The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
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Mechanisms of CFTR Folding at the Endoplasmic ReticulumMolecular Chaperones as Targets to Circumvent the CFTR Defect in Cystic FibrosisHsp90: a specialized but essential protein-folding toolThe tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulumDab2 is a key regulator of endocytosis and post-endocytic trafficking of the cystic fibrosis transmembrane conductance regulatorCHIP interacts with heat shock factor 1 during heat stressInteraction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradationCHIP controls the sensitivity of transforming growth factor-beta signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradationHuman HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulumRING finger protein RNF207, a novel regulator of cardiac excitationUbiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligaseDeubiquitinases sharpen substrate discrimination during membrane protein degradation from the ERDeletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperoneEndoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligaseRNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membraneCHIP-dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic responseCHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesThe human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulatorSmall glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activityTwo Hsp70 family members expressed in atherosclerotic lesionsCHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcriptionDiversity of degradation signals in the ubiquitin-proteasome systemCytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulumHsp70 chaperones: cellular functions and molecular mechanismOne step at a time: endoplasmic reticulum-associated degradationHistone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradationHSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradationThe PEST sequence does not contribute to the stability of the cystic fibrosis transmembrane conductance regulatorThe nucleotide exchange factors of Hsp70 molecular chaperonesDNAJs: more than substrate delivery to HSPAMolecular chaperones and co-chaperones in Parkinson diseaseMolecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradationMechanisms for quality control of misfolded transmembrane proteinsQuality control and fate determination of Hsp90 client proteinsMechanisms of protein-folding diseases at a glanceRoles for the ubiquitin-proteasome pathway in protein quality control and signaling in the retina: implications in the pathogenesis of age-related macular degenerationThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology
P2860
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P2860
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
@ast
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
@en
type
label
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
@ast
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
@en
prefLabel
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
@ast
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
@en
P2093
P3181
P356
P1433
P1476
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
@en
P2093
P2888
P3181
P356
10.1038/35050509
P407
P577
2001-01-01T00:00:00Z
P5875
P6179
1049531372