(Q38310098)

2 September 2017

Hsp90 chaperone activity requires the full-length protein and interaction among its multiple domains (English)

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2 September 2017

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Johnson BD

1

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2 September 2017

Chadli A

2

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2 September 2017

Felts SJ

3

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2 September 2017

Bouhouche I

4

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2 September 2017

Catelli MG

5

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2 September 2017

Toft DO

6

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2 September 2017

language of work or name

English

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publication date

1 October 2000

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Journal of Biological Chemistry

2 September 2017

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2 September 2017

275

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2 September 2017

32499-32507

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2 September 2017

42

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2 September 2017

The heat-shock proteins

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https://api.crossref.org/works/10.1074%2FJBC.M005195200

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

Hsp90 & Co. - a holding for folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

ATP sensitive tryptophans of hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

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.M005195200

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.M005195200

ATP-binding properties of human Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

Hop modulates Hsp70/Hsp90 interactions in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

Steroid receptor interactions with heat shock protein and immunophilin chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

The assembly of progesterone receptor-hsp90 complexes using purified proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

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.M005195200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

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.M005195200

Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

The steroid binding domain influences intracellular solubility of the baculovirus overexpressed glucocorticoid and mineralocorticoid receptors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

The charged region of Hsp90 modulates the function of the N-terminal domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

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.M005195200

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.M005195200

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.M005195200

Mechanism of dimer formation of the 90-kDa heat-shock protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

Structure and in vivo function of Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005195200

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.M005195200

21 January 2018

Identifiers

DOI

10.1074/JBC.M005195200

1 reference

2 September 2017

1 reference