ArticleAntimicrobial agents and chemotherapy2011
Purification and biochemical characterization of IMP-13 metallo-beta-lactamase.
Article in Antimicrobial agents and chemotherapy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The synergistic effect ofFrontiers in pharmacology · 2025Article
- Structural insights into the substrate specificity of IMP-6 and IMP-1 metallo-β-lactamases.Journal of biochemistry · 2022Article
- Expression and purification of soluble recombinant β-lactamases using Escherichia coli as expression host and pET-28a as cloning vector.Microbial cell factories · 2022Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Structure and Molecular Recognition Mechanism of IMP-13 Metallo-β-Lactamase.Antimicrobial agents and chemotherapy · 2020Article
- B1-Metallo-β-Lactamases: Where Do We Stand?Current drug targets · 2016Review
- Antimicrobial active herbal compounds against Acinetobacter baumannii and other pathogens.Frontiers in microbiology · 2015Review
- Systematic analysis of metallo-β-lactamases using an automated database.Antimicrobial agents and chemotherapy · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The IMP-13 metallo-β-lactamase was overproduced in Escherichia coli BL21(DE3) and purified by chromatography. Analysis of kinetic parameters revealed some notable differences with other IMP-type enzymes, noteworthily a higher catalytic efficiency toward ticarcillin and piperacillin and a marked preference for imipenem over meropenem.
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Registered trials
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