ArticleBioorganic & medicinal chemistry letters2013
A small molecule inhibitor of fungal histone acetyltransferase Rtt109.
Article in Bioorganic & medicinal chemistry letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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.
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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.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- Lysine crotonylation enhances fungal effector activity and promotes invasion of host plants.Plant communications · 2026Article
- Inhibition of Histone Lysine Acetyltransferases by Coenzyme A Analogs.Molecules (Basel, Switzerland) · 2026Article
- Two Subunits of the Rpd3 Histone Deacetylase Complex of Cochliobolus heterostrophus Are Essential for Nitrosative Stress Response and Virulence, and Interact With Stress-Response Regulators ChHog1 and ChCrz1.Molecular plant pathology · 2025Article
- Is a Fungal Apocalypse Inevitable or Just a Hallucination? An Overview of the Antifungal Armamentarium Used in the Fight against Pathogenic Fungi.ACS medicinal chemistry letters · 2025Review
- Targeting lysine acetylation readers and writers.Nature reviews. Drug discovery · 2025Review
- In-silico guided chemical exploration of KDM4A fragments hits.Clinical epigenetics · 2023Article
- Potential antifungal targets based on histones post-translational modifications against invasive aspergillosis.Frontiers in microbiology · 2022Review
- Article
- Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Review
- Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.Nucleic acids research · 2018Article
- Assay interference and off-target liabilities of reported histone acetyltransferase inhibitors.Nature communications · 2017Article
- Discovery of a selective catalytic p300/CBP inhibitor that targets lineage-specific tumours.Nature · 2017Article
- Environmental change drives accelerated adaptation through stimulated copy number variation.PLoS biology · 2017Article
- Post-HTS case report and structural alert: Promiscuous 4-aroyl-1,5-disubstituted-3-hydroxy-2H-pyrrol-2-one actives verified by ALARM NMR.Bioorganic & medicinal chemistry letters · 2015Article
- The WOR1 5' untranslated region regulates white-opaque switching in Candida albicans by reducing translational efficiency.Molecular microbiology · 2015Article
- PAINS in the assay: chemical mechanisms of assay interference and promiscuous enzymatic inhibition observed during a sulfhydryl-scavenging HTS.Journal of medicinal chemistry · 2015Article
- Pneumocystis jirovecii Rtt109, a novel drug target for Pneumocystis pneumonia in immunosuppressed humans.Antimicrobial agents and chemotherapy · 2014Article
- A cell-free fluorometric high-throughput screen for inhibitors of Rtt109-catalyzed histone acetylation.PloS one · 2013Article
- Histone-modifying enzymes, histone modifications and histone chaperones in nucleosome assembly: Lessons learned from Rtt109 histone acetyltransferases.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The histone acetyltransferase Rtt109 is the sole enzyme responsible for acetylation of histone H3 lysine 56 (H3K56) in fungal organisms. Loss of Rtt109 renders fungal cells extremely sensitive to genotoxic agents, and prevents pathogenesis in several clinically important species. Here, via a high throughput chemical screen of >300,000 compounds, we discovered a chemical inhibitor of Rtt109 that does not inhibit other acetyltransferase enzymes. This compound inhibits Rtt109 regardless of which histone chaperone cofactor protein (Asf1 or Vps75) is present, and appears to inhibit Rtt109 via a tight-binding, uncompetitive mechanism.
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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.