ReviewMolecular & cellular proteomics : MCP2012
Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes.
Review in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.
- Differential alkylation-based redox proteomics--Lessons learnt.Redox biology · 2015Pooled it
- Beyond DCFH-DA: A Critical Review of Hydrogen Peroxide and Superoxide Detection Strategies in Mammalian Living Systems (2015-2026).International journal of molecular sciences · 2026Review
- Protein Oxidative Modifications in Neurodegenerative Diseases: From Advances in Detection and Modelling to Their Use as Disease Biomarkers.Antioxidants (Basel, Switzerland) · 2024Review
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Recombinant Myeloperoxidase as a New Class of Antimicrobial Agents.Microbiology spectrum · 2022Article
- Protein Lipidation Types: Current Strategies for Enrichment and Characterization.International journal of molecular sciences · 2022Review
- Automating Assignment, Quantitation, and Biological Annotation of Redox Proteomics Datasets with ProteoSushi.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The versatile utility of cysteine as a target for cancer treatment.Frontiers in oncology · 2022Review
- Proteome-wide identification of S-sulfenylated cysteines reveals metabolic response to freezing stress after cold acclimation inFrontiers in plant science · 2022Article
- Targeted protein oxidation using a chromophore-modified rapamycin analog.Chemical science · 2021Article
- Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases.Redox biology · 2021Review
- Endogenous SORedox biology · 2021Article
- Automation of On-Resin Enrichment of S-Nitrosylated Proteins for Oxidized Cysteine-Selective cPILOT.Vanderbilt undergraduate research journal : VURJ · 2021Article
- Characterization of cellular oxidative stress response by stoichiometric redox proteomics.American journal of physiology. Cell physiology · 2021Review
- Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease.International journal of molecular sciences · 2020Review
- A clickable probe for versatile characterization of S-nitrosothiols.Redox biology · 2020Article
- Redox Systems Biology: Harnessing the Sentinels of the Cysteine Redoxome.Antioxidants & redox signaling · 2020Review
- Thiol regulation by Mn porphyrins, commonly known as SOD mimics.Redox biology · 2019Review
- oxSWATH: An integrative method for a comprehensive redox-centered analysis combined with a generic differential proteomics screening.Redox biology · 2019Article
- Measurement of the total angiotensinogen and its reduced and oxidised forms in human plasma using targeted LC-MS/MS.Analytical and bioanalytical chemistry · 2019Article
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
Oxidation is a double-edged sword for cellular processes and its role in normal physiology, cancer and aging remains only partially understood. Although oxidative stress may disrupt biological function, oxidation-reduction (redox) reactions in a cell are often tightly regulated and play essential physiological roles. Cysteines lie at the interface between these extremes since the chemical properties that make specific thiols exquisitely redox-sensitive also predispose them to oxidative damage by reactive oxygen or nitrogen species during stress. Thus, these modifications can be either under reversible redox regulatory control or, alternatively, a result of reversible or irreversible oxidative damage. In either case, it has become increasingly important to assess the redox status of protein thiols since these modifications often impact such processes as catalytic activity, conformational alterations, or metal binding. To better understand the redox changes that accompany protein cysteine residues in complex biological systems, new experimental approaches have been developed to identify and characterize specific thiol modifications and/or changes in their overall redox status. In this review, we describe the recent technologies in redox proteomics that have pushed the boundaries for detecting and quantifying redox cysteine modifications in a cellular context. While there is no one-size-fits-all analytical solution, we highlight the rationale, strengths, and limitations of each technology in order to effectively apply them to specific biological questions. Several technological limitations still remain unsolved, however these approaches and future developments play an important role toward understanding the interplay between oxidative stress and redox signaling in health and disease.
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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.