ReviewProteomics2017
From structure to redox: The diverse functional roles of disulfides and implications in disease.
Review in Proteomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 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
89 citing papers in PubMed, 197 citations in OpenAlex.
- TMT-Based Quantitative Proteomics Reveals the Molecular Mechanism Underlying Quality Deterioration of Refrigerated Northern Pike (Foods (Basel, Switzerland) · 2026Article
- AlphaFold reveals how pathogenicmBio · 2026Article
- Computational design and molecular characterization of a multi-epitope peptide vaccine targeting pancreatic cancer.Journal, genetic engineering & biotechnology · 2026Article
- Oxidative stress impairs processive motility of the axonal transport motor KIF1A.The Journal of biological chemistry · 2026Article
- Article
- Residue-level determinants of the thermal stability of the extremophilic Ts2631 endolysin.Scientific reports · 2026Article
- QSOX1: A Mysterious Golgi-Localized Disulfide Bond Catalyst and an Emerging Cancer Regulator.Cancers · 2026Article
- Proteome-Wide Analysis and Surface Protein Isolation for Secretome Characterization Reveal Insights into the Biology of the Leaf-Cutter AntAnalytical chemistry · 2025Article
- Article
- Identification and Characterization of a Small-Molecule Inhibitor of theACS infectious diseases · 2025Article
- Review
- Evaluation of LIGHT-derived peptides to disrupt the HVEM/LIGHT immune checkpoint.Scientific reports · 2025Article
- DiPTH-Cystine and PTH-Cysteine in Disulfide Bond Analysis Using Automated Edman Degradation.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- Review
- Amide Chemistry Enables Redox Locking of Cyclic Disulfides for Polypeptide Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Integrating Redox Proteomics and Computational Modeling to Decipher Thiol-Based Oxidative Post-Translational Modifications (oxiPTMs) in Plant Stress Physiology.International journal of molecular sciences · 2025Review
- DrugProtAI: A machine learning-driven approach for predicting protein druggability through feature engineering and robust partition-based ensemble methods.Briefings in bioinformatics · 2025Article
- Molecular signatures of disulfidptosis: interplay with programmed cell death pathways and therapeutic implications in oncology.Cellular & molecular biology letters · 2025Review
- CHCHD4 Oxidoreductase Activity: A Comprehensive Analysis of the Molecular, Functional, and Structural Properties of Its Redox-Regulated Substrates.Molecules (Basel, Switzerland) · 2025Review
- Improving pJournal of chemical theory and computation · 2025Article
29 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
This review provides a comprehensive overview of the functional roles of disulfide bonds and their relevance to human disease. The critical roles of disulfide bonds in protein structure stabilization and redox regulation of protein activity are addressed. Disulfide bonds are essential to the structural stability of many proteins within the secretory pathway and can exist as intramolecular or inter-domain disulfides. The proper formation of these bonds often relies on folding chaperones and oxidases such as members of the protein disulfide isomerase (PDI) family. Many of the PDI family members catalyze disulfide-bond formation, reduction, and isomerization through redox-active disulfides and perturbed PDI activity is characteristic of carcinomas and neurodegenerative diseases. In addition to catalytic function in oxidoreductases, redox-active disulfides are also found on a diverse array of cellular proteins and act to regulate protein activity and localization in response to oxidative changes in the local environment. These redox-active disulfides are either dynamic intramolecular protein disulfides or mixed disulfides with small-molecule thiols generating glutathionylation and cysteinylation adducts. The oxidation and reduction of redox-active disulfides are mediated by cellular reactive oxygen species and activity of reductases, such as glutaredoxin and thioredoxin. Dysregulation of cellular redox conditions and resulting changes in mixed disulfide formation are directly linked to diseases such as cardiovascular disease and Parkinson's disease.
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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.