In one paragraphArticle in ACS infectious diseases, 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
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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
13 authors.
Caitlyn A ThomasDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.ORCID 0000-0001-9115-7350 John Paul AlaoDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.
Thomas SmisekDepartment of Molecular Biosciences, The University of Texas, Austin, Texas 78712, United States.ORCID 0009-0007-4085-1976 Zishuo ChengDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.
Christopher R BethelMedical Service, VA Northeast Ohio Health Care System Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, Ohio 44106, United States.
Kundi YangDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.
Ikponwmosa ObasekiDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.
Richard C PageDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.ORCID 0000-0002-3006-3171 Robert A BonomoMedical Service, VA Northeast Ohio Health Care System Louis Stokes Cleveland Department of Veterans Affairs Medical Center, Cleveland, Ohio 44106, United States.ORCID 0000-0002-3299-894X Peter OelschlaegerDepartment of Biotechnology and Pharmaceutical Sciences, College of Pharmacy, Western University of Health Sciences, Pomona, California 91766, United States.ORCID 0000-0001-5949-9297 Walter FastDepartment of Molecular Biosciences, The University of Texas, Austin, Texas 78712, United States.ORCID 0000-0001-7567-2213 Andrea N KravatsDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.ORCID 0000-0001-8930-0170 Michael W CrowderDepartment of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States.ORCID 0000-0002-3138-0283 Funding
Triage mechanisms for directing protein refolding and degradationR35GM128595 · NIGMS · MIAMI UNIVERSITY OXFORD · PI Richard C Page · 2018 to 2026
$2.8MElucidating the Mechanistic Details of the Grp94 Molecular Chaperone through an Integrated Computational and Experimental ApproachR35GM146963 · NIGMS · MIAMI UNIVERSITY OXFORD · PI Andrea N Kravats · 2022 to 2026
$1.7MMachine Learning Approach for finding novel metallo-b-lactamase inhibitorsR15GM134454 · NIGMS · MIAMI UNIVERSITY OXFORD · PI CROWDER, MICHAEL W · 2019 to 2022
$867kBLRD VA I01 BX001974BLRD VA I01 BX005307NIGMS NIH HHS R15 GM134454NIGMS NIH HHS R35 GM128595NIGMS NIH HHS R35 GM146963
6 · The paper itselfAbstract
β-Lactam-resistant bacterial infections are a serious concern worldwide. A common mechanism of β-lactam resistance is the expression of β-lactamases, which are capable of hydrolyzing the β-lactam bond in the most commonly used β-lactam antibiotics. Metallo-β-lactamases (MBLs) utilize 1 or 2 zinc ions for catalysis. One of the three most clinically relevant MBLs is Imipenemase (IMP). An important potential way to combat MBLs is to use an inhibitor in combination with an existing β-lactam drug. The current study investigates the mechanism of inhibition of preclinical boronic acid β-lactamase inhibitor RPX 7546 and mercaptomethyl bisthiazolidine D-CS319, which are two previously reported MBL inhibitors, with IMP-1 and its variant IMP-78 (V67F/S262G), chosen due to its improved efficiency hydrolyzing carbapenem β-lactams. A combination of analytical and biochemical experiments and
Indexed as
Anti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-LactamasesDrug DesignHumansModels, MolecularAnti-Bacterial Agentsbeta-lactamase IMP-1beta-Lactamase Inhibitorsbeta-Lactamasesantibiotic resistanceimipenemasemechanism of inhibitionmetallo-β-lactamasemetallo-β-lactamase inhibitors
Identifiers
PMID40704846
PMCPMC12336985
What OpenQuestion holds
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