Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.
Identifieur interne : 001A19 ( PubMed/Corpus ); précédent : 001A18; suivant : 001A20Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.
Auteurs : Amarnath Chatterjee ; Margaret A. Johnson ; Pedro Serrano ; Bill Pedrini ; Jeremiah S. Joseph ; Benjamin W. Neuman ; Kumar Saikatendu ; Michael J. Buchmeier ; Peter Kuhn ; Kurt WüthrichSource :
- Journal of virology [ 1098-5514 ] ; 2009.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : RNA Replicase, RNA-Binding Proteins, Viral Nonstructural Proteins.
- chemical , metabolism : RNA.
- chemistry : SARS Virus.
- Electrophoretic Mobility Shift Assay, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Binding, Protein Structure, Tertiary.
Abstract
The nuclear magnetic resonance (NMR) structure of a central segment of the previously annotated severe acute respiratory syndrome (SARS)-unique domain (SUD-M, for "middle of the SARS-unique domain") in SARS coronavirus (SARS-CoV) nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1"-phosphatase nsp3b, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection.
DOI: 10.1128/JVI.01781-08
PubMed: 19052085
Links to Exploration step
pubmed:19052085Le document en format XML
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Johnson</name></author><author><name sortKey="Serrano, Pedro" sort="Serrano, Pedro" uniqKey="Serrano P" first="Pedro" last="Serrano">Pedro Serrano</name></author><author><name sortKey="Pedrini, Bill" sort="Pedrini, Bill" uniqKey="Pedrini B" first="Bill" last="Pedrini">Bill Pedrini</name></author><author><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S" last="Joseph">Jeremiah S. Joseph</name></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W" last="Neuman">Benjamin W. Neuman</name></author><author><name sortKey="Saikatendu, Kumar" sort="Saikatendu, Kumar" uniqKey="Saikatendu K" first="Kumar" last="Saikatendu">Kumar Saikatendu</name></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J" last="Buchmeier">Michael J. Buchmeier</name></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name></author><author><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19052085</idno><idno type="pmid">19052085</idno><idno type="doi">10.1128/JVI.01781-08</idno><idno type="wicri:Area/PubMed/Corpus">001A19</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001A19</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.</title><author><name sortKey="Chatterjee, Amarnath" sort="Chatterjee, Amarnath" uniqKey="Chatterjee A" first="Amarnath" last="Chatterjee">Amarnath Chatterjee</name><affiliation><nlm:affiliation>Department of Molecular Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A" last="Johnson">Margaret A. Johnson</name></author><author><name sortKey="Serrano, Pedro" sort="Serrano, Pedro" uniqKey="Serrano P" first="Pedro" last="Serrano">Pedro Serrano</name></author><author><name sortKey="Pedrini, Bill" sort="Pedrini, Bill" uniqKey="Pedrini B" first="Bill" last="Pedrini">Bill Pedrini</name></author><author><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S" last="Joseph">Jeremiah S. Joseph</name></author><author><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W" last="Neuman">Benjamin W. Neuman</name></author><author><name sortKey="Saikatendu, Kumar" sort="Saikatendu, Kumar" uniqKey="Saikatendu K" first="Kumar" last="Saikatendu">Kumar Saikatendu</name></author><author><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J" last="Buchmeier">Michael J. Buchmeier</name></author><author><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name></author><author><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Electrophoretic Mobility Shift Assay</term><term>Magnetic Resonance Spectroscopy</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>RNA (metabolism)</term><term>RNA Replicase (chemistry)</term><term>RNA-Binding Proteins (chemistry)</term><term>SARS Virus (chemistry)</term><term>Viral Nonstructural Proteins (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA Replicase</term><term>RNA-Binding Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrophoretic Mobility Shift Assay</term><term>Magnetic Resonance Spectroscopy</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The nuclear magnetic resonance (NMR) structure of a central segment of the previously annotated severe acute respiratory syndrome (SARS)-unique domain (SUD-M, for "middle of the SARS-unique domain") in SARS coronavirus (SARS-CoV) nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1"-phosphatase nsp3b, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19052085</PMID><DateCompleted><Year>2009</Year><Month>02</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>83</Volume><Issue>4</Issue><PubDate><Year>2009</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.</ArticleTitle><Pagination><MedlinePgn>1823-36</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.01781-08</ELocationID><Abstract><AbstractText>The nuclear magnetic resonance (NMR) structure of a central segment of the previously annotated severe acute respiratory syndrome (SARS)-unique domain (SUD-M, for "middle of the SARS-unique domain") in SARS coronavirus (SARS-CoV) nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1"-phosphatase nsp3b, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chatterjee</LastName><ForeName>Amarnath</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>Margaret A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Serrano</LastName><ForeName>Pedro</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Pedrini</LastName><ForeName>Bill</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Joseph</LastName><ForeName>Jeremiah S</ForeName><Initials>JS</Initials></Author><Author ValidYN="Y"><LastName>Neuman</LastName><ForeName>Benjamin W</ForeName><Initials>BW</Initials></Author><Author ValidYN="Y"><LastName>Saikatendu</LastName><ForeName>Kumar</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Buchmeier</LastName><ForeName>Michael J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Kuhn</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Wüthrich</LastName><ForeName>Kurt</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>U54 GM074898</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HHSN266200400058C</GrantID><Agency>PHS HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U54-GM074898</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="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>12</Month><Day>03</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="D016601">RNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.48</RegistryNumber><NameOfSubstance UI="D012324">RNA Replicase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.48</RegistryNumber><NameOfSubstance UI="C510959">nonstructural protein 3, SARS coronovirus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D024202" MajorTopicYN="N">Electrophoretic Mobility Shift Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="Y">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000378" 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PubStatus="medline"><Year>2009</Year><Month>2</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>12</Month><Day>5</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19052085</ArticleId><ArticleId IdType="pii">JVI.01781-08</ArticleId><ArticleId IdType="doi">10.1128/JVI.01781-08</ArticleId><ArticleId IdType="pmc">PMC2643772</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Virol. 2004 Sep;78(18):9977-86</Citation><ArticleIdList><ArticleId IdType="pubmed">15331731</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2002 May 24;319(1):209-27</Citation><ArticleIdList><ArticleId IdType="pubmed">12051947</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomol NMR. 1995 Sep;6(2):135-40</Citation><ArticleIdList><ArticleId IdType="pubmed">8589602</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Jul;80(14):7136-45</Citation><ArticleIdList><ArticleId IdType="pubmed">16809319</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 Virol. 2001 Jul;75(14):6676-81</Citation><ArticleIdList><ArticleId IdType="pubmed">11413334</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1997 Oct 17;273(1):283-98</Citation><ArticleIdList><ArticleId IdType="pubmed">9367762</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Jan;78(2):980-94</Citation><ArticleIdList><ArticleId IdType="pubmed">14694129</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 2005 Nov;13(11):1665-75</Citation><ArticleIdList><ArticleId IdType="pubmed">16271890</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Microbiol. 1992 Feb;6(3):283-91</Citation><ArticleIdList><ArticleId IdType="pubmed">1552844</ArticleId></ArticleIdList></Reference><Reference><Citation>Biomol NMR Assign. 2007 Dec;1(2):191-4</Citation><ArticleIdList><ArticleId IdType="pubmed">19636862</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Microbiol. 2006;60:211-30</Citation><ArticleIdList><ArticleId IdType="pubmed">16712436</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1982;1(8):945-51</Citation><ArticleIdList><ArticleId IdType="pubmed">6329717</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Struct Biol. 1997 Jun;4(6):463-7</Citation><ArticleIdList><ArticleId IdType="pubmed">9187654</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomol NMR. 2008 Jul;41(3):127-38</Citation><ArticleIdList><ArticleId IdType="pubmed">18512031</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Aug 2;102(31):10876-81</Citation><ArticleIdList><ArticleId IdType="pubmed">16043707</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Graph. 1996 Feb;14(1):51-5, 29-32</Citation><ArticleIdList><ArticleId IdType="pubmed">8744573</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4884-7</Citation><ArticleIdList><ArticleId IdType="pubmed">1534409</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomol NMR. 2002 May;23(1):23-33</Citation><ArticleIdList><ArticleId IdType="pubmed">12061715</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 May 30;300(5624):1399-404</Citation><ArticleIdList><ArticleId IdType="pubmed">12730501</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomol NMR. 2006 May;35(1):27-37</Citation><ArticleIdList><ArticleId IdType="pubmed">16791738</ArticleId></ArticleIdList></Reference><Reference><Citation>J Neurovirol. 2004 Apr;10(2):75-85</Citation><ArticleIdList><ArticleId IdType="pubmed">15204926</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomol NMR. 2002 Nov;24(3):171-89</Citation><ArticleIdList><ArticleId IdType="pubmed">12522306</ArticleId></ArticleIdList></Reference><Reference><Citation>J Magn Reson B. 1996 Aug;112(2):200-5</Citation><ArticleIdList><ArticleId IdType="pubmed">8812906</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1993 Sep 5;233(1):123-38</Citation><ArticleIdList><ArticleId IdType="pubmed">8377180</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2007 Nov;81(21):12049-60</Citation><ArticleIdList><ArticleId IdType="pubmed">17728234</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Biochem Sci. 1995 Nov;20(11):478-80</Citation><ArticleIdList><ArticleId IdType="pubmed">8578593</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomol NMR. 1996 Sep;8(2):136-46</Citation><ArticleIdList><ArticleId IdType="pubmed">8914272</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1995 Apr 7;247(4):536-40</Citation><ArticleIdList><ArticleId IdType="pubmed">7723011</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2003 Jul 11;330(3):503-11</Citation><ArticleIdList><ArticleId IdType="pubmed">12842467</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 2007 Dec 28;364(4):877-82</Citation><ArticleIdList><ArticleId IdType="pubmed">17976532</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>J Virol. 2008 Dec;82(24):12392-405</Citation><ArticleIdList><ArticleId IdType="pubmed">18842706</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 Magn Reson. 2000 Apr;143(2):423-6</Citation><ArticleIdList><ArticleId IdType="pubmed">10729271</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioinformatics. 2004 Feb 12;20(3):426-7</Citation><ArticleIdList><ArticleId IdType="pubmed">14960472</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Sep;80(17):8493-502</Citation><ArticleIdList><ArticleId IdType="pubmed">16912299</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 2005 Sep;25(17):7616-24</Citation><ArticleIdList><ArticleId IdType="pubmed">16107708</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2007 Feb;81(4):1574-85</Citation><ArticleIdList><ArticleId IdType="pubmed">17121802</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2008 Jun;82(11):5279-94</Citation><ArticleIdList><ArticleId IdType="pubmed">18367524</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Biochem Sci. 1990 Nov;15(11):430-4</Citation><ArticleIdList><ArticleId IdType="pubmed">2126155</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiol Mol Biol Rev. 2005 Dec;69(4):635-64</Citation><ArticleIdList><ArticleId IdType="pubmed">16339739</ArticleId></ArticleIdList></Reference><Reference><Citation>Virus Res. 2006 Jul;119(1):29-42</Citation><ArticleIdList><ArticleId IdType="pubmed">16310880</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioinformatics. 2007 Nov 1;23(21):2947-8</Citation><ArticleIdList><ArticleId IdType="pubmed">17846036</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>Nucleic Acids Res. 1997 Sep 1;25(17):3389-402</Citation><ArticleIdList><ArticleId IdType="pubmed">9254694</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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