ArticleThe Journal of biological chemistry2018
Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 35 citations in OpenAlex.
- Unveiling the thioredoxin fold: a systematic review and bioinformatic analysis of protein disulfide isomerase and Dsb family proteins.Frontiers in bioinformatics · 2026Pooled it
- A mechanism for the disrupted redox regulation of vascular contractility during aging.iScience · 2026Article
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- Is uric acid a true antioxidant? Identification of uric acid oxidation products and their biological effects.Redox report : communications in free radical research · 2025Review
- Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols.Antioxidants (Basel, Switzerland) · 2025Review
- Recent advances in vascular thiol isomerases and redox systems in platelet function and thrombosis.Journal of thrombosis and haemostasis : JTH · 2024Review
- Article
- Sulfenylation links oxidative stress to protein disulfide isomerase oxidase activity and thrombus formation.Journal of thrombosis and haemostasis : JTH · 2023Article
- A pilot study on nitration/dysfunction of NK1 segment of myogenic stem cell activator HGF.Biochemistry and biophysics reports · 2022Article
- Oxidative Cysteine Modification of Thiol Isomerases in Thrombotic Disease: A Hypothesis.Antioxidants & redox signaling · 2021Review
- The bicarbonate/carbon dioxide pair increases hydrogen peroxide-mediated hyperoxidation of human peroxiredoxin 1.The Journal of biological chemistry · 2019Article
- Protein disulfide isomerase plasma levels in healthy humans reveal proteomic signatures involved in contrasting endothelial phenotypes.Redox biology · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-disulfide isomerase (PDI) is a ubiquitous dithiol-disulfide oxidoreductase that performs an array of cellular functions, such as cellular signaling and responses to cell-damaging events. PDI can become dysfunctional by post-translational modifications, including those promoted by biological oxidants, and its dysfunction has been associated with several diseases in which oxidative stress plays a role. Because the kinetics and products of the reaction of these oxidants with PDI remain incompletely characterized, we investigated the reaction of PDI with the biological oxidant peroxynitrite. First, by determining the rate constant of the oxidation of PDI's redox-active Cys residues (Cys
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