Competitive Activity-Based Protein Profiling Identifies Aza-β-Lactams as a Versatile Chemotype for Serine Hydrolase Inhibition-Reference-Cited by-同舟云学术

Competitive Activity-Based Protein Profiling Identifies Aza-β-Lactams as a Versatile Chemotype for Serine Hydrolase Inhibition

Published:2012-03-08 Issue:11 Volume:134 Page:5068-5071
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Zuhl Andrea M.¹,Mohr Justin T.²,Bachovchin Daniel A.¹,Niessen Sherry¹,Hsu Ku-Lung¹,Berlin Jacob M.²,Dochnahl Maximilian²,López-Alberca María P.²,Fu Gregory C.²,Cravatt Benjamin F.¹

Affiliation:

1. The Skaggs Institute for Chemical Biology and Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States

2. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja300799t

Reference21 articles.

1. The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease

2. The pharmacological landscape and therapeutic potential of serine hydrolases

3. Acylating drugs: redesigning natural covalent inhibitors

4. β-Lactones as Privileged Structures for the Active-Site Labeling of Versatile Bacterial Enzyme Classes

5. Superfamily-wide portrait of serine hydrolase inhibition achieved by library-versus-library screening

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