ArticleRSC advances2025
Enzyme graphene oxide interaction: the case system of β-lactamases.
Article in RSC advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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
1 citing paper in PubMed.
- Methods for the establishment of enzymatic mechanisms - from QM to ML.Chemical science · 2026Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report an extensive survey of the inhibition effect of graphene oxide (GO) on the enzymatic activity of β-lactamases (BLs), namely: serine β-lactamases (SBLs) SHV-1, CTX-M-15, GES-1, KPC-3, OXA-23, and metallo-β-lactamases (MBLs) (NDM-1, VIM-1, CphA, and L1). The inhibition study has been performed with GO dose-dependent kinetic assays (using nitrocefin as a substrate). On all the SBLs, a formidable inhibition activity is demonstrated already at a GO concentration of 0.5 µg ml
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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.