ReviewJournal of molecular and cellular cardiology2012
Protein S-glutathiolation: redox-sensitive regulation of protein function.
Review in Journal of molecular and cellular cardiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
51 citing papers in PubMed, 120 citations in OpenAlex.
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- Glutathionyl Hemoglobin and Its Emerging Role as a Clinical Biomarker of Chronic Oxidative Stress.Antioxidants (Basel, Switzerland) · 2023Review
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- Tip110 Expression Facilitates the Release of HEXIM1 and pTEFb from the 7SK Ribonucleoprotein Complex Involving Regulation of the Intracellular Redox Level.Aging and disease · 2021Article
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- Redox and Antioxidant Modulation of Circadian Rhythms: Effects of Nitroxyl, N-Acetylcysteine and Glutathione.Molecules (Basel, Switzerland) · 2021Article
- Evaluation of Cysteine Metabolism in the Rat Liver and Kidney Following Intravenous Cocaine Administration and Abstinence.Antioxidants (Basel, Switzerland) · 2021Article
- Mitochondrial Glutathione: Recent Insights and Role in Disease.Antioxidants (Basel, Switzerland) · 2020Review
- Reactive Oxygen Species and Antioxidant Defense in Plants under Abiotic Stress: Revisiting the Crucial Role of a Universal Defense Regulator.Antioxidants (Basel, Switzerland) · 2020Review
- xCT (SLC7A11) expression confers intrinsic resistance to physical plasma treatment in tumor cells.Redox biology · 2020Article
- GSTpi regulates VE-cadherin stabilization through promoting S-glutathionylation of Src.Redox biology · 2020Article
- Circadian rhythm of redox state regulates membrane excitability in hippocampal CA1 neurons.The European journal of neuroscience · 2020Article
- Metabolic Dysregulation Contributes to the Progression of Alzheimer's Disease.Frontiers in neuroscience · 2020Review
- Antidiabetic and cardiovascular beneficial effects of a liver-localized mitochondrial uncoupler.Nature communications · 2019Article
- Myalgic encephalomyelitis or chronic fatigue syndrome: how could the illness develop?Metabolic brain disease · 2019Review
- Cardiac Resynchronisation Therapy and Cellular Bioenergetics: Effects Beyond Chamber Mechanics.European cardiology · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Reversible protein S-glutathiolation has emerged as an important mechanism of post-translational modification. Under basal conditions several proteins remain adducted to glutathione, and physiological glutathiolation of proteins has been shown to regulate protein function. Enzymes that promote glutathiolation (e.g., glutathione-S-transferase-P) or those that remove glutathione from proteins (e.g., glutaredoxin) have been identified. Modification by glutathione has been shown to affect protein catalysis, ligand binding, oligomerization and protein-protein interactions. Conditions associated with oxidative or nitrosative stress, such as ischemia-reperfusion, hypertension and tachycardia increase protein glutathiolation via changes in the glutathione redox status (GSH/GSSG) or through the formation of sulfenic acid (SOH) or nitrosated (SNO) cysteine intermediates. These "activated" thiols promote reversible S-glutathiolation of key proteins involved in cell signaling, energy production, ion transport, and cell death. Hence, S-glutathiolation is ideally suited for integrating and mounting fine-tuned responses to changes in the redox state. S-glutathiolation also provides a temporary glutathione "cap" to protect protein thiols from irreversible oxidation and it could be an important mechanism of protein "encryption" to maintain proteins in a functionally silent state until they are needed during conditions of stress. Current evidence suggests that the glutathiolation-deglutathiolation cycle integrates and interacts with other post-translational mechanisms to regulate signal transduction, metabolism, inflammation, and apoptosis. This article is part of a Special Section entitled "Post-translational Modification."
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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.