therapy, prophylaxis and treatment of influenza</title></titleInfo><name type="personal"><namePart type="given">RG</namePart><namePart type="family">Douglas Jr</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Douglas Jr RG. 1990. Drug therapy, prophylaxis and treatment of influenza. N Engl J Med 322:443–450.Medline</note><part><date>1990</date><detail type="volume"><caption>vol.</caption><number>322</number></detail><extent unit="pages"><start>443</start><end>450</end></extent></part><relatedItem type="host"><titleInfo><title>N Engl J Med</title></titleInfo><part><date>1990</date><detail type="volume"><caption>vol.</caption><number>322</number></detail><extent unit="pages"><start>443</start><end>450</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit34"><titleInfo><title>Electron microscopy of purified influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">R</namePart><namePart type="family">Drzenick</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Drzenick R, Frank H, Rott R. 1968. Electron microscopy of purified influenza virus neuraminidase. Virology 36:703–707.Medline</note><part><date>1968</date><detail type="volume"><caption>vol.</caption><number>36</number></detail><extent unit="pages"><start>703</start><end>707</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1968</date><detail type="volume"><caption>vol.</caption><number>36</number></detail><extent unit="pages"><start>703</start><end>707</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit35"><titleInfo><title>The inhibition of neuraminidase and antiviral action</title></titleInfo><name type="personal"><namePart type="given">JD</namePart><namePart type="family">Edmond</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Edmond JD, Johnston RG, Kidd D, Rylance HJ, Sommerville RG. 1966. The inhibition of neuraminidase and antiviral action. Br J Pharmacol Chemother 27:415–426.</note><part><date>1966</date><detail type="volume"><caption>vol.</caption><number>27</number></detail><extent unit="pages"><start>415</start><end>426</end></extent></part><relatedItem type="host"><titleInfo><title>Br J Pharmacol Chemother</title></titleInfo><part><date>1966</date><detail type="volume"><caption>vol.</caption><number>27</number></detail><extent unit="pages"><start>415</start><end>426</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit36"><titleInfo><title>Penetration of GS 4071, a novel influenza neuraminidase inhibitor, into rat bronchoalveolar lining fluid following oral administration of prodrug GS4104.</title></titleInfo><name type="personal"><namePart type="given">EJ</namePart><namePart type="family">Eisenberg</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Eisenberg EJ, Bidgood A, Cundy KC. 1997. Penetration of GS 4071, a novel influenza neuraminidase inhibitor, into rat bronchoalveolar lining fluid following oral administration of prodrug GS4104. Antimicrob Agents Chemother 41:1949–1952.Medline</note><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>41</number></detail><extent unit="pages"><start>1949</start><end>1952</end></extent></part><relatedItem type="host"><titleInfo><title>Antimicrob Agents Chemother</title></titleInfo><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>41</number></detail><extent unit="pages"><start>1949</start><end>1952</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit37"><titleInfo><title>Immune interferon produced to high levels antigenic stimulation of human lymphocytes with influenza virus</title></titleInfo><name type="personal"><namePart type="given">FA</namePart><namePart type="family">Ennis</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Ennis FA, Meager A. 1981. Immune interferon produced to high levels antigenic stimulation of human lymphocytes with influenza virus. J Exp Med 154:1279–1289.Medline</note><part><date>1981</date><detail type="volume"><caption>vol.</caption><number>154</number></detail><extent unit="pages"><start>1279</start><end>1289</end></extent></part><relatedItem type="host"><titleInfo><title>J Exp Med</title></titleInfo><part><date>1981</date><detail type="volume"><caption>vol.</caption><number>154</number></detail><extent unit="pages"><start>1279</start><end>1289</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit38"><titleInfo><title>Influenza virus infections in Seattle families, 1975–1979. II. Pattern of infection of invaded households and relation of age and prior antibody to occurrence of infection by time and age</title></titleInfo><name type="personal"><namePart type="given">JP</namePart><namePart type="family">Fox</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Fox JP, Cooney MK, Hall CE, Foy HM. 1982. Influenza virus infections in Seattle families, 1975–1979. II. Pattern of infection of invaded households and relation of age and prior antibody to occurrence of infection by time and age. Am J Epidemiol 116:228–242.Medline</note><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>116</number></detail><extent unit="pages"><start>228</start><end>242</end></extent></part><relatedItem type="host"><titleInfo><title>Am J Epidemiol</title></titleInfo><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>116</number></detail><extent unit="pages"><start>228</start><end>242</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit39"><titleInfo><title>A study of the neurotropic tendency in strains of the virus of epidemic influenza</title></titleInfo><name type="personal"><namePart type="given">T</namePart><namePart type="family">Francis Jr</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Francis Jr T, Moore AE. 1940. A study of the neurotropic tendency in strains of the virus of epidemic influenza. J Exp Med 72:717–728.</note><part><date>1940</date><detail type="volume"><caption>vol.</caption><number>72</number></detail><extent unit="pages"><start>717</start><end>728</end></extent></part><relatedItem type="host"><titleInfo><title>J Exp Med</title></titleInfo><part><date>1940</date><detail type="volume"><caption>vol.</caption><number>72</number></detail><extent unit="pages"><start>717</start><end>728</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit40"><titleInfo><title>Supp M. 1H‐NMR spektroskopischer nachweis der N‐acetyl‐a‐D‐neuraminsaure als primares spaltprodukt der neuraminidasen</title></titleInfo><name type="personal"><namePart type="given">H</namePart><namePart type="family">Friebolin</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Friebolin H, Brossmer R, Keilich G, Ziegler D. 1980. Supp M. 1H‐NMR spektroskopischer nachweis der N‐acetyl‐a‐D‐neuraminsaure als primares spaltprodukt der neuraminidasen. Hoppe Seyler’s Z Physiol Chem 361:697–702.Medline</note><part><date>1980</date><detail type="volume"><caption>vol.</caption><number>361</number></detail><extent unit="pages"><start>697</start><end>702</end></extent></part><relatedItem type="host"><titleInfo><title>Hoppe Seyler’s Z Physiol Chem</title></titleInfo><part><date>1980</date><detail type="volume"><caption>vol.</caption><number>361</number></detail><extent unit="pages"><start>697</start><end>702</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit41"><titleInfo><title>A computational procedure for determining energetically favourable binding sites on biologically important macromolecules</title></titleInfo><name type="personal"><namePart type="given">PJ</namePart><namePart type="family">Goodford</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Goodford PJ. 1985. A computational procedure for determining energetically favourable binding sites on biologically important macromolecules. J Med Chem 28:849–857.Medline</note><part><date>1985</date><detail type="volume"><caption>vol.</caption><number>28</number></detail><extent unit="pages"><start>849</start><end>857</end></extent></part><relatedItem type="host"><titleInfo><title>J Med Chem</title></titleInfo><part><date>1985</date><detail type="volume"><caption>vol.</caption><number>28</number></detail><extent unit="pages"><start>849</start><end>857</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit42"><titleInfo><title>Neuraminidase: the specific enzyme of influenza virus and vibrio cholerae</title></titleInfo><name type="personal"><namePart type="given">A</namePart><namePart type="family">Gottschalk</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Gottschalk A. 1957. Neuraminidase: the specific enzyme of influenza virus and vibrio cholerae. Biochem Biophys Acta 23:645–646.</note><part><date>1957</date><detail type="volume"><caption>vol.</caption><number>23</number></detail><extent unit="pages"><start>645</start><end>646</end></extent></part><relatedItem type="host"><titleInfo><title>Biochem Biophys Acta</title></titleInfo><part><date>1957</date><detail type="volume"><caption>vol.</caption><number>23</number></detail><extent unit="pages"><start>645</start><end>646</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit43"><titleInfo><title>Neuraminidase: its substrate and mode of action</title></titleInfo><name type="personal"><namePart type="given">A</namePart><namePart type="family">Gottschalk</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Gottschalk A. 1958. Neuraminidase: its substrate and mode of action. Adv Enzymol 20:135–145.</note><part><date>1958</date><detail type="volume"><caption>vol.</caption><number>20</number></detail><extent unit="pages"><start>135</start><end>145</end></extent></part><relatedItem type="host"><titleInfo><title>Adv Enzymol</title></titleInfo><part><date>1958</date><detail type="volume"><caption>vol.</caption><number>20</number></detail><extent unit="pages"><start>135</start><end>145</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit44"><titleInfo><title>A novel mechanism for the acquisition of virulence by a human influenza A virus</title></titleInfo><name type="personal"><namePart type="given">H</namePart><namePart type="family">Goto</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Goto H, Kawaoka Y. 1998. A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc Natl Acad Sci USA 95:10224–10228.</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>95</number></detail><extent unit="pages"><start>10224</start><end>10228</end></extent></part><relatedItem type="host"><titleInfo><title>Proc Natl Acad Sci USA</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>95</number></detail><extent unit="pages"><start>10224</start><end>10228</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit45"><titleInfo><title>Effect of cytochalsin B on the maturation of enveloped viruses</title></titleInfo><name type="personal"><namePart type="given">JA</namePart><namePart type="family">Griffin</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Griffin JA, Compans RW. 1979. Effect of cytochalsin B on the maturation of enveloped viruses. J Exp Med 150:379–391.Medline</note><part><date>1979</date><detail type="volume"><caption>vol.</caption><number>150</number></detail><extent unit="pages"><start>379</start><end>391</end></extent></part><relatedItem type="host"><titleInfo><title>J Exp Med</title></titleInfo><part><date>1979</date><detail type="volume"><caption>vol.</caption><number>150</number></detail><extent unit="pages"><start>379</start><end>391</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit46"><titleInfo><title>Characterization of mutants of influenza virus selected with 4‐guanidino‐Neu5Ac2en</title></titleInfo><name type="personal"><namePart type="given">LV</namePart><namePart type="family">Gubareva</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1995</date></part></relatedItem><relatedItem type="references" displayLabel="cit47"><titleInfo><title>Catalytic framework mutations in the neuraminidase active site of influenza viruses that are resistant to 4‐guanidino‐Neu5Ac2en</title></titleInfo><name type="personal"><namePart type="given">LV</namePart><namePart type="family">Gubareva</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Gubareva LV, Robinson MJ, Bethell R, Webster RG. 1997. Catalytic framework mutations in the neuraminidase active site of influenza viruses that are resistant to 4‐guanidino‐Neu5Ac2en. J Virol 71:3385–3390.Medline</note><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>71</number></detail><extent unit="pages"><start>3385</start><end>3390</end></extent></part><relatedItem type="host"><titleInfo><title>J Virol</title></titleInfo><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>71</number></detail><extent unit="pages"><start>3385</start><end>3390</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit48"><titleInfo><title>Evidence for Zanamivir resistence in an immunocompromised child infected with influenza B virus</title></titleInfo><name type="personal"><namePart type="given">LV</namePart><namePart type="family">Gubareva</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Gubareva LV, Matrosovich MN, Brenner MK, Bethel RC, Webster RG. 1998. Evidence for Zanamivir resistence in an immunocompromised child infected with influenza B virus. J Infect Diseases 178:1257–1262.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>178</number></detail><extent unit="pages"><start>1257</start><end>1262</end></extent></part><relatedItem type="host"><titleInfo><title>J Infect Diseases</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>178</number></detail><extent unit="pages"><start>1257</start><end>1262</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit49"><titleInfo><title>N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity</title></titleInfo><name type="personal"><namePart type="given">J</namePart><namePart type="family">Hausmann</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Hausmann J, Kretzschmar E, Garten W, Klenk H‐D. 1995. N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity. J Gen Virol 76:1719–1728.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>76</number></detail><extent unit="pages"><start>1719</start><end>1728</end></extent></part><relatedItem type="host"><titleInfo><title>J Gen Virol</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>76</number></detail><extent unit="pages"><start>1719</start><end>1728</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit50"><titleInfo><title>The role of the M2 protein in influenza virus infection</title></titleInfo><name type="personal"><namePart type="given">AJ</namePart><namePart type="family">Hay</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Options for the control of influenza virus II</title></titleInfo><originInfo><publisher>Excerpta Medica</publisher><place><placeTerm type="text">Amsterdam</placeTerm></place></originInfo><part><date>1993</date><extent unit="pages"><start>281</start><end>288</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit51"><titleInfo><title>Update on antiviral agents and viral drug resistance</title></titleInfo><name type="personal"><namePart type="given">FG</namePart><namePart type="family">Hayden</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Principles and practice of infectious disease</title></titleInfo><originInfo><publisher>Churchill Livingston</publisher><place><placeTerm type="text">New York</placeTerm></place></originInfo><part><date>1993</date><extent unit="pages"><start>2(2):3</start><end>15</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit52"><titleInfo><title>Amantidine and rimantidine – clinical aspects</title></titleInfo><name type="personal"><namePart type="given">FG</namePart><namePart type="family">Hayden</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Antiviral drug resistance</title></titleInfo><originInfo><publisher>John Wiley</publisher><place><placeTerm type="text">Chichester, UK</placeTerm></place></originInfo><part><date>1996</date><extent unit="pages"><start>69</start><end>77</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit53"><titleInfo><title>Anti‐influenza activity of the neuraminidase inhibitor 4‐guanidino‐Neu5Ac2en in cell culture and in human respiratory epithelium</title></titleInfo><name type="personal"><namePart type="given">FG</namePart><namePart type="family">Hayden</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Hayden FG, Rollins BS, Madren LK. 1994. Anti‐influenza activity of the neuraminidase inhibitor 4‐guanidino‐Neu5Ac2en in cell culture and in human respiratory epithelium. Antiviral Res 25:123–131.Medline</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>25</number></detail><extent unit="pages"><start>123</start><end>131</end></extent></part><relatedItem type="host"><titleInfo><title>Antiviral Res</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>25</number></detail><extent unit="pages"><start>123</start><end>131</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit54"><titleInfo><title>Safety and efficacy of the neuraminidase inhibitor GG167 in experimental human influenza</title></titleInfo><name type="personal"><namePart type="given">FG</namePart><namePart type="family">Hayden</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Hayden FG, Treanor JJ, Betts RF, Lobo M, Esinhart JD, Hussey EK. 1996. Safety and efficacy of the neuraminidase inhibitor GG167 in experimental human influenza. JAMA 275:295–299.Medline</note><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>275</number></detail><extent unit="pages"><start>295</start><end>299</end></extent></part><relatedItem type="host"><titleInfo><title>JAMA</title></titleInfo><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>275</number></detail><extent unit="pages"><start>295</start><end>299</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit55"><titleInfo><title>Efficacy and safety of the neuramimnidase inhibitor Zanamivir in the treatment of influenza virus infections</title></titleInfo><name type="personal"><namePart type="given">FG</namePart><namePart type="family">Hayden</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Hayden FG, Osterhaus ADME, Treanor JJ, Fleming DM, Aoki FY, Nicholson KG, Bohnen AM, Hirst HM, Keene O, Whiteman K. 1997. Efficacy and safety of the neuramimnidase inhibitor Zanamivir in the treatment of influenza virus infections. N Engl J Med 337:874–880.Medline</note><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>337</number></detail><extent unit="pages"><start>874</start><end>880</end></extent></part><relatedItem type="host"><titleInfo><title>N Engl J Med</title></titleInfo><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>337</number></detail><extent unit="pages"><start>874</start><end>880</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit56"><titleInfo><title>Safety and efficacy of oral GS4104 in longterm prophylaxis of natural influenza.</title></titleInfo><name type="personal"><namePart type="given">FG</namePart><namePart type="family">Hayden</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1998</date></part></relatedItem><relatedItem type="references" displayLabel="cit57"><titleInfo><title>The perpetuation of orthomyxoviruses and paramyxoviruses in Canadian waterfowl</title></titleInfo><name type="personal"><namePart type="given">VS</namePart><namePart type="family">Hinshaw</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Hinshaw VS, Webster RG, Turner B. 1980. The perpetuation of orthomyxoviruses and paramyxoviruses in Canadian waterfowl. Can J Microbiol 26:622–629.Medline</note><part><date>1980</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><extent unit="pages"><start>622</start><end>629</end></extent></part><relatedItem type="host"><titleInfo><title>Can J Microbiol</title></titleInfo><part><date>1980</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><extent unit="pages"><start>622</start><end>629</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit58"><titleInfo><title>Adsorption of influenza hemagglutinins and virus by red blood cells</title></titleInfo><name type="personal"><namePart type="given">GK</namePart><namePart type="family">Hirst</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Hirst GK. 1942. Adsorption of influenza hemagglutinins and virus by red blood cells. J Exp Med 76:1740–1743.</note><part><date>1942</date><detail type="volume"><caption>vol.</caption><number>76</number></detail><extent unit="pages"><start>1740</start><end>1743</end></extent></part><relatedItem type="host"><titleInfo><title>J Exp Med</title></titleInfo><part><date>1942</date><detail type="volume"><caption>vol.</caption><number>76</number></detail><extent unit="pages"><start>1740</start><end>1743</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit59"><titleInfo><title>Complete nucleotide sequences of the neuraminidase gene of human influenza virus A/WSN/33</title></titleInfo><name type="personal"><namePart type="given">AL</namePart><namePart type="family">Hitte</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Hitte AL, Nayak DP. 1982. Complete nucleotide sequences of the neuraminidase gene of human influenza virus A/WSN/33. J Virol 41:730–734.Medline</note><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>41</number></detail><extent unit="pages"><start>730</start><end>734</end></extent></part><relatedItem type="host"><titleInfo><title>J Virol</title></titleInfo><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>41</number></detail><extent unit="pages"><start>730</start><end>734</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit60"><titleInfo><title>Structure of influenza virus neuraminidase B/Lee/40 complexed with sialic acid and a dehydro analog at 1. 8A‐resolution: implications for the catalytic mechanism</title></titleInfo><name type="personal"><namePart type="given">MN</namePart><namePart type="family">Janakiraman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Janakiraman MN, White CL, Laver WG, Air MA, Luo M. 1994. Structure of influenza virus neuraminidase B/Lee/40 complexed with sialic acid and a dehydro analog at 1. 8A‐resolution: implications for the catalytic mechanism. Biochemstry 33:8172–8179.</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>33</number></detail><extent unit="pages"><start>8172</start><end>8179</end></extent></part><relatedItem type="host"><titleInfo><title>Biochemstry</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>33</number></detail><extent unit="pages"><start>8172</start><end>8179</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit61"><titleInfo><title>Influenza</title></titleInfo><name type="personal"><namePart type="given">ED</namePart><namePart type="family">Kilbourne</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><genre>book</genre><originInfo><publisher>Plenum Press</publisher></originInfo><part><date>1987</date></part></relatedItem><relatedItem type="references" displayLabel="cit62"><titleInfo><title>Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti‐influenza activity</title></titleInfo><name type="personal"><namePart type="given">CU</namePart><namePart type="family">Kim</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Kim CU, Lew W, Williams MA, Liu H, Zhang L, Swaminathan S, Bischofberger N, Chen MS, Mendel DB, Tai CY, Laver WG, Stevens RC. 1997. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti‐influenza activity. J Am Chem Soc 119:681–690.</note><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>119</number></detail><extent unit="pages"><start>681</start><end>690</end></extent></part><relatedItem type="host"><titleInfo><title>J Am Chem Soc</title></titleInfo><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>119</number></detail><extent unit="pages"><start>681</start><end>690</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit63"><titleInfo><title>Antiviral resistance in clinical practice</title></titleInfo><name type="personal"><namePart type="given">DW</namePart><namePart type="family">Kimberlin</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Kimberlin DW, Crumpacker CS, Straus SE, Biron KK, Drew WL, Hayden FG, McKinlay M, Richman DD, Whitley RJ. 1995. Antiviral resistance in clinical practice. Antiviral Res 26:423–438.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><extent unit="pages"><start>423</start><end>438</end></extent></part><relatedItem type="host"><titleInfo><title>Antiviral Res</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><extent unit="pages"><start>423</start><end>438</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit64"><titleInfo><title>Uber die enzymatishe Wirkung von Ifluenza</title></titleInfo><name type="personal"><namePart type="given">E</namePart><namePart type="family">Klenk</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Klenk E, Faillard H, Lempfrid H. 1955. Uber die enzymatishe Wirkung von Ifluenza. Z Physiol Chem 301:235–246.</note><part><date>1955</date><detail type="volume"><caption>vol.</caption><number>301</number></detail><extent unit="pages"><start>235</start><end>246</end></extent></part><relatedItem type="host"><titleInfo><title>Z Physiol Chem</title></titleInfo><part><date>1955</date><detail type="volume"><caption>vol.</caption><number>301</number></detail><extent unit="pages"><start>235</start><end>246</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit65"><titleInfo><title>MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures</title></titleInfo><name type="personal"><namePart type="given">PJ</namePart><namePart type="family">Kraulis</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1991</date></part></relatedItem><relatedItem type="references" displayLabel="cit66"><titleInfo><title>Rapid and efficient site‐specific mutagenesis without phenotypic selection</title></titleInfo><name type="personal"><namePart type="given">TA</namePart><namePart type="family">Kunkel</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Kunkel TA, Roberts JD, Zakaur RA. 1987. Rapid and efficient site‐specific mutagenesis without phenotypic selection. Methods Enzymol 154:369–382.</note><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>154</number></detail><extent unit="pages"><start>369</start><end>382</end></extent></part><relatedItem type="host"><titleInfo><title>Methods Enzymol</title></titleInfo><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>154</number></detail><extent unit="pages"><start>369</start><end>382</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit67"><titleInfo><title>Genes and proteins of the influenza virus</title></titleInfo><name type="personal"><namePart type="given">RA</namePart><namePart type="family">Lamb</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>The influenza viruses</title></titleInfo><originInfo><publisher>Plenum Press</publisher><place><placeTerm type="text">New York</placeTerm></place></originInfo><part><date>1989</date><extent unit="pages"><start>1</start><end>87</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit68"><titleInfo><title>The structure of influenza virus 3. Disruption of the virus particle and separation of neuraminidase activity</title></titleInfo><name type="personal"><namePart type="given">WG</namePart><namePart type="family">Laver</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Laver WG. 1963. The structure of influenza virus 3. Disruption of the virus particle and separation of neuraminidase activity. Virology 20:251–262.</note><part><date>1963</date><detail type="volume"><caption>vol.</caption><number>20</number></detail><extent unit="pages"><start>251</start><end>262</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1963</date><detail type="volume"><caption>vol.</caption><number>20</number></detail><extent unit="pages"><start>251</start><end>262</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit69"><titleInfo><title>Crystallization and peptide maps of neuraminidase “heads” from H2N2 and H3N2 influenza virus strains</title></titleInfo><name type="personal"><namePart type="given">WG</namePart><namePart type="family">Laver</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Laver WG. 1978. Crystallization and peptide maps of neuraminidase “heads” from H2N2 and H3N2 influenza virus strains. Virology 86:78–87.Medline</note><part><date>1978</date><detail type="volume"><caption>vol.</caption><number>86</number></detail><extent unit="pages"><start>78</start><end>87</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1978</date><detail type="volume"><caption>vol.</caption><number>86</number></detail><extent unit="pages"><start>78</start><end>87</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit70"><titleInfo><title>Morphology of the isolated hemagglutinin and neuraminidase subunits of influenza virus</title></titleInfo><name type="personal"><namePart type="given">WG</namePart><namePart type="family">Laver</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Laver WG, Valentine RC. 1969. Morphology of the isolated hemagglutinin and neuraminidase subunits of influenza virus. Virology 38:105–119.Medline</note><part><date>1969</date><detail type="volume"><caption>vol.</caption><number>38</number></detail><extent unit="pages"><start>105</start><end>119</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1969</date><detail type="volume"><caption>vol.</caption><number>38</number></detail><extent unit="pages"><start>105</start><end>119</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit71"><titleInfo><title>Influenza virus neuraminidase with hemagglutinin activity</title></titleInfo><name type="personal"><namePart type="given">WG</namePart><namePart type="family">Laver</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Laver WG, Colman PM, Webster RG, Hinshaw VS, Air GM. 1984. Influenza virus neuraminidase with hemagglutinin activity. Virology 137:314–323.Medline</note><part><date>1984</date><detail type="volume"><caption>vol.</caption><number>137</number></detail><extent unit="pages"><start>314</start><end>323</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1984</date><detail type="volume"><caption>vol.</caption><number>137</number></detail><extent unit="pages"><start>314</start><end>323</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit72"><titleInfo><title>Site‐directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism</title></titleInfo><name type="personal"><namePart type="given">MR</namePart><namePart type="family">Lentz</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Lentz MR, Webster RG, Air GM. 1987. Site‐directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism. Biochemistry 26:5351–5358.Medline</note><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><extent unit="pages"><start>5351</start><end>5358</end></extent></part><relatedItem type="host"><titleInfo><title>Biochemistry</title></titleInfo><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>26</number></detail><extent unit="pages"><start>5351</start><end>5358</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit73"><titleInfo><title>Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus</title></titleInfo><name type="personal"><namePart type="given">S</namePart><namePart type="family">Li</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Li S, Schulman J, Itamura S, Palase P. 1993. Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus. J Virol 67:6667–6673.Medline</note><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>67</number></detail><extent unit="pages"><start>6667</start><end>6673</end></extent></part><relatedItem type="host"><titleInfo><title>J Virol</title></titleInfo><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>67</number></detail><extent unit="pages"><start>6667</start><end>6673</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit74"><titleInfo><title>Identification of GS4104 as an orally bioavailable prodrug of the influenza virus neuraminidase inhibitor GS4071</title></titleInfo><name type="personal"><namePart type="given">W</namePart><namePart type="family">Li</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Li W, Escarpe PA, Eisenberg EJ, Cundy KC, Sweet C, Jakeman KJ, Merson J, Lew W, Williams M, Zhang L, Kim CU, Bischofberger N, Chen MS, Mendel DB. 1998. Identification of GS4104 as an orally bioavailable prodrug of the influenza virus neuraminidase inhibitor GS4071. Antimicrob Agents Chemother 42:647–653.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>42</number></detail><extent unit="pages"><start>647</start><end>653</end></extent></part><relatedItem type="host"><titleInfo><title>Antimicrob Agents Chemother</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>42</number></detail><extent unit="pages"><start>647</start><end>653</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit75"><titleInfo><title>Selection and characterization of a neuraminidase‐minus mutant of influenza virus and its rescue by cloned neuraminidase genes</title></titleInfo><name type="personal"><namePart type="given">C</namePart><namePart type="family">Liu</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Liu C, Air GM. 1993. Selection and characterization of a neuraminidase‐minus mutant of influenza virus and its rescue by cloned neuraminidase genes. Virology 194:403–407.Medline</note><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>194</number></detail><extent unit="pages"><start>403</start><end>407</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>194</number></detail><extent unit="pages"><start>403</start><end>407</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit76"><titleInfo><title>Influenza type A viurs neuraminidase does not play a role in viral entry, replication, assembly, or budding</title></titleInfo><name type="personal"><namePart type="given">C</namePart><namePart type="family">Liu</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Liu C, Eichelberger MC, Compans RW, Air GM. 1995. Influenza type A viurs neuraminidase does not play a role in viral entry, replication, assembly, or budding. J Virol 69:1099–1106.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>69</number></detail><extent unit="pages"><start>1099</start><end>1106</end></extent></part><relatedItem type="host"><titleInfo><title>J Virol</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>69</number></detail><extent unit="pages"><start>1099</start><end>1106</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit77"><titleInfo><title>Benzoic acid inhibitors of influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">M</namePart><namePart type="family">Luo</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Luo M, Jedrzejas MJ, Singh S, White CL, Brouillette WJ, Air GM, Laver WG. 1995. Benzoic acid inhibitors of influenza virus neuraminidase. Acta Crystallogr D 51:504–510.</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>51</number></detail><extent unit="pages"><start>504</start><end>510</end></extent></part><relatedItem type="host"><titleInfo><title>Acta Crystallogr D</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>51</number></detail><extent unit="pages"><start>504</start><end>510</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit78"><titleInfo><title>In vitro inhibitory effects of combinations of anti‐influenza agents</title></titleInfo><name type="personal"><namePart type="given">LK</namePart><namePart type="family">Madren</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Madren LK, Shipman C, Hayden FG. 1995. In vitro inhibitory effects of combinations of anti‐influenza agents. Antiviral Chem Chemother 6(2):109–113.</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>6(2)</number></detail><extent unit="pages"><start>109</start><end>113</end></extent></part><relatedItem type="host"><titleInfo><title>Antiviral Chem Chemother</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>6(2)</number></detail><extent unit="pages"><start>109</start><end>113</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit79"><titleInfo><title>The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody</title></titleInfo><name type="personal"><namePart type="given">RL</namePart><namePart type="family">Malby</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Malby RL, Tulip WR, Harley VR, McKimm‐Breschkin JL, Laver WG, Webster RG, Colman PM. 1994. The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody. Structure 2:733–746.Medline</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>2</number></detail><extent unit="pages"><start>733</start><end>746</end></extent></part><relatedItem type="host"><titleInfo><title>Structure</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>2</number></detail><extent unit="pages"><start>733</start><end>746</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit80"><titleInfo><title>Phenotypic changes observed in influenza viruses passaged in 4‐amino or 4‐guanidino‐Neu5Ac2en in vitro</title></titleInfo><name type="personal"><namePart type="given">JL</namePart><namePart type="family">McKimm‐Breschkin</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1994</date></part></relatedItem><relatedItem type="references" displayLabel="cit81"><titleInfo><title>Generation and characterisation of variants of the NWS/G70C influenza virus after in vitro passage in 4‐amino‐Neu5Ac2en and 4‐guanidino‐Neu5Ac2en</title></titleInfo><name type="personal"><namePart type="given">JL</namePart><namePart type="family">McKimm‐Breschkin</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">McKimm‐Breschkin JL, Blick TJ, Sarasrabudhe AV, Tiong T, Marshall D, Hart GJ, Bethell RC, Penn CR. 1996. Generation and characterisation of variants of the NWS/G70C influenza virus after in vitro passage in 4‐amino‐Neu5Ac2en and 4‐guanidino‐Neu5Ac2en. Antimicrob Agents Chemother 40:40–46.Medline</note><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>40</number></detail><extent unit="pages"><start>40</start><end>46</end></extent></part><relatedItem type="host"><titleInfo><title>Antimicrob Agents Chemother</title></titleInfo><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>40</number></detail><extent unit="pages"><start>40</start><end>46</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit82"><titleInfo><title>Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en derivatives</title></titleInfo><name type="personal"><namePart type="given">JL</namePart><namePart type="family">McKimm‐Breschkin</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">McKimm‐Breschkin JL, Sahasrabudhe A, Blick TJ, McDonald M, Colman PM, Hart GJ, Bethell RC, Varghese JN. 1998. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en derivatives. J Virol 72:2456–2462.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>72</number></detail><extent unit="pages"><start>2456</start><end>2462</end></extent></part><relatedItem type="host"><titleInfo><title>J Virol</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>72</number></detail><extent unit="pages"><start>2456</start><end>2462</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit83"><titleInfo><title>2‐Deoxy‐2,3‐dehydrosialic acids. I. Synthesis and properties of 2‐deoxy‐2,3‐dehydro‐N‐acetylneuraminic acids and their methyl esters. Monatsh Chem</title></titleInfo><name type="personal"><namePart type="given">P</namePart><namePart type="family">Meindl</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1969</date></part></relatedItem><relatedItem type="references" displayLabel="cit84"><titleInfo><title>Inhibition of neuraminidase activity by derivatives of 2‐deoxy‐2,3‐dehydro‐N‐acetylneuraminic</title></titleInfo><name type="personal"><namePart type="given">P</namePart><namePart type="family">Meindl</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Meindl P, Bodo G, Palase P, Schulman J, Tuppy H. 1974. Inhibition of neuraminidase activity by derivatives of 2‐deoxy‐2,3‐dehydro‐N‐acetylneuraminic. Virology 58:457–463.Medline</note><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>58</number></detail><extent unit="pages"><start>457</start><end>463</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>58</number></detail><extent unit="pages"><start>457</start><end>463</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit85"><titleInfo><title>Oral administration of a prodrug of the influenza virus neuraminidase inhibitor GS4071 protects mice and ferrets against influenza infection</title></titleInfo><name type="personal"><namePart type="given">DB</namePart><namePart type="family">Mendel</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Mendel DB, Tai CY, Escarpe PA, Sidwell RW, Huffman JH, Sweet C, Jakeman KJ, Merson J, Lacy SA, Lew W, Williams MA, Zhang L, Chen MS, Bischofberger N, Kim CU. 1998. Oral administration of a prodrug of the influenza virus neuraminidase inhibitor GS4071 protects mice and ferrets against influenza infection. Antimicrob Agents Chemother 42:640–646.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>42</number></detail><extent unit="pages"><start>640</start><end>646</end></extent></part><relatedItem type="host"><titleInfo><title>Antimicrob Agents Chemother</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>42</number></detail><extent unit="pages"><start>640</start><end>646</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit86"><titleInfo><title>Mechanism of Arthro‐bacter sialophilus neuraminidase: the binding of substrates and transition state analogues</title></titleInfo><name type="personal"><namePart type="given">CA</namePart><namePart type="family">Miller</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Miller CA, Wang P, Flashner M. 1978. Mechanism of Arthro‐bacter sialophilus neuraminidase: the binding of substrates and transition state analogues. Biochem Biophys Res Commun 83:1479–1487.Medline</note><part><date>1978</date><detail type="volume"><caption>vol.</caption><number>83</number></detail><extent unit="pages"><start>1479</start><end>1487</end></extent></part><relatedItem type="host"><titleInfo><title>Biochem Biophys Res Commun</title></titleInfo><part><date>1978</date><detail type="volume"><caption>vol.</caption><number>83</number></detail><extent unit="pages"><start>1479</start><end>1487</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit87"><titleInfo><title>Safety and efficacy of long term use of rimantadine for prophylaxis of type 1 influenza in nursing homes</title></titleInfo><name type="personal"><namePart type="given">AS</namePart><namePart type="family">Monto</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Monto AS, Ohmir Se, Hornbuckle K, Pearce CL. 1995. Safety and efficacy of long term use of rimantadine for prophylaxis of type 1 influenza in nursing homes. Antimicrob Agents Chemother 39:2224–2228.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>39</number></detail><extent unit="pages"><start>2224</start><end>2228</end></extent></part><relatedItem type="host"><titleInfo><title>Antimicrob Agents Chemother</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>39</number></detail><extent unit="pages"><start>2224</start><end>2228</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit88"><titleInfo><title>Efficacy and safety of zanamivir in prevention of influenza among healthy adults.</title></titleInfo><name type="personal"><namePart type="given">AS</namePart><namePart type="family">Monto</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1998</date></part></relatedItem><relatedItem type="references" displayLabel="cit89"><titleInfo><title>Observations with the electron microscope on cells of chick chorio‐allantoic membrane infected with influenza virus</title></titleInfo><name type="personal"><namePart type="given">JS</namePart><namePart type="family">Murphy</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Murphy JS, Bang FB. 1952. Observations with the electron microscope on cells of chick chorio‐allantoic membrane infected with influenza virus. J Exp Med 95:259.</note><part><date>1952</date><detail type="volume"><caption>vol.</caption><number>95</number></detail><extent unit="pages"><start>259</start></extent></part><relatedItem type="host"><titleInfo><title>J Exp Med</title></titleInfo><part><date>1952</date><detail type="volume"><caption>vol.</caption><number>95</number></detail><extent unit="pages"><start>259</start></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit90"><titleInfo><title>Orthomyxovirus</title></titleInfo><name type="personal"><namePart type="given">BR</namePart><namePart type="family">Murphy</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><originInfo><publisher>Raven Press</publisher><place><placeTerm type="text">New York</placeTerm></place></originInfo><part><date>1990</date><extent unit="pages"><start>1091</start><end>1152</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit91"><titleInfo><title>In vivo anti‐influenza virus activity of Kampo (Japanese herbal) medicine “Sho‐seiryu‐to” and its mode of action</title></titleInfo><name type="personal"><namePart type="given">T</namePart><namePart type="family">Nagai</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Nagai T, Yamada H. 1994. In vivo anti‐influenza virus activity of Kampo (Japanese herbal) medicine “Sho‐seiryu‐to” and its mode of action. Int J Immunopharmacol 16(8):605–613.Medline</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>16(8)</number></detail><extent unit="pages"><start>605</start><end>613</end></extent></part><relatedItem type="host"><titleInfo><title>Int J Immunopharmacol</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>16(8)</number></detail><extent unit="pages"><start>605</start><end>613</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit92"><titleInfo><title>Inhibition of influenza virus sialidase and anti‐influenza virus activity by plant flavonoids</title></titleInfo><name type="personal"><namePart type="given">T</namePart><namePart type="family">Nagai</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Nagai T, Miyaichi Y, Tomimori T, Suzuki Y, Yamada H. 1990. Inhibition of influenza virus sialidase and anti‐influenza virus activity by plant flavonoids. Chem Pharm Bull 38(5):1329–1332.Medline</note><part><date>1990</date><detail type="volume"><caption>vol.</caption><number>38(5)</number></detail><extent unit="pages"><start>1329</start><end>1332</end></extent></part><relatedItem type="host"><titleInfo><title>Chem Pharm Bull</title></titleInfo><part><date>1990</date><detail type="volume"><caption>vol.</caption><number>38(5)</number></detail><extent unit="pages"><start>1329</start><end>1332</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit93"><titleInfo><title>Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons</title></titleInfo><name type="personal"><namePart type="given">A</namePart><namePart type="family">Nicholls</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Nicholls A, Sharp K, Honig B. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281–296.Medline</note><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>11</number></detail><extent unit="pages"><start>281</start><end>296</end></extent></part><relatedItem type="host"><titleInfo><title>Proteins</title></titleInfo><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>11</number></detail><extent unit="pages"><start>281</start><end>296</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit94"><titleInfo><title>Uptake, metabolism and excretion of orally and intravenously administered, double‐labeled N‐glycoloylneuraminic and single‐labeled 2‐deoxy‐2,3‐dehydro‐N‐acetylneuraminic acid in mouse and rat</title></titleInfo><name type="personal"><namePart type="given">U</namePart><namePart type="family">Nohle</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Nohle U, Beau J‐M, Schauer R. 1982. Uptake, metabolism and excretion of orally and intravenously administered, double‐labeled N‐glycoloylneuraminic and single‐labeled 2‐deoxy‐2,3‐dehydro‐N‐acetylneuraminic acid in mouse and rat. Eur J Biochem 126:543–548.Medline</note><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>126</number></detail><extent unit="pages"><start>543</start><end>548</end></extent></part><relatedItem type="host"><titleInfo><title>Eur J Biochem</title></titleInfo><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>126</number></detail><extent unit="pages"><start>543</start><end>548</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit95"><titleInfo><title>Transfer of the hemagglutinin activity of influenza virus neuraminidase subtype N9 into N2 neuraminidase background</title></titleInfo><name type="personal"><namePart type="given">JM</namePart><namePart type="family">Nuss</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Nuss JM, Air GM. 1991. Transfer of the hemagglutinin activity of influenza virus neuraminidase subtype N9 into N2 neuraminidase background. Virology 183:496–504.Medline</note><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>183</number></detail><extent unit="pages"><start>496</start><end>504</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>183</number></detail><extent unit="pages"><start>496</start><end>504</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit96"><titleInfo><title>Double blind randomised trial of zanamivir in the treatment of acute influenza — clinical and virological efficacy results.</title></titleInfo><name type="personal"><namePart type="given">ADME</namePart><namePart type="family">Osterhaus</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1998</date></part></relatedItem><relatedItem type="references" displayLabel="cit97"><titleInfo><title>Inhibition of influenza virus replication in tissue culture 2‐deoxy‐2,3‐dehydro‐N‐trifluroacetylneuraminic acid. FANA: mechanism of action</title></titleInfo><name type="personal"><namePart type="given">P</namePart><namePart type="family">Palese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Palese P, Compans RW. 1976. Inhibition of influenza virus replication in tissue culture 2‐deoxy‐2,3‐dehydro‐N‐trifluroacetylneuraminic acid. FANA: mechanism of action. J Gen Virol 33:159–163.Medline</note><part><date>1976</date><detail type="volume"><caption>vol.</caption><number>33</number></detail><extent unit="pages"><start>159</start><end>163</end></extent></part><relatedItem type="host"><titleInfo><title>J Gen Virol</title></titleInfo><part><date>1976</date><detail type="volume"><caption>vol.</caption><number>33</number></detail><extent unit="pages"><start>159</start><end>163</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit98"><titleInfo><title>Inhibitors of viral neuraminidase as potential antiviral drugs</title></titleInfo><name type="personal"><namePart type="given">P</namePart><namePart type="family">Palese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>In: Chemoprophylaxis and virus infections of the upper respiratory tract, vol 1</title></titleInfo><originInfo><publisher>CRC Press</publisher><place><placeTerm type="text">Boca Raton, FL</placeTerm></place></originInfo><part><date>1977</date><extent unit="pages"><start>189</start><end>205</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit99"><titleInfo><title>Characterisation of temperature sensitive influenza virus mutants defective in neuraminidase</title></titleInfo><name type="personal"><namePart type="given">P</namePart><namePart type="family">Palese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Palese P, Tobita K, Ueda M, Compans RW. 1974a. Characterisation of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61:397–410.Medline</note><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>61</number></detail><extent unit="pages"><start>397</start><end>410</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>61</number></detail><extent unit="pages"><start>397</start><end>410</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit100"><titleInfo><title>Inhibition of influenza and parainfluenza virus replication in tissue culture by 2‐deoxy‐2,3‐dehydro–N–trifluroacetylneuraminic acid</title></titleInfo><name type="personal"><namePart type="given">P</namePart><namePart type="family">Palese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Palese P, Schulman JL, Bodo G, Meidl P. 1974b. Inhibition of influenza and parainfluenza virus replication in tissue culture by 2‐deoxy‐2,3‐dehydro–N–trifluroacetylneuraminic acid. FANA Virol 59:490–498.</note><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>59</number></detail><extent unit="pages"><start>490</start><end>498</end></extent></part><relatedItem type="host"><titleInfo><title>FANA Virol</title></titleInfo><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>59</number></detail><extent unit="pages"><start>490</start><end>498</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit101"><titleInfo><title>AMBER 4.0.</title></titleInfo><name type="personal"><namePart type="given">DA</namePart><namePart type="family">Pearlman</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1990</date></part></relatedItem><relatedItem type="references" displayLabel="cit102"><titleInfo><title>Influenza virus M2 protein has ion channel activity</title></titleInfo><name type="personal"><namePart type="given">LH</namePart><namePart type="family">Pinto</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Pinto LH, Holsinger LJ, Lamb RA. 1992. Influenza virus M2 protein has ion channel activity. Cell 69:517–528.Medline</note><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>69</number></detail><extent unit="pages"><start>517</start><end>528</end></extent></part><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>69</number></detail><extent unit="pages"><start>517</start><end>528</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit103"><titleInfo><title>Receptor determinants of human and animal influenza virus isolates: difference in receptor specificity of the H3 haemagglutinin based on species of origin</title></titleInfo><name type="personal"><namePart type="given">GN</namePart><namePart type="family">Rogers</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Rogers GN, Paulson JC. 1983. Receptor determinants of human and animal influenza virus isolates: difference in receptor specificity of the H3 haemagglutinin based on species of origin. Virology 127:361–373.Medline</note><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>127</number></detail><extent unit="pages"><start>361</start><end>373</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>127</number></detail><extent unit="pages"><start>361</start><end>373</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit104"><titleInfo><title>Inhibition of influenza virus replication in mice by GG167 (4‐guanidino‐2,4‐dideoxy‐2,3‐dehydro‐N‐acetylneuraminic acid) is consistent with extracellular activity of viral neuraminidase</title></titleInfo><name type="personal"><namePart type="given">DM</namePart><namePart type="family">Ryan</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Ryan DM, Ticehurst J, Dempsey MH, Penn CR. 1994. Inhibition of influenza virus replication in mice by GG167 (4‐guanidino‐2,4‐dideoxy‐2,3‐dehydro‐N‐acetylneuraminic acid) is consistent with extracellular activity of viral neuraminidase. Antimicrob Chem Chemother 38(10):2270–2275.</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>38(10)</number></detail><extent unit="pages"><start>2270</start><end>2275</end></extent></part><relatedItem type="host"><titleInfo><title>Antimicrob Chem Chemother</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>38(10)</number></detail><extent unit="pages"><start>2270</start><end>2275</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit105"><titleInfo><title>Substrate, inhibitor, or antibody stabilises the Glu 119 Gly mutant influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">A</namePart><namePart type="family">Sahasrabudhe</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Sahasrabudhe A, Lawrence L, Epa VC, Varghese JN, Colman PM, McKimm‐Breschkin JL. 1998. Substrate, inhibitor, or antibody stabilises the Glu 119 Gly mutant influenza virus neuraminidase. Virology 247:14–21.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>247</number></detail><extent unit="pages"><start>14</start><end>21</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>247</number></detail><extent unit="pages"><start>14</start><end>21</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit106"><titleInfo><title>The origin of pandemic influenza virus</title></titleInfo><name type="personal"><namePart type="given">JJ</namePart><namePart type="family">Skehel</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Skehel JJ. 1974. The origin of pandemic influenza virus. Symp Soc Gen Microbiol 24:321–342.</note><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>24</number></detail><extent unit="pages"><start>321</start><end>342</end></extent></part><relatedItem type="host"><titleInfo><title>Symp Soc Gen Microbiol</title></titleInfo><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>24</number></detail><extent unit="pages"><start>321</start><end>342</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit107"><titleInfo><title>Type A influenza viruses iosloated from wild free‐flying ducks in California</title></titleInfo><name type="personal"><namePart type="given">RD</namePart><namePart type="family">Slemons</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Slemons RD, Johnson DC, Osborn JS, Hayes F. 1974. Type A influenza viruses iosloated from wild free‐flying ducks in California. Avian Dis 18:119–125.Medline</note><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>18</number></detail><extent unit="pages"><start>119</start><end>125</end></extent></part><relatedItem type="host"><titleInfo><title>Avian Dis</title></titleInfo><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>18</number></detail><extent unit="pages"><start>119</start><end>125</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit108"><titleInfo><title>Variation in influenza virus genes. Epidemiological, pathogenic, and evolutionary consequences</title></titleInfo><name type="personal"><namePart type="given">FI</namePart><namePart type="family">Smith</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>The influenza viruses</title></titleInfo><originInfo><publisher>Plenum Press</publisher><place><placeTerm type="text">New York</placeTerm></place></originInfo><part><date>1989</date><extent unit="pages"><start>319</start><end>359</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit109"><titleInfo><title>A virus obtained from influenza patients</title></titleInfo><name type="personal"><namePart type="given">W</namePart><namePart type="family">Smith</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Smith W, Andrewes CH, Laidlaw PP. 1933. A virus obtained from influenza patients. Lancet 2:66–68.</note><part><date>1933</date><detail type="volume"><caption>vol.</caption><number>2</number></detail><extent unit="pages"><start>66</start><end>68</end></extent></part><relatedItem type="host"><titleInfo><title>Lancet</title></titleInfo><part><date>1933</date><detail type="volume"><caption>vol.</caption><number>2</number></detail><extent unit="pages"><start>66</start><end>68</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit110"><titleInfo><title>Novel inhibitors of influenza sialidases related to GG167. Structure‐activity, crystallographic and molecular dynamics studies with 4H‐pyran‐2‐carboxylic acid 6‐carboxamides</title></titleInfo><name type="personal"><namePart type="given">PW</namePart><namePart type="family">Smith</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Smith PW, Sollis SL, Howes PD, Cherry PC, Cobley KN, Taylor H, Whittington AR, Scicinski J, Bethell RC, Taylor N, Skarzynski T, Cleasby A, Singh O, Wonacott A, Varghese J, Colman P. 1996. Novel inhibitors of influenza sialidases related to GG167. Structure‐activity, crystallographic and molecular dynamics studies with 4H‐pyran‐2‐carboxylic acid 6‐carboxamides. Bioorg Med Chem Lett 6(24):2931–2936.</note><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>6(24)</number></detail><extent unit="pages"><start>2931</start><end>2936</end></extent></part><relatedItem type="host"><titleInfo><title>Bioorg Med Chem Lett</title></titleInfo><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>6(24)</number></detail><extent unit="pages"><start>2931</start><end>2936</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit111"><titleInfo><title>Novel inhibitors of influenza sialidase related to GG167. Synthesis of 4‐amino and 4‐guanidino‐4H‐pyran‐2‐carboxylic acid‐6‐propylamides; selective inhibitors of influenza A virus sialidase</title></titleInfo><name type="personal"><namePart type="given">SL</namePart><namePart type="family">Sollis</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Sollis SL, Smith PW, Howes PD, Cherry PC, Bethell RC. 1996. Novel inhibitors of influenza sialidase related to GG167. Synthesis of 4‐amino and 4‐guanidino‐4H‐pyran‐2‐carboxylic acid‐6‐propylamides; selective inhibitors of influenza A virus sialidase. Bioorg Med Chem Lett 6(15):1805–1808.</note><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>6(15)</number></detail><extent unit="pages"><start>1805</start><end>1808</end></extent></part><relatedItem type="host"><titleInfo><title>Bioorg Med Chem Lett</title></titleInfo><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>6(15)</number></detail><extent unit="pages"><start>1805</start><end>1808</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit112"><titleInfo><title>Risk factors for influenza mortality</title></titleInfo><name type="personal"><namePart type="given">MJW</namePart><namePart type="family">Sprenger</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Options for the control of influenza virus II</title></titleInfo><originInfo><publisher>Excerpta Medica</publisher><place><placeTerm type="text">Amsterdam</placeTerm></place></originInfo><part><date>1993</date><extent unit="pages"><start>15</start><end>23</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit113"><titleInfo><title>Adverse reactions to amantadine prophylaxis of influenza in a retirement home</title></titleInfo><name type="personal"><namePart type="given">KC</namePart><namePart type="family">Srange</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Srange KC, Little DW, Blarnik B. 1991. Adverse reactions to amantadine prophylaxis of influenza in a retirement home. J Am Geriatr Soc 33:700–705.</note><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>33</number></detail><extent unit="pages"><start>700</start><end>705</end></extent></part><relatedItem type="host"><titleInfo><title>J Am Geriatr Soc</title></titleInfo><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>33</number></detail><extent unit="pages"><start>700</start><end>705</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit114"><titleInfo><title>Characterisation of an avian influenza A (H5N1) virus isolated from a child with fatal respiratory illness</title></titleInfo><name type="personal"><namePart type="given">K</namePart><namePart type="family">Subbarao</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Subbarao K, Klimov A, Katz J, Regnery H, Lim W, Hall H, Perdue M, Swayne D, Bender C, Huang J, Hemphill M, Rowe T, Shaw M, Xu X, Fukuda K, Cox N. 1998. Characterisation of an avian influenza A (H5N1) virus isolated from a child with fatal respiratory illness. Science 279:393–396.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>279</number></detail><extent unit="pages"><start>393</start><end>396</end></extent></part><relatedItem type="host"><titleInfo><title>Science</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>279</number></detail><extent unit="pages"><start>393</start><end>396</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit115"><titleInfo><title>New ganglioside analogs that inhibit influenza virus sialidase</title></titleInfo><name type="personal"><namePart type="given">Y</namePart><namePart type="family">Suzuki</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Suzuki Y, Sato K, Kiso M, Hasegawa A. 1990. New ganglioside analogs that inhibit influenza virus sialidase. Glycoconjugate J 7:349–356.Medline</note><part><date>1990</date><detail type="volume"><caption>vol.</caption><number>7</number></detail><extent unit="pages"><start>349</start><end>356</end></extent></part><relatedItem type="host"><titleInfo><title>Glycoconjugate J</title></titleInfo><part><date>1990</date><detail type="volume"><caption>vol.</caption><number>7</number></detail><extent unit="pages"><start>349</start><end>356</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit116"><titleInfo><title>Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis</title></titleInfo><name type="personal"><namePart type="given">NR</namePart><namePart type="family">Taylor</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Taylor NR, von Itzstein M. 1994. Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis. J Med Chem 37:616–624.Medline</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>37</number></detail><extent unit="pages"><start>616</start><end>624</end></extent></part><relatedItem type="host"><titleInfo><title>J Med Chem</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>37</number></detail><extent unit="pages"><start>616</start><end>624</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit117"><titleInfo><title>Dihydropyran carboxamides related to Zanamivir. A new series of inhibitors of influenza virus sialidases. Part 2: A crystallographic and molecular modeling study of complexes of 4‐amino‐4H‐pyran‐6‐carboxamides and sialidase from influenza types A and B</title></titleInfo><name type="personal"><namePart type="given">NR</namePart><namePart type="family">Taylor</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Taylor NR, Cleasby A, Singh O, Skarzynski T, Wanacott A, Smith PW, Sollis SL, Howes PD, Cherry PC, Bethell R, Colman P, Varghese J. 1998. Dihydropyran carboxamides related to Zanamivir. A new series of inhibitors of influenza virus sialidases. Part 2: A crystallographic and molecular modeling study of complexes of 4‐amino‐4H‐pyran‐6‐carboxamides and sialidase from influenza types A and B. J Med Chem 41:798–807.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>41</number></detail><extent unit="pages"><start>798</start><end>807</end></extent></part><relatedItem type="host"><titleInfo><title>J Med Chem</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>41</number></detail><extent unit="pages"><start>798</start><end>807</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit118"><titleInfo><title>Inhibition of growth of influenza virus in vitro by 4‐guanidino‐2,4‐dideoxy‐2,3‐dehydro‐N‐acetylneuraminic acid</title></titleInfo><name type="personal"><namePart type="given">GP</namePart><namePart type="family">Thomas</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Thomas GP, Forsyth M, Penn CR, McCauley JW. 1994. Inhibition of growth of influenza virus in vitro by 4‐guanidino‐2,4‐dideoxy‐2,3‐dehydro‐N‐acetylneuraminic acid. Antiviral Res 24:351–356.Medline</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>24</number></detail><extent unit="pages"><start>351</start><end>356</end></extent></part><relatedItem type="host"><titleInfo><title>Antiviral Res</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>24</number></detail><extent unit="pages"><start>351</start><end>356</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit119"><titleInfo><title>Efficacy of oral GS4104 in treating acute influenza.</title></titleInfo><name type="personal"><namePart type="given">JJ</namePart><namePart type="family">Treanor</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>other</genre><part><date>1998</date></part></relatedItem><relatedItem type="references" displayLabel="cit120"><titleInfo><title>Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants</title></titleInfo><name type="personal"><namePart type="given">WG</namePart><namePart type="family">Tulip</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Tulip WG, Varghese JN, Baker AT, van Donkelaar A, Laver WG, Webster RG, Colman PM. 1992a. Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants. J Mol Biol 221:487–497.</note><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>221</number></detail><extent unit="pages"><start>487</start><end>497</end></extent></part><relatedItem type="host"><titleInfo><title>J Mol Biol</title></titleInfo><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>221</number></detail><extent unit="pages"><start>487</start><end>497</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit121"><titleInfo><title>Refined crystal structure of the influenza virus N9 neuraminidase‐NC41 Fab complex</title></titleInfo><name type="personal"><namePart type="given">WG</namePart><namePart type="family">Tulip</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Tulip WG, Varghese JN, Laver WG, Webster RG, Colman PM. 1992b. Refined crystal structure of the influenza virus N9 neuraminidase‐NC41 Fab complex. J Mol Biol 227:122–148.Medline</note><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>227</number></detail><extent unit="pages"><start>122</start><end>148</end></extent></part><relatedItem type="host"><titleInfo><title>J Mol Biol</title></titleInfo><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>227</number></detail><extent unit="pages"><start>122</start><end>148</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit122"><titleInfo><title>Influenza vaccines</title></titleInfo><name type="personal"><namePart type="given">DAJ</namePart><namePart type="family">Tyrrell</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Tyrrell DAJ. 1980. Influenza vaccines. Phil Trans R Soc Lond B 288:449–460.Medline</note><part><date>1980</date><detail type="volume"><caption>vol.</caption><number>288</number></detail><extent unit="pages"><start>449</start><end>460</end></extent></part><relatedItem type="host"><titleInfo><title>Phil Trans R Soc Lond B</title></titleInfo><part><date>1980</date><detail type="volume"><caption>vol.</caption><number>288</number></detail><extent unit="pages"><start>449</start><end>460</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit123"><titleInfo><title>The design of anti‐influenza virus drugs from the X‐ray molecular structure of influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">JN</namePart><namePart type="family">Varghese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Structure based drug design: diseases, targets, techniques and developments, vol 1</title></titleInfo><originInfo><publisher>Marcel Dekker</publisher><place><placeTerm type="text">New York</placeTerm></place></originInfo><part><date>1997</date><extent unit="pages"><start>459</start><end>486</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit124"><titleInfo><title>Three‐dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2Å resolution</title></titleInfo><name type="personal"><namePart type="given">JN</namePart><namePart type="family">Varghese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Varghese JN, Colman PM. 1991. Three‐dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2Å resolution. J Mol Biol 221:473–486.Medline</note><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>221</number></detail><extent unit="pages"><start>473</start><end>486</end></extent></part><relatedItem type="host"><titleInfo><title>J Mol Biol</title></titleInfo><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>221</number></detail><extent unit="pages"><start>473</start><end>486</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit125"><titleInfo><title>Structure of the influenza virus glycoprotein antigen neuraminidase at 2. 9Å resolution</title></titleInfo><name type="personal"><namePart type="given">JN</namePart><namePart type="family">Varghese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Varghese JN, Laver WG, Colman PM. 1983. Structure of the influenza virus glycoprotein antigen neuraminidase at 2. 9Å resolution. Nature 303:35–40.Medline</note><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>303</number></detail><extent unit="pages"><start>35</start><end>40</end></extent></part><relatedItem type="host"><titleInfo><title>Nature</title></titleInfo><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>303</number></detail><extent unit="pages"><start>35</start><end>40</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit126"><titleInfo><title>The three‐dimensional structure of an escape mutant of the neuraminidase of influenza virus A/Tokyo/3/67</title></titleInfo><name type="personal"><namePart type="given">JN</namePart><namePart type="family">Varghese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Varghese JN, Webster RG, Laver WG, Colman PM. 1988. The three‐dimensional structure of an escape mutant of the neuraminidase of influenza virus A/Tokyo/3/67. J Mol Biol 200:201–203.Medline</note><part><date>1988</date><detail type="volume"><caption>vol.</caption><number>200</number></detail><extent unit="pages"><start>201</start><end>203</end></extent></part><relatedItem type="host"><titleInfo><title>J Mol Biol</title></titleInfo><part><date>1988</date><detail type="volume"><caption>vol.</caption><number>200</number></detail><extent unit="pages"><start>201</start><end>203</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit127"><titleInfo><title>The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor</title></titleInfo><name type="personal"><namePart type="given">JN</namePart><namePart type="family">Varghese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Varghese JN, McKimm‐Breschkin JL, Caldwell JB, Kortt AA, Colman PM. 1992. The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 14:327–332.Medline</note><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>14</number></detail><extent unit="pages"><start>327</start><end>332</end></extent></part><relatedItem type="host"><titleInfo><title>Proteins</title></titleInfo><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>14</number></detail><extent unit="pages"><start>327</start><end>332</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit128"><titleInfo><title>Three‐dimensional structure of 4‐guanidino‐Neu5Ac2en and influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">JN</namePart><namePart type="family">Varghese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Varghese JN, Epa VC, Colman PM. 1995. Three‐dimensional structure of 4‐guanidino‐Neu5Ac2en and influenza virus neuraminidase. Protein Sci 4:1081–1087.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>4</number></detail><extent unit="pages"><start>1081</start><end>1087</end></extent></part><relatedItem type="host"><titleInfo><title>Protein Sci</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>4</number></detail><extent unit="pages"><start>1081</start><end>1087</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit129"><titleInfo><title>Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">JN</namePart><namePart type="family">Varghese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Varghese JN, Colman PM, van Donkelaar A, Blick TJ, Sahasrabudhe A, McKimm‐Breschkin JL. 1997. Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidase. Proc Natl Acad Sci USA 94:11808–11812.</note><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>94</number></detail><extent unit="pages"><start>11808</start><end>11812</end></extent></part><relatedItem type="host"><titleInfo><title>Proc Natl Acad Sci USA</title></titleInfo><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>94</number></detail><extent unit="pages"><start>11808</start><end>11812</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit130"><titleInfo><title>Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">JN</namePart><namePart type="family">Varghese</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Varghese JN, Smith PW, Sollis SL, Blick TJ, Sahasrabudhe A, McKimm‐Breschkin JL, Colman PM. 1998. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 6:735–746.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>6</number></detail><extent unit="pages"><start>735</start><end>746</end></extent></part><relatedItem type="host"><titleInfo><title>Structure</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>6</number></detail><extent unit="pages"><start>735</start><end>746</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit131"><titleInfo><title>Rational design of potent sialidase‐based inhibitors of influenza virus replication</title></titleInfo><name type="personal"><namePart type="given">M</namePart><namePart type="family">von Itzstein</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">von Itzstein M, Wu W‐Y, Kok GB, Pegg MS, Dyson JC, Jin B, VanPhan T, Symthe ML, White HF, Oliver SW, Colman PM, Varghese JN, Ryan DM, Woods JM, Bethell RC, Hotham VJ, Cameron JM, Penn CR. 1993. Rational design of potent sialidase‐based inhibitors of influenza virus replication. Nature 363:418–423.Medline</note><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>363</number></detail><extent unit="pages"><start>418</start><end>423</end></extent></part><relatedItem type="host"><titleInfo><title>Nature</title></titleInfo><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>363</number></detail><extent unit="pages"><start>418</start><end>423</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit132"><titleInfo><title>The synthesis 2,3‐didehydro‐2,4‐dideoxy‐4‐guanidinyl‐N‐acetylneuraminic acid: a potent influenza virus inhibitor</title></titleInfo><name type="personal"><namePart type="given">M</namePart><namePart type="family">von Itzstein</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">von Itzstein M, Wu W‐Y, Jin B. 1994. The synthesis 2,3‐didehydro‐2,4‐dideoxy‐4‐guanidinyl‐N‐acetylneuraminic acid: a potent influenza virus inhibitor. Carbohydr Res 259:301–305.Medline</note><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>259</number></detail><extent unit="pages"><start>301</start><end>305</end></extent></part><relatedItem type="host"><titleInfo><title>Carbohydr Res</title></titleInfo><part><date>1994</date><detail type="volume"><caption>vol.</caption><number>259</number></detail><extent unit="pages"><start>301</start><end>305</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit133"><titleInfo><title>Sugar residues on proteins</title></titleInfo><name type="personal"><namePart type="given">PV</namePart><namePart type="family">Wagh</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Wagh PV, Bahl OP. 1981. Sugar residues on proteins. Crit Rev Biochem 307–377.</note><part><date>1981</date><extent unit="pages"><start>307</start><end>377</end></extent></part><relatedItem type="host"><titleInfo><title>Crit Rev Biochem</title></titleInfo><part><date>1981</date><extent unit="pages"><start>307</start><end>377</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit134"><titleInfo><title>Structure of influenza virus hemagglutinin</title></titleInfo><name type="personal"><namePart type="given">CW</namePart><namePart type="family">Ward</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Ward CW. 1981. Structure of influenza virus hemagglutinin. Curr Top Microbiol Immunol 94/95:1–74.Medline</note><part><date>1981</date><detail type="volume"><caption>vol.</caption><number>94/95</number></detail><extent unit="pages"><start>1</start><end>74</end></extent></part><relatedItem type="host"><titleInfo><title>Curr Top Microbiol Immunol</title></titleInfo><part><date>1981</date><detail type="volume"><caption>vol.</caption><number>94/95</number></detail><extent unit="pages"><start>1</start><end>74</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit135"><titleInfo><title>Amino acid sequence of the pronase‐released heads of neuraminidase subtype N2 from the Asian strain A/Tokyo/3/67 of influenza virus</title></titleInfo><name type="personal"><namePart type="given">CW</namePart><namePart type="family">Ward</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Ward CW, Elleman TC, Azad AA. 1982. Amino acid sequence of the pronase‐released heads of neuraminidase subtype N2 from the Asian strain A/Tokyo/3/67 of influenza virus. Biochem J 207:91–95.Medline</note><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>207</number></detail><extent unit="pages"><start>91</start><end>95</end></extent></part><relatedItem type="host"><titleInfo><title>Biochem J</title></titleInfo><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>207</number></detail><extent unit="pages"><start>91</start><end>95</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit136"><titleInfo><title>Chemical and antigenic characterisation of the carbohydrate side chains of an Asian (N2) influenza virus neuraminidase</title></titleInfo><name type="personal"><namePart type="given">CW</namePart><namePart type="family">Ward</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Ward CW, Murry JM, Roxburgh CM, Jackson DC. 1983. Chemical and antigenic characterisation of the carbohydrate side chains of an Asian (N2) influenza virus neuraminidase. Virology 126:370–375.Medline</note><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>126</number></detail><extent unit="pages"><start>370</start><end>375</end></extent></part><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><part><date>1983</date><detail type="volume"><caption>vol.</caption><number>126</number></detail><extent unit="pages"><start>370</start><end>375</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit137"><titleInfo><title>Antigenic variation in influenza viruses</title></titleInfo><name type="personal"><namePart type="given">RG</namePart><namePart type="family">Webster</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Influenza virus and influenza</title></titleInfo><originInfo><publisher>Academic Press</publisher><place><placeTerm type="text">New York</placeTerm></place></originInfo><part><date>1975</date><extent unit="pages"><start>269</start><end>314</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit138"><titleInfo><title>Antigenic structure and variation in an influenza N9 neuraminidase</title></titleInfo><name type="personal"><namePart type="given">RG</namePart><namePart type="family">Webster</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Webster RG, Air GM, Metzger DW, Colman PM, Varghese JN, Baker AT, Laver WG. 1987. Antigenic structure and variation in an influenza N9 neuraminidase. J Virol 61:2910–2916.Medline</note><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>61</number></detail><extent unit="pages"><start>2910</start><end>2916</end></extent></part><relatedItem type="host"><titleInfo><title>J Virol</title></titleInfo><part><date>1987</date><detail type="volume"><caption>vol.</caption><number>61</number></detail><extent unit="pages"><start>2910</start><end>2916</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit139"><titleInfo><title>Evolution and ecology of influenza A viruses</title></titleInfo><name type="personal"><namePart type="given">RG</namePart><namePart type="family">Webster</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Webster RG, Bean WJ, Gorman OT, Chambers TM, Kawaoka Y. 1992. Evolution and ecology of influenza A viruses. Microbiol Rev 56:152–179.Medline</note><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>56</number></detail><extent unit="pages"><start>152</start><end>179</end></extent></part><relatedItem type="host"><titleInfo><title>Microbiol Rev</title></titleInfo><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>56</number></detail><extent unit="pages"><start>152</start><end>179</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit140"><titleInfo><title>Evolution and ecology of influenza viruses</title></titleInfo><name type="personal"><namePart type="given">RG</namePart><namePart type="family">Webster</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>book-chapter</genre><relatedItem type="host"><titleInfo><title>Options for the control of influenza virus II</title></titleInfo><originInfo><publisher>Excerpta Medica</publisher><place><placeTerm type="text">Amsterdam</placeTerm></place></originInfo><part><date>1993</date><extent unit="pages"><start>177</start><end>185</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit141"><titleInfo><title>Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid</title></titleInfo><name type="personal"><namePart type="given">W</namePart><namePart type="family">Weis</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Weis W, Brown JH, Cusack S, Paulson JC, Skehel JJ, Wiley DC. 1988. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333:426–431.Medline</note><part><date>1988</date><detail type="volume"><caption>vol.</caption><number>333</number></detail><extent unit="pages"><start>426</start><end>431</end></extent></part><relatedItem type="host"><titleInfo><title>Nature</title></titleInfo><part><date>1988</date><detail type="volume"><caption>vol.</caption><number>333</number></detail><extent unit="pages"><start>426</start><end>431</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit142"><titleInfo><title>Influenza viral proteins: identification and synthesis</title></titleInfo><name type="personal"><namePart type="given">DO</namePart><namePart type="family">White</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">White DO. 1974. Influenza viral proteins: identification and synthesis. Curr Top Microbiol Immunol 63:1–48.</note><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>63</number></detail><extent unit="pages"><start>1</start><end>48</end></extent></part><relatedItem type="host"><titleInfo><title>Curr Top Microbiol Immunol</title></titleInfo><part><date>1974</date><detail type="volume"><caption>vol.</caption><number>63</number></detail><extent unit="pages"><start>1</start><end>48</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit143"><titleInfo><title>Rimantadine: a clinical perspective</title></titleInfo><name type="personal"><namePart type="given">SM</namePart><namePart type="family">Wintermeyer</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Wintermeyer SM, Nahata MC. 1995. Rimantadine: a clinical perspective. Ann Pharmacother 29:299–310.Medline</note><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>29</number></detail><extent unit="pages"><start>299</start><end>310</end></extent></part><relatedItem type="host"><titleInfo><title>Ann Pharmacother</title></titleInfo><part><date>1995</date><detail type="volume"><caption>vol.</caption><number>29</number></detail><extent unit="pages"><start>299</start><end>310</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit144"><titleInfo><title>4‐Guanidino‐2‐4‐dideoxy‐2,3‐dehydro‐n‐acetylneuraminic acid is a highly effective inhibitor both of the Sialidase (Neuraminidase) and growth of a wide range of influenza A and B viruses in vitro</title></titleInfo><name type="personal"><namePart type="given">JM</namePart><namePart type="family">Woods</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Woods JM, Bethell RC, Coates JAV, Healy N, Hiscox SA, Pearson BA, Ryan DM, Ticehurst J, Tilling J, Walcott SM, Penn CR. 1993. 4‐Guanidino‐2‐4‐dideoxy‐2,3‐dehydro‐n‐acetylneuraminic acid is a highly effective inhibitor both of the Sialidase (Neuraminidase) and growth of a wide range of influenza A and B viruses in vitro. Antimicrob Agents Chemother 37:1473–1479.Medline</note><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>37</number></detail><extent unit="pages"><start>1473</start><end>1479</end></extent></part><relatedItem type="host"><titleInfo><title>Antimicrob Agents Chemother</title></titleInfo><part><date>1993</date><detail type="volume"><caption>vol.</caption><number>37</number></detail><extent unit="pages"><start>1473</start><end>1479</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit145"><titleInfo><title>Preliminary crystallographic data for influenza virus neuraminidase ‘heads’</title></titleInfo><name type="personal"><namePart type="given">CE</namePart><namePart type="family">Wright</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Wright CE, Laver WG. 1978. Preliminary crystallographic data for influenza virus neuraminidase ‘heads’. J Mol Biol 120:133–136.Medline</note><part><date>1978</date><detail type="volume"><caption>vol.</caption><number>120</number></detail><extent unit="pages"><start>133</start><end>136</end></extent></part><relatedItem type="host"><titleInfo><title>J Mol Biol</title></titleInfo><part><date>1978</date><detail type="volume"><caption>vol.</caption><number>120</number></detail><extent unit="pages"><start>133</start><end>136</end></extent></part></relatedItem></relatedItem><relatedItem type="references" displayLabel="cit146"><titleInfo><title>Clinical features and rapid viral diagnosis of human disease associated with avian influenza A H5N1 virus</title></titleInfo><name type="personal"><namePart type="given">KY</namePart><namePart type="family">Yeun</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Yeun KY, Chan PK, Peiris M, Tsang DN, Que TL, Shortridge KF, Cheung PT, To WK, Ho ET, Sung R, Cheng AF. 1998. Clinical features and rapid viral diagnosis of human disease associated with avian influenza A H5N1 virus. Lancet 351:467–471.Medline</note><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>351</number></detail><extent unit="pages"><start>467</start><end>471</end></extent></part><relatedItem type="host"><titleInfo><title>Lancet</title></titleInfo><part><date>1998</date><detail type="volume"><caption>vol.</caption><number>351</number></detail><extent unit="pages"><start>467</start><end>471</end></extent></part></relatedItem></relatedItem><identifier type="istex">D278CB41B6488D1E899E112332E3EB59889CA5FF</identifier><identifier type="ark">ark:/67375/WNG-VV4CKQ2F-F</identifier><identifier type="DOI">10.1002/(SICI)1098-2299(199903/04)46:3/4<176::AID-DDR4>3.0.CO;2-6</identifier><identifier type="ArticleID">DDR4</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 1999 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-L0C46X92-X">wiley</recordContentSource><recordOrigin>Converted from (version ) to MODS version 3.6.</recordOrigin><recordCreationDate encoding="w3cdtf">2019-11-14</recordCreationDate></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-VV4CKQ2F-F/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001674 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 001674 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:D278CB41B6488D1E899E112332E3EB59889CA5FF
|texte= Development of neuraminidase inhibitors as anti‐influenza virus drugs
}}
| This area was generated with Dilib version V0.6.33. |  |