ReviewAntioxidants (Basel, Switzerland)2022
Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.
Review in Antioxidants (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Evolutionary divergence of nocturnin led to redox regulation in mammalian orthologs.Biochemistry and biophysics reports · 2026Article
- 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
- Defining and refining the cysteine redoxome through sulfur chemical biology.Nature chemical biology · 2026Review
- NLRP3 Inflammasome Activation in Oxidative Stress: A Key Mechanism Driving Neuroinflammation.Neuroimmunomodulation · 2026Review
- Car4-positive adipocyte progenitor cells adapt to the aging environment and work as protection against ROS via glutathione metabolism.Scientific reports · 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
- Loss of CD98HC phosphorylation by ATM impairs antiporter trafficking and drives glutamate toxicity in Ataxia telangiectasia.Nature communications · 2025Article
- In-depth characterization of S-glutathionylation in ventricular myosin light chain 1 across species by top-down proteomics.Journal of molecular and cellular cardiology · 2025Article
- Structural, functional, and regulatory evaluation of a cysteine post-translationally modified Gcn5-related N-acetyltransferase.Biochemical and biophysical research communications · 2025Article
- Using Redox Proteomics to Gain New Insights into Neurodegenerative Disease and Protein Modification.Antioxidants (Basel, Switzerland) · 2024Review
- Glutathione and Glutaredoxin-Key Players in Cellular Redox Homeostasis and Signaling.Antioxidants (Basel, Switzerland) · 2023Review
- Mechanistic insights into the biological activity of S-Sulfocysteine in CHO cells using a multi-omics approach.Frontiers in bioengineering and biotechnology · 2023Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein S-glutathionylation (SSG) is a reversible post-translational modification (PTM) featuring the conjugation of glutathione to a protein cysteine thiol. SSG can alter protein structure, activity, subcellular localization, and interaction with small molecules and other proteins. Thus, it plays a critical role in redox signaling and regulation in various physiological activities and pathological events. In this review, we summarize current biochemical and analytical approaches for characterizing SSG at both the proteome level and at individual protein levels. To illustrate the mechanism underlying SSG-mediated redox regulation, we highlight recent examples of functional and structural consequences of SSG modifications. Finally, we discuss the analytical challenges in characterizing SSG and the thiol PTM landscape, future directions for understanding of the role of SSG in redox signaling and regulation and its interplay with other PTMs, and the potential role of computational approaches to accelerate functional discovery.
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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.