Evidence map›Paper›PMID 40513263›Full record

ArticleJournal of inorganic biochemistry2025

Mutation of an active site-adjacent residue in VIM indirectly dictates interactions with and blunts inhibition by D-captopril.

Surendra Bikram Silwal, Bode Wamsley, Zongyao Wang, Benjamin W Gung, Jay C Nix, Richard C Page

Abstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Surendra Bikram SilwalDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, USA.
Bode WamsleyDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, USA.
Zongyao WangDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, USA.
Benjamin W GungDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, USA.
Jay C NixMolecular Biology Consortium, Advanced Light Source, Lawrence Berkeley National Laboratory, Beamline 4.2.2, Berkeley, CA, USA.
Richard C PageDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, USA. Electronic address: pagerc@miamioh.edu.

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
Triage mechanisms for directing protein refolding and degradationR35GM128595 · NIGMS · MIAMI UNIVERSITY OXFORD · PI Richard C Page · 2018 to 2026
$2.8M
Machine Learning Approach for finding novel metallo-b-lactamase inhibitorsR15GM134454 · NIGMS · MIAMI UNIVERSITY OXFORD · PI CROWDER, MICHAEL W · 2019 to 2022
$867k
NIGMS NIH HHS P30 GM124169NIGMS NIH HHS R15 GM134454NIGMS NIH HHS R35 GM128595
6 · The paper itself

Abstract

Activity assays and X-ray crystallographic studies were undertaken to elucidate the inhibitory mechanism of captopril stereoisomers on Verona integron-encoded metallo-β-lactamases, specifically VIM-20, VIM-31, and VIM-15. All three VIM-2-like variants (VIM-20, VIM-31, and VIM-15) and VIM-2 expressed in Escherichia coli exhibited catalytic activity with comparable steady-state kinetic parameters. Among the tested thiol drugs (L- and D-captopril, D,L-thiorphan, and 2,3-dimercaprol), IC

Indexed as

beta-Lactamase Inhibitorsbeta-LactamasesCaptoprilCatalytic DomainCrystallography, X-RayEscherichia coliMutationbeta-Lactamase Inhibitorsbeta-LactamasesCaptoprilAntibiotic resistanceEnzyme inhibitionMetallo-β-lactamaseProtein crystallography

Identifiers

PMID40513263
PMCPMC12218919

What OpenQuestion holds

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Registered trials

None linked

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.