ReviewJournal of cellular biochemistry2013
Emerging mechanisms of glutathione-dependent chemistry in biology and disease.
Review in Journal of cellular biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
21 citing papers in PubMed, 43 citations in OpenAlex.
- Identification of metabolism-associated molecular classification and prognostic genes for medulloblastoma based on bioinformatics analysis.Clinics (Sao Paulo, Brazil) · 2026Article
- Methionine restriction for cancer therapy: From preclinical studies to clinical trials.Cancer pathogenesis and therapy · 2026Review
- Methionine restriction in cancer: a dietary insight for therapy.Frontiers in nutrition · 2026Review
- Glutathione-Dependent Pathways in Cancer Cells.International journal of molecular sciences · 2024Review
- The Multifaceted Role of Glutathione S-Transferases in Health and Disease.Biomolecules · 2023Review
- Article
- Oxidized GAPDH transfers S-glutathionylation to a nuclear protein Sirtuin-1 leading to apoptosis.Free radical biology & medicine · 2021Article
- Glutathionylation Decreases Methyltransferase Activity of PRMT5 and Inhibits Cell Proliferation.Molecular & cellular proteomics : MCP · 2020Article
- Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease.International journal of molecular sciences · 2020Review
- Association between Metabolites and the Risk of Lung Cancer: A Systematic Literature Review and Meta-Analysis of Observational Studies.Metabolites · 2020Review
- Endoplasmic reticulum stress and glutathione therapeutics in chronic lung diseases.Redox biology · 2020Review
- Methionine Restriction and Cancer Biology.Nutrients · 2020Review
- Thiol regulation by Mn porphyrins, commonly known as SOD mimics.Redox biology · 2019Review
- GlutathioneScience signaling · 2019Article
- Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker.Free radical biology & medicine · 2016Article
- S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- The cytoskeletal arrangements necessary to neurogenesis.Oncotarget · 2016Review
- c-Myc and AMPK Control Cellular Energy Levels by Cooperatively Regulating Mitochondrial Structure and Function.PloS one · 2015Article
- Aging alters circadian regulation of redox in Drosophila.Frontiers in genetics · 2015Article
- Upregulation of capacity for glutathione synthesis in response to amino acid deprivation: regulation of glutamate-cysteine ligase subunits.Amino acids · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione disulfide is considered a classical parameter of oxidative stress that is increased in diseases. Recent studies have emerged that demonstrate that glutathione plays a more direct role in biological and pathophysiological processes through covalent modification to reactive cysteines within proteins, a process known as S-glutathionylation. The formation of an S-glutathionylated moiety within the protein can lead to structural and functional modifications. Activation, inactivation, loss of function, and gain of function have all been attributed to S-glutathionylation. In pathophysiological settings, S-glutathionylation is tightly regulated. This perspective offers a concise overview of the emerging field of protein thiol redox modifications. We will also cover newly developed methodology to detect S-glutathionylation in situ, which will enable further discovery into the role of S-glutathionylation in biology and disease.
Indexed as
Identifiers
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.