CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein.
about
DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3CHIP interacts with heat shock factor 1 during heat stressCHIP controls the sensitivity of transforming growth factor-beta signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradationA novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomesUbiquitylation 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 ligasesCHIP-dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic responseBAG-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 regulatorCHIP 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 CHIPDiversity of degradation signals in the ubiquitin-proteasome systemCHIP promotes Runx2 degradation and negatively regulates osteoblast differentiationHistone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradationThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemHSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradationDorfin localizes to the ubiquitylated inclusions in Parkinson's disease, dementia with Lewy bodies, multiple system atrophy, and amyotrophic lateral sclerosisGaleterone for the treatment of advanced prostate cancer: the evidence to dateCHIP: A new modulator of human malignant disordersSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationQuality control and fate determination of Hsp90 client proteinsHeat shock proteins at the crossroads between cancer and Alzheimer's diseaseRoles for the ubiquitin-proteasome pathway in protein quality control and signaling in the retina: implications in the pathogenesis of age-related macular degenerationProtein Oxidation in Aging: Does It Play a Role in Aging Progression?Structural insights into the U-box, a domain associated with multi-ubiquitinationInteractions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymesINSIG: a broadly conserved transmembrane chaperone for sterol-sensing domain proteinsA Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survivalErbB2 degradation mediated by the co-chaperone protein CHIPAn androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP)The structural basis of XRCC1-mediated DNA repairBiochemical and Proteomic Analysis of Ubiquitination of Hsc70 and Hsp70 by the E3 Ligase CHIPRegulation of the cytoplasmic quality control protein degradation pathway by BAG2A proteomic snapshot of the human heat shock protein 90 interactomeCHIP has a protective role against oxidative stress-induced cell death through specific regulation of endonuclease GCHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stabilitySTUB1/CHIP is required for HIF1A degradation by chaperone-mediated autophagy
P2860
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P2860
CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein.
description
2001 nî lūn-bûn
@nan
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
2001年论文
@zh
2001年论文
@zh-cn
name
CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein.
@en
type
label
CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein.
@en
prefLabel
CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein.
@en
P2093
P2860
P356
P1433
P1476
CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein.
@en
P2093
P2860
P304
P356
10.1093/EMBO-REPORTS/KVE246
P577
2001-11-21T00:00:00Z