Evidence map›Paper›PMID 42187199›Full record

ReviewMedicinal research reviews2026

Hydroxamic Acids as HDAC Inhibitor Drug Leads for Malaria.

Wisam A Dawood, Jacinta R Macdonald, Christian Anzenhofer, Tina S Skinner-Adams, Robert C Reid, Thomas Kurz, David P Fairlie, Katherine T Andrews

Abstract readReview
In one paragraph

Review in Medicinal research reviews, 2026. 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

8 authors.

Wisam A DawoodInstitute for Biomedicine and Glycomics, Griffith University, Southport, Queensland, Australia.ORCID https://orcid.org/0000-0001-9059-7020
Jacinta R MacdonaldInstitute for Biomedicine and Glycomics, Griffith University, Southport, Queensland, Australia.ORCID https://orcid.org/0000-0003-1516-8415
Christian AnzenhoferInstitut für pharmazeutische und medizinische Chemie, Heinrich-Heine Universität, Germany.
Tina S Skinner-AdamsInstitute for Biomedicine and Glycomics, Griffith University, Southport, Queensland, Australia.ORCID https://orcid.org/0000-0001-7011-3850
Robert C ReidCentre for Chemistry and Drug Discovery, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland, Australia.
Thomas KurzInstitut für pharmazeutische und medizinische Chemie, Heinrich-Heine Universität, Germany.ORCID https://orcid.org/0000-0002-9474-4224
David P FairlieCentre for Chemistry and Drug Discovery, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland, Australia.
Katherine T AndrewsInstitute for Biomedicine and Glycomics, Griffith University, Southport, Queensland, Australia.ORCID https://orcid.org/0000-0002-1591-8979

Funding

Australian Government Research Training ProgramAustralian Research Council CE200100012Australian Research Council DP250102295National Health and Medical Council of Australia 2009551
6 · The paper itself

Abstract

Malaria is a global health threat, with an estimated 282 million cases and 610,000 malaria-associated deaths reported in 2024. Most mortality is due to infection by Plasmodium falciparum parasites, with the highest burden occurring in Sub-Saharan Africa. Malaria eradication is a global priority; however, progress has been hampered by the lack of broadly applicable and highly effective vaccines and by parasite drug resistance. To address drug resistance, the discovery of drugs with novel modes of action is crucial. Histone/lysine deacetylases (HDACs) are enzymes that control the posttranslational modification of lysine acetylation on histone and non-histone proteins. Due to their essential roles in regulating key processes in Plasmodium parasites, including transcriptional and developmental control, HDACs are prospective drug targets for malaria. Here, the potential of HDAC inhibitors as antimalarial drug leads is reviewed, including an assessment of antiplasmodial structure-activity relationships for more than 750 hydroxamic acids with published in vitro activity against P. falciparum. These comparative data provide unprecedented insights into potency, selectivity and physicochemical properties that can help to guide investigations of this chemotype as drug leads for malaria and other parasitic diseases.

Indexed as

AntimalarialsHistone Deacetylase InhibitorsHydroxamic AcidsMalariaAnimalsHistone DeacetylasesHumansPlasmodium falciparumStructure-Activity RelationshipAntimalarialsHistone Deacetylase InhibitorsHistone DeacetylasesHydroxamic AcidsHDAC inhibitorhydroxamic acidmalariaPlasmodiumstructure‐activity relationship

Identifiers

PMID42187199
PMCPMC13637067

What OpenQuestion holds

Textmetadata
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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.