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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Binding of aryl hydrocarbon receptor (AhR) to AhR-interacting protein - The role of hsp90Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerasesA structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domainsHsp90 Inhibitors for the Treatment of Chronic Myeloid LeukemiaChaperone ligand-discrimination by the TPR-domain protein Tah1.Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae.The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperoneAttenuation of the activity of the cAMP-specific phosphodiesterase PDE4A5 by interaction with the immunophilin XAP2Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos.Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.To fold or not to fold: modulation and consequences of Hsp90 inhibition.In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90.Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 In vivoDifferential impact of tetratricopeptide repeat proteins on the steroid hormone receptorsThe adaptor protein 14-3-3 binds to the calcium-sensing receptor and attenuates receptor-mediated Rho kinase signalling.Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteinsNeuroimmunophilins: novel neuroprotective and neuroregenerative targets.The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains.Control of glucocorticoid and progesterone receptor subcellular localization by the ligand-binding domain is mediated by distinct interactions with tetratricopeptide repeat proteins.Versatile TPR domains accommodate different modes of target protein recognition and functionRegulation of the Hsp90-binding immunophilin, cyclophilin 40, is mediated by multiple sites for GA-binding protein (GABP).The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress.Binding of the cyclophilin 40 ortholog SQUINT to Hsp90 protein is required for SQUINT function in Arabidopsis.Cyclophilin 40 facilitates HSP90-mediated RISC assembly in plants.Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90Tetratricopeptide repeat cochaperones in steroid receptor complexesNatural product inhibitors of Hsp90: potential leads for drug discoveryCalcineurin inhibition enhances motor neuron survival following injurySGTA: a new player in the molecular co-chaperone game.The biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity.HSP90AB1: Helping the good and the bad.FKBP38 protects Bcl-2 from caspase-dependent degradation.Aryl hydrocarbon (Ah) receptor levels are selectively modulated by hsp90-associated immunophilin homolog XAP2.
P2860
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P2860
The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին 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
The common tetratricopeptide r ...... dimerization domain of Hsp90.
@ast
The common tetratricopeptide r ...... dimerization domain of Hsp90.
@en
type
label
The common tetratricopeptide r ...... dimerization domain of Hsp90.
@ast
The common tetratricopeptide r ...... dimerization domain of Hsp90.
@en
prefLabel
The common tetratricopeptide r ...... dimerization domain of Hsp90.
@ast
The common tetratricopeptide r ...... dimerization domain of Hsp90.
@en
P2093
P2860
P356
P1476
The common tetratricopeptide r ...... dimerization domain of Hsp90.
@en
P2093
P2860
P304
P356
10.1074/JBC.274.5.2682
P407
P577
1999-01-01T00:00:00Z