A Structurally Unique E2-Binding Domain Activates Ubiquitination by the ERAD E2, Ubc7p, through Multiple Mechanisms
about
Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machineE2 enzymes: more than just middle menRecent technical developments in the study of ER-associated degradationEndoplasmic reticulum-mediated protein quality control in ArabidopsisRole of E2-Ub-conjugating enzymes during skeletal muscle atrophyRING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitinationThe cytosolic domain of Pex22p stimulates the Pex4p-dependent ubiquitination of the PTS1-receptor.Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3Cleaning up in the endoplasmic reticulum: ubiquitin in chargeExploring the RING-catalyzed ubiquitin transfer mechanism by MD and QM/MM calculations.Structural and functional insights to ubiquitin-like protein conjugation.The ubiquitin-associated domain of cellular inhibitor of apoptosis proteins facilitates ubiquitylationgp78 elongates of polyubiquitin chains from the distal end through the cooperation of its G2BR and CUE domainsDistinct activation of an E2 ubiquitin-conjugating enzyme by its cognate E3 ligases.Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.Protein quality control at the inner nuclear membraneRING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complexInsights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiaeSpecificity and disease in the ubiquitin systemStructural insights into the catalysis and regulation of E3 ubiquitin ligases.Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Bimolecular Fluorescence Complementation to Assay the Interactions of Ubiquitylation Enzymes in Living Yeast Cells.A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotesThe ubiquitin-conjugating enzyme, UbcM2, is restricted to monoubiquitylation by a two-fold mechanism that involves backside residues of E2 and Lys48 of ubiquitin.The Ubiquitin Ligase (E3) Psh1p Is Required for Proper Segregation of both Centromeric and Two-Micron Plasmids in Saccharomyces cerevisiae.MARCH6 and TRC8 facilitate the quality control of cytosolic and tail-anchored proteins.
P2860
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P2860
A Structurally Unique E2-Binding Domain Activates Ubiquitination by the ERAD E2, Ubc7p, through Multiple Mechanisms
description
2013 nî lūn-bûn
@nan
2013 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@ast
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@en
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@nl
type
label
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@ast
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@en
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@nl
prefLabel
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@ast
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@en
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@nl
P2093
P2860
P3181
P1433
P1476
A Structurally Unique E2-Bindi ...... p, through Multiple Mechanisms
@en
P2093
Allan M Weissman
Jennifer Mariano
Meredith B Metzger
R Andrew Byrd
Ranabir Das
Shengjian Li
Yu-He Liang
Zlatka Kostova
P2860
P304
P3181
P356
10.1016/J.MOLCEL.2013.04.004
P577
2013-05-23T00:00:00Z