ArticleAngewandte Chemie (International ed. in English)2017
Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Structural and functional characterization of an active site-influencing variant (IMP-1-F218Y) in IMP-1 metallo-β-lactamase.The FEBS journal · 2026Article
- Article
- Mechanism of sensor kinase CitA transmembrane signaling.Nature communications · 2025Article
- Review
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Monitoring protein-metal binding byRSC medicinal chemistry · 2020Article
- Discovery of [1,2,4]Triazole Derivatives as New Metallo-β-Lactamase Inhibitors.Molecules (Basel, Switzerland) · 2019Article
- Article
- Profiling interactions of vaborbactam with metallo-β-lactamases.Bioorganic & medicinal chemistry letters · 2019Article
- The Reaction Mechanism of Metallo-β-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop.Antimicrobial agents and chemotherapy · 2019Article
- The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.Trends in pharmacological sciences · 2018Review
- Cyclobutanone Mimics of Intermediates in Metallo-β-Lactamase Catalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Shaping Substrate Selectivity in a Broad-Spectrum Metallo-β-Lactamase.Antimicrobial agents and chemotherapy · 2018Article
- Selective Radical Trifluoromethylation of Native Residues in Proteins.Journal of the American Chemical Society · 2018Article
- Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-β-lactamase inhibition.Chemical communications (Cambridge, England) · 2017Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
Abstract
Resistance to β-lactam antibiotics mediated by metallo-β-lactamases (MBLs) is a growing problem. We describe the use of protein-observe
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.