Literature DB >> 19013629

Manipulation of the ubiquitin-proteasome pathway by small DNA tumor viruses.

Paola Blanchette1, Philip E Branton.   

Abstract

Viruses have evolved to use cellular pathways to their advantage, including the ubiquitin-proteasome pathway of protein degradation. In several cases, viruses produce proteins that highjack cellular E3 ligases to modify their substrate specificity in order to eliminate unwanted cellular proteins, in particular inhibitors of the cell cycle. They can also inhibit E3 ligase to prevent specific protein degradation or even use the system to control the level of expression of their own proteins. In this review we explore the specific ways that small DNA tumor viruses exploit the ubiquitin-proteasome pathway for their own benefit.

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Year:  2008        PMID: 19013629     DOI: 10.1016/j.virol.2008.10.005

Source DB:  PubMed          Journal:  Virology        ISSN: 0042-6822            Impact factor:   3.616


  44 in total

1.  Transformation by E1A oncoprotein involves ubiquitin-mediated proteolysis of the neuronal and tumor repressor REST in the nucleus.

Authors:  Hancheng Guan; Robert P Ricciardi
Journal:  J Virol       Date:  2012-03-14       Impact factor: 5.103

2.  The adenovirus E1b55K/E4orf6 complex induces degradation of the Bloom helicase during infection.

Authors:  Nicole I Orazio; Colleen M Naeger; Jan Karlseder; Matthew D Weitzman
Journal:  J Virol       Date:  2010-12-01       Impact factor: 5.103

3.  Human cytomegalovirus UL76 elicits novel aggresome formation via interaction with S5a of the ubiquitin proteasome system.

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Journal:  J Virol       Date:  2013-08-21       Impact factor: 5.103

4.  HIV-1 Vpr induces the K48-linked polyubiquitination and proteasomal degradation of target cellular proteins to activate ATR and promote G2 arrest.

Authors:  Jean-Philippe Belzile; Jonathan Richard; Nicole Rougeau; Yong Xiao; Eric A Cohen
Journal:  J Virol       Date:  2010-01-20       Impact factor: 5.103

5.  A proteomic approach to identify candidate substrates of human adenovirus E4orf6-E1B55K and other viral cullin-based E3 ubiquitin ligases.

Authors:  Frédéric Dallaire; Paola Blanchette; Philip E Branton
Journal:  J Virol       Date:  2009-09-16       Impact factor: 5.103

6.  Analysis of the Cullin binding sites of the E4orf6 proteins of human adenovirus E3 ubiquitin ligases.

Authors:  Timra Gilson; Chi Ying Cheng; Woosuk Steve Hur; Paola Blanchette; Philip E Branton
Journal:  J Virol       Date:  2014-01-22       Impact factor: 5.103

7.  Proteomic analysis of ubiquitin-like posttranslational modifications induced by the adenovirus E4-ORF3 protein.

Authors:  Sook-Young Sohn; Rebecca G Bridges; Patrick Hearing
Journal:  J Virol       Date:  2014-11-19       Impact factor: 5.103

8.  Role of E1B55K in E4orf6/E1B55K E3 ligase complexes formed by different human adenovirus serotypes.

Authors:  Chi Ying Cheng; Timra Gilson; Peter Wimmer; Sabrina Schreiner; Gary Ketner; Thomas Dobner; Philip E Branton; Paola Blanchette
Journal:  J Virol       Date:  2013-03-27       Impact factor: 5.103

9.  Aggresome formation by the adenoviral protein E1B55K is not conserved among adenovirus species and is not required for efficient degradation of nuclear substrates.

Authors:  Paola Blanchette; Peter Wimmer; Frédéric Dallaire; Chi Ying Cheng; Philip E Branton
Journal:  J Virol       Date:  2013-02-13       Impact factor: 5.103

10.  The myxoma virus m-t5 ankyrin repeat host range protein is a novel adaptor that coordinately links the cellular signaling pathways mediated by Akt and Skp1 in virus-infected cells.

Authors:  Steven J Werden; Jerry Lanchbury; Donna Shattuck; Chris Neff; Max Dufford; Grant McFadden
Journal:  J Virol       Date:  2009-09-23       Impact factor: 5.103

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