ArticleJournal of medicinal chemistry2013
Selective inhibition of extracellular thioredoxin by asymmetric disulfides.
Article in Journal of medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 63 citations in OpenAlex.
- Preparation of Unsymmetrical Disulfides via Catalytic Lewis Base Activation ofThe Journal of organic chemistry · 2026Article
- Conformational activation and disulfide exchange in HIV-1 Env induce cell-free lytic/fusogenic transformation and enhance infection.Journal of virology · 2025Article
- Targeting transglutaminase 2: pathways to celiac disease therapies.Gastroenterology report · 2025Article
- Exploring the Thioredoxin System as a Therapeutic Target in Cancer: Mechanisms and Implications.Antioxidants (Basel, Switzerland) · 2024Review
- Solvent-Free Reaction for Unsymmetrical Organodisulfides with High Purity and Application as Cathode-Active Materials.Materials (Basel, Switzerland) · 2024Article
- Inhibition of Transglutaminase 2 as a Therapeutic Strategy in Celiac Disease-In Vitro Studies in Intestinal Cells and Duodenal Biopsies.International journal of molecular sciences · 2023Article
- Tissue Transglutaminase but Not Microbial Transglutaminase Is Inhibited by Exogenous Oxidative Substances in Celiac Disease.International journal of molecular sciences · 2022Article
- Disulfide Reduction Allosterically Destabilizes the β-Ladder Subdomain Assembly within the NS1 Dimer of ZIKV.Biophysical journal · 2020Article
- Interleukin 4 is inactivated via selective disulfide-bond reduction by extracellular thioredoxin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Endoplasmic reticulum-resident protein 57 (ERp57) oxidatively inactivates human transglutaminase 2.The Journal of biological chemistry · 2018Article
- Redox-Inactive Peptide Disrupting Trx1-Ask1 Interaction for Selective Activation of Stress Signaling.Biochemistry · 2018Article
- Review
- Discovery of unsymmetrical aromatic disulfides as novel inhibitors of SARS-CoV main protease: Chemical synthesis, biological evaluation, molecular docking and 3D-QSAR study.European journal of medicinal chemistry · 2017Article
- Thioredoxin-1 Selectively Activates Transglutaminase 2 in the Extracellular Matrix of the Small Intestine: IMPLICATIONS FOR CELIAC DISEASE.The Journal of biological chemistry · 2017Article
- Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.Annual review of chemical and biomolecular engineering · 2016Review
- Binding of phenothiazines into allosteric hydrophobic pocket of human thioredoxin 1.European biophysics journal : EBJ · 2016Article
- An unprecedented dual antagonist and agonist of human Transglutaminase 2.Bioorganic & medicinal chemistry letters · 2015Article
- Elevated transglutaminase 2 activity is associated with hypoxia-induced experimental pulmonary hypertension in mice.ACS chemical biology · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Whereas the role of mammalian thioredoxin (Trx) as an intracellular protein cofactor is widely appreciated, its function in the extracellular environment is not well-understood. Only few extracellular targets of Trx-mediated thiol-disulfide exchange are known. For example, Trx activates extracellular transglutaminase 2 (TG2) via reduction of an intramolecular disulfide bond. Because hyperactive TG2 is thought to play a role in various diseases, understanding the biological role of extracellular Trx may provide critical insight into the pathogenesis of these disorders. Starting from a clinical-stage asymmetric disulfide lead, we have identified analogs with >100-fold specificity for Trx. Structure-activity relationship and computational docking model analyses have provided insights into the features important for enhancing potency and specificity. The most active compound identified had an IC(50) below 0.1 μM in cell culture and may be appropriate for in vivo use to interrogate the role of extracellular Trx in health and disease.
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What OpenQuestion holds
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 OpenQuestion graph.