ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- An Ion-Pair Induced Intermediate Complex Captured in Class D Carbapenemase Reveals Chloride Ion as a Janus Effector Modulating Activity.ACS central science · 2023Article
- Studies on the Reactions of Biapenem with VIM Metallo β-Lactamases and the Serine β-Lactamase KPC-2.Antibiotics (Basel, Switzerland) · 2022Article
- X-ray free-electron laser studies reveal correlated motion during isopenicillinScience advances · 2021Article
- Antimicrobial Resistance Conferred by OXA-48 β-Lactamases: Towards a Detailed Mechanistic Understanding.Antimicrobial agents and chemotherapy · 2021Review
- Faropenem reacts with serine and metallo-β-lactamases to give multiple products.European journal of medicinal chemistry · 2021Article
- Interactions of the Diazabicyclooctane Serine β-Lactamase Inhibitor ETX1317 with Target Enzymes.ACS infectious diseases · 2021Article
- Analysis of β-lactone formation by clinically observed carbapenemases informs on a novel antibiotic resistance mechanism.The Journal of biological chemistry · 2020Article
- Monitoring protein-metal binding byRSC medicinal chemistry · 2020Article
- 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
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Bacterial production of β-lactamases with carbapenemase activity is a global health threat. The active sites of class D carbapenemases such as OXA-48, which is of major clinical importance, uniquely contain a carbamylated lysine residue which is essential for catalysis. Although there is significant interest in characterizing this post-translational modification, and it is a promising inhibition target, protein carbamylation is challenging to monitor in solution. We report the use of
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.