Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis.

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

4 citing papers in PubMed, 6 citations in OpenAlex.

1. Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup-emerging targets to combat antibiotic resistance.Frontiers in chemistry · 2023
   Review
2. Bicyclic Boronate VNRX-5133 Inhibits Metallo- and Serine-β-Lactamases.Journal of medicinal chemistry · 2019
   Article
3. The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.Trends in pharmacological sciences · 2018
   Review
4. Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates.Nature communications · 2016
   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

4 authors at 2 institutions in 2 countries.

Funding

Abstract