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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5647
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pubmed:dateCreated |
2003-11-7
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pubmed:abstractText |
Human immunodeficiency virus-1 (HIV-1) Vif is essential for viral evasion of host antiviral factor CEM15/APOBEC3G. We report that Vif interacts with cellular proteins Cul5, elongins B and C, and Rbx1 to form an Skp1-cullin-F-box (SCF)-like complex. The ability of Vif to suppress antiviral activity of APOBEC3G was specifically dependent on Cul5-SCF function, allowing Vif to interact with APOBEC3G and induce its ubiquitination and degradation. A Vif mutant that interacted with APOBEC3G but not with Cul5-SCF was functionally inactive. The Cul5-SCF was also required for Vif function in distantly related simian immunodeficiency virus mac. These results indicate that the conserved Cul5-SCF pathway used by Vif is a potential target for antiviral development.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/APOBEC3G protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cullin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytidine Deaminase,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, vif,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside Deaminases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/elongin,
http://linkedlifedata.com/resource/pubmed/chemical/vif Gene Products, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
7
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pubmed:volume |
302
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1056-60
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:14564014-Animals,
pubmed-meshheading:14564014-Carrier Proteins,
pubmed-meshheading:14564014-Cell Line,
pubmed-meshheading:14564014-Cullin Proteins,
pubmed-meshheading:14564014-Cytidine Deaminase,
pubmed-meshheading:14564014-Gene Products, vif,
pubmed-meshheading:14564014-HIV-1,
pubmed-meshheading:14564014-Humans,
pubmed-meshheading:14564014-Mutation,
pubmed-meshheading:14564014-Nucleoside Deaminases,
pubmed-meshheading:14564014-Proteins,
pubmed-meshheading:14564014-Repressor Proteins,
pubmed-meshheading:14564014-Transcription Factors,
pubmed-meshheading:14564014-Transfection,
pubmed-meshheading:14564014-Ubiquitin,
pubmed-meshheading:14564014-Virus Replication,
pubmed-meshheading:14564014-vif Gene Products, Human Immunodeficiency Virus
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pubmed:year |
2003
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pubmed:articleTitle |
Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.
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pubmed:affiliation |
Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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