Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. (Q34120745)

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8 December 2019

title

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

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8 December 2019

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Chrisostomos Prodromou

8

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8 December 2019

Philippe Meyer

3

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8 December 2019

Laurence Pearl

7

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8 December 2019

author name string

Giuliano Siligardi

1

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8 December 2019

Barry Panaretou

2

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8 December 2019

Shradha Singh

4

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8 December 2019

Derek N Woolfson

5

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8 December 2019

Peter W Piper

6

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8 December 2019

language of work or name

English

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publication date

26 March 2002

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Journal of Biological Chemistry

8 December 2019

published in

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8 December 2019

volume

277

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8 December 2019

issue

23

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8 December 2019

page(s)

20151-20159

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Structure, function, and mechanism of the Hsp90 molecular chaperone

8 December 2019

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M201287200

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M201287200

Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M201287200

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Hop modulates Hsp70/Hsp90 interactions in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

A 50 kilodalton protein associated with raf and pp60(v-src) protein kinases is a mammalian homolog of the cell cycle control protein cdc37.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Cdc37: a protein kinase chaperone?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Chaperones in progesterone receptor complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Cdc37 promotes the stability of protein kinases Cdc28 and Cak1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Modulation of Akt kinase activity by binding to Hsp90

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex: the roles of heat shock protein 90 (Hsp90) and MEK2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201287200

21 January 2018

Identifiers

DOI

10.1074/JBC.M201287200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11916974%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

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