Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent.
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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysisBAG-1 modulates the chaperone activity of Hsp70/Hsc70.Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptorInteraction of the Hsp90 cochaperone cyclophilin 40 with Hsc70Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signalingGenetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteinsPerturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasomeThe Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRGrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1The hsp90 chaperone complex regulates intracellular localization of the dioxin receptorp50(cdc37) acting in concert with Hsp90 is required for Raf-1 functionThe ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domainsHsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and traffickingMutational analysis of the hsp70-interacting protein HipChaperoning steroid hormone signaling via reversible acetylation.Anatomy of RISC: how do small RNAs and chaperones activate Argonaute proteins?The 'active life' of Hsp90 complexesA molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperoneSBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteinsContribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90.Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cellsIn vivo analysis of the Hsp90 cochaperone Sti1 (p60)In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone.Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptorDisruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activationThe heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperoneThe Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone systemHop modulates Hsp70/Hsp90 interactions in protein foldingPhase I trial of 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), a heat shock protein inhibitor, administered twice weekly in patients with advanced malignanciesMutations at positions 547-553 of rat glucocorticoid receptors reveal that hsp90 binding requires the presence, but not defined composition, of a seven-amino acid sequence at the amino terminus of the ligand binding domainCharacterization of the molecular-chaperone function of the heat-shock-cognate-70-interacting proteinThe carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactorsCharacterization of functional domains of the eukaryotic co-chaperone HipThe physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agentBacterial lipopolysaccharide induces expression of the stress response genes hop and H411.Evidence that hsp90 is involved in the altered interactions of Acanthamoeba castellanii variants with bacteria.Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex: the roles of heat shock protein 90 (Hsp90) and MEK2.The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.
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P2860
Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Progesterone receptor structur ...... mycin, an hsp90-binding agent.
@ast
Progesterone receptor structur ...... mycin, an hsp90-binding agent.
@en
type
label
Progesterone receptor structur ...... mycin, an hsp90-binding agent.
@ast
Progesterone receptor structur ...... mycin, an hsp90-binding agent.
@en
prefLabel
Progesterone receptor structur ...... mycin, an hsp90-binding agent.
@ast
Progesterone receptor structur ...... mycin, an hsp90-binding agent.
@en
P2093
P2860
P356
P1476
Progesterone receptor structur ...... mycin, an hsp90-binding agent.
@en
P2093
L Whitesell
R A Rimerman
V Prapapanich
P2860
P304
P356
10.1128/MCB.15.12.6804
P407
P577
1995-12-01T00:00:00Z