Evidence map›Paper›PMID 41850401›Full record

ArticleThe Journal of biological chemistry2026

Hydroxamate-based inhibitors reveal structural determinants of selectivity for Plasmodium falciparum aminopeptidase P.

Belinda J Mills, Kyle S Gregory, Gyles E Cozier, Supannee Taweechai, Eve Loughlan, Glenn A McConkey, R Elwyn Isaac, Richard Foster, K Ravi Acharya

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 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

9 authors.

Belinda J MillsSchool of Chemistry, University of Leeds, Leeds, UK.
Kyle S GregoryDepartment of Life Sciences, University of Bath, Bath, UK.
Gyles E CozierDepartment of Life Sciences, University of Bath, Bath, UK.
Supannee TaweechaiSchool of Biology, Faculty of Biological Sciences, Clarendon Way, University of Leeds, Leeds, UK.
Eve LoughlanSchool of Chemistry, University of Leeds, Leeds, UK.
Glenn A McConkeySchool of Biology, Faculty of Biological Sciences, Clarendon Way, University of Leeds, Leeds, UK.
R Elwyn IsaacSchool of Biology, Faculty of Biological Sciences, Clarendon Way, University of Leeds, Leeds, UK. Electronic address: R.E.Isaac@leeds.ac.uk.
Richard FosterSchool of Chemistry, University of Leeds, Leeds, UK. Electronic address: R.Foster@leeds.ac.uk.
K Ravi AcharyaDepartment of Life Sciences, University of Bath, Bath, UK. Electronic address: bsskra@bath.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The malarial parasite, Plasmodium falciparum (Pf), utilizes aminopeptidases in the breakdown of hemoglobin-derived oligopeptides to release amino acids for protein synthesis during growth and asexual reproduction of erythrocytic stages of the parasite. However, a N-terminal peptide bond that involves proline is difficult to hydrolyze. Aminopeptidase P (APP) is capable of cleaving peptide bonds with proline in the second position. Inhibition of PfAPP is therefore an attractive strategy for developing therapeutics for the treatment of malaria by limiting the supply of amino acids at the erythrocytic stage. We employed the structure-activity relationship of an existing APP inhibitor, apstatin, to design a more potent PfAPP inhibitor by introducing a hydroxamic acid metal-binding group in place of the amino-alcohol of apstatin and an aromatic P4' moiety. A hydroxamic tetrapeptide with phenylalanine at P4' (6d) greatly increased the inhibitory potency (apstatin K

Indexed as

AminopeptidasesAntimalarialsEnzyme InhibitorsHydroxamic AcidsPlasmodium falciparumProtease InhibitorsHumansMolecular StructureStructure-Activity RelationshipAminopeptidasesAntimalarialsEnzyme InhibitorsHydroxamic Acidsprolyl aminopeptidaseProtease Inhibitorsapstatinhydroxamic peptide inhibitormalariametalloproteasePlasmodium falciparum aminopeptidase PX-ray crystallography

Identifiers

PMID41850401
PMCPMC13100289

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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.