Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.
about
Structural and functional characterization of the monomeric U-box domain from E4BInteraction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymesThe tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulumIdentification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arraysDPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradationCHIP controls the sensitivity of transforming growth factor-beta signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradationCytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6The Ras signaling inhibitor LOX-PP interacts with Hsp70 and c-Raf to reduce Erk activation and transformed phenotype of breast cancer cellsRING finger protein RNF207, a novel regulator of cardiac excitationUbiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligaseCYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligasesEndoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligaseHuman Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activityCHIP-dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic responseCHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesInteraction of the Hsp90 cochaperone cyclophilin 40 with Hsc70Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its functionBAG-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 activityHECT and RING finger families of E3 ubiquitin ligases at a glanceCHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcriptionDocking-dependent ubiquitination of the interferon regulatory factor-1 tumor suppressor protein by the ubiquitin ligase CHIPHsp70 chaperones: cellular functions and molecular mechanismRegulation of death-associated protein kinase. Stabilization by HSP90 heterocomplexesAkt and CHIP coregulate tau degradation through coordinated interactionsCHIP promotes Runx2 degradation and negatively regulates osteoblast differentiationHistone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradationCHIP: A new modulator of human malignant disordersInsights into the molecular mechanism of allostery in Hsp70s.Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationTargeting heat shock proteins to modulate α-synuclein toxicityMolecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradationQuality control and fate determination of Hsp90 client proteinsUbiquitin-dependent regulation of Foxp3 and Treg functionTreg functional stability and its responsiveness to the microenvironmentProtein homeostasis at the plasma membraneThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyA genetic screening strategy identifies novel regulators of the proteostasis network
P2860
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P2860
Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Identification of CHIP, a nove ...... regulates chaperone functions
@nl
Identification of CHIP, a nove ...... regulates chaperone functions.
@ast
Identification of CHIP, a nove ...... regulates chaperone functions.
@en
Identification of CHIP, a nove ...... regulates chaperone functions.
@en-gb
type
label
Identification of CHIP, a nove ...... regulates chaperone functions
@nl
Identification of CHIP, a nove ...... regulates chaperone functions.
@ast
Identification of CHIP, a nove ...... regulates chaperone functions.
@en
Identification of CHIP, a nove ...... regulates chaperone functions.
@en-gb
prefLabel
Identification of CHIP, a nove ...... regulates chaperone functions
@nl
Identification of CHIP, a nove ...... regulates chaperone functions.
@ast
Identification of CHIP, a nove ...... regulates chaperone functions.
@en
Identification of CHIP, a nove ...... regulates chaperone functions.
@en-gb
P2093
P2860
P921
P3181
P356
P1476
Identification of CHIP, a nove ...... regulates chaperone functions.
@en
P2093
C A Ballinger
C Patterson
L J Thompson
P2860
P304
P3181
P356
10.1128/MCB.19.6.4535
P407
P577
1999-06-01T00:00:00Z