Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63.
Identifieur interne : 001D29 ( PubMed/Checkpoint ); précédent : 001D28; suivant : 001D30Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63.
Auteurs : Zhongbin Chen [États-Unis] ; Yanhua Wang ; Kiira Ratia ; Andrew D. Mesecar ; Keith D. Wilkinson ; Susan C. BakerSource :
- Journal of virology [ 0022-538X ] ; 2007.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Coronavirus.
- métabolisme : Cysteine endopeptidases, Papaïne, Protéines de l'enveloppe virale, Ubiquitine.
- physiologie : Coronavirus, Maturation post-traductionnelle des protéines, Réplication virale.
- Humains.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Cysteine Endopeptidases, Papain, Ubiquitin, Viral Envelope Proteins.
- enzymology : Coronavirus.
- physiology : Coronavirus, Protein Processing, Post-Translational, Virus Replication.
- Humans.
Abstract
Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is associated with both upper and lower respiratory tract disease in children and adults. Currently, no antiviral drugs are available to treat CoV infections; thus, potential drug targets need to be identified and characterized. Here, we identify HCoV-NL63 replicase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which process the viral replicase polyprotein. We generated polyclonal antisera directed against two of the predicted replicase nonstructural proteins (nsp3 and nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence, immunoprecipitation, and Western blot assays. We found that HCoV-NL63 replicase products can be detected at 24 h postinfection and that these proteins accumulate in perinuclear sites, consistent with membrane-associated replication complexes. To determine which viral proteases are responsible for processing these products, we generated constructs representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cleavage assays. We found that PLP1 processes cleavage site 1 to release nsp1, whereas PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. We expressed and purified PLP2 and used a peptide-based assay to identify the cleavage sites recognized by this enzyme. Furthermore, by using K48-linked hexa-ubiquitin substrate and ubiquitin-vinylsulfone inhibitor specific for deubiquitinating enzymes (DUBs), we confirmed that, like severe acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity. The identification of the replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative studies of CoV proteases and aid in the development of novel antiviral reagents directed against human pathogens such as HCoV-NL63 and SARS-CoV.
DOI: 10.1128/JVI.02747-06
PubMed: 17392370
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:17392370Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63.</title>
<author><name sortKey="Chen, Zhongbin" sort="Chen, Zhongbin" uniqKey="Chen Z" first="Zhongbin" last="Chen">Zhongbin Chen</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Bldg. 105, Rm. 3929, Maywood, IL 60153, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Bldg. 105, Rm. 3929, Maywood, IL 60153</wicri:regionArea>
<placeName><region type="state">Illinois</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Wang, Yanhua" sort="Wang, Yanhua" uniqKey="Wang Y" first="Yanhua" last="Wang">Yanhua Wang</name>
</author>
<author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</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>
<author><name sortKey="Wilkinson, Keith D" sort="Wilkinson, Keith D" uniqKey="Wilkinson K" first="Keith D" last="Wilkinson">Keith D. Wilkinson</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>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2007">2007</date>
<idno type="RBID">pubmed:17392370</idno>
<idno type="pmid">17392370</idno>
<idno type="doi">10.1128/JVI.02747-06</idno>
<idno type="wicri:Area/PubMed/Corpus">001E61</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001E61</idno>
<idno type="wicri:Area/PubMed/Curation">001E61</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001E61</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001D29</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001D29</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63.</title>
<author><name sortKey="Chen, Zhongbin" sort="Chen, Zhongbin" uniqKey="Chen Z" first="Zhongbin" last="Chen">Zhongbin Chen</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Bldg. 105, Rm. 3929, Maywood, IL 60153, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Bldg. 105, Rm. 3929, Maywood, IL 60153</wicri:regionArea>
<placeName><region type="state">Illinois</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Wang, Yanhua" sort="Wang, Yanhua" uniqKey="Wang Y" first="Yanhua" last="Wang">Yanhua Wang</name>
</author>
<author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</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>
<author><name sortKey="Wilkinson, Keith D" sort="Wilkinson, Keith D" uniqKey="Wilkinson K" first="Keith D" last="Wilkinson">Keith D. Wilkinson</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>
</analytic>
<series><title level="j">Journal of virology</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date when="2007" type="published">2007</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus (enzymology)</term>
<term>Coronavirus (physiology)</term>
<term>Cysteine Endopeptidases (metabolism)</term>
<term>Humans</term>
<term>Papain (metabolism)</term>
<term>Protein Processing, Post-Translational (physiology)</term>
<term>Ubiquitin (metabolism)</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Virus Replication (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Coronavirus (enzymologie)</term>
<term>Coronavirus (physiologie)</term>
<term>Cysteine endopeptidases (métabolisme)</term>
<term>Humains</term>
<term>Maturation post-traductionnelle des protéines (physiologie)</term>
<term>Papaïne (métabolisme)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Réplication virale (physiologie)</term>
<term>Ubiquitine (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term>
<term>Papain</term>
<term>Ubiquitin</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Coronavirus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Papaïne</term>
<term>Protéines de l'enveloppe virale</term>
<term>Ubiquitine</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Réplication virale</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term>
<term>Protein Processing, Post-Translational</term>
<term>Virus Replication</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Humans</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Humains</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is associated with both upper and lower respiratory tract disease in children and adults. Currently, no antiviral drugs are available to treat CoV infections; thus, potential drug targets need to be identified and characterized. Here, we identify HCoV-NL63 replicase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which process the viral replicase polyprotein. We generated polyclonal antisera directed against two of the predicted replicase nonstructural proteins (nsp3 and nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence, immunoprecipitation, and Western blot assays. We found that HCoV-NL63 replicase products can be detected at 24 h postinfection and that these proteins accumulate in perinuclear sites, consistent with membrane-associated replication complexes. To determine which viral proteases are responsible for processing these products, we generated constructs representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cleavage assays. We found that PLP1 processes cleavage site 1 to release nsp1, whereas PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. We expressed and purified PLP2 and used a peptide-based assay to identify the cleavage sites recognized by this enzyme. Furthermore, by using K48-linked hexa-ubiquitin substrate and ubiquitin-vinylsulfone inhibitor specific for deubiquitinating enzymes (DUBs), we confirmed that, like severe acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity. The identification of the replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative studies of CoV proteases and aid in the development of novel antiviral reagents directed against human pathogens such as HCoV-NL63 and SARS-CoV.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17392370</PMID>
<DateCompleted><Year>2007</Year>
<Month>07</Month>
<Day>12</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-538X</ISSN>
<JournalIssue CitedMedium="Print"><Volume>81</Volume>
<Issue>11</Issue>
<PubDate><Year>2007</Year>
<Month>Jun</Month>
</PubDate>
</JournalIssue>
<Title>Journal of virology</Title>
<ISOAbbreviation>J. Virol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63.</ArticleTitle>
<Pagination><MedlinePgn>6007-18</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Human coronavirus NL63 (HCoV-NL63), a common human respiratory pathogen, is associated with both upper and lower respiratory tract disease in children and adults. Currently, no antiviral drugs are available to treat CoV infections; thus, potential drug targets need to be identified and characterized. Here, we identify HCoV-NL63 replicase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which process the viral replicase polyprotein. We generated polyclonal antisera directed against two of the predicted replicase nonstructural proteins (nsp3 and nsp4) and detected replicase proteins from HCoV-NL63-infected LLC-MK2 cells by immunofluorescence, immunoprecipitation, and Western blot assays. We found that HCoV-NL63 replicase products can be detected at 24 h postinfection and that these proteins accumulate in perinuclear sites, consistent with membrane-associated replication complexes. To determine which viral proteases are responsible for processing these products, we generated constructs representing the amino-terminal end of the HCoV-NL63 replicase gene and established protease cis-cleavage assays. We found that PLP1 processes cleavage site 1 to release nsp1, whereas PLP2 is responsible for processing both cleavage sites 2 and 3 to release nsp2 and nsp3. We expressed and purified PLP2 and used a peptide-based assay to identify the cleavage sites recognized by this enzyme. Furthermore, by using K48-linked hexa-ubiquitin substrate and ubiquitin-vinylsulfone inhibitor specific for deubiquitinating enzymes (DUBs), we confirmed that, like severe acute respiratory syndrome (SARS) CoV PLpro, HCoV-NL63 PLP2 has DUB activity. The identification of the replicase products and characterization of HCoV-NL63 PLP DUB activity will facilitate comparative studies of CoV proteases and aid in the development of novel antiviral reagents directed against human pathogens such as HCoV-NL63 and SARS-CoV.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Zhongbin</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Loyola University Medical Center, 2160 South First Avenue, Bldg. 105, Rm. 3929, Maywood, IL 60153, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Yanhua</ForeName>
<Initials>Y</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ratia</LastName>
<ForeName>Kiira</ForeName>
<Initials>K</Initials>
</Author>
<Author ValidYN="Y"><LastName>Mesecar</LastName>
<ForeName>Andrew D</ForeName>
<Initials>AD</Initials>
</Author>
<Author ValidYN="Y"><LastName>Wilkinson</LastName>
<ForeName>Keith D</ForeName>
<Initials>KD</Initials>
</Author>
<Author ValidYN="Y"><LastName>Baker</LastName>
<ForeName>Susan C</ForeName>
<Initials>SC</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>P01 AI060915</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>P01-AI060915</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01-A1045798</GrantID>
<Agency>PHS 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>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2007</Year>
<Month>03</Month>
<Day>28</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Virol</MedlineTA>
<NlmUniqueID>0113724</NlmUniqueID>
<ISSNLinking>0022-538X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D025801">Ubiquitin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014759">Viral Envelope Proteins</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="D017934" MajorTopicYN="N">Coronavirus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010206" MajorTopicYN="N">Papain</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D025801" MajorTopicYN="N">Ubiquitin</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014779" MajorTopicYN="N">Virus Replication</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year>
<Month>3</Month>
<Day>30</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2007</Year>
<Month>7</Month>
<Day>13</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2007</Year>
<Month>3</Month>
<Day>30</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">17392370</ArticleId>
<ArticleId IdType="pii">JVI.02747-06</ArticleId>
<ArticleId IdType="doi">10.1128/JVI.02747-06</ArticleId>
<ArticleId IdType="pmc">PMC1900296</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>J Virol. 2004 Jun;78(11):5957-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15140993</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):10012-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15226499</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2004;32(14):e115</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15304544</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Sep;78(18):9977-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15331731</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1967 Apr;57(4):933-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">5231356</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1999 Apr;73(4):2658-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10074111</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1999 Jul;73(7):5957-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10364348</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Dec;78(24):13600-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15564471</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Med. 2004 Dec;10(12):1374-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15531891</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Top Microbiol Immunol. 2005;287:57-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15609509</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Jan;79(2):884-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15613317</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Infect Dis. 2005 Feb 15;191(4):503-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15655772</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Med Virol. 2005 Mar;75(3):463-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15648061</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Med Virol. 2005 Mar;75(3):455-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15648064</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2430-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15695582</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Apr;79(7):4550-1</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15767458</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Clin Infect Dis. 2005 Jun 15;40(12):1721-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15909257</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 May 31;102(22):7988-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15897467</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Pediatr Infect Dis J. 2005 Jul;24(7):645-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15999010</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Mol Cell Biol. 2005 Aug;6(8):599-609</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16064136</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Emerg Infect Dis. 2005 Aug;11(8):1225-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16102311</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>PLoS Med. 2005 Aug;2(8):e240</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16104827</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Clin Microbiol. 2005 Sep;43(9):4567-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16145108</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):14040-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16169905</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS Biol. 2005 Oct;3(10):e324</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16128623</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Essays Biochem. 2005;41:139-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16250903</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>Science. 2005 Oct 28;310(5748):676-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16195424</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Structure. 2005 Nov;13(11):1665-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16271890</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1967 Apr;1(2):175-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4293939</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1992 Jul;189(1):274-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1318604</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1995 Jun 1;209(2):420-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7778277</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1995 Jun 1;209(2):489-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7539970</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1997 Feb;71(2):900-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8995606</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Feb;74(4):1674-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10644337</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Sep;74(17):7911-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10933699</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>Virology. 1995 Apr 1;208(1):1-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11831690</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>Chem Biol. 2002 Oct;9(10):1149-59</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12401499</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Lancet. 2003 Apr 19;361(9366):1319-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12711465</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2003 May 15;348(20):1967-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12690091</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>J Virol. 2003 Jul;77(13):7376-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12805436</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 Virol. 2003 Oct;77(19):10515-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12970436</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Cell Dev Biol. 2003;19:141-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14570567</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>Emerg Infect Dis. 2004 Feb;10(2):320-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15030705</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Med. 2004 Apr;10(4):368-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15034574</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6212-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15073334</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Pediatr Infect Dis J. 2005 Nov;24(11):1015-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16282944</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>Virol J. 2004;1:7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15548333</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2005 Dec 2;123(5):773-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16325574</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteins. 2006 Mar 15;62(3):760-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16358325</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2006 Apr 11;103(15):5717-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16581910</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 May;80(9):4211-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16611880</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antimicrob Agents Chemother. 2006 Jun;50(6):2000-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16723558</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Jun;80(12):5927-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16731931</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Jun;80(12):6003-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16731939</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS Pathog. 2005 Dec;1(4):e39</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16341254</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Clin Infect Dis. 2006 Sep 1;43(5):585-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16886150</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Sep;80(17):8639-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16912312</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Dec;80(23):11610-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16971428</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="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D" last="Mesecar">Andrew D. Mesecar</name>
<name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name>
<name sortKey="Wang, Yanhua" sort="Wang, Yanhua" uniqKey="Wang Y" first="Yanhua" last="Wang">Yanhua Wang</name>
<name sortKey="Wilkinson, Keith D" sort="Wilkinson, Keith D" uniqKey="Wilkinson K" first="Keith D" last="Wilkinson">Keith D. Wilkinson</name>
</noCountry>
<country name="États-Unis"><region name="Illinois"><name sortKey="Chen, Zhongbin" sort="Chen, Zhongbin" uniqKey="Chen Z" first="Zhongbin" last="Chen">Zhongbin Chen</name>
</region>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001D29 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 001D29 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= PubMed |étape= Checkpoint |type= RBID |clé= pubmed:17392370 |texte= Proteolytic processing and deubiquitinating activity of papain-like proteases of human coronavirus NL63. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i -Sk "pubmed:17392370" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |