Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme.
Identifieur interne : 001439 ( Ncbi/Merge ); précédent : 001438; suivant : 001440Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme.
Auteurs : Kiira Ratia [États-Unis] ; Kumar Singh Saikatendu ; Bernard D. Santarsiero ; Naina Barretto ; Susan C. Baker ; Raymond C. Stevens ; Andrew D. MesecarSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Virus du SRAS.
- métabolisme : Papaïne, Peptide hydrolases, Ubiquitine.
- Cristallographie aux rayons X, Cysteine endopeptidases, Modèles moléculaires, Protéines virales, Sites de fixation, Structure secondaire des protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Viral Proteins.
- chemical , metabolism : Papain, Peptide Hydrolases, Ubiquitin.
- enzymology : SARS Virus.
- Binding Sites, Crystallography, X-Ray, Models, Molecular, Protein Structure, Secondary.
Abstract
Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. In this work, we describe the 1.85-A crystal structure of the catalytic core of SARS-CoV PLpro and show that the overall architecture adopts a fold closely resembling that of known deubiquitinating enzymes. Key features, however, distinguish PLpro from characterized deubiquitinating enzymes, including an intact zinc-binding motif, an unobstructed catalytically competent active site, and the presence of an intriguing, ubiquitin-like N-terminal domain. To gain insight into the active-site recognition of the C-terminal tail of ubiquitin and the related LXGG motif, we propose a model of PLpro in complex with ubiquitin-aldehyde that reveals well defined sites within the catalytic cleft that help to account for strict substrate-recognition motifs.
DOI: 10.1073/pnas.0510851103
PubMed: 16581910
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002292
- to stream PubMed, to step Curation: 002292
- to stream PubMed, to step Checkpoint: 001F99
Links to Exploration step
pubmed:16581910Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme.</title>
<author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name>
<affiliation wicri:level="2"><nlm:affiliation>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois, Chicago, IL 60607, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois, Chicago, IL 60607</wicri:regionArea>
<placeName><region type="state">Illinois</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Saikatendu, Kumar Singh" sort="Saikatendu, Kumar Singh" uniqKey="Saikatendu K" first="Kumar Singh" last="Saikatendu">Kumar Singh Saikatendu</name>
</author>
<author><name sortKey="Santarsiero, Bernard D" sort="Santarsiero, Bernard D" uniqKey="Santarsiero B" first="Bernard D" last="Santarsiero">Bernard D. Santarsiero</name>
</author>
<author><name sortKey="Barretto, Naina" sort="Barretto, Naina" uniqKey="Barretto N" first="Naina" last="Barretto">Naina Barretto</name>
</author>
<author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C" last="Baker">Susan C. Baker</name>
</author>
<author><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C" last="Stevens">Raymond C. Stevens</name>
</author>
<author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D" last="Mesecar">Andrew D. Mesecar</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2006">2006</date>
<idno type="RBID">pubmed:16581910</idno>
<idno type="pmid">16581910</idno>
<idno type="doi">10.1073/pnas.0510851103</idno>
<idno type="wicri:Area/PubMed/Corpus">002292</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002292</idno>
<idno type="wicri:Area/PubMed/Curation">002292</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002292</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001F99</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001F99</idno>
<idno type="wicri:Area/Ncbi/Merge">001439</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme.</title>
<author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name>
<affiliation wicri:level="2"><nlm:affiliation>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois, Chicago, IL 60607, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois, Chicago, IL 60607</wicri:regionArea>
<placeName><region type="state">Illinois</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Saikatendu, Kumar Singh" sort="Saikatendu, Kumar Singh" uniqKey="Saikatendu K" first="Kumar Singh" last="Saikatendu">Kumar Singh Saikatendu</name>
</author>
<author><name sortKey="Santarsiero, Bernard D" sort="Santarsiero, Bernard D" uniqKey="Santarsiero B" first="Bernard D" last="Santarsiero">Bernard D. Santarsiero</name>
</author>
<author><name sortKey="Barretto, Naina" sort="Barretto, Naina" uniqKey="Barretto N" first="Naina" last="Barretto">Naina Barretto</name>
</author>
<author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C" last="Baker">Susan C. Baker</name>
</author>
<author><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C" last="Stevens">Raymond C. Stevens</name>
</author>
<author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D" last="Mesecar">Andrew D. Mesecar</name>
</author>
</analytic>
<series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
<idno type="ISSN">0027-8424</idno>
<imprint><date when="2006" type="published">2006</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term>
<term>Crystallography, X-Ray</term>
<term>Cysteine Endopeptidases (chemistry)</term>
<term>Models, Molecular</term>
<term>Papain (metabolism)</term>
<term>Peptide Hydrolases (metabolism)</term>
<term>Protein Structure, Secondary</term>
<term>SARS Virus (enzymology)</term>
<term>Ubiquitin (metabolism)</term>
<term>Viral Proteins (chemistry)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases ()</term>
<term>Modèles moléculaires</term>
<term>Papaïne (métabolisme)</term>
<term>Peptide hydrolases (métabolisme)</term>
<term>Protéines virales ()</term>
<term>Sites de fixation</term>
<term>Structure secondaire des protéines</term>
<term>Ubiquitine (métabolisme)</term>
<term>Virus du SRAS (enzymologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Papain</term>
<term>Peptide Hydrolases</term>
<term>Ubiquitin</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Papaïne</term>
<term>Peptide hydrolases</term>
<term>Ubiquitine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Crystallography, X-Ray</term>
<term>Models, Molecular</term>
<term>Protein Structure, Secondary</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases</term>
<term>Modèles moléculaires</term>
<term>Protéines virales</term>
<term>Sites de fixation</term>
<term>Structure secondaire des protéines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. In this work, we describe the 1.85-A crystal structure of the catalytic core of SARS-CoV PLpro and show that the overall architecture adopts a fold closely resembling that of known deubiquitinating enzymes. Key features, however, distinguish PLpro from characterized deubiquitinating enzymes, including an intact zinc-binding motif, an unobstructed catalytically competent active site, and the presence of an intriguing, ubiquitin-like N-terminal domain. To gain insight into the active-site recognition of the C-terminal tail of ubiquitin and the related LXGG motif, we propose a model of PLpro in complex with ubiquitin-aldehyde that reveals well defined sites within the catalytic cleft that help to account for strict substrate-recognition motifs.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16581910</PMID>
<DateCompleted><Year>2006</Year>
<Month>06</Month>
<Day>09</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>25</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN>
<JournalIssue CitedMedium="Print"><Volume>103</Volume>
<Issue>15</Issue>
<PubDate><Year>2006</Year>
<Month>Apr</Month>
<Day>11</Day>
</PubDate>
</JournalIssue>
<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation>
</Journal>
<ArticleTitle>Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme.</ArticleTitle>
<Pagination><MedlinePgn>5717-22</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. In this work, we describe the 1.85-A crystal structure of the catalytic core of SARS-CoV PLpro and show that the overall architecture adopts a fold closely resembling that of known deubiquitinating enzymes. Key features, however, distinguish PLpro from characterized deubiquitinating enzymes, including an intact zinc-binding motif, an unobstructed catalytically competent active site, and the presence of an intriguing, ubiquitin-like N-terminal domain. To gain insight into the active-site recognition of the C-terminal tail of ubiquitin and the related LXGG motif, we propose a model of PLpro in complex with ubiquitin-aldehyde that reveals well defined sites within the catalytic cleft that help to account for strict substrate-recognition motifs.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ratia</LastName>
<ForeName>Kiira</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois, Chicago, IL 60607, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Saikatendu</LastName>
<ForeName>Kumar Singh</ForeName>
<Initials>KS</Initials>
</Author>
<Author ValidYN="Y"><LastName>Santarsiero</LastName>
<ForeName>Bernard D</ForeName>
<Initials>BD</Initials>
</Author>
<Author ValidYN="Y"><LastName>Barretto</LastName>
<ForeName>Naina</ForeName>
<Initials>N</Initials>
</Author>
<Author ValidYN="Y"><LastName>Baker</LastName>
<ForeName>Susan C</ForeName>
<Initials>SC</Initials>
</Author>
<Author ValidYN="Y"><LastName>Stevens</LastName>
<ForeName>Raymond C</ForeName>
<Initials>RC</Initials>
</Author>
<Author ValidYN="Y"><LastName>Mesecar</LastName>
<ForeName>Andrew D</ForeName>
<Initials>AD</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName>
<AccessionNumberList><AccessionNumber>2FE8</AccessionNumber>
</AccessionNumberList>
</DataBank>
</DataBankList>
<GrantList CompleteYN="Y"><Grant><GrantID>P01 AI060915</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>AI266200400058C</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>Y1-CO-1020</GrantID>
<Acronym>CO</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>Y1-GM-1104</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2006</Year>
<Month>03</Month>
<Day>31</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Proc Natl Acad Sci U S A</MedlineTA>
<NlmUniqueID>7505876</NlmUniqueID>
<ISSNLinking>0027-8424</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D025801">Ubiquitin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.-</RegistryNumber>
<NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber>
<NameOfSubstance UI="C099456">3C-like proteinase, Coronavirus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber>
<NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber>
<NameOfSubstance UI="D010206">Papain</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010206" MajorTopicYN="N">Papain</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010447" MajorTopicYN="N">Peptide Hydrolases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D025801" MajorTopicYN="N">Ubiquitin</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year>
<Month>4</Month>
<Day>4</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2006</Year>
<Month>6</Month>
<Day>10</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2006</Year>
<Month>4</Month>
<Day>4</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">16581910</ArticleId>
<ArticleId IdType="pii">0510851103</ArticleId>
<ArticleId IdType="doi">10.1073/pnas.0510851103</ArticleId>
<ArticleId IdType="pmc">PMC1458639</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):849-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10089316</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1999 May 21;274(21):14918-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10329692</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Biol. 1999 May;6(5):458-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10331874</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1999 Jul;73(7):5957-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10364348</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Sci. 1999 Jun;8(6):1268-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10386876</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Feb;74(4):1674-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10644337</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):965-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10944333</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Jan 5;276(1):780-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11031264</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2001 Feb 1;20(3):362-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11157743</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2000 Oct 6;302(5):1227-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11183785</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Aug 31;276(35):33220-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11431476</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biol Chem. 2001 May;382(5):727-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11517925</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2001 Sep 17;20(18):5187-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11566882</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2002 Apr;76(8):3697-708</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11907209</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2002 Jun;76(12):6323-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12021365</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2002 Sep;10(3):495-507</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12408819</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2002 Dec 27;111(7):1041-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12507430</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2003 Jan 15;31(2):532-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12527760</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2003 May 15;348(20):1953-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12690092</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2003 Jun 13;300(5626):1763-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12746549</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2003 Jul;77(13):7376-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12805436</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Lancet. 2003 Jul 26;362(9380):263-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12892955</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2003 Aug 1;307(3):431-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12893238</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2003 Sep;84(Pt 9):2305-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12917450</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2003 Aug 29;331(5):991-1004</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12927536</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 Dec 26;278(52):52102-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14559899</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13190-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14585926</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Mar 12;279(11):10136-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14699140</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Microbiol. 2004 Aug;7(4):412-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15358261</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Chem Biol. 2004 Oct;11(10):1445-53</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15489171</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Med. 2004 Dec;10(12):1374-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15531891</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Dec;78(24):13600-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15564471</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2256-68</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15572779</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Apr;79(7):4550-1</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15767458</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2005 Aug 2;44(30):10349-59</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16042412</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2005 Aug 19;19(4):547-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16109378</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Dec 2;280(48):40058-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16183633</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2005 Nov 2;24(21):3747-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16211010</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Med Chem. 2005 Nov 3;48(22):6767-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16250632</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Structure. 2005 Nov;13(11):1665-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16271890</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Dec;79(24):15189-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306590</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Dec;79(24):15199-208</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306591</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Dec;79(24):15582-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306630</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2025413</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1995 Feb 17;246(2):273-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7869379</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1997 Jul 11;277(5323):202-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9211842</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1997 Jul 1;16(13):3787-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9233788</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9757107</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1999 Mar;73(3):2016-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9971782</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Illinois</li>
</region>
</list>
<tree><noCountry><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C" last="Baker">Susan C. Baker</name>
<name sortKey="Barretto, Naina" sort="Barretto, Naina" uniqKey="Barretto N" first="Naina" last="Barretto">Naina Barretto</name>
<name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D" last="Mesecar">Andrew D. Mesecar</name>
<name sortKey="Saikatendu, Kumar Singh" sort="Saikatendu, Kumar Singh" uniqKey="Saikatendu K" first="Kumar Singh" last="Saikatendu">Kumar Singh Saikatendu</name>
<name sortKey="Santarsiero, Bernard D" sort="Santarsiero, Bernard D" uniqKey="Santarsiero B" first="Bernard D" last="Santarsiero">Bernard D. Santarsiero</name>
<name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C" last="Stevens">Raymond C. Stevens</name>
</noCountry>
<country name="États-Unis"><region name="Illinois"><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name>
</region>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Ncbi/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001439 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 001439 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= Ncbi |étape= Merge |type= RBID |clé= pubmed:16581910 |texte= Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i -Sk "pubmed:16581910" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |