ArticleRSC medicinal chemistry2022
Structure-activity relationships of hydrophobic alkyl acrylamides as tissue transglutaminase inhibitors.
Article in RSC medicinal chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Trylons: Polyamide Surrogate Substrates Enable High-Throughput Screening of Nylon-Degrading Enzymes.Chembiochem : a European journal of chemical biology · 2026Article
- Structure-activity relationships of hydrophobic small molecule irreversible inhibitors of tissue transglutaminase.RSC medicinal chemistry · 2026Article
- Novel PROTACs targeting tissue transglutaminase (TG2) suppress tumorigenicity of ovarian cancer cells.European journal of medicinal chemistry · 2026Article
- Conformational Modulation of Tissue Transglutaminase via Active Site Thiol Alkylating Agents: Size Does Not Matter.Biomolecules · 2024Article
- Preclinical evaluation of anEJNMMI radiopharmacy and chemistry · 2024Article
- Cell-Impermeable Inhibitors Confirm That Intracellular Human Transglutaminase 2 Is Responsible for the Transglutaminase-Associated Cancer Phenotype.International journal of molecular sciences · 2023Article
- Novel irreversible peptidic inhibitors of transglutaminase 2.RSC medicinal chemistry · 2023Article
- The war on hTG2: warhead optimization in small molecule human tissue transglutaminase inhibitors.RSC medicinal chemistry · 2023Article
- Peptidic Inhibitors and a Fluorescent Probe for the Selective Inhibition and Labelling of Factor XIIIa Transglutaminase.Molecules (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tissue transglutaminase (TG2) is a multifunctional protein that plays biological roles based on its ability to catalyse protein cross-linking and to function as a non-canonical G-protein known as Ghα. The non-regulated activity of TG2 has been implicated in fibrosis, celiac disease and the survival of cancer stem cells, underpinning the therapeutic potential of cell permeable small molecule inhibitors of TG2. In the current study, we designed a small library of inhibitors to explore the importance of a terminal hydrophobic moiety, as well as the length of the tether to the irreversible acrylamide warhead. Subsequent kinetic evaluation using an
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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 Socratic graph.