Expression and purification of SARS coronavirus proteins using SUMO-fusions.
Identifieur interne : 000F92 ( Ncbi/Merge ); précédent : 000F91; suivant : 000F93Expression and purification of SARS coronavirus proteins using SUMO-fusions.
Auteurs : Xun Zuo [États-Unis] ; 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.
Descripteurs français
- KwdFr :
- Cysteine endopeptidases (biosynthèse), Cysteine endopeptidases (génétique), Cysteine endopeptidases (isolement et purification), Escherichia coli (génétique), Expression des gènes (génétique), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (biosynthèse), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (isolement et purification), Histidine (génétique), Peptide hydrolases (métabolisme), Petites protéines modificatrices apparentées à l'ubiquitine (génétique), Protéines de fusion recombinantes (biosynthèse), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines de l'enveloppe virale (biosynthèse), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (isolement et purification), Protéines nucléocapside (biosynthèse), Protéines nucléocapside (génétique), Protéines nucléocapside (isolement et purification), Protéines virales (génétique), Protéines virales (isolement et purification), Protéines virales (métabolisme), Vecteurs génétiques (génétique), Virus du SRAS (génétique).
- MESH :
- biosynthèse : Cysteine endopeptidases, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Protéines nucléocapside.
- génétique : Cysteine endopeptidases, Escherichia coli, Expression des gènes, Glycoprotéines membranaires, Histidine, Petites protéines modificatrices apparentées à l'ubiquitine, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Protéines nucléocapside, Protéines virales, Vecteurs génétiques, Virus du SRAS.
- isolement et purification : Cysteine endopeptidases, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines nucléocapside, Protéines virales.
- métabolisme : Peptide hydrolases, Protéines de fusion recombinantes, Protéines virales.
- Glycoprotéine de spicule des coronavirus.
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 toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002701
- to stream PubMed, to step Curation: 002701
- to stream PubMed, to step Checkpoint: 002711
Links to Exploration step
pubmed:15939295Le document en format XML
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<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="KwdFr" xml:lang="fr"><term>Cysteine endopeptidases (biosynthèse)</term>
<term>Cysteine endopeptidases (génétique)</term>
<term>Cysteine endopeptidases (isolement et purification)</term>
<term>Escherichia coli (génétique)</term>
<term>Expression des gènes (génétique)</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (biosynthèse)</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (isolement et purification)</term>
<term>Histidine (génétique)</term>
<term>Peptide hydrolases (métabolisme)</term>
<term>Petites protéines modificatrices apparentées à l'ubiquitine (génétique)</term>
<term>Protéines de fusion recombinantes (biosynthèse)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines de l'enveloppe virale (biosynthèse)</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (isolement et purification)</term>
<term>Protéines nucléocapside (biosynthèse)</term>
<term>Protéines nucléocapside (génétique)</term>
<term>Protéines nucléocapside (isolement et purification)</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (isolement et purification)</term>
<term>Protéines virales (métabolisme)</term>
<term>Vecteurs génétiques (génétique)</term>
<term>Virus du SRAS (génétique)</term>
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<term>Membrane Glycoproteins</term>
<term>Nucleocapsid Proteins</term>
<term>Recombinant Fusion Proteins</term>
<term>Viral Envelope Proteins</term>
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<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>
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<term>Nucleocapsid Proteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines nucléocapside</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" qualifier="génétique" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Escherichia coli</term>
<term>Expression des gènes</term>
<term>Glycoprotéines membranaires</term>
<term>Histidine</term>
<term>Petites protéines modificatrices apparentées à l'ubiquitine</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines nucléocapside</term>
<term>Protéines virales</term>
<term>Vecteurs génétiques</term>
<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines nucléocapside</term>
<term>Protéines virales</term>
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<term>Recombinant Fusion Proteins</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peptide hydrolases</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Spike Glycoprotein, Coronavirus</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
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<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>
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<DateCompleted><Year>2005</Year>
<Month>12</Month>
<Day>05</Day>
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<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>15</Day>
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<Month>Jul</Month>
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<Title>Protein expression and purification</Title>
<ISOAbbreviation>Protein Expr. Purif.</ISOAbbreviation>
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<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>
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<Author ValidYN="Y"><LastName>Tan</LastName>
<ForeName>Robin</ForeName>
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<Initials>SG</Initials>
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<ForeName>Lubna</ForeName>
<Initials>L</Initials>
</Author>
<Author ValidYN="Y"><LastName>Navas-Martin</LastName>
<ForeName>Sonia</ForeName>
<Initials>S</Initials>
</Author>
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<ForeName>Susan R</ForeName>
<Initials>SR</Initials>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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<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>
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