Identification of covalent inhibitors that disrupt M. tuberculosis growth by targeting multiple serine hydrolases involved in lipid metabolism-Reference-Cited by-同舟云学术

Identification of covalent inhibitors that disrupt M. tuberculosis growth by targeting multiple serine hydrolases involved in lipid metabolism

Published:2021-10 Issue: Volume: Page:
ISSN:2451-9456
Container-title:Cell Chemical Biology
language:en
Short-container-title:Cell Chemical Biology

Author:

Babin Brett M.^ORCID,Keller Laura J.,Pinto Yishay,Li Veronica L.^ORCID,Eneim Andrew S.^ORCID,Vance Summer E.^ORCID,Terrell Stephanie M.,Bhatt Ami S.,Long Jonathan Z.,Bogyo Matthew^ORCID

Publisher

Elsevier BV

Subject

Clinical Biochemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,Biochemistry

Reference54 articles.

1. Click-generated triazole ureas as ultrapotent in vivo-active serine hydrolase inhibitors;Adibekian;Nat. Chem. Biol.,2011

2. The pharmacological landscape and therapeutic potential of serine hydrolases;Bachovchin;Nat. Rev. Drug Discov.,2012

3. Superfamily-wide portrait of serine hydrolase inhibition achieved by library-versus-library screening;Bachovchin;Proc. Natl. Acad. Sci. U S A,2010

4. Distinct bacterial pathways influence the efficacy of antibiotics against Mycobacterium tuberculosis;Bellerose;mSystems,2020

5. Mode of action of tetrahydrolipstatin: a derivative of the naturally occurring lipase inhibitor lipstatin;Borgstrom;Biochim. Biophys. Acta,1988

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