6SLN-lipo PGA specifically catches (coats) human influenza virus and synergizes neuraminidase-targeting drugs for human influenza therapeutic potential.
Identifieur interne : 000635 ( PubMed/Curation ); précédent : 000634; suivant : 0006366SLN-lipo PGA specifically catches (coats) human influenza virus and synergizes neuraminidase-targeting drugs for human influenza therapeutic potential.
Auteurs : Nongluk Sriwilaijaroen [Oman] ; Katsuhiko Suzuki [Japon] ; Emi Takashita [Japon] ; Hiroaki Hiramatsu [Japon] ; Osamu Kanie [Japon] ; Yasuo Suzuki [Japon]Source :
- The Journal of antimicrobial chemotherapy [ 1460-2091 ] ; 2015.
Descripteurs français
- KwdFr :
- Acide polyglutamique (), Acide polyglutamique (analogues et dérivés), Acide polyglutamique (pharmacologie), Acide polyglutamique (synthèse chimique), Animaux, Antienzymes (pharmacologie), Antiviraux (), Antiviraux (pharmacologie), Antiviraux (synthèse chimique), Attachement viral (), Concentration inhibitrice 50, Glycolipides (), Glycolipides (pharmacologie), Glycolipides (synthèse chimique), Humains, Liaison aux protéines, Lignée cellulaire, Protéines virales (antagonistes et inhibiteurs), Relation dose-effet des médicaments, Récepteurs viraux (métabolisme), Sialidase (antagonistes et inhibiteurs), Synergie des médicaments, Virus de la grippe A (), Virus de la grippe A (physiologie), Érythrocytes (), Érythrocytes (virologie).
- MESH :
- analogues et dérivés : Acide polyglutamique.
- antagonistes et inhibiteurs : Protéines virales, Sialidase.
- métabolisme : Récepteurs viraux.
- pharmacologie : Acide polyglutamique, Antienzymes, Antiviraux, Glycolipides.
- physiologie : Virus de la grippe A.
- synthèse chimique : Acide polyglutamique, Antiviraux, Glycolipides.
- virologie : Érythrocytes.
- Acide polyglutamique, Animaux, Antiviraux, Attachement viral, Concentration inhibitrice 50, Glycolipides, Humains, Liaison aux protéines, Lignée cellulaire, Relation dose-effet des médicaments, Synergie des médicaments, Virus de la grippe A, Érythrocytes.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (chemical synthesis), Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Cell Line, Dose-Response Relationship, Drug, Drug Synergism, Enzyme Inhibitors (pharmacology), Erythrocytes (drug effects), Erythrocytes (virology), Glycolipids (chemical synthesis), Glycolipids (chemistry), Glycolipids (pharmacology), Humans, Influenza A virus (drug effects), Influenza A virus (physiology), Inhibitory Concentration 50, Neuraminidase (antagonists & inhibitors), Polyglutamic Acid (analogs & derivatives), Polyglutamic Acid (chemical synthesis), Polyglutamic Acid (chemistry), Polyglutamic Acid (pharmacology), Protein Binding, Receptors, Virus (metabolism), Viral Proteins (antagonists & inhibitors), Virus Attachment (drug effects).
- MESH :
- chemical , analogs & derivatives : Polyglutamic Acid.
- chemical , antagonists & inhibitors : Neuraminidase, Viral Proteins.
- chemical , chemical synthesis : Antiviral Agents, Glycolipids, Polyglutamic Acid.
- chemical , chemistry : Antiviral Agents, Glycolipids, Polyglutamic Acid.
- chemical , metabolism : Receptors, Virus.
- chemical , pharmacology : Antiviral Agents, Enzyme Inhibitors, Glycolipids, Polyglutamic Acid.
- drug effects : Erythrocytes, Influenza A virus, Virus Attachment.
- physiology : Influenza A virus.
- virology : Erythrocytes.
- Animals, Cell Line, Dose-Response Relationship, Drug, Drug Synergism, Humans, Inhibitory Concentration 50, Protein Binding.
Abstract
The purpose of this study was to develop a new compound to overcome influenza epidemics and pandemics as well as drug resistance.
DOI: 10.1093/jac/dkv193
PubMed: 26169554
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000635
Links to Exploration step
pubmed:26169554Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">6SLN-lipo PGA specifically catches (coats) human influenza virus and synergizes neuraminidase-targeting drugs for human influenza therapeutic potential.</title><author><name sortKey="Sriwilaijaroen, Nongluk" sort="Sriwilaijaroen, Nongluk" uniqKey="Sriwilaijaroen N" first="Nongluk" last="Sriwilaijaroen">Nongluk Sriwilaijaroen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Preclinical Sciences, Faculty of Medicine, Thammasat University (Rangsit Campus), Pathumthani 12120, Thailand College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan snongluk@hotmail.com.</nlm:affiliation><country wicri:rule="url">Oman</country><wicri:regionArea>Department of Preclinical Sciences, Faculty of Medicine, Thammasat University (Rangsit Campus), Pathumthani 12120, Thailand College of Life and Health Sciences, Chubu University, Aichi 487-8501</wicri:regionArea></affiliation></author><author><name sortKey="Suzuki, Katsuhiko" sort="Suzuki, Katsuhiko" uniqKey="Suzuki K" first="Katsuhiko" last="Suzuki">Katsuhiko Suzuki</name><affiliation wicri:level="1"><nlm:affiliation>Synthetic Cellular Chemistry Laboratory, RIKEN, Saitama 351-0198, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Synthetic Cellular Chemistry Laboratory, RIKEN, Saitama 351-0198</wicri:regionArea></affiliation></author><author><name sortKey="Takashita, Emi" sort="Takashita, Emi" uniqKey="Takashita E" first="Emi" last="Takashita">Emi Takashita</name><affiliation wicri:level="1"><nlm:affiliation>Influenza Virus Research Center, National Institute of Infectious Diseases, Tokyo 208-0011, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Influenza Virus Research Center, National Institute of Infectious Diseases, Tokyo 208-0011</wicri:regionArea></affiliation></author><author><name sortKey="Hiramatsu, Hiroaki" sort="Hiramatsu, Hiroaki" uniqKey="Hiramatsu H" first="Hiroaki" last="Hiramatsu">Hiroaki Hiramatsu</name><affiliation wicri:level="1"><nlm:affiliation>College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>College of Life and Health Sciences, Chubu University, Aichi 487-8501</wicri:regionArea></affiliation></author><author><name sortKey="Kanie, Osamu" sort="Kanie, Osamu" uniqKey="Kanie O" first="Osamu" last="Kanie">Osamu Kanie</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Glycoscience, Tokai University, Kanagawa 259-1292, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Institute of Glycoscience, Tokai University, Kanagawa 259-1292</wicri:regionArea></affiliation></author><author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name><affiliation wicri:level="1"><nlm:affiliation>College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>College of Life and Health Sciences, Chubu University, Aichi 487-8501</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:26169554</idno><idno type="pmid">26169554</idno><idno type="doi">10.1093/jac/dkv193</idno><idno type="wicri:Area/PubMed/Corpus">000635</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000635</idno><idno type="wicri:Area/PubMed/Curation">000635</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000635</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">6SLN-lipo PGA specifically catches (coats) human influenza virus and synergizes neuraminidase-targeting drugs for human influenza therapeutic potential.</title><author><name sortKey="Sriwilaijaroen, Nongluk" sort="Sriwilaijaroen, Nongluk" uniqKey="Sriwilaijaroen N" first="Nongluk" last="Sriwilaijaroen">Nongluk Sriwilaijaroen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Preclinical Sciences, Faculty of Medicine, Thammasat University (Rangsit Campus), Pathumthani 12120, Thailand College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan snongluk@hotmail.com.</nlm:affiliation><country wicri:rule="url">Oman</country><wicri:regionArea>Department of Preclinical Sciences, Faculty of Medicine, Thammasat University (Rangsit Campus), Pathumthani 12120, Thailand College of Life and Health Sciences, Chubu University, Aichi 487-8501</wicri:regionArea></affiliation></author><author><name sortKey="Suzuki, Katsuhiko" sort="Suzuki, Katsuhiko" uniqKey="Suzuki K" first="Katsuhiko" last="Suzuki">Katsuhiko Suzuki</name><affiliation wicri:level="1"><nlm:affiliation>Synthetic Cellular Chemistry Laboratory, RIKEN, Saitama 351-0198, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Synthetic Cellular Chemistry Laboratory, RIKEN, Saitama 351-0198</wicri:regionArea></affiliation></author><author><name sortKey="Takashita, Emi" sort="Takashita, Emi" uniqKey="Takashita E" first="Emi" last="Takashita">Emi Takashita</name><affiliation wicri:level="1"><nlm:affiliation>Influenza Virus Research Center, National Institute of Infectious Diseases, Tokyo 208-0011, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Influenza Virus Research Center, National Institute of Infectious Diseases, Tokyo 208-0011</wicri:regionArea></affiliation></author><author><name sortKey="Hiramatsu, Hiroaki" sort="Hiramatsu, Hiroaki" uniqKey="Hiramatsu H" first="Hiroaki" last="Hiramatsu">Hiroaki Hiramatsu</name><affiliation wicri:level="1"><nlm:affiliation>College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>College of Life and Health Sciences, Chubu University, Aichi 487-8501</wicri:regionArea></affiliation></author><author><name sortKey="Kanie, Osamu" sort="Kanie, Osamu" uniqKey="Kanie O" first="Osamu" last="Kanie">Osamu Kanie</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Glycoscience, Tokai University, Kanagawa 259-1292, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Institute of Glycoscience, Tokai University, Kanagawa 259-1292</wicri:regionArea></affiliation></author><author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name><affiliation wicri:level="1"><nlm:affiliation>College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>College of Life and Health Sciences, Chubu University, Aichi 487-8501</wicri:regionArea></affiliation></author></analytic><series><title level="j">The Journal of antimicrobial chemotherapy</title><idno type="eISSN">1460-2091</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antiviral Agents (chemical synthesis)</term><term>Antiviral Agents (chemistry)</term><term>Antiviral Agents (pharmacology)</term><term>Cell Line</term><term>Dose-Response Relationship, Drug</term><term>Drug Synergism</term><term>Enzyme Inhibitors (pharmacology)</term><term>Erythrocytes (drug effects)</term><term>Erythrocytes (virology)</term><term>Glycolipids (chemical synthesis)</term><term>Glycolipids (chemistry)</term><term>Glycolipids (pharmacology)</term><term>Humans</term><term>Influenza A virus (drug effects)</term><term>Influenza A virus (physiology)</term><term>Inhibitory Concentration 50</term><term>Neuraminidase (antagonists & inhibitors)</term><term>Polyglutamic Acid (analogs & derivatives)</term><term>Polyglutamic Acid (chemical synthesis)</term><term>Polyglutamic Acid (chemistry)</term><term>Polyglutamic Acid (pharmacology)</term><term>Protein Binding</term><term>Receptors, Virus (metabolism)</term><term>Viral Proteins (antagonists & inhibitors)</term><term>Virus Attachment (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide polyglutamique ()</term><term>Acide polyglutamique (analogues et dérivés)</term><term>Acide polyglutamique (pharmacologie)</term><term>Acide polyglutamique (synthèse chimique)</term><term>Animaux</term><term>Antienzymes (pharmacologie)</term><term>Antiviraux ()</term><term>Antiviraux (pharmacologie)</term><term>Antiviraux (synthèse chimique)</term><term>Attachement viral ()</term><term>Concentration inhibitrice 50</term><term>Glycolipides ()</term><term>Glycolipides (pharmacologie)</term><term>Glycolipides (synthèse chimique)</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Protéines virales (antagonistes et inhibiteurs)</term><term>Relation dose-effet des médicaments</term><term>Récepteurs viraux (métabolisme)</term><term>Sialidase (antagonistes et inhibiteurs)</term><term>Synergie des médicaments</term><term>Virus de la grippe A ()</term><term>Virus de la grippe A (physiologie)</term><term>Érythrocytes ()</term><term>Érythrocytes (virologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Polyglutamic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Neuraminidase</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Antiviral Agents</term><term>Glycolipids</term><term>Polyglutamic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antiviral Agents</term><term>Glycolipids</term><term>Polyglutamic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Enzyme Inhibitors</term><term>Glycolipids</term><term>Polyglutamic Acid</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acide polyglutamique</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Protéines virales</term><term>Sialidase</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Erythrocytes</term><term>Influenza A virus</term><term>Virus Attachment</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide polyglutamique</term><term>Antienzymes</term><term>Antiviraux</term><term>Glycolipides</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Influenza A virus</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Acide polyglutamique</term><term>Antiviraux</term><term>Glycolipides</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Érythrocytes</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Erythrocytes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Dose-Response Relationship, Drug</term><term>Drug Synergism</term><term>Humans</term><term>Inhibitory Concentration 50</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acide polyglutamique</term><term>Animaux</term><term>Antiviraux</term><term>Attachement viral</term><term>Concentration inhibitrice 50</term><term>Glycolipides</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Relation dose-effet des médicaments</term><term>Synergie des médicaments</term><term>Virus de la grippe A</term><term>Érythrocytes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The purpose of this study was to develop a new compound to overcome influenza epidemics and pandemics as well as drug resistance.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26169554</PMID><DateCompleted><Year>2016</Year><Month>06</Month><Day>27</Day></DateCompleted><DateRevised><Year>2015</Year><Month>09</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2091</ISSN><JournalIssue CitedMedium="Internet"><Volume>70</Volume><Issue>10</Issue><PubDate><Year>2015</Year><Month>Oct</Month></PubDate></JournalIssue><Title>The Journal of antimicrobial chemotherapy</Title><ISOAbbreviation>J. Antimicrob. Chemother.</ISOAbbreviation></Journal><ArticleTitle>6SLN-lipo PGA specifically catches (coats) human influenza virus and synergizes neuraminidase-targeting drugs for human influenza therapeutic potential.</ArticleTitle><Pagination><MedlinePgn>2797-809</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/jac/dkv193</ELocationID><Abstract><AbstractText Label="OBJECTIVES" NlmCategory="OBJECTIVE">The purpose of this study was to develop a new compound to overcome influenza epidemics and pandemics as well as drug resistance.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">We synthesized a new compound carrying: (i) Neu5Acα2-6Galβ1-4GlcNAc (6SLN) for targeting immutable haemagglutinins (HAs) unless switched from human-type receptor preference; (ii) an acyl chain (lipo) for locking the compound with the viral HA via hydrophobic interactions; and (iii) a flexible poly-α-L-glutamic acid (PGA) for enhancing the compound solubility and for coating the viral surface, precluding accessibility of the PGA-coated virus to the negatively charged sialic acid on the host cell surface.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">6SLN-lipo PGA appears to subvert binding of pandemic H1 and seasonal H3 HAs to receptors, as assessed by using guinea pig erythrocytes, which is critical for virus entry into host cells for multiplication. It shows high potency with IC50 values in the range of 300-500 nM against multiplication of both influenza pandemic H1N1/2009 and seasonal H3N2/2004 viruses in cell culture. It acts in synergism with either of the two FDA-approved neuraminidase inhibitor (NAI) clinical drugs, zanamivir (Relenza(®)) and oseltamivir carboxylate (active form of Tamiflu(®)), and it has the potential to aid NAI drugs to achieve complete clearance of the virus from the culture.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">6SLN-lipo PGA is a new potential candidate drug for influenza control and is an attractive candidate for use in combination with an NAI drug for minimized toxicity, delayed development of resistance, prevention and treatment with the potential for eradication of human influenza.</AbstractText><CopyrightInformation>© The Author 2015. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sriwilaijaroen</LastName><ForeName>Nongluk</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Preclinical Sciences, Faculty of Medicine, Thammasat University (Rangsit Campus), Pathumthani 12120, Thailand College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan snongluk@hotmail.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Suzuki</LastName><ForeName>Katsuhiko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Synthetic Cellular Chemistry Laboratory, RIKEN, Saitama 351-0198, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Takashita</LastName><ForeName>Emi</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Influenza Virus Research Center, National Institute of Infectious Diseases, Tokyo 208-0011, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hiramatsu</LastName><ForeName>Hiroaki</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kanie</LastName><ForeName>Osamu</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>Institute of Glycoscience, Tokai University, Kanagawa 259-1292, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Suzuki</LastName><ForeName>Yasuo</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>College of Life and Health Sciences, Chubu University, Aichi 487-8501, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>07</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Antimicrob Chemother</MedlineTA><NlmUniqueID>7513617</NlmUniqueID><ISSNLinking>0305-7453</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000608519">6SLN-lipo PGA</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006017">Glycolipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>25513-46-6</RegistryNumber><NameOfSubstance UI="D011099">Polyglutamic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.18</RegistryNumber><NameOfSubstance UI="C487630">NA protein, influenza A virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.18</RegistryNumber><NameOfSubstance UI="D009439">Neuraminidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004357" MajorTopicYN="N">Drug Synergism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006017" MajorTopicYN="N">Glycolipids</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009980" MajorTopicYN="N">Influenza A virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020128" MajorTopicYN="N">Inhibitory Concentration 50</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011099" MajorTopicYN="N">Polyglutamic Acid</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053585" MajorTopicYN="N">Virus Attachment</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>02</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>06</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>7</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>7</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>6</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26169554</ArticleId><ArticleId IdType="pii">dkv193</ArticleId><ArticleId IdType="doi">10.1093/jac/dkv193</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/PandemieGrippaleV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000635 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 000635 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= PandemieGrippaleV1
|flux= PubMed
|étape= Curation
|type= RBID
|clé= pubmed:26169554
|texte= 6SLN-lipo PGA specifically catches (coats) human influenza virus and synergizes neuraminidase-targeting drugs for human influenza therapeutic potential.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:26169554" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a PandemieGrippaleV1
| This area was generated with Dilib version V0.6.34. |  |