(Q44153094)

30 November 2017

title

The influence of ATP and p23 on the conformation of hsp90. (English)

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30 November 2017

William P Sullivan

1

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30 November 2017

Barbara A L Owen

series ordinal

2

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30 November 2017

David O Toft

series ordinal

3

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30 November 2017

language of work or name

English

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publication date

24 September 2002

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Journal of Biological Chemistry

30 November 2017

published in

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30 November 2017

volume

277

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30 November 2017

issue

48

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30 November 2017

page(s)

45942-45948

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Steroid receptor interactions with heat shock protein and immunophilin chaperones

30 November 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Hsp90: a specialized but essential protein-folding tool

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Structure and in vivo function of Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Hsp90: chaperoning signal transduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Mutation of Hip's carboxy-terminal region inhibits a transitional stage of progesterone receptor assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Continuous recycling: a mechanism for modulatory signal transduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

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.M207754200

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.M207754200

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.M207754200

Regulation of heat shock protein 90 ATPase activity by sequences in the carboxyl terminus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

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.M207754200

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.M207754200

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.M207754200

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.M207754200

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.M207754200

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.M207754200

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.M207754200

Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Functional requirement of p23 and Hsp90 in telomerase complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

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.M207754200

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.M207754200

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.M207754200

The assembly of progesterone receptor-hsp90 complexes using purified proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

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.M207754200

Disassembly of transcriptional regulatory complexes by molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

Aluminum fluoride inhibition of glucocorticoid receptor inactivation and transformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207754200

21 January 2018

Identifiers

DOI

10.1074/JBC.M207754200

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30 November 2017

1 reference