ArticleThe Journal of biological chemistry2012
Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a'.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers, 1 of them a synthesis that pooled it.
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Who cites it
75 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Unveiling the thioredoxin fold: a systematic review and bioinformatic analysis of protein disulfide isomerase and Dsb family proteins.Frontiers in bioinformatics · 2026Pooled it
- Identification of the thiol isomerase-binding peptide, mastoparan, as a novel inhibitor of shear-induced transforming growth factor β1 (TGF-β1) activation.The Journal of biological chemistry · 2013Trial
- Exacerbated expansive vascular remodeling due to disturbed flow in male mice overexpressing protein disulfide isomerase-A1.Physiological reports · 2026Article
- Oxidative protein folding and CaCellular and molecular life sciences : CMLS · 2026Review
- Evaluation of AlphaFold3 for Predicting Human Heme-Binding Protein Structures.International journal of molecular sciences · 2026Article
- Inhibition of the SerpinB3/protease-activated receptor 2 axis reduces liver cancer development and affects lipid metabolism.British journal of cancer · 2026Article
- Omeprazole activation of CD4+ and CD8+ T-cells through off-target covalent modification of cellular proteins.Toxicological sciences : an official journal of the Society of Toxicology · 2026Article
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- Hydroxyurea induces an oxidative stress response that triggers ER expansion and cytoplasmic protein aggregation.PLoS biology · 2025Article
- A multichaperone condensate enhances protein folding in the endoplasmic reticulum.Nature cell biology · 2025Article
- Extracellular PDI in thrombosis and vascular injury.Thrombosis journal · 2025Review
- Article
- Spatial covariance reveals isothiocyanate natural products adjust redox stress to restore function in alpha-1-antitrypsin deficiency.Cell reports. Medicine · 2025Article
- The Role of NRF2 in Trinucleotide Repeat Expansion Disorders.Antioxidants (Basel, Switzerland) · 2024Review
- The IRE1β-mediated unfolded protein response is repressed by the chaperone AGR2 in mucin producing cells.The EMBO journal · 2024Article
- Exploring the Influence of Zinc Ions on the Conformational Stability and Activity of Protein Disulfide Isomerase.International journal of molecular sciences · 2024Article
- The Clinical Utility of the Saliva Proteome in Rare Diseases: A Pilot Study for Biomarker Discovery in Primary Sclerosing Cholangitis.Journal of clinical medicine · 2024Article
- Molecular Design of FRET Probes Based on Domain Rearrangement of Protein Disulfide Isomerase for Monitoring Intracellular Redox Status.International journal of molecular sciences · 2023Article
- Probing the conformational dynamics of thiol-isomerases using non-canonical amino acids and single-molecule FRET.Methods (San Diego, Calif.) · 2023Article
- Synergistic antitumor activity of sorafenib and MG149 in hepatocellular carcinoma cells.BMB reports · 2022Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-disulfide isomerase (PDI), with domains arranged as abb'xa'c, is a key enzyme and chaperone localized in the endoplasmic reticulum (ER) catalyzing oxidative folding and preventing misfolding/aggregation of proteins. It has been controversial whether the chaperone activity of PDI is redox-regulated, and the molecular basis is unclear. Here, we show that both the chaperone activity and the overall conformation of human PDI are redox-regulated. We further demonstrate that the conformational changes are triggered by the active site of domain a', and the minimum redox-regulated cassette is located in b'xa'. The structure of the reduced bb'xa' reveals for the first time that domain a' packs tightly with both domain b' and linker x to form one compact structural module. Oxidation of domain a' releases the compact conformation and exposes the shielded hydrophobic areas to facilitate its high chaperone activity. Thus, the study unequivocally provides mechanistic insights into the redox-regulated chaperone activity of human PDI.
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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.