(Q28145815)

English

The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system

scientific article (publication date: 10 March 2000)

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scholarly article

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The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system (English)

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protein folding

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molecular chaperones

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author name string

Y Morishima

1

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K C Kanelakis

2

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A M Silverstein

3

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K D Dittmar

4

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L Estrada

5

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W B Pratt

6

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language of work or name

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publication date

10 March 2000

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Journal of Biological Chemistry

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275

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10

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6894-900

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Steroid receptor interactions with heat shock protein and immunophilin chaperones

1 reference

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The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors

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Reconstitution of progesterone receptor with heat shock proteins

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Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain

1 reference

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21 January 2018

Steroid-induced Conformational Changes at Ends of the Hormone-binding Domain in the Rat Glucocorticoid Receptor Are Independent of Agonist Versus Antagonist Activity

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21 January 2018

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

1 reference

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

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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

1 reference

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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

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21 January 2018

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

1 reference

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The assembly of progesterone receptor-hsp90 complexes using purified proteins

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Molecular chaperones in cellular protein folding

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The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

1 reference

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21 January 2018

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

1 reference

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

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21 January 2018

Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70

1 reference

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Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae

1 reference

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21 January 2018

Hop modulates Hsp70/Hsp90 interactions in protein folding

1 reference

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Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

1 reference

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21 January 2018

Mutation of Hip’s Carboxy-Terminal Region Inhibits a Transitional Stage of Progesterone Receptor Assembly

1 reference

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21 January 2018

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

1 reference

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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

1 reference

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21 January 2018

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation

1 reference

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21 January 2018

Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.10.6894

21 January 2018

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.10.6894

21 January 2018

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10.1074/JBC.275.10.6894

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