Evidence map›Paper›PMID 40341627›Full record

ArticleDrug development research2025

Development of Efficient Covalent Inactivators of a Fungal Aspartate Semialdehyde Dehydrogenase.

Samantha N Friday, Liezel A Koellner, Spencer W Brown, Christopher N Calbat, Catherine F Curran, Jordan D Dietz, Andreas Koenig-Dummer, Paul D Friday, James A Parker, Noah A Simmons and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Drug development research, 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

15 authors.

Samantha N FridayDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, Ohio, USA.
Liezel A KoellnerDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Spencer W BrownDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Christopher N CalbatDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Catherine F CurranDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Jordan D DietzDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Andreas Koenig-DummerDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Paul D FridayDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, Ohio, USA.
James A ParkerDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Noah A SimmonsDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Finnean A UrmeyDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Alexis N WestDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.
Sebastian G ZaglerDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.ORCID 0009-0002-7337-3652
Ronald E ViolaDepartment of Chemistry and Biochemistry, University of Toledo, Toledo, Ohio, USA.ORCID 0000-0002-3117-9168
Christopher J HalkidesDepartment of Chemistry and Biochemistry, University of North Carolina Wilmington, Wilmington, North Carolina, USA.ORCID 0000-0003-3034-1124

Funding

The AVANCE III 300 NMR spectrometer used to obtain results in this publication was supported by the National Science Foundation under Grant No. 0821552.
6 · The paper itself

Abstract

Aspartate semialdehyde dehydrogenase (ASADH) catalyzes the second step in the fungal pathway towards the synthesis of threonine, isoleucine, and methionine, and it has been identified as a viable target for antifungal drug development. Our previous work produced a group of vinyl sulfones that function as irreversible covalent inactivators of this enzyme. We have now expanded this initial set to produce vinyl sulfones with higher kinetic efficiency as covalent inactivators of ASADH purified from the pathogenic fungal species Candida albicans. The catalytic efficiency of these inactivators has also been compared to related classes of irreversible inactivators, vinyl sulfonamides, acrylamides, and sulfonyl ketones.

Indexed as

Antifungal AgentsAspartate-Semialdehyde DehydrogenaseCandida albicansEnzyme InhibitorsFungal ProteinsKineticsAntifungal AgentsAspartate-Semialdehyde DehydrogenaseEnzyme InhibitorsFungal Proteinsantifungal agentscovalent inactivatorsMichael acceptorsvinyl sulfones

Identifiers

PMID40341627
PMCPMC12060211

What OpenQuestion holds

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LicenceCC BY
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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.