The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
about
Heat shock protein-90-alpha, a prolactin-STAT5 target gene identified in breast cancer cells, is involved in apoptosis regulationCo-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.Regulation of Mutant p53 Protein ExpressionQuality control and fate determination of Hsp90 client proteinsThe yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.A mouse homologue of the Drosophila tumor suppressor l(2)tid gene defines a novel Ras GTPase-activating protein (RasGAP)-binding proteinHeat and heavy metal stress synergize to mediate transcriptional hyperactivation by metal-responsive transcription factor MTF-1A role for Hsc70 in regulating nucleocytoplasmic transport of a temperature-sensitive p53 (p53Val-135)Inhibition of MDM2 by hsp90 contributes to mutant p53 stabilizationPhosphorylation and hsp90 binding mediate heat shock stabilization of p53Substrate-binding characteristics of proteins in the 90 kDa heat shock protein familyGeldanamycin: the prototype of a class of antitumor drugs targeting the heat shock protein 90 family of molecular chaperonesHigh-content, high-throughput analysis of cell cycle perturbations induced by the HSP90 inhibitor XL888Arsenic trioxide reactivates proteasome-dependent degradation of mutant p53 protein in cancer cells in part via enhanced expression of Pirh2 E3 ligaseP53 is transported into the nucleus via an Hsf1-dependent nuclear localization mechanismA novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxinMisfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.Dynamic Interaction of Hsp90 with Its Client Protein p53.Synthetic small interfering RNA targeting heat shock protein 105 induces apoptosis of various cancer cells both in vitro and in vivo.Development of anaplastic lymphoma kinase (ALK) small-molecule inhibitors for cancer therapy.TGF-beta1-induced expression of human Mdm2 correlates with late-stage metastatic breast cancer.Different redox states in malignant and nonmalignant esophageal epithelial cells and differential cytotoxic responses to bile acid and honokiol.Hsp90-Sgt1 and Skp1 target human Mis12 complexes to ensure efficient formation of kinetochore-microtubule binding sites.Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90.Inhibition of NAD(P)H:quinone oxidoreductase 1 activity and induction of p53 degradation by the natural phenolic compound curcumin.p53 Interacts with RNA polymerase II through its core domain and impairs Pol II processivity in vivo.NQO1 stabilizes p53 through a distinct pathway.Strategies for manipulating the p53 pathway in the treatment of human cancer.Chaperones in cell cycle regulation and mitogenic signal transduction: a review.17-N-Allylamino-17-demethoxygeldanamycin induces a diverse response in human acute myelogenous cells.The heat shock protein-90 co-chaperone, Cyclophilin 40, promotes ALK-positive, anaplastic large cell lymphoma viability and its expression is regulated by the NPM-ALK oncoprotein.Hsp70 interactions with the p53 tumour suppressor protein.HSP90 as a new therapeutic target for cancer therapy: the story unfolds.The client protein p53 adopts a molten globule-like state in the presence of Hsp90.Functional inactivation of endogenous MDM2 and CHIP by HSP90 causes aberrant stabilization of mutant p53 in human cancer cellsSAHA shows preferential cytotoxicity in mutant p53 cancer cells by destabilizing mutant p53 through inhibition of the HDAC6-Hsp90 chaperone axis.Mutant p53 - Heat Shock Response Oncogenic Cooperation: A New Mechanism of Cancer Cell Survival.Anaplastic lymphoma kinase proteins in growth control and cancer.Improving survival by exploiting tumour dependence on stabilized mutant p53 for treatmentHSP90: a rising star on the horizon of anticancer targets.
P2860
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P2860
The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
description
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1998
@ast
im März 1998 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1998/03/01)
@sk
vědecký článek publikovaný v roce 1998
@cs
wetenschappelijk artikel (gepubliceerd op 1998/03/01)
@nl
наукова стаття, опублікована в березні 1998
@uk
مقالة علمية (نشرت في مارس 1998)
@ar
name
The physical association of mu ...... amycin, an hsp90-binding agent
@ast
The physical association of mu ...... amycin, an hsp90-binding agent
@en
The physical association of mu ...... amycin, an hsp90-binding agent
@nl
type
label
The physical association of mu ...... amycin, an hsp90-binding agent
@ast
The physical association of mu ...... amycin, an hsp90-binding agent
@en
The physical association of mu ...... amycin, an hsp90-binding agent
@nl
prefLabel
The physical association of mu ...... amycin, an hsp90-binding agent
@ast
The physical association of mu ...... amycin, an hsp90-binding agent
@en
The physical association of mu ...... amycin, an hsp90-binding agent
@nl
P2093
P2860
P356
P1476
The physical association of mu ...... amycin, an hsp90-binding agent
@en
P2093
E. J. Pulcini
J. D. Martinez
L. Whitesell
P. D. Sutphin
P. H. Cook
P2860
P304
P356
10.1128/MCB.18.3.1517
P407
P577
1998-03-01T00:00:00Z