In vitro and in vivo activity of ML302F: a thioenolate inhibitor of VIM-subfamily metallo β-lactamases-Reference-Cited by-同舟云学术

In vitro and in vivo activity of ML302F: a thioenolate inhibitor of VIM-subfamily metallo β-lactamases

Published:2016 Issue:1 Volume:7 Page:190-193
ISSN:2040-2503
Container-title:MedChemComm
language:en
Short-container-title:Med. Chem. Commun.

Author:

Betts Jonathan W.¹²³⁴⁵,Phee Lynette M.¹²³⁴⁵,Abdul Momin Muhd H. F.¹²³⁴⁵,Umland Klaus-Daniel⁶⁷⁸⁵,Brem Jurgen⁶⁷⁸⁵,Schofield Christopher J.⁶⁷⁸⁵,Wareham David W.¹²³⁴⁵

Affiliation:

1. Antimicrobial Research Group

2. Barts & The London School of Medicine and Dentistry

3. Queen Mary University of London

4. London

5. UK

6. Department of Chemistry

7. University of Oxford

8. Oxford

Abstract

The thioenol ML302F, recently identified as an inhibitor of class B metallo-β-lactamases (MBLs), restores antibiotic susceptibility to meropenem resistant strains in cells and the Galleria mellonella invertebrate model.

Publisher

Royal Society of Chemistry (RSC)

Subject

Pharmaceutical Science,Biochemistry,Drug Discovery,Molecular Medicine,Pharmacology,Organic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/MD/C5MD00380F

Reference16 articles.

1. Proliferation and significance of clinically relevant β-lactamases

2. New β-Lactamase Inhibitors: a Therapeutic Renaissance in an MDR World

3. Metallo-β-lactamase: Inhibitors and reporter substrates

4. T. Spicer , D.Minond , I.Enogieru , S. A.Saldanha , C.Allais , Q.Liu , B. A.Mercer , W. R.Roush and P.Hodder , Probe Reports from the NIH Molecular Libraries Program (US National Center for Biotechnology Information) , 2010

5. Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibition

Cited by 9 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases;Journal of Enzyme Inhibition and Medicinal Chemistry;2024-03-15

2. Medicinal Chemistry of β‐Lactam Antibiotics;Burger's Medicinal Chemistry and Drug Discovery;2021-04-26

3. Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms;Scientific Reports;2020-07-30

4. Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms;2020-03-25

5. Crystal structures of VIM‐1 complexes explain active site heterogeneity in VIM‐class metallo‐β‐lactamases;The FEBS Journal;2018-11-23