Structure of a RING E3 Trapped in Action Reveals Ligation Mechanism for the Ubiquitin-like Protein NEDD8-Reference-Cited by-同舟云学术

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Structure of a RING E3 Trapped in Action Reveals Ligation Mechanism for the Ubiquitin-like Protein NEDD8

Published:2014-06 Issue:7 Volume:157 Page:1671-1684
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Scott Daniel C.,Sviderskiy Vladislav O.,Monda Julie K.,Lydeard John R.,Cho Shein Ei,Harper J. Wade,Schulman Brenda A.

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference77 articles.

1. Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery;Angers;Nature,2006

2. A conserved asparagine has a structural role in ubiquitin-conjugating enzymes;Berndsen;Nat. Chem. Biol.,2013

3. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1;Bernier-Villamor;Cell,2002

4. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases;Calabrese;Nat. Struct. Mol. Biol.,2011

5. The human Cdc34 carboxyl terminus contains a non-covalent ubiquitin binding activity that contributes to SCF-dependent ubiquitination;Choi;J. Biol. Chem.,2010

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