Literature DB >> 23859206

Targeting metallo-β-lactamase enzymes in antibiotic resistance.

Dustin T King1, Natalie C J Strynadka.   

Abstract

The β-lactam antibiotics are essential for the treatment of a wide range of human bacterial diseases. However, a class of zinc-dependent hydrolases known as the metallo-β-lactamase (MBL) can confer bacteria with extended spectrum β-lactam resistance. To date, there are no clinically approved MBL inhibitors, making these enzymes a serious threat to human health. In this review, a structural approach is taken to outline some of the more promising MBL inhibitors and shed light on how the resistance conferred by this emerging class of enzymes may be circumvented in the future.

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Year:  2013        PMID: 23859206     DOI: 10.4155/fmc.13.55

Source DB:  PubMed          Journal:  Future Med Chem        ISSN: 1756-8919            Impact factor:   3.808


  17 in total

1.  Identification and Characterization of the Sulfazecin Monobactam Biosynthetic Gene Cluster.

Authors:  Rongfeng Li; Ryan A Oliver; Craig A Townsend
Journal:  Cell Chem Biol       Date:  2016-12-22       Impact factor: 8.116

Review 2.  Fragment-based inhibitor discovery against β-lactamase.

Authors:  Derek A Nichols; Adam R Renslo; Yu Chen
Journal:  Future Med Chem       Date:  2014-03       Impact factor: 3.808

3.  Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopy.

Authors:  Mahesh Aitha; Lindsay Moritz; Indra D Sahu; Omar Sanyurah; Zahilyn Roche; Robert McCarrick; Gary A Lorigan; Brian Bennett; Michael W Crowder
Journal:  J Biol Inorg Chem       Date:  2015-02-10       Impact factor: 3.358

Review 4.  B1-Metallo-β-Lactamases: Where Do We Stand?

Authors:  Maria F Mojica; Robert A Bonomo; Walter Fast
Journal:  Curr Drug Targets       Date:  2016       Impact factor: 3.465

5.  Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase Inhibitors.

Authors:  Ya-Nan Chang; Yang Xiang; Yue-Juan Zhang; Wen-Ming Wang; Cheng Chen; Peter Oelschlaeger; Ke-Wu Yang
Journal:  ACS Med Chem Lett       Date:  2017-04-24       Impact factor: 4.345

Review 6.  NDM Metallo-β-Lactamases and Their Bacterial Producers in Health Care Settings.

Authors:  Wenjing Wu; Yu Feng; Guangmin Tang; Fu Qiao; Alan McNally; Zhiyong Zong
Journal:  Clin Microbiol Rev       Date:  2019-01-30       Impact factor: 26.132

Review 7.  β-lactam/β-lactamase inhibitor combinations: an update.

Authors:  Kamaleddin H M E Tehrani; Nathaniel I Martin
Journal:  Medchemcomm       Date:  2018-08-17       Impact factor: 3.597

Review 8.  One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams.

Authors:  Dustin T King; Solmaz Sobhanifar; Natalie C J Strynadka
Journal:  Protein Sci       Date:  2016-03-09       Impact factor: 6.725

9.  Virtual Screening and Experimental Testing of B1 Metallo-β-lactamase Inhibitors.

Authors:  Joon S Kang; Antonia L Zhang; Mohammad Faheem; Charles J Zhang; Ni Ai; John D Buynak; William J Welsh; Peter Oelschlaeger
Journal:  J Chem Inf Model       Date:  2018-08-29       Impact factor: 4.956

10.  Mercaptoacetate thioesters and their hydrolysate mercaptoacetic acids jointly inhibit metallo-β-lactamase L1.

Authors:  Cheng Chen; Yang Xiang; Ya Liu; Xiangdong Hu; Ke-Wu Yang
Journal:  Medchemcomm       Date:  2018-05-17       Impact factor: 3.597

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