Closing In on the Hsp90 Chaperone-Client Relationship
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference11 articles.
1. Bacterial Hsp90 - desperately seeking clients
2. Structural Organization of Procaryotic and Eucaryotic Hsp90. INFLUENCE OF DIVALENT CATIONS ON STRUCTURE AND FUNCTION
3. Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle
4. Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von Heijne
5. Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity
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1. Regulation of the Extracellular Matrix by Heat Shock Proteins and Molecular Chaperones;Heat Shock Proteins in the Immune System;2018
2. Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop;Nature Communications;2014-11-19
3. Interaction of Heat Shock Protein 90 and the Co-chaperone Cpr6 with Ura2, a Bifunctional Enzyme Required for Pyrimidine Biosynthesis;Journal of Biological Chemistry;2013-09
4. Genome-scale Co-evolutionary Inference Identifies Functions and Clients of Bacterial Hsp90;PLoS Genetics;2013-07-11
5. Heat shock protein 90AB1 and hyperthermia rescue infectivity of HIV with defective cores;Virology;2013-02
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