ReviewMolecular bioSystems2017
Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.
Review in Molecular bioSystems, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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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
30 citing papers in PubMed, 72 citations in OpenAlex.
- Thiol post-translational modifications modulate allosteric regulation of the OpcA-G6PDH complex through conformational gate control.Protein science : a publication of the Protein Society · 2026Article
- CFEM proteins: unique to fungi with essential roles in plant host interactions.Frontiers in fungal biology · 2026Review
- More questions than answers: insights into potential cysteine-rich receptor-like kinases redox signalling in Arabidopsis.The Plant journal : for cell and molecular biology · 2025Review
- Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications.Food chemistry: X · 2025Article
- Post-translational modifications of proteins in cardiovascular diseases examined by proteomic approaches.The FEBS journal · 2025Review
- Using Redox Proteomics to Gain New Insights into Neurodegenerative Disease and Protein Modification.Antioxidants (Basel, Switzerland) · 2024Review
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Arsenic co-carcinogenesis: Inhibition of DNA repair and interaction with zinc finger proteins.Seminars in cancer biology · 2021Review
- Cys-SH based quantitative redox proteomics of salt induced response in sugar beet monosomic addition line M14.Botanical studies · 2021Article
- Review
- Bull Sperm Capacitation Is Accompanied by Redox Modifications of Proteins.International journal of molecular sciences · 2021Article
- Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation.Journal of visualized experiments : JoVE · 2021Article
- Contemporary proteomic strategies for cysteine redoxome profiling.Plant physiology · 2021Review
- Mapping the plant proteome: tools for surveying coordinating pathways.Emerging topics in life sciences · 2021Review
- Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.Antioxidants (Basel, Switzerland) · 2021Review
- Characterization of cellular oxidative stress response by stoichiometric redox proteomics.American journal of physiology. Cell physiology · 2021Review
- Covalent Modification of Proteins by Plant-Derived Natural Products: Proteomic Approaches and Biological Impacts.Proteomics · 2021Review
- The Central Role of Redox-Regulated Switch Proteins in Bacteria.Frontiers in molecular biosciences · 2021Review
- 3D interaction homology: Hydropathic interaction environments of serine and cysteine are strikingly different and their roles adapt in membrane proteins.Current research in structural biology · 2021Article
- Vimentin S-glutathionylation at Cys328 inhibits filament elongation and induces severing of mature filaments in vitro.The FEBS journal · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein thiols play a crucial role in redox signaling, in the regulation of enzymatic activity and protein function, and in maintaining redox homeostasis in living systems. The unique chemical reactivity of the thiol group makes protein cysteines susceptible to reactions with reactive oxygen and nitrogen species that form various reversible and irreversible post-translational modifications (PTMs). The reversible PTMs in particular are major components of redox signaling and are involved in the regulation of various cellular processes under physiological and pathological conditions. The biological significance of these redox PTMs in both healthy and disease states has been increasingly recognized. Herein, we review recent advances in quantitative proteomic approaches for investigating redox PTMs in complex biological systems, including general considerations of sample processing, chemical or affinity enrichment strategies, and quantitative approaches. We also highlight a number of redox proteomic approaches that enable effective profiling of redox PTMs for specific biological applications. Although technical limitations remain, redox proteomics is paving the way to a better understanding of redox signaling and regulation in both healthy and disease states.
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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.