Expression and purification of SARS coronavirus proteins using SUMO-fusions.
Identifieur interne : 002701 ( PubMed/Corpus ); précédent : 002700; suivant : 002702Expression and purification of SARS coronavirus proteins using SUMO-fusions.
Auteurs : Xun Zuo ; Michael R. Mattern ; Robin Tan ; Shuisen Li ; John Hall ; David E. Sterner ; Joshua Shoo ; Hiep Tran ; Peter Lim ; Stefan G. Sarafianos ; Lubna Kazi ; Sonia Navas-Martin ; Susan R. Weiss ; Tauseef R. ButtSource :
- Protein expression and purification [ 1046-5928 ] ; 2005.
English descriptors
- KwdEn :
- Cysteine Endopeptidases (biosynthesis), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (isolation & purification), Escherichia coli (genetics), Gene Expression (genetics), Genetic Vectors (genetics), Histidine (genetics), Membrane Glycoproteins (biosynthesis), Membrane Glycoproteins (genetics), Membrane Glycoproteins (isolation & purification), Nucleocapsid Proteins (biosynthesis), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (isolation & purification), Peptide Hydrolases (metabolism), Recombinant Fusion Proteins (biosynthesis), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (genetics), Small Ubiquitin-Related Modifier Proteins (genetics), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (biosynthesis), Viral Envelope Proteins (genetics), Viral Envelope Proteins (isolation & purification), Viral Proteins (genetics), Viral Proteins (isolation & purification), Viral Proteins (metabolism).
- MESH :
- chemical , biosynthesis : Cysteine Endopeptidases, Membrane Glycoproteins, Nucleocapsid Proteins, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , genetics : Cysteine Endopeptidases, Histidine, Membrane Glycoproteins, Nucleocapsid Proteins, Recombinant Fusion Proteins, Small Ubiquitin-Related Modifier Proteins, Viral Envelope Proteins, Viral Proteins.
- chemical , isolation & purification : Cysteine Endopeptidases, Membrane Glycoproteins, Nucleocapsid Proteins, Viral Envelope Proteins, Viral Proteins.
- genetics : Escherichia coli, Gene Expression, Genetic Vectors, SARS Virus.
- chemical , metabolism : Peptide Hydrolases, Recombinant Fusion Proteins, Viral Proteins.
- chemical : Spike Glycoprotein, Coronavirus.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) proteins belong to a large group of proteins that is difficult to express in traditional expression systems. The ability to express and purify SARS-CoV proteins in large quantities is critical for basic research and for development of pharmaceutical agents. The work reported here demonstrates: (1) fusion of SUMO (small ubiquitin-related modifier), a 100 amino acid polypeptide, to the N-termini of SARS-CoV proteins dramatically enhances expression in Escherichia coli cells and (2) 6x His-tagged SUMO-fusions facilitate rapid purification of the viral proteins on a large scale. We have exploited the natural chaperoning properties of SUMO to develop an expression system suitable for proteins that cannot be expressed by traditional methodologies. A unique feature of the system is the SUMO tag, which enhances expression, facilitates purification, and can be efficiently cleaved by a SUMO-specific protease to generate native protein with a desired N-terminus. We have purified various SARS-CoV proteins under either native or denaturing conditions. These purified proteins have been used to generate highly specific polyclonal antibodies. Our study suggests that the SUMO-fusion technology will be useful for enhancing expression and purification of the viral proteins for structural and functional studies as well as for therapeutic uses.
DOI: 10.1016/j.pep.2005.02.004
PubMed: 15939295
Links to Exploration step
pubmed:15939295Le document en format XML
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Mattern</name></author><author><name sortKey="Tan, Robin" sort="Tan, Robin" uniqKey="Tan R" first="Robin" last="Tan">Robin Tan</name></author><author><name sortKey="Li, Shuisen" sort="Li, Shuisen" uniqKey="Li S" first="Shuisen" last="Li">Shuisen Li</name></author><author><name sortKey="Hall, John" sort="Hall, John" uniqKey="Hall J" first="John" last="Hall">John Hall</name></author><author><name sortKey="Sterner, David E" sort="Sterner, David E" uniqKey="Sterner D" first="David E" last="Sterner">David E. 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Mattern</name></author><author><name sortKey="Tan, Robin" sort="Tan, Robin" uniqKey="Tan R" first="Robin" last="Tan">Robin Tan</name></author><author><name sortKey="Li, Shuisen" sort="Li, Shuisen" uniqKey="Li S" first="Shuisen" last="Li">Shuisen Li</name></author><author><name sortKey="Hall, John" sort="Hall, John" uniqKey="Hall J" first="John" last="Hall">John Hall</name></author><author><name sortKey="Sterner, David E" sort="Sterner, David E" uniqKey="Sterner D" first="David E" last="Sterner">David E. Sterner</name></author><author><name sortKey="Shoo, Joshua" sort="Shoo, Joshua" uniqKey="Shoo J" first="Joshua" last="Shoo">Joshua Shoo</name></author><author><name sortKey="Tran, Hiep" sort="Tran, Hiep" uniqKey="Tran H" first="Hiep" last="Tran">Hiep Tran</name></author><author><name sortKey="Lim, Peter" sort="Lim, Peter" uniqKey="Lim P" first="Peter" last="Lim">Peter Lim</name></author><author><name sortKey="Sarafianos, Stefan G" sort="Sarafianos, Stefan G" uniqKey="Sarafianos S" first="Stefan G" last="Sarafianos">Stefan G. Sarafianos</name></author><author><name sortKey="Kazi, Lubna" sort="Kazi, Lubna" uniqKey="Kazi L" first="Lubna" last="Kazi">Lubna Kazi</name></author><author><name sortKey="Navas Martin, Sonia" sort="Navas Martin, Sonia" uniqKey="Navas Martin S" first="Sonia" last="Navas-Martin">Sonia Navas-Martin</name></author><author><name sortKey="Weiss, Susan R" sort="Weiss, Susan R" uniqKey="Weiss S" first="Susan R" last="Weiss">Susan R. Weiss</name></author><author><name sortKey="Butt, Tauseef R" sort="Butt, Tauseef R" uniqKey="Butt T" first="Tauseef R" last="Butt">Tauseef R. Butt</name></author></analytic><series><title level="j">Protein expression and purification</title><idno type="ISSN">1046-5928</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cysteine Endopeptidases (biosynthesis)</term><term>Cysteine Endopeptidases (genetics)</term><term>Cysteine Endopeptidases (isolation & purification)</term><term>Escherichia coli (genetics)</term><term>Gene Expression (genetics)</term><term>Genetic Vectors (genetics)</term><term>Histidine (genetics)</term><term>Membrane Glycoproteins (biosynthesis)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (isolation & purification)</term><term>Nucleocapsid Proteins (biosynthesis)</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (isolation & purification)</term><term>Peptide Hydrolases (metabolism)</term><term>Recombinant Fusion Proteins (biosynthesis)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (genetics)</term><term>Small Ubiquitin-Related Modifier Proteins (genetics)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (biosynthesis)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (isolation & purification)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (isolation & purification)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Membrane Glycoproteins</term><term>Nucleocapsid Proteins</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Histidine</term><term>Membrane Glycoproteins</term><term>Nucleocapsid Proteins</term><term>Recombinant Fusion Proteins</term><term>Small Ubiquitin-Related Modifier Proteins</term><term>Viral Envelope Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Membrane Glycoproteins</term><term>Nucleocapsid Proteins</term><term>Viral Envelope Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Gene Expression</term><term>Genetic Vectors</term><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Hydrolases</term><term>Recombinant Fusion Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) proteins belong to a large group of proteins that is difficult to express in traditional expression systems. The ability to express and purify SARS-CoV proteins in large quantities is critical for basic research and for development of pharmaceutical agents. The work reported here demonstrates: (1) fusion of SUMO (small ubiquitin-related modifier), a 100 amino acid polypeptide, to the N-termini of SARS-CoV proteins dramatically enhances expression in Escherichia coli cells and (2) 6x His-tagged SUMO-fusions facilitate rapid purification of the viral proteins on a large scale. We have exploited the natural chaperoning properties of SUMO to develop an expression system suitable for proteins that cannot be expressed by traditional methodologies. A unique feature of the system is the SUMO tag, which enhances expression, facilitates purification, and can be efficiently cleaved by a SUMO-specific protease to generate native protein with a desired N-terminus. We have purified various SARS-CoV proteins under either native or denaturing conditions. These purified proteins have been used to generate highly specific polyclonal antibodies. Our study suggests that the SUMO-fusion technology will be useful for enhancing expression and purification of the viral proteins for structural and functional studies as well as for therapeutic uses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15939295</PMID><DateCompleted><Year>2005</Year><Month>12</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1046-5928</ISSN><JournalIssue CitedMedium="Print"><Volume>42</Volume><Issue>1</Issue><PubDate><Year>2005</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Protein expression and purification</Title><ISOAbbreviation>Protein Expr. Purif.</ISOAbbreviation></Journal><ArticleTitle>Expression and purification of SARS coronavirus proteins using SUMO-fusions.</ArticleTitle><Pagination><MedlinePgn>100-10</MedlinePgn></Pagination><Abstract><AbstractText>Severe acute respiratory syndrome coronavirus (SARS-CoV) proteins belong to a large group of proteins that is difficult to express in traditional expression systems. The ability to express and purify SARS-CoV proteins in large quantities is critical for basic research and for development of pharmaceutical agents. The work reported here demonstrates: (1) fusion of SUMO (small ubiquitin-related modifier), a 100 amino acid polypeptide, to the N-termini of SARS-CoV proteins dramatically enhances expression in Escherichia coli cells and (2) 6x His-tagged SUMO-fusions facilitate rapid purification of the viral proteins on a large scale. We have exploited the natural chaperoning properties of SUMO to develop an expression system suitable for proteins that cannot be expressed by traditional methodologies. A unique feature of the system is the SUMO tag, which enhances expression, facilitates purification, and can be efficiently cleaved by a SUMO-specific protease to generate native protein with a desired N-terminus. We have purified various SARS-CoV proteins under either native or denaturing conditions. These purified proteins have been used to generate highly specific polyclonal antibodies. Our study suggests that the SUMO-fusion technology will be useful for enhancing expression and purification of the viral proteins for structural and functional studies as well as for therapeutic uses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zuo</LastName><ForeName>Xun</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>LifeSensors, Inc., Malvern, PA 19355, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mattern</LastName><ForeName>Michael R</ForeName><Initials>MR</Initials></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Robin</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Shuisen</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Hall</LastName><ForeName>John</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Sterner</LastName><ForeName>David E</ForeName><Initials>DE</Initials></Author><Author ValidYN="Y"><LastName>Shoo</LastName><ForeName>Joshua</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Tran</LastName><ForeName>Hiep</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Lim</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Sarafianos</LastName><ForeName>Stefan G</ForeName><Initials>SG</Initials></Author><Author ValidYN="Y"><LastName>Kazi</LastName><ForeName>Lubna</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Navas-Martin</LastName><ForeName>Sonia</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Weiss</LastName><ForeName>Susan R</ForeName><Initials>SR</Initials></Author><Author ValidYN="Y"><LastName>Butt</LastName><ForeName>Tauseef R</ForeName><Initials>TR</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI017418</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R43 GM067271</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R43 GM067271-01</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01-AI 17418</GrantID><Acronym>AI</Acronym><Agency>NIAID 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="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>02</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Protein Expr Purif</MedlineTA><NlmUniqueID>9101496</NlmUniqueID><ISSNLinking>1046-5928</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D025841">Small Ubiquitin-Related Modifier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical><Chemical><RegistryNumber>26062-48-6</RegistryNumber><NameOfSubstance UI="C033223">polyhistidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>4QD397987E</RegistryNumber><NameOfSubstance UI="D006639">Histidine</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005822" MajorTopicYN="N">Genetic Vectors</DescriptorName><QualifierName UI="Q000235" 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Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D025841" MajorTopicYN="N">Small Ubiquitin-Related Modifier Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral 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PubStatus="pubmed"><Year>2005</Year><Month>6</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>12</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>6</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15939295</ArticleId><ArticleId IdType="pii">S1046-5928(05)00046-X</ArticleId><ArticleId IdType="doi">10.1016/j.pep.2005.02.004</ArticleId><ArticleId IdType="pmc">PMC7129641</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Virol. 2004 Jun;78(11):5612-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15140958</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Mol Cell Biol. 2000 Apr;20(7):2367-77</Citation><ArticleIdList><ArticleId IdType="pubmed">10713161</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2004 May 14;317(4):1030-6</Citation><ArticleIdList><ArticleId IdType="pubmed">15094372</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 1998 Jul 10;280(2):275-86</Citation><ArticleIdList><ArticleId IdType="pubmed">9654451</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Sci. 2004 May;13(5):1331-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15096636</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nucleic Acids Res. 2003 Dec 15;31(24):7117-30</Citation><ArticleIdList><ArticleId IdType="pubmed">14654687</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nature. 1999 Mar 18;398(6724):246-51</Citation><ArticleIdList><ArticleId IdType="pubmed">10094048</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nat Biotechnol. 1999 Jul;17(7):691-5</Citation><ArticleIdList><ArticleId IdType="pubmed">10404163</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Expr Purif. 1997 Oct;11(1):1-16</Citation><ArticleIdList><ArticleId IdType="pubmed">9325133</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 1989 May 5;264(13):7715-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2540202</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Arch Virol Suppl. 1993;7:63-74</Citation><ArticleIdList><ArticleId IdType="pubmed">8219814</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 1999 Oct 29;274(44):31131-4</Citation><ArticleIdList><ArticleId IdType="pubmed">10531301</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virology. 1993 Aug;195(2):680-91</Citation><ArticleIdList><ArticleId IdType="pubmed">8337838</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1953-66</Citation><ArticleIdList><ArticleId IdType="pubmed">12690092</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Mol Cell Biol. 1989 Aug;9(8):3517-23</Citation><ArticleIdList><ArticleId IdType="pubmed">2552296</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2000 May 12;275(19):14102-6</Citation><ArticleIdList><ArticleId IdType="pubmed">10799485</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Am J Physiol. 1998 Oct;275(4):L694-700</Citation><ArticleIdList><ArticleId IdType="pubmed">9755101</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2003 Aug 29;331(5):991-1004</Citation><ArticleIdList><ArticleId IdType="pubmed">12927536</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2003 Dec 26;312(4):1159-64</Citation><ArticleIdList><ArticleId IdType="pubmed">14651994</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1989 Apr;86(8):2540-4</Citation><ArticleIdList><ArticleId IdType="pubmed">2539593</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2000 Mar 3;275(9):6252-8</Citation><ArticleIdList><ArticleId IdType="pubmed">10692421</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Immunol Lett. 2004 Sep;95(2):139-43</Citation><ArticleIdList><ArticleId IdType="pubmed">15388253</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biotechnol Appl Biochem. 2002 Apr;35(2):91-105</Citation><ArticleIdList><ArticleId IdType="pubmed">11916451</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Gene. 2000 May 2;248(1-2):1-14</Citation><ArticleIdList><ArticleId IdType="pubmed">10806345</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Cell Physiol. 2002 Jun;191(3):257-68</Citation><ArticleIdList><ArticleId IdType="pubmed">12012321</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2004 Jul;78(13):6938-45</Citation><ArticleIdList><ArticleId IdType="pubmed">15194770</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Front Biosci. 2002 Aug 01;7:a148-62</Citation><ArticleIdList><ArticleId IdType="pubmed">12133807</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Struct Funct Genomics. 2005;6(2-3):103-11</Citation><ArticleIdList><ArticleId IdType="pubmed">16211506</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Annu Rev Cell Dev Biol. 2000;16:591-626</Citation><ArticleIdList><ArticleId IdType="pubmed">11031248</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Trends Cell Biol. 2000 Aug;10(8):335-42</Citation><ArticleIdList><ArticleId IdType="pubmed">10884686</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Struct Funct Genomics. 2004;5(1-2):75-86</Citation><ArticleIdList><ArticleId IdType="pubmed">15263846</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Adv Exp Med Biol. 1993;342:75-9</Citation><ArticleIdList><ArticleId IdType="pubmed">8209774</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2004 Oct 15;279(42):43661-6</Citation><ArticleIdList><ArticleId IdType="pubmed">15304515</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nat Rev Mol Cell Biol. 2001 Mar;2(3):202-10</Citation><ArticleIdList><ArticleId IdType="pubmed">11265250</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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