ReviewFrontiers in chemistry2014
Methods of measuring protein disulfide isomerase activity: a critical overview.
Review in Frontiers in chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- Targeting the Endoplasmic Reticulum Oxidoreductin-1 Alpha-Protein Disulfide Isomerase Redox Interface as a Therapeutic Strategy in Cancer.Biomedicines · 2026Review
- Assays of Thiol Isomerase Activity.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols.Antioxidants (Basel, Switzerland) · 2025Review
- Protein disulfide isomerase 1 is required for RodA assembling-based conidial hydrophobicity ofApplied and environmental microbiology · 2024Article
- Protein disulfide isomerase cleaves allosteric disulfides in histidine-rich glycoprotein to regulate thrombosis.Nature communications · 2024Article
- Aromatic sulphonamides of aziridine-2-carboxylic acid derivatives as novel PDIA1 and PDIA3 inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- The Role of Reprogrammed Glucose Metabolism in Cancer.Metabolites · 2023Review
- Protein disulfide isomerase family mediated redox regulation in cancer.Advances in cancer research · 2023Review
- Endoplasmic Reticulum (ER) Stress and Its Role in Pancreatic β-Cell Dysfunction and Senescence in Type 2 Diabetes.International journal of molecular sciences · 2022Review
- Tuning isoform selectivity and bortezomib sensitivity with a new class of alkenyl indene PDI inhibitor.European journal of medicinal chemistry · 2020Article
- The Role of ERO1α in Modulating Cancer Progression and Immune Escape.Journal of cancer immunology · 2020Article
- Gaussia princeps luciferase: a bioluminescent substrate for oxidative protein folding.Protein science : a publication of the Protein Society · 2018Article
- An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation.Free radical biology & medicine · 2018Review
- Article
- Challenges in the evaluation of thiol-reactive inhibitors of human protein disulfide Isomerase.Free radical biology & medicine · 2017Article
- Mechanistic insights on the reduction of glutathione disulfide by protein disulfide isomerase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Adverse Outcomes Associated with Cigarette Smoke Radicals Related to Damage to Protein-disulfide Isomerase.The Journal of biological chemistry · 2016Article
- The C-terminal CGHC motif of protein disulfide isomerase supports thrombosis.The Journal of clinical investigation · 2015Article
- The dehydrogenase region of the NADPH oxidase component Nox2 acts as a protein disulfide isomerase (PDI) resembling PDIA3 with a role in the binding of the activator protein p67 (phox.).Frontiers in chemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide isomerase is an essential redox chaperone from the endoplasmic reticulum (ER) and is responsible for correct disulfide bond formation in nascent proteins. PDI is also found in other cellular locations in the cell, particularly the cell surface. Overall, PDI contributes to ER and global cell redox homeostasis and signaling. The knowledge about PDI structure and function progressed substantially based on in vitro studies using recombinant PDI and chimeric proteins. In these experimental scenarios, PDI reductase and chaperone activities are readily approachable. In contrast, assays to measure PDI isomerase activity, the hallmark of PDI family, are more complex. Assessment of PDI roles in cells and tissues mainly relies on gain- or loss-of-function studies. However, there is limited information regarding correlation of experimental readouts with the distinct types of PDI activities. In this mini-review, we evaluate the main methods described for measuring the different kinds of PDI activity: thiol reductase, thiol oxidase, thiol isomerase and chaperone. We emphasize the need to use appropriate controls and the role of critical interferents (e.g., detergent, presence of reducing agents). We also discuss the translation of results from in vitro studies with purified recombinant PDI to cellular and tissue samples, with critical comments on the interpretation of results.
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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 OpenQuestion graph.