(Q28248831)

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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

scientific article published on September 19, 1997

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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 (English)

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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 (English)

1 reference

10.1074/JBC.272.38.23843

https://api.crossref.org/works/10.1074/JBC.272.38.23843

15 November 2024

11

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L M Neckers

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Edward G Mimnaugh

6

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E Mimnaugh

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Theodor W Schulte

9

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T W Schulte

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author name string

J. P. Grenert

1

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9295332

15 November 2024

W. P. Sullivan

2

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9295332

15 November 2024

P. Fadden

3

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15 November 2024

T. A. Haystead

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Europe PubMed Central

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15 November 2024

J. Clark

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15 November 2024

E. Mimnaugh

6

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Europe PubMed Central

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15 November 2024

H. Krutzsch

7

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15 November 2024

H. J. Ochel

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15 November 2024

E. Sausville

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Europe PubMed Central

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15 November 2024

L. M. Neckers

11

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9295332

15 November 2024

D. O. Toft

12

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9295332

15 November 2024

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19 September 1997

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http://www.jbc.org/content/272/38/23843.full.pdf

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9295332

15 November 2024

https://api.elsevier.com/content/article/PII:S0021925819658643?httpAccept=text/xml

1 reference

10.1074/JBC.272.38.23843

https://api.crossref.org/works/10.1074/JBC.272.38.23843

15 November 2024

https://api.elsevier.com/content/article/PII:S0021925819658643?httpAccept=text/plain

1 reference

10.1074/JBC.272.38.23843

https://api.crossref.org/works/10.1074/JBC.272.38.23843

15 November 2024

https://syndication.highwire.org/content/doi/10.1074/jbc.272.38.23843

1 reference

10.1074/JBC.272.38.23843

https://api.crossref.org/works/10.1074/JBC.272.38.23843

15 November 2024

Journal of Biological Chemistry

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272

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38

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23843-50

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The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase

2

1 reference

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Cell cycle-dependent association of Gag-Mil and hsp90.

4

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Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras Association

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Nerve Growth Factor-mediated Activation of the Mitogen-activated Protein (MAP) Kinase Cascade Involves a Signaling Complex Containing B-Raf and HSP90

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Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function

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p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2.

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A role for Hsp90 in retinoid receptor signal transduction

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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

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Endocrine Reviews

13

18

306

author name string

Pratt

publication date

1997

1 reference

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The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.

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Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

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A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

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Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase

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Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation

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Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

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Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate

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

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Depletion of p185erbB2, Raf-1 and mutant p53 proteins by geldanamycin derivatives correlates with antiproliferative activity

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Assessment of the ATP binding properties of Hsp90.

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

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