(Q43670725)

25 November 2017

title

Localization of sites of interaction between p23 and Hsp90 in solution (English)

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25 November 2017

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25 November 2017

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25 November 2017

author name string

Maria A Martinez-Yamout

1

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25 November 2017

Rani P Venkitakrishnan

2

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25 November 2017

Nicholas E Preece

3

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25 November 2017

Gerard Kroon

4

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25 November 2017

language of work or name

English

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publication date

25 March 2006

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Journal of Biological Chemistry

25 November 2017

published in

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25 November 2017

volume

281

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25 November 2017

issue

20

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25 November 2017

page(s)

14457-14464

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Steroid receptor interactions with heat shock protein and immunophilin chaperones

25 November 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M601759200

Hsp90: chaperoning signal transduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Constantly updated knowledge of Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

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.M601759200

Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

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.M601759200

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.M601759200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

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.M601759200

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.M601759200

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.M601759200

The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Rho-modifying C3-like ADP-ribosyltransferases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Hsp90 chaperones protein folding in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Structure, function, and mechanism of the Hsp90 molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Stimulation of the weak ATPase activity of human hsp90 by a client protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

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.M601759200

The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

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.M601759200

An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

The influence of ATP and p23 on the conformation of hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

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.M601759200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Predicting intrinsic disorder from amino acid sequence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

Speeding molecular recognition by using the folding funnel: the fly-casting mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M601759200

21 January 2018

Identifiers

DOI

10.1074/JBC.M601759200

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25 November 2017

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