Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
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Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylationA Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?Biochemical and Proteomic Analysis of Ubiquitination of Hsc70 and Hsp70 by the E3 Ligase CHIPCotargeting HSP90 and Its Client Proteins for Treatment of Prostate Cancer.17-Allylamino-17-demethoxygeldanamycin induces downregulation of critical Hsp90 protein clients and results in cell cycle arrest and apoptosis of human urinary bladder cancer cellsHaploinsufficiency of the E3 ubiquitin ligase C-terminus of heat shock cognate 70 interacting protein (CHIP) produces specific behavioral impairments.Ubiquitin-associated (UBA) domain in human Fas associated factor 1 inhibits tumor formation by promoting Hsp70 degradationQuality control for unfolded proteins at the plasma membrane.Polyubiquitin linkage profiles in three models of proteolytic stress suggest the etiology of Alzheimer disease.Pnck induces ligand-independent EGFR degradation by probable perturbation of the Hsp90 chaperone complex.Human liver cytochrome P450 3A4 ubiquitination: molecular recognition by UBC7-gp78 autocrine motility factor receptor and UbcH5a-CHIP-Hsc70-Hsp40 E2-E3 ubiquitin ligase complexesA bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteinsTumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.OLA1 protects cells in heat shock by stabilizing HSP70.Proteomic identification of protein ubiquitination events.Ubiquibodies, synthetic E3 ubiquitin ligases endowed with unnatural substrate specificity for targeted protein silencingStability of the cancer target DDIAS is regulated by the CHIP/HSP70 pathway in lung cancer cells.Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code.Chaperoning proteins for destruction: diverse roles of Hsp70 chaperones and their co-chaperones in targeting misfolded proteins to the proteasomeHeat-shock protein 90 (Hsp90) as anticancer target for drug discovery: an ample computational perspective.Deacetylation of HSPA5 by HDAC6 leads to GP78-mediated HSPA5 ubiquitination at K447 and suppresses metastasis of breast cancer.The Evolutionarily Conserved E3 Ubiquitin Ligase AtCHIP Contributes to Plant Immunity.Centrosomes at M phase act as a scaffold for the accumulation of intracellular ubiquitinated proteins.Carboxy terminus of heat shock protein (HSP) 70-interacting protein (CHIP) inhibits HSP70 in the heart.Diverse Regulation of the CreA Carbon Catabolite Repressor in Aspergillus nidulans.Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.CHIP/Stub1 regulates the Warburg effect by promoting degradation of PKM2 in ovarian carcinoma.The HSP90 chaperone machinery.UBXN2A enhances CHIP-mediated proteasomal degradation of oncoprotein mortalin-2 in cancer cells
P2860
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P2860
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
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
name
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@ast
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@en
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@nl
type
label
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@ast
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@en
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@nl
prefLabel
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@ast
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@en
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@nl
P2860
P1476
Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP
@en
P2093
Lenka Kundrat
P2860
P304
P356
10.1016/J.JMB.2009.11.017
P407
P50
P577
2009-11-12T00:00:00Z