The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation-Reference-Cited by-同舟云学术

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

Published:1997-09 Issue:38 Volume:272 Page:23843-23850
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Grenert James P.,Sullivan William P.,Fadden Patrick,Haystead Timothy A.J.,Clark Jenny,Mimnaugh Edward,Krutzsch Henry,Ochel Hans-Joachim,Schulte Theodor W.,Sausville Edward,Neckers Leonard M.,Toft David O.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference57 articles.

1. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system.

2. 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

3. The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex.

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

5. 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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