Probing the Effect of the Non-Active-Site Mutation Y229W in New Delhi Metallo-β-lactamase-1 by Site-Directed Mutagenesis, Kinetic Studies, and Molecular Dynamics Simulations-Reference-Cited by-同舟云学术

Probing the Effect of the Non-Active-Site Mutation Y229W in New Delhi Metallo-β-lactamase-1 by Site-Directed Mutagenesis, Kinetic Studies, and Molecular Dynamics Simulations

Published:2013-12-10 Issue:12 Volume:8 Page:e82080
ISSN:1932-6203
Container-title:PLoS ONE
language:en
Short-container-title:PLoS ONE

Author:

Chen Jiao,Chen Hui,Shi Yun,Hu Feng,Lao Xingzhen,Gao Xiangdong,Zheng Heng,Yao Wenbing

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference38 articles.

1. Multidrug-resistant Gram-negative infections: what are the treatment options?;H Giamarellou;Drugs,2009

2. Metallo-β-lactamase structure and function;T Palzkill;Ann N Y Acad Sci,2013

3. Hybrid QM/MM and DFT investigations of the catalytic mechanism and inhibition of the dinuclear zinc metallo-β-lactamase CcrA from Bacteroides fragilis;H Park;J Am Chem Soc,2005

4. Beta-lactamase inhibitors: the story so far;FJ Perez-Llarena;Curr Med Chem,2009

5. Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumonia sequence type 14 from India;D Yong;Antimicrob Agents Chemother,2009

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