The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically. - Test2 - elhamkhani - TriplyDB

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

http://www.wikidata.org/entity/Q34159497

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Combined analysis of genome-wide association studies for Crohn disease and psoriasis identifies seven shared susceptibility loci Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae Multiple kinases and system robustness: a link between Cdc37 and genome integrity.Post-translational modifications of Hsp90 and their contributions to chaperone regulation Cdc37 goes beyond Hsp90 and kinases Functional specificity of co-chaperone interactions with Hsp90 client proteins.HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis.Hyperactivity and attention deficits in mice with decreased levels of stress-inducible phosphoprotein 1 (STIP1).Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae.Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function.Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.Functional coevolutionary networks of the Hsp70-Hop-Hsp90 system revealed through computational analyses

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P2860

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

http://www.wikidata.org/entity/Q34159497

description

2002 nî lūn-bûn

@nan

2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@ast

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@en

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@nl

type

label

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@ast

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@en

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@nl

prefLabel

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@ast

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@en

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@nl

P1433

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P2860

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P356

P1433

Biological Chemistry

P1476

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.

@en

P2093

Didier Picard

http://www.w3.org/2001/XMLSchema#string

Olivier Donzé

http://www.w3.org/2001/XMLSchema#string

Pierre-André Briand

http://www.w3.org/2001/XMLSchema#string

Toufik Abbas-Terki

http://www.w3.org/2001/XMLSchema#string

P2860

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

Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40

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

The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR

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

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

Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation.

The KIN28 gene is required both for RNA polymerase II mediated transcription and phosphorylation of the Rpb1p CTD.

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

Cdc37 is a molecular chaperone with specific functions in signal transduction.

P304

1335-1342

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P31

scholarly article

P356

10.1515/BC.2002.152

http://www.w3.org/2001/XMLSchema#string

P433

9

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P478

383

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P577

2002-09-01T00:00:00Z

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P698

12437126

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P921

molecular chaperones