(Q40585096)

21 September 2017

Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90. (English)

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21 September 2017

5

F Ulrich Hartl

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21 September 2017

4

Florian Holsboer

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21 September 2017

Gabriela M Wochnik

1

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21 September 2017

Jason C Young

series ordinal

2

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21 September 2017

Ulrike Schmidt

series ordinal

3

1 reference

21 September 2017

Theo Rein

series ordinal

6

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21 September 2017

language of work or name

English

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publication date

1 February 2004

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21 September 2017

4

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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21 September 2017

560

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21 September 2017

1-3

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21 September 2017

35-38

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Molecular chaperones in the cytosol: from nascent chain to folded protein

21 September 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Hsp90 & Co. - a holding for folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Hsp90: a specialized but essential protein-folding tool

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

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/10.1016%2FS0014-5793%2804%2900066-3

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/10.1016%2FS0014-5793%2804%2900066-3

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/10.1016%2FS0014-5793%2804%2900066-3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Disassembly of transcriptional regulatory complexes by molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Essential role of the unusual DNA-binding motif of BAG-1 for inhibition of the glucocorticoid receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

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/10.1016%2FS0014-5793%2804%2900066-3

Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Recruitment of chromatin remodelling factors during gene activation via the glucocorticoid receptor N-terminal domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Colocalization of DNA-binding and transcriptional activation functions in the human glucocorticoid receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Nucleotides and two functional states of hsp90

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Chaperone function of Hsp90-associated proteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2804%2900066-3

10.1016/S0014-5793(04)00066-3

7 January 2021

Identifiers

DOI

1 reference

21 September 2017

1 reference