(Q40387255)

20 September 2017

title

Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone (English)

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20 September 2017

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Patrick J M Murphy

1

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20 September 2017

Yoshihiro Morishima

2

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20 September 2017

Jeffrey J Kovacs

3

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20 September 2017

Tso-Pang Yao

4

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20 September 2017

William B Pratt

5

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20 September 2017

language of work or name

English

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publication date

8 August 2005

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Journal of Biological Chemistry

20 September 2017

number of pages

8

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based on heuristic

inferred from page(s)

published in

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20 September 2017

volume

280

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20 September 2017

issue

40

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20 September 2017

page(s)

33792-33799

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

20 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M506997200

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Heat shock protein 90 as a molecular target for cancer therapeutics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Histone deacetylase as a new target for cancer chemotherapy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Histone deacetylase inhibitors as new cancer drugs

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

HDAC6 is a microtubule-associated deacetylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Aggresomes, inclusion bodies and protein aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Evidence for glucocorticoid receptor transport on microtubules by dynein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Nuclear protein CBP is a coactivator for the transcription factor CREB

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

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.M506997200

The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

The role of hsp90 in heme-dependent activation of apo-neuronal nitric-oxide synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Neuronal nitric-oxide synthase is regulated by the Hsp90-based chaperone system in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Binding of hsp90 to the glucocorticoid receptor requires a specific 7-amino acid sequence at the amino terminus of the hormone-binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Mutations at positions 547-553 of rat glucocorticoid receptors reveal that hsp90 binding requires the presence, but not defined composition, of a seven-amino acid sequence at the amino terminus of the ligand binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

p23, a simple protein with complex activities

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

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.M506997200

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.M506997200

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.M506997200

The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506997200

21 January 2018

Identifiers

DOI

10.1074/JBC.M506997200

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20 September 2017

1 reference