ArticleActa crystallographica. Section F, Structural biology communications2016
The structure of the metallo-β-lactamase VIM-2 in complex with a triazolylthioacetamide inhibitor.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 36 citations in OpenAlex.
- Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors.Communications chemistry · 2025Article
- Neutralizing Carbapenem Resistance by Co-Administering Meropenem with Novel β-Lactam-Metallo-β-Lactamase Inhibitors.Antibiotics (Basel, Switzerland) · 2023Article
- Carbapenem Use Is Driving the Evolution of Imipenemase 1 Variants.Antimicrobial agents and chemotherapy · 2021Article
- Binding of 2-(Triazolylthio)acetamides to Metallo-β-lactamase CcrA Determined with NMR.ACS omega · 2020Article
- 4-(Biomolecules · 2020Article
- Synthesis of New Planar-Chiral Linked [2.2]Paracyclophanes-Molecules (Basel, Switzerland) · 2020Article
- Kinetic, Thermodynamic, and Crystallographic Studies of 2-Triazolylthioacetamides as Verona Integron-Encoded Metallo-β-Lactamase 2 (VIM-2) Inhibitor.Biomolecules · 2020Article
- Azolylthioacetamides as potential inhibitors of New Delhi metallo-β-lactamase-1 (NDM-1).The Journal of antibiotics · 2019Article
- Targeting Metalloenzymes for Therapeutic Intervention.Chemical reviews · 2019Review
- Crystal structures of VIM-1 complexes explain active site heterogeneity in VIM-class metallo-β-lactamases.The FEBS journal · 2019Article
- Rhodanine as a Potent Scaffold for the Development of Broad-Spectrum Metallo-β-lactamase Inhibitors.ACS medicinal chemistry letters · 2018Article
- Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding.Antimicrobial agents and chemotherapy · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The increasing number of pathogens expressing metallo-β-lactamases (MBLs), and in this way achieving resistance to β-lactam antibiotics, is a significant threat to global public health. A promising strategy to treat such resistant pathogens is the co-administration of MBL inhibitors together with β-lactam antibiotics. However, an MBL inhibitor suitable for clinical use has not yet been identified. Verona integron-encoded metallo-β-lactamase 2 (VIM-2) is a widespread MBL with a broad substrate spectrum and hence is an interesting drug target for the treatment of β-lactam-resistant infections. In this study, three triazolylthioacetamides were tested as inhibitors of VIM-2. One of the tested compounds showed clear inhibition of VIM-2, with an IC
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