ArticleProceedings of the National Academy of Sciences of the United States of America2008
Quantifying changes in the thiol redox proteome upon oxidative stress in vivo.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 255 papers, 1 of them a synthesis that pooled it.
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Who cites it
255 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Differential alkylation-based redox proteomics--Lessons learnt.Redox biology · 2015Pooled it
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- Integrated analysis of the redoxome and zinc proteome links ribosomal protein oxidation to zinc homeostasis.Redox biology · 2026Article
- Cryptic DNA sequences encode a temperature sensor to regulate mitochondrial suicide during neuronal differentiation.Cell communication and signaling : CCS · 2026Article
- Defining and refining the cysteine redoxome through sulfur chemical biology.Nature chemical biology · 2026Review
- Chemical Proteomics Reveals Regulation of Bile Salt Hydrolases via Oxidative Post-translational Modifications.Journal of the American Chemical Society · 2026Article
- Future Research Directions on Mycobacterium tuberculosis Proteins.Advances in experimental medicine and biology · 2026Review
- Chemical proteomics reveals regulation of bile salt hydrolases via oxidative post-translational modifications.bioRxiv : the preprint server for biology · 2025Article
- SICyLIA-cTMT dissects redox proteome dynamics with high accuracy and depth at microgram scale.Cell reports methods · 2025Article
- Beyond Antioxidants: How Redox Pathways Shape Cellular Signaling and Disease Outcomes.Antioxidants (Basel, Switzerland) · 2025Review
- Involvement of Oxidative Stress in Mitochondrial Abnormalities During the Development of Heart Disease.Biomedicines · 2025Review
- Redox Mechanisms Driving Skin Fibroblast-to-Myofibroblast Differentiation.Antioxidants (Basel, Switzerland) · 2025Article
- The assessment of thiol-disulfide homeostasis and ıschemia-modified albumin levels in patients with acromegaly.Pituitary · 2025Article
- Promising tools into oxidative stress: A review of non-rodent model organisms.Redox biology · 2024Review
- Chemoproteogenomic stratification of the missense variant cysteinome.Nature communications · 2024Article
- Multifaceted Proteome Analysis at Solubility, Redox, and Expression Dimensions for Target Identification.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024Review
- Mitochondrial ribosome biogenesis and redox sensing.FEBS open bio · 2024Review
- Ten "Cheat Codes" for Measuring Oxidative Stress in Humans.Antioxidants (Basel, Switzerland) · 2024Review
195 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors.
Funding
Abstract
Antimicrobial levels of reactive oxygen species (ROS) are produced by the mammalian host defense to kill invading bacteria and limit bacterial colonization. One main in vivo target of ROS is the thiol group of proteins. We have developed a quantitative thiol trapping technique termed OxICAT to identify physiologically important target proteins of hydrogen peroxide (H(2)O(2)) and hypochlorite (NaOCl) stress in vivo. OxICAT allows the precise quantification of oxidative thiol modifications in hundreds of different proteins in a single experiment. It also identifies the affected proteins and defines their redox-sensitive cysteine(s). Using this technique, we identified a group of Escherichia coli proteins with significantly (30-90%) oxidatively modified thiol groups, which appear to be specifically sensitive to either H(2)O(2) or NaOCl stress. These results indicate that individual oxidants target distinct proteins in vivo. Conditionally essential E. coli genes encode one-third of redox-sensitive proteins, a finding that might explain the bacteriostatic effect of oxidative stress treatment. We identified a select group of redox-regulated proteins, which protect E. coli against oxidative stress conditions. These experiments illustrate that OxICAT, which can be used in a variety of different cell types and organisms, is a powerful tool to identify, quantify, and monitor oxidative thiol modifications in vivo.
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