Protein–Protein Interactions in the Molecular Chaperone Network-Reference-Cited by-同舟云学术

Protein–Protein Interactions in the Molecular Chaperone Network

Published:2018-04-03 Issue:4 Volume:51 Page:940-949
ISSN:0001-4842
Container-title:Accounts of Chemical Research
language:en
Short-container-title:Acc. Chem. Res.

Author:

Freilich Rebecca¹,Arhar Taylor¹,Abrams Jennifer L.¹,Gestwicki Jason E.¹^ORCID

Affiliation:

1. Department of Pharmaceutical Chemistry and The Institute for Neurodegenerative Disease, University of California—San Francisco, San Francisco, California 94158, United States

Funder

National Institute of Neurological Disorders and Stroke

Publisher

American Chemical Society (ACS)

Subject

General Medicine,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.accounts.8b00036

Reference92 articles.

1. Molecular chaperones in protein folding and proteostasis

2. Binding of Human Nucleotide Exchange Factors to Heat Shock Protein 70 (Hsp70) Generates Functionally Distinct Complexes in Vitro

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

4. Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex

5. Binding of a Small Molecule at a Protein–Protein Interface Regulates the Chaperone Activity of Hsp70–Hsp40

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