ReviewAntioxidants & redox signaling2008
Molecular mechanisms and clinical implications of reversible protein S-glutathionylation.
Review in Antioxidants & redox signaling, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 259 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.
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.
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Who cites it
259 citing papers in PubMed, 524 citations in OpenAlex.
- Organ-specific redox imbalances in spinal muscular atrophy mice are partially rescued by SMN antisense oligonucleotides.FEBS letters · 2026Article
- ARHGEF7 S-glutathionylation promotes cancer cell migration through Rac1 activation.bioRxiv : the preprint server for biology · 2026Article
- Redox regulation of cell migration via Nischarin S-glutathionylation.Free radical biology & medicine · 2026Article
- Energy stress-induced PKCζ S-glutathionylation is essential for LKB1 cytoplasmic translocation and AMPK activation.Life metabolism · 2025Article
- Redox Potential (EMolecules (Basel, Switzerland) · 2025Article
- An In Vitro Study of Protein S-Glutathionylation by Members of the CLIC Protein Family.Biomolecules · 2025Article
- Genome-wide identification and expression analysis of glutaredoxin in Puccinellia tenuiflora under salinity stress.BMC plant biology · 2025Article
- Polysulfides promote protein disulfide bond formation in microorganisms growing under anaerobic conditions.Applied and environmental microbiology · 2025Article
- Implication of Thioredoxin 1 and Glutaredoxin 1 in HCurrent molecular medicine · 2025Article
- Protein Oxidative Modifications in Neurodegenerative Diseases: From Advances in Detection and Modelling to Their Use as Disease Biomarkers.Antioxidants (Basel, Switzerland) · 2024Review
- Glutaredoxin 2 Protein (Grx2) as an Independent Prognostic Factor Associated with the Survival of Colon Adenocarcinoma Patients.International journal of molecular sciences · 2024Article
- Exploring the Role of Unconventional Post-Translational Modifications in Cancer Diagnostics and Therapy.Current protein & peptide science · 2024Review
- Glutathione Non-Covalent Binding Sites on Hemoglobin and Major Glutathionylation Target betaCys93 Are Conservative among Both Hypoxia-Sensitive and Hypoxia-Tolerant Mammal Species.International journal of molecular sciences · 2023Article
- Glutaredoxin-1 alleviates acetaminophen-induced liver injury by decreasing its toxic metabolites.Journal of pharmaceutical analysis · 2023Article
- Glutathionyl Hemoglobin and Its Emerging Role as a Clinical Biomarker of Chronic Oxidative Stress.Antioxidants (Basel, Switzerland) · 2023Review
- Nuclear factor kappa B expression in non-small cell lung cancer.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023Review
- Combination of On-Line and Off-Line Two-Dimensional Liquid Chromatography-Mass Spectrometry for Comprehensive Characterization of mAb Charge Variants and Precise Instructions for Rapid Process Development.International journal of molecular sciences · 2023Article
- Changes in Hemoglobin Properties in Complex with Glutathione and after Glutathionylation.International journal of molecular sciences · 2023Article
- Glutathione and Glutaredoxin-Key Players in Cellular Redox Homeostasis and Signaling.Antioxidants (Basel, Switzerland) · 2023Review
- Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023Review
199 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Sulfhydryl chemistry plays a vital role in normal biology and in defense of cells against oxidants, free radicals, and electrophiles. Modification of critical cysteine residues is an important mechanism of signal transduction, and perturbation of thiol-disulfide homeostasis is an important consequence of many diseases. A prevalent form of cysteine modification is reversible formation of protein mixed disulfides (protein-SSG) with glutathione (GSH). The abundance of GSH in cells and the ready conversion of sulfenic acids and S-nitroso derivatives to S-glutathione mixed disulfides suggests that reversible S-glutathionylation may be a common feature of redox signal transduction and regulation of the activities of redox sensitive thiol-proteins. The glutaredoxin enzyme has served as a focal point and important tool for evolution of this regulatory mechanism, because it is a specific and efficient catalyst of protein-SSG deglutathionylation. However, mechanisms of control of intracellular Grx activity in response to various stimuli are not well understood, and delineation of specific mechanisms and enzyme(s) involved in formation of protein-SSG intermediates requires further attention. A large number of proteins have been identified as potentially regulated by reversible S-glutathionylation, but only a few studies have documented glutathionylation-dependent changes in activity of specific proteins in a physiological context. Oxidative stress is a hallmark of many diseases which may interrupt or divert normal redox signaling and perturb protein-thiol homeostasis. Examples involving changes in S-glutathionylation of specific proteins are discussed in the context of diabetes, cardiovascular and lung diseases, cancer, and neurodegenerative diseases.
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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.