(Q28142898)

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The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor

scientific article (publication date: 21 July 2000)

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The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor (English)

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T Rajapandi

1

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L E Greene

series ordinal

2

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E Eisenberg

series ordinal

3

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language of work or name

English

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publication date

21 July 2000

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published in

Journal of Biological Chemistry

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volume

275

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page(s)

22597-604

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issue

29

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cites work

Steroid receptor interactions with heat shock protein and immunophilin chaperones

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Reconstitution of the steroid receptor.hsp90 heterocomplex assembly system of rabbit reticulocyte lysate.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

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

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

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.

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex.

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Hop modulates Hsp70/Hsp90 interactions in protein folding

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Optimal ligand binding by the recombinant human glucocorticoid receptor and assembly of the receptor complex with heat shock protein 90 correlate with high intracellular ATP levels in Spodoptera frugiperda cells

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

The assembly of progesterone receptor-hsp90 complexes using purified proteins

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

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

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor-hsp90 Heterocomplex Assembly

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Characterization of D10S and K71E mutants of human cytosolic hsp70

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Nucleotides and two functional states of hsp90

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.M002035200

retrieved

21 January 2018

Identifiers

DOI

10.1074/JBC.M002035200

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Fatcat ID

release_e2kwgkquendv3bd2mmscz3uf7u

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https://api.fatcat.wiki/v0/release/e2kwgkquendv3bd2mmscz3uf7u

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24 November 2022

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PubMed ID

10781595

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(Q28142898)

The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor

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