Structure–Activity Relationship Study Reveals ML240 and ML241 as Potent and Selective Inhibitors of p97 ATPase-Reference-Cited by-同舟云学术

Structure–Activity Relationship Study Reveals ML240 and ML241 as Potent and Selective Inhibitors of p97 ATPase

Published:2013-01-11 Issue:2 Volume:8 Page:297-312
ISSN:1860-7179
Container-title:ChemMedChem
language:en
Short-container-title:ChemMedChem

Author:

Chou Tsui‐Fen¹²,Li Kelin³,Frankowski Kevin J.³,Schoenen Frank J.³,Deshaies Raymond J.¹

Affiliation:

1. Division of Biology and Howard Hughes Medical Institute, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125 (USA)

2. Division of Medical Genetics, Department of Pediatrics, Harbor‐UCLA Medical Center and Los Angeles Biomedical Research Institute, 1124 West Carson Street, Torrance, CA 90502 (USA)

3. University of Kansas Specialized Chemistry Center, 2034 Becker Drive, Structural Biology Center, West Campus, Lawrence, KS 66047 (USA)

Publisher

Wiley

Subject

Organic Chemistry,General Pharmacology, Toxicology and Pharmaceutics,Molecular Medicine,Drug Discovery,Biochemistry,Pharmacology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.201200520

Reference36 articles.

1. Functional profiling of the Saccharomyces cerevisiae genome

2. Targeted deletion of p97 (VCP/CDC48) in mouse results in early embryonic lethality

3. p47 is a cofactor for p97-mediated membrane fusion

4. The Janus Face of the Archaeal Cdc48/p97 Homologue VAT: Protein Folding versus Unfolding

5. An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic golgi fragments

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