Evidence map›Paper›PMID 41280339›Full record

ArticleRSC medicinal chemistry2026

Structure-activity relationships of hydrophobic small molecule irreversible inhibitors of tissue transglutaminase.

Daniel A Wallace, Sarah Tribe, Pauline Navals, Christina Bi, Tarasha Sharma, Jeffrey W Keillor

Abstract read
In one paragraph

Article in RSC medicinal 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

6 authors.

Daniel A WallaceDepartment of Chemistry and Biomolecular Sciences, University of Ottawa Ottawa ON N6H 1N5 Canada jkeillor@uottawa.ca.
Sarah TribeDepartment of Chemistry and Biomolecular Sciences, University of Ottawa Ottawa ON N6H 1N5 Canada jkeillor@uottawa.ca.ORCID https://orcid.org/0009-0004-8418-8174
Pauline NavalsDepartment of Chemistry and Biomolecular Sciences, University of Ottawa Ottawa ON N6H 1N5 Canada jkeillor@uottawa.ca.
Christina BiDepartment of Chemistry and Biomolecular Sciences, University of Ottawa Ottawa ON N6H 1N5 Canada jkeillor@uottawa.ca.
Tarasha SharmaDepartment of Chemistry and Biomolecular Sciences, University of Ottawa Ottawa ON N6H 1N5 Canada jkeillor@uottawa.ca.
Jeffrey W KeillorDepartment of Chemistry and Biomolecular Sciences, University of Ottawa Ottawa ON N6H 1N5 Canada jkeillor@uottawa.ca.ORCID https://orcid.org/0000-0002-8133-6862

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tissue transglutaminase (TG2) is both an enzyme and a G-protein that is implicated in many diseases, such that small molecule inhibitors of TG2 have broad potential as drugs or research tools. Previous work has demonstrated how the structure of EB-2-16, a highly potent irreversible inhibitor of TG2, has been optimised with respect to its warhead, tether and bridge moieties. In this work, we studied the structure-activity relationships of the pendant hydrophobic group of the scaffold. This confirmed the superior affinity conferred by the parent adamantyl moiety, over other cycloalkyl, aryl, biaryl and bridged biaryl groups. Additionally, some substituted adamantyl derivatives were shown to exhibit superior inhibitory efficiency over the parent inhibitor, with

Identifiers

PMID41280339
PMCPMC12631574

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Registered trials

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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.