Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle (Q45091596)

9 December 2017

title

Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle (English)

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9 December 2017

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5

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9 December 2017

Chrisostomos Prodromou

6

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9 December 2017

Giuliano Siligardi

1

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9 December 2017

Bin Hu

2

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9 December 2017

Barry Panaretou

3

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9 December 2017

Peter W Piper

4

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9 December 2017

language of work or name

English

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publication date

2 October 2004

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Journal of Biological Chemistry

9 December 2017

published in

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9 December 2017

volume

279

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9 December 2017

issue

50

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9 December 2017

page(s)

51989-51998

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Heat-shock protein 90, a chaperone for folding and regulation

9 December 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M410562200

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Structure and functional relationships of Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

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.M410562200

An atypical topoisomerase II from Archaea with implications for meiotic recombination

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Crystal structure of an N-terminal fragment of the DNA gyrase B protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

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.M410562200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Crystal structure of an Xrcc4-DNA ligase IV complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

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.M410562200

p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M410562200

21 January 2018

Identifiers

DOI

10.1074/JBC.M410562200

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9 December 2017

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