ArticleProtein science : a publication of the Protein Society2020
Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 28 citations in OpenAlex.
- Ceftazidime retainsmSphere · 2025Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Protein-protein interaction network study of metallo-beta-lactamase-L1 present inIn silico pharmacology · 2024Article
- Article
- Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup-emerging targets to combat antibiotic resistance.Frontiers in chemistry · 2023Review
- Time-resolved β-lactam cleavage by L1 metallo-β-lactamase.Nature communications · 2022Article
- Identification of natural inhibitor against L1 β-lactamase present in Stenotrophomonas maltophilia.Journal of molecular modeling · 2022Article
- Fixed-target serial crystallography at the Structural Biology Center.Journal of synchrotron radiation · 2022Article
- Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active-Site Glutamic Acid.Antimicrobial agents and chemotherapy · 2021Article
- 2-Mercaptomethyl Thiazolidines (MMTZs) Inhibit All Metallo-β-Lactamase Classes by Maintaining a Conserved Binding Mode.ACS infectious diseases · 2021Article
- Dual Activity BLEG-1 fromInternational journal of molecular sciences · 2021Article
- A Novel Cooperative Metallo-β-Lactamase Fold Metallohydrolase from Pathogen Vibrio vulnificus Exhibits β-Lactam Antibiotic-Degrading Activities.Antimicrobial agents and chemotherapy · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity.Protein science : a publication of the Protein Society · 2020Article
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6 authors at 2 institutions in 1 country.
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Abstract
Emergence of Enterobacteriaceae harboring metallo-β-lactamases (MBL) has raised global threats due to their broad antibiotic resistance profiles and the lack of effective inhibitors against them. We have been studied one of the emerging environmental MBL, the L1 from Stenotrophomonas maltophilia K279a. We determined several crystal structures of L1 complexes with three different classes of β-lactam antibiotics (penicillin G, moxalactam, meropenem, and imipenem), with the inhibitor captopril and different metal ions (Zn
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