Evidence map›Paper›PMID 41611522›Full record

ArticleJournal of medicinal chemistry2026

Biological Activity and Structural Biology of Current KAT6A Inhibitor Chemotypes.

Adi Suwandi, Jianwen Jin, Yichao Zhao, Ramesh Mudududdla, Yi Sing Gee, Girdhar Singh Deora, Yuxin Sun, Heping Wei, Fei Huang, Jin-Shu He and 5 more

Abstract read
In one paragraph

Article in Journal of medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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.

Adi SuwandiMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), Parkville, VIC 3052, Australia.
Jianwen JinInstitute for Advanced and Applied Chemical Synthesis, College of Pharmacy, Jinan University, Guangzhou, Guangdong 510632, China.
Yichao ZhaoMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), Parkville, VIC 3052, Australia.
Ramesh MudududdlaMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), Parkville, VIC 3052, Australia.
Yi Sing GeeMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), Parkville, VIC 3052, Australia.ORCID 0000-0002-2707-6270
Girdhar Singh DeoraMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), Parkville, VIC 3052, Australia.
Yuxin SunMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), Parkville, VIC 3052, Australia.
Heping WeiSchool of Pharmaceutical Sciences, Nanjing Tech University, No. 30 South Puzhu Road, Nanjing 211816, People's Republic of China.
Fei HuangSchool of Pharmaceutical Sciences, Nanjing Tech University, No. 30 South Puzhu Road, Nanjing 211816, People's Republic of China.ORCID 0000-0002-5290-2490
Jin-Shu HeJohn Curtin School of Medical Research, Australian National University, Canberra, ACT 2600, Australia.ORCID 0000-0001-7354-0233
Amee J GeorgeJohn Curtin School of Medical Research, Australian National University, Canberra, ACT 2600, Australia.ORCID 0000-0002-0265-4476
Stefan J HermansACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, VIC 3065, Australia.ORCID 0000-0002-2513-5054
David J LeaverSchool of Dentistry and Medical Sciences, Charles Sturt University, Wagga Wagga, NSW 2678, Australia.ORCID 0009-0004-7513-1627
Michael W ParkerACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, VIC 3065, Australia.
Jonathan B BaellMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), Parkville, VIC 3052, Australia.ORCID 0000-0003-2114-8242

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

All lysine acetyltransferases (KATs) modulate biological outcomes through the acetylation of lysine side-chain amino groups facilitated by acetyl coenzyme A (AcCoA). KAT6A belongs to the class of MYST domain histone acetyltransferases (HATs), which had been regarded as undruggable. The first on-target KAT6A inhibitors with

Indexed as

Enzyme InhibitorsHistone AcetyltransferasesAnimalsCrystallography, X-RayHumansModels, MolecularStructure-Activity RelationshipEnzyme InhibitorsHistone AcetyltransferasesKAT6A protein, human

Identifiers

PMID41611522
PMCPMC12910677

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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 Socratic graph.