Inhibition of Histone Lysine Acetyltransferases by Coenzyme A Analogs.

Faidra Voukia, Nurgül Bilgin, Steffen Bundgaard Andersen, Jasmin Mecinović

Abstract read

In one paragraph

Article in Molecules (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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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

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5 · Who and what money

Authors and funding

4 authors.

Faidra VoukiaDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark.ORCID 0000-0002-7700-2579

Nurgül BilginDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark.ORCID 0000-0002-7097-7218

Steffen Bundgaard AndersenDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark.

Jasmin MecinovićDepartment of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark.ORCID 0000-0002-5559-3822

Funding

European Research Council 715691Lundbeck Foundation R344-2020-1051

6 · The paper itself

Abstract

Histone lysine acetylation is a widespread posttranslational modification, essential for vital functions in eukaryotic organisms. Histone lysine acetyltransferases (KATs) employ acetyl-coenzyme A as a universal acetyl donor for acetylation of lysine residues in histone and non-histone proteins. Despite the biomedicinal importance of modulation of the KAT activity, application of the acetyl-coenzyme A cosubstrate structure for the design of potent and selective inhibitors has been underexplored. Here, we developed functionalized coenzyme A analogs as inhibitors against human histone lysine acetyltransferases GCN5, KAT8, and HAT1. In contrast to the unmodified coenzyme A, which was found to be a poor inhibitor of GCN5 and KAT8 (IC

Indexed as

Coenzyme AEnzyme InhibitorsHistone AcetyltransferasesLysine AcetyltransferasesAcetylationHistonesHumansLysinep300-CBP-Associated FactorCoenzyme AEnzyme InhibitorsHistone AcetyltransferasesHistonesKAT8 protein, humanLysineLysine Acetyltransferasesp300-CBP-Associated Factoracetylationcoenzyme Aepigeneticshistonelysine acetyltransferases

Identifiers

PMID41683453

DOI10.3390/molecules31030477

PMCPMC12899889

What OpenQuestion holds

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LicenceCC BY

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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.