ArticleJournal of proteomics & bioinformatics2011
Protein Cysteines Map to Functional Networks According to Steady-state Level of Oxidation.
Article in Journal of proteomics & bioinformatics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 52 citations in OpenAlex.
- ROMO1 overexpression protects the mitochondrial cysteinome from oxidations in aging.Nature communications · 2025Article
- Redox organization of living systems.Free radical biology & medicine · 2024Review
- Ageing-dependent thiol oxidation reveals early oxidation of proteins with core proteostasis functions.Life science alliance · 2024Article
- 3-Mercaptopyruvate sulfur transferase is a protein persulfidase.Nature chemical biology · 2023Article
- Article
- Redox Post-translational Modifications of Protein Thiols in Brain Aging and Neurodegenerative Conditions-Focus on S-Nitrosation.Frontiers in aging neuroscience · 2020Review
- Review
- Quantification of cellular protein and redox imbalance using SILAC-iodoTMT methodology.Redox biology · 2019Article
- Redox regulation of type-I inositol trisphosphate receptors in intact mammalian cells.The Journal of biological chemistry · 2018Article
- Selenium at the redox interface of the genome, metabolome and exposome.Free radical biology & medicine · 2018Review
- Target identification reveals protein arginine methyltransferase 1 is a potential target of phenyl vinyl sulfone and its derivatives.Bioscience reports · 2018Article
- Quantitative proteomics identifies redox switches for global translation modulation by mitochondrially produced reactive oxygen species.Nature communications · 2018Article
- Redox environment in stem and differentiated cells: A quantitative approach.Redox biology · 2017Article
- Redox theory of aging: implications for health and disease.Clinical science (London, England : 1979) · 2017Review
- A Direct Comparison of Metabolic Responses to High-Fat Diet in C57BL/6J and C57BL/6NJ Mice.Diabetes · 2016Article
- Mitochondrial thiol modification by a targeted electrophile inhibits metabolism in breast adenocarcinoma cells by inhibiting enzyme activity and protein levels.Redox biology · 2016Article
- Hydrogen peroxide and central redox theory for aerobic life: A tribute to Helmut Sies: Scout, trailblazer, and redox pioneer.Archives of biochemistry and biophysics · 2016Article
- The balance of powers: Redox regulation of fibrogenic pathways in kidney injury.Redox biology · 2015Review
- Redox theory of aging.Redox biology · 2015Review
- The cysteine proteome.Free radical biology & medicine · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The cysteine (Cys) proteome serves critical roles in protein structure, function and regulation, and includes key targets in oxidative mechanisms of disease. Thioredoxins maintain Cys residues in thiol forms, and previous research shows that the redox potential of thioredoxin in mitochondria and nuclei is more reduced than cytoplasm, suggesting that proteins in these compartments may have different steady-state oxidation. This study measured fractional oxidation of 641 peptidyl Cys residues from 333 proteins in HT29 cells by mass spectrometry. Average oxidation of cytoplasmic, nuclear and mitochondrial proteins was similar (15.8, 15.5, 14%, respectively). Pathway analysis showed that more reduced cytoplasmic Cys were in proteins associated with the cytoskeleton, more reduced nuclear Cys with Ran signaling and RNA post-transcriptional modifcation, and more reduced mitochondrial Cys with energy metabolism, cell growth and cell proliferation. More oxidized cytoplasmic Cys included associations with PI3/Akt, Myc-mediated apoptosis and 14-3-3-mediated signaling. Weaker associations of oxidized nuclear and mitochondrial Cys occurred with granzyme B signaling and intermediary metabolism, respectively. Thus, steady-state peptidyl Cys oxidation is associated with functional pathways rather than simply with organellar distribution. This suggests that oxidative mechanisms of disease could target functional pathways or networks rather than individual proteins or subcellular compartments.
Identifiers
What OpenQuestion holds
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.