Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation-Reference-Cited by-同舟云学术

Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation

Published:2015-11-25 Issue:48 Volume:54 Page:7120-7131
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Assimon Victoria A.¹,Southworth Daniel R.¹,Gestwicki Jason E.²

Affiliation:

1. Program in Chemical Biology, University of Michigan, Ann Arbor, Michigan 48109, United States

2. Department of Pharmaceutical Chemistry, University of California at San Francisco, San Francisco, California 94158, United States

Funder

National Institute of Neurological Disorders and Stroke

National Institute of General Medical Sciences

National Institute on Aging

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00801

Reference69 articles.

1. Balance between Folding and Degradation for Hsp90-Dependent Client Proteins: A Key Role for CHIP

2. A Role for a 70-Kilodalton Heat Shock Protein in Lysosomal Degradation of Intracellular Proteins

3. Ubiquitin-dependent Degradation of Certain Protein Substrates in Vitro Requires the Molecular Chaperone Hsc70

4. Molecular Chaperones and Protein Quality Control

5. Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein

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