Flexible loops of New Delhi metallo-β-lactamase modulate its activity towards different substrates-Reference-Cited by-同舟云学术

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Flexible loops of New Delhi metallo-β-lactamase modulate its activity towards different substrates

Published:2020-09 Issue: Volume:158 Page:104-115
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Raczynska Joanna E.,Imiolczyk Barbara,Komorowska Marlena,Sliwiak Joanna,Czyrko-Horczak Justyna,Brzezinski Krzysztof,Jaskolski Mariusz

Funder

National Center for Research and Development

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference54 articles.

1. Characterization of a new metallo-β-lactamase gene, blaNDM-1, and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India;Yong;Antimicrob. Agents Chemother.,2009

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

3. Structural insights into the subclass B3 metallo-β-lactamase SMB-1 and the mode of inhibition by the common metallo-β-lactamase inhibitor mercaptoacetate;Wachino;Antimicrob. Agents Chemother.,2013

4. Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1;Brem;Chem. Sci.,2015

5. Metallo-β-lactamases: novel weaponry for antibiotic resistance in bacteria;Crowder;Acc. Chem. Res.,2006

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1. Structural insight into the subclass B1 metallo-β-lactamase AFM-1;Biochemical and Biophysical Research Communications;2024-08

2. Interplay between the β-lactam side chain and an active-site mobile loop of NDM-1 in penicillin hydrolysis as a potential target for mechanism-based inhibitor design;International Journal of Biological Macromolecules;2024-03

3. Worldwide trend discovery of structural and functional relationship of metallo-β-lactamase for structure-based drug design: A bibliometric evaluation and patent analysis;International Journal of Biological Macromolecules;2024-01

4. Structural basis of metallo-β-lactamase resistance to taniborbactam;Antimicrobial Agents and Chemotherapy;2023-12-08

5. Relative inhibitory activities of the broad-spectrum β-lactamase inhibitor taniborbactam against metallo-β-lactamases;Antimicrobial Agents and Chemotherapy;2023-12-04

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