Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.
Identifieur interne : 001D37 ( PubMed/Corpus ); précédent : 001D36; suivant : 001D38Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.
Auteurs : Pedro Serrano ; Margaret A. Johnson ; Marcius S. Almeida ; Reto Horst ; Torsten Herrmann ; Jeremiah S. Joseph ; Benjamin W. Neuman ; Vanitha Subramanian ; Kumar S. Saikatendu ; Michael J. Buchmeier ; Raymond C. Stevens ; Peter Kuhn ; Kurt WüthrichSource :
- Journal of virology [ 0022-538X ] ; 2007.
English descriptors
- KwdEn :
- Amino Acid Sequence, Dose-Response Relationship, Drug, Magnetic Resonance Spectroscopy (methods), Mass Spectrometry, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, RNA Replicase (chemistry), RNA Replicase (metabolism), RNA, Viral (chemistry), SARS Virus (metabolism), Sequence Homology, Amino Acid, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism), Viral Proteins (chemistry).
- MESH :
- chemical , chemistry : RNA Replicase, RNA, Viral, Viral Nonstructural Proteins, Viral Proteins.
- chemical , metabolism : RNA Replicase, Viral Nonstructural Proteins.
- metabolism : SARS Virus.
- methods : Magnetic Resonance Spectroscopy.
- Amino Acid Sequence, Dose-Response Relationship, Drug, Mass Spectrometry, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid.
Abstract
This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.
DOI: 10.1128/JVI.00969-07
PubMed: 17728234
Links to Exploration step
pubmed:17728234Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.</title>
<author><name sortKey="Serrano, Pedro" sort="Serrano, Pedro" uniqKey="Serrano P" first="Pedro" last="Serrano">Pedro Serrano</name>
<affiliation><nlm:affiliation>Department of Molecular Biology, MB-44, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 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="Almeida, Marcius S" sort="Almeida, Marcius S" uniqKey="Almeida M" first="Marcius S" last="Almeida">Marcius S. Almeida</name>
</author>
<author><name sortKey="Horst, Reto" sort="Horst, Reto" uniqKey="Horst R" first="Reto" last="Horst">Reto Horst</name>
</author>
<author><name sortKey="Herrmann, Torsten" sort="Herrmann, Torsten" uniqKey="Herrmann T" first="Torsten" last="Herrmann">Torsten Herrmann</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="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</name>
</author>
<author><name sortKey="Saikatendu, Kumar S" sort="Saikatendu, Kumar S" uniqKey="Saikatendu K" first="Kumar S" last="Saikatendu">Kumar S. 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="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C" last="Stevens">Raymond C. Stevens</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="2007">2007</date>
<idno type="RBID">pubmed:17728234</idno>
<idno type="pmid">17728234</idno>
<idno type="doi">10.1128/JVI.00969-07</idno>
<idno type="wicri:Area/PubMed/Corpus">001D37</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001D37</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.</title>
<author><name sortKey="Serrano, Pedro" sort="Serrano, Pedro" uniqKey="Serrano P" first="Pedro" last="Serrano">Pedro Serrano</name>
<affiliation><nlm:affiliation>Department of Molecular Biology, MB-44, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 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="Almeida, Marcius S" sort="Almeida, Marcius S" uniqKey="Almeida M" first="Marcius S" last="Almeida">Marcius S. Almeida</name>
</author>
<author><name sortKey="Horst, Reto" sort="Horst, Reto" uniqKey="Horst R" first="Reto" last="Horst">Reto Horst</name>
</author>
<author><name sortKey="Herrmann, Torsten" sort="Herrmann, Torsten" uniqKey="Herrmann T" first="Torsten" last="Herrmann">Torsten Herrmann</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="Subramanian, Vanitha" sort="Subramanian, Vanitha" uniqKey="Subramanian V" first="Vanitha" last="Subramanian">Vanitha Subramanian</name>
</author>
<author><name sortKey="Saikatendu, Kumar S" sort="Saikatendu, Kumar S" uniqKey="Saikatendu K" first="Kumar S" last="Saikatendu">Kumar S. 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="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C" last="Stevens">Raymond C. Stevens</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="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>Amino Acid Sequence</term>
<term>Dose-Response Relationship, Drug</term>
<term>Magnetic Resonance Spectroscopy (methods)</term>
<term>Mass Spectrometry</term>
<term>Models, Molecular</term>
<term>Molecular Conformation</term>
<term>Molecular Sequence Data</term>
<term>Protein Conformation</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>RNA Replicase (chemistry)</term>
<term>RNA Replicase (metabolism)</term>
<term>RNA, Viral (chemistry)</term>
<term>SARS Virus (metabolism)</term>
<term>Sequence Homology, Amino Acid</term>
<term>Viral Nonstructural Proteins (chemistry)</term>
<term>Viral Nonstructural Proteins (metabolism)</term>
<term>Viral Proteins (chemistry)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA Replicase</term>
<term>RNA, Viral</term>
<term>Viral Nonstructural Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA Replicase</term>
<term>Viral Nonstructural Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Magnetic Resonance Spectroscopy</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Dose-Response Relationship, Drug</term>
<term>Mass Spectrometry</term>
<term>Models, Molecular</term>
<term>Molecular Conformation</term>
<term>Molecular Sequence Data</term>
<term>Protein Conformation</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17728234</PMID>
<DateCompleted><Year>2007</Year>
<Month>11</Month>
<Day>27</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>21</Issue>
<PubDate><Year>2007</Year>
<Month>Nov</Month>
</PubDate>
</JournalIssue>
<Title>Journal of virology</Title>
<ISOAbbreviation>J. Virol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.</ArticleTitle>
<Pagination><MedlinePgn>12049-60</MedlinePgn>
</Pagination>
<Abstract><AbstractText>This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Serrano</LastName>
<ForeName>Pedro</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biology, MB-44, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Johnson</LastName>
<ForeName>Margaret A</ForeName>
<Initials>MA</Initials>
</Author>
<Author ValidYN="Y"><LastName>Almeida</LastName>
<ForeName>Marcius S</ForeName>
<Initials>MS</Initials>
</Author>
<Author ValidYN="Y"><LastName>Horst</LastName>
<ForeName>Reto</ForeName>
<Initials>R</Initials>
</Author>
<Author ValidYN="Y"><LastName>Herrmann</LastName>
<ForeName>Torsten</ForeName>
<Initials>T</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>Subramanian</LastName>
<ForeName>Vanitha</ForeName>
<Initials>V</Initials>
</Author>
<Author ValidYN="Y"><LastName>Saikatendu</LastName>
<ForeName>Kumar S</ForeName>
<Initials>KS</Initials>
</Author>
<Author ValidYN="Y"><LastName>Buchmeier</LastName>
<ForeName>Michael J</ForeName>
<Initials>MJ</Initials>
</Author>
<Author ValidYN="Y"><LastName>Stevens</LastName>
<ForeName>Raymond C</ForeName>
<Initials>RC</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>
<DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName>
<AccessionNumberList><AccessionNumber>2GRI</AccessionNumber>
<AccessionNumber>2IDY</AccessionNumber>
</AccessionNumberList>
</DataBank>
</DataBankList>
<GrantList CompleteYN="Y"><Grant><GrantID>U54 GM074898</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>U54 GM 074898</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>2007</Year>
<Month>08</Month>
<Day>29</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="D012367">RNA, Viral</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014764">Viral Proteins</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="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName>
<QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008968" MajorTopicYN="N">Molecular Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012324" MajorTopicYN="N">RNA Replicase</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012367" MajorTopicYN="N">RNA, Viral</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year>
<Month>8</Month>
<Day>31</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2007</Year>
<Month>12</Month>
<Day>6</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2007</Year>
<Month>8</Month>
<Day>31</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">17728234</ArticleId>
<ArticleId IdType="pii">JVI.00969-07</ArticleId>
<ArticleId IdType="doi">10.1128/JVI.00969-07</ArticleId>
<ArticleId IdType="pmc">PMC2168779</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>J Biol Chem. 1999 Nov 19;274(47):33732-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10559265</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 2006;581:503-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17037585</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>Nature. 2002 Feb 7;415(6872):662-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11832950</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. 2002 May;23(1):23-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12061715</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2002 Oct 2;124(39):11596-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12296715</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 Mol Biol. 2003 Aug 29;331(5):991-1004</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12927536</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Jun;78(11):5658-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15140963</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Neurovirol. 2004 Apr;10(2):75-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15204926</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Semin Cell Dev Biol. 2004 Apr;15(2):237-46</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15209384</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1994 Aug;14(8):5441-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8035821</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1995 Jun 15;375(6532):554-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7791872</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 Mol Graph. 1996 Feb;14(1):51-5, 29-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8744573</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>Nature. 1997 Mar 13;386(6621):177-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9062190</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>Nat Struct Biol. 1998 Jun;5(6):422-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9628477</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Biol. 1999 Apr;6(4):336-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10201401</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 1999 Aug 15;342 ( Pt 1):119-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10432308</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1999 Aug 20;274(34):23850-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10446149</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Dec;78(24):14043-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15564512</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15572765</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2005 Jul 4;579(17):3837-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15978580</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 2005 Jul 4;170(1):15-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15983058</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Jul 22;280(29):27356-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15917233</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virol J. 2005;2:66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16107218</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Structure. 2005 Nov;13(11):1665-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16271890</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2006 Jan 27;355(4):821-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16310215</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Jan;80(2):785-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16378980</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Mol Biol. 2005 Nov;12(11):980-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16228002</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol NMR. 2006;36 Suppl 1:45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16799860</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2007 Jan;81(2):548-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17108024</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Dec;79(24):15189-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306590</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>Virol J. 2006;3:17</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16571117</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2006 Aug 22;103(34):12885-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16912115</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 2006;581:37-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17037501</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Biochem. 2000 Jan;267(2):295-304</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10632699</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001D37 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 001D37 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= PubMed |étape= Corpus |type= RBID |clé= pubmed:17728234 |texte= Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:17728234" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |