Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine-Reference-Cited by-同舟云学术

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Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine

Published:2013-08-13 Issue:18 Volume:32 Page:2504-2516
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Das Ranabir,Liang Yu-He,Mariano Jennifer,Li Jess,Huang Tao,King Aaren,Tarasov Sergey G,Weissman Allan M,Ji Xinhua,Byrd R Andrew

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference37 articles.

1. Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)

2. A UbcH5/Ubiquitin Noncovalent Complex Is Required for Processive BRCA1-Directed Ubiquitination

3. The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

4. Allosteric Activation of E2-RING Finger-Mediated Ubiquitylation by a Structurally Defined Specific E2-Binding Region of gp78

5. The HADDOCK web server for data-driven biomolecular docking

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