The ubiquitin ligase Hul5 promotes proteasomal processivity.
about
Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationMolecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradationProtein quality control in the nucleusEndoplasmic Reticulum-associated Degradation of Pca1p, a Polytopic Protein, via Interaction with the Proteasome at the MembraneGeneration of free ubiquitin chains is up-regulated in stress and facilitated by the HECT domain ubiquitin ligases UFD4 and HUL5.Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress.Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress responseLiganded ERα Stimulates the E3 Ubiquitin Ligase Activity of UBE3C to Facilitate Cell Proliferation.Paradigms of protein degradation by the proteasome.Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization.Gates, Channels, and Switches: Elements of the Proteasome MachineUbp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome.Isoform-specific SCF(Fbw7) ubiquitination mediates differential regulation of PGC-1α.Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes.The ubiquitin-proteasome system of Saccharomyces cerevisiae.The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates.Context-dependent resistance to proteolysis of intrinsically disordered proteins.Hul5 ubiquitin ligase: good riddance to bad proteinsThe evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.The Logic of the 26S Proteasome.Repair or destruction-an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasisIncomplete proteasomal degradation of green fluorescent proteins in the context of tandem fluorescent protein timers.Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteinsLoss of malin, but not laforin, results in compromised autophagic flux and proteasomal dysfunction in cells exposed to heat shock.Ubiquitinated proteins promote the association of proteasomes with the deubiquitinating enzyme Usp14 and the ubiquitin ligase Ube3c.MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins in Arabidopsis thaliana.
P2860
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P2860
The ubiquitin ligase Hul5 promotes proteasomal processivity.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
The ubiquitin ligase Hul5 promotes proteasomal processivity.
@en
The ubiquitin ligase Hul5 promotes proteasomal processivity.
@nl
type
label
The ubiquitin ligase Hul5 promotes proteasomal processivity.
@en
The ubiquitin ligase Hul5 promotes proteasomal processivity.
@nl
prefLabel
The ubiquitin ligase Hul5 promotes proteasomal processivity.
@en
The ubiquitin ligase Hul5 promotes proteasomal processivity.
@nl
P2860
P356
P1476
The ubiquitin ligase Hul5 promotes proteasomal processivity.
@en
P2093
Daniel Kornitzer
Sharon Aviram
P2860
P304
P356
10.1128/MCB.00909-09
P407
P577
2009-12-14T00:00:00Z