The acidic tail of the Cdc34 ubiquitin-conjugating enzyme functions in both binding to and catalysis with ubiquitin ligase SCFCdc4.
about
Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8E2 enzymes: more than just middle menA Dual E3 Mechanism for Rub1 Ligation to Cdc53Selective Recruitment of an E2 Ubiquitin Complex by an E3 Ubiquitin LigaseE2s: structurally economical and functionally repletePerilous journey: a tour of the ubiquitin-proteasome systemEssential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrateTwists and turns in ubiquitin-like protein conjugation cascades.Ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase Skp1-cullin-F-box ligase (SCF) interact through multiple conformations.Deconjugation of Nedd8 from Cul1 is directly regulated by Skp1-F-box and substrate, and the COP9 signalosome inhibits deneddylated SCF by a noncatalytic mechanism.Regulation of lipid droplet and membrane biogenesis by the acidic tail of the phosphatidate phosphatase Pah1p.Molecular and structural insight into lysine selection on substrate and ubiquitin lysine 48 by the ubiquitin-conjugating enzyme Cdc34Multimodal mechanism of action for the Cdc34 acidic loop: a case study for why ubiquitin-conjugating enzymes have loops and tailsThe San1 Ubiquitin Ligase Functions Preferentially with Ubiquitin-conjugating Enzyme Ubc1 during Protein Quality Control.The ubiquitin-conjugating enzyme, UbcM2, is restricted to monoubiquitylation by a two-fold mechanism that involves backside residues of E2 and Lys48 of ubiquitin.The loop-less tmCdc34 E2 mutant defective in polyubiquitination in vitro and in vivo supports yeast growth in a manner dependent on Ubp14 and Cka2.Conformational Dynamics and Allostery in E2:E3 Interactions Drive Ubiquitination: gp78 and Ube2g2.
P2860
Q24299638-EBE89A57-0262-4B2E-855B-50727F52943AQ26752818-15EB77D7-D719-45E0-9000-F961E2306355Q27664416-588C8E9A-D5F4-4A9C-AB85-1930B9CD754BQ27678117-A7FA0463-7B64-4607-8295-64713A4F837BQ28301074-EFCCE40B-2D35-4120-975A-2E3F372FE884Q28306492-C54B6C8B-384C-4874-B762-782879ADF513Q28740322-F56DA327-78CE-4478-BC6F-778FFA68B5AEQ34225698-94C5CA8D-C780-479E-BDAB-9A971F00447EQ34958467-5DF7EC60-3F1F-41AC-B2F3-4E4616CC5BD4Q36216079-B059C32B-C0B1-45C7-A2C5-B58F2A8B0C8CQ36961102-51AB7CF7-F597-4A3A-BCB1-2807443ED7C3Q37018242-C9661C80-7C43-4078-AC36-EED53BA08468Q37349016-1673CD81-A6EE-4198-AE4B-08811F61FD7EQ41002609-44EF09E6-CF70-4576-A0E9-B5D7D2B0BA15Q41277138-4682B46D-DDDC-4107-8C8F-DEC3CE853ED0Q42720645-6BEF01CF-4691-464A-8C51-348F1D6E4F71Q55082402-B0A50C0F-D0A6-40B7-BA8B-462FA79F8A91
P2860
The acidic tail of the Cdc34 ubiquitin-conjugating enzyme functions in both binding to and catalysis with ubiquitin ligase SCFCdc4.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 29 October 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The acidic tail of the Cdc34 u ...... with ubiquitin ligase SCFCdc4.
@en
The acidic tail of the Cdc34 u ...... with ubiquitin ligase SCFCdc4.
@nl
type
label
The acidic tail of the Cdc34 u ...... with ubiquitin ligase SCFCdc4.
@en
The acidic tail of the Cdc34 u ...... with ubiquitin ligase SCFCdc4.
@nl
prefLabel
The acidic tail of the Cdc34 u ...... with ubiquitin ligase SCFCdc4.
@en
The acidic tail of the Cdc34 u ...... with ubiquitin ligase SCFCdc4.
@nl
P2093
P2860
P356
P1476
The acidic tail of the Cdc34 u ...... with ubiquitin ligase SCFCdc4.
@en
P2093
Dane A Mohl
Gary Kleiger
Raymond J Deshaies
P2860
P304
36012-36023
P356
10.1074/JBC.M109.058529
P407
P577
2009-10-29T00:00:00Z