Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. - Wikidata - awgldk - TriplyDB

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

http://www.wikidata.org/entity/Q34120745

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Heterozygous yeast deletion collection screens reveal essential targets of Hsp90 Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway.Mechanisms of Hsp90 regulation Purification of bacterial membrane sensor kinases and biophysical methods for determination of their ligand and inhibitor interactions Review: The HSP90 molecular chaperone-an enigmatic ATPase The 'active life' of Hsp90 complexes Features of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinity Functions of the Hsp90 chaperone system: lifting client proteins to new heights Chaperone machines for protein folding, unfolding and disaggregation Ca-Dependent Folding of Human Calumenin The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy Structural Basis for Assembly of Hsp90-Sgt1-CHORD Protein Complexes: Implications for Chaperoning of NLR Innate Immunity Receptors Structural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1 Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae.Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.FKBP12 controls aspartate pathway flux in Saccharomyces cerevisiae to prevent toxic intermediate accumulation.Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine A comparison of Hsp90alpha and Hsp90beta interactions with cochaperones and substrates Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex The SH3 domain of HS1 protein recognizes lysine-rich polyproline motifs.Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: protein structure network modeling CDApps: integrated software for experimental planning and data processing at beamline B23, Diamond Light Source.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.Cdc37 engages in stable, S14A mutation-reinforced association with the most atypical member of the yeast kinome, Cdk-activating kinase (Cak1).ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system.Cell surface Cdc37 participates in extracellular HSP90 mediated cancer cell invasion Structure of an Hsp90-Cdc37-Cdk4 complex.Functional characterization of SbmA, a bacterial inner membrane transporter required for importing the antimicrobial peptide Bac7(1-35).Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.Stability of the human Hsp90-p50Cdc37 chaperone complex against nucleotides and Hsp90 inhibitors, and the influence of phosphorylation by casein kinase 2 Post-translational modifications of Hsp90 and their contributions to chaperone regulation Cdc37 goes beyond Hsp90 and kinases Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90.Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.

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P2860

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

http://www.wikidata.org/entity/Q34120745

description

2002 nî lūn-bûn

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2002 թուականի Մարտին հրատարակուած գիտական յօդուած

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2002 թվականի մարտին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@ast

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@en

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@nl

type

label

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@ast

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@en

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@nl

prefLabel

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@ast

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@en

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

@nl

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P1433

Journal of Biological Chemistry

P1476

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37

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P2093

Barry Panaretou

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Derek N Woolfson

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Giuliano Siligardi

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Peter W Piper

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Shradha Singh

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P2860

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase

Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

Modulation of Akt kinase activity by binding to Hsp90

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase

Cdc37 is required for association of the protein kinase Cdc28 with G1 and mitotic cyclins.

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20151-20159

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P356

10.1074/JBC.M201287200

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P407

P433

23

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P478

277

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P50

Chrisostomos Prodromou

Laurence H Pearl

P577

2002-03-26T00:00:00Z

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P698

11916974

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P921

molecular chaperones