Nucleotide-Free sB-Raf is Preferentially Bound by Hsp90 and Cdc37 In Vitro-Reference-Cited by-同舟云学术

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Nucleotide-Free sB-Raf is Preferentially Bound by Hsp90 and Cdc37 In Vitro

Published:2016-10 Issue:20 Volume:428 Page:4185-4196
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Eckl Julia M.,Daake Marina,Schwartz Sebastian,Richter Klaus

Funder

Deutsche Forschungsgemeinschaft

Center for integrated protein science CIPSM

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference47 articles.

1. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase;Nathan;Mol. Cell. Biol.,1995

2. Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition;Taipale;Cell,2012

3. Hsp70 and Hsp90—a relay team for protein folding;Wegele;Rev. Physiol. Biochem. Pharmacol.,2004

4. Stimulation of the weak ATPase activity of human hsp90 by a client protein;McLaughlin;J. Mol. Biol.,2002

5. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation;Grenert;J. Biol. Chem.,1997

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1. Hsp90: From Cellular to Organismal Proteostasis;Cells;2022-08-10

2. HSP-90/kinase complexes are stabilized by the large PPIase FKB-6;Scientific Reports;2021-06-11

3. Structure, Function, and Regulation of the Hsp90 Machinery;Cold Spring Harbor Perspectives in Biology;2019-02-11

4. Regulation of the Hsp90 system;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2018-06

5. Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains;PLOS ONE;2017-12-21

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