S-glutathionylation, friend or foe in cardiovascular health and disease [PDF]
Redox Biology, 2020 Glutathione is a low molecular weight thiol that is present at high levels in the cell. The high levels of glutathione in the cell make it one of the most abundant antioxidants contributing to cellular redox homeostasis.
N.A. Rashdan, B. Shrestha, C.B. Pattillo
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S-glutathionylation reactions in mitochondrial function and disease [PDF]
Frontiers in Cell and Developmental Biology, 2014 Mitochondria are highly efficient energy-transforming organelles that convert energy stored in carbon bonds into the universal energy currency ATP. The production of ATP by mitochondria is dependent on oxidation of nutrients and coupling of exergonic ...
Ryan J. Mailloux, William G. Willmore
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Prediction of S-glutathionylation sites based on protein sequences. [PDF]
PLoS ONE, 2013 S-glutathionylation, the reversible formation of mixed disulfides between glutathione(GSH) and cysteine residues in proteins, is a specific form of post-translational modification that plays important roles in various biological processes, including ...
Chenglei Sun +4 more
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Activation of Nrf2 at Critical Windows of Development Alters Tissue-Specific Protein S-Glutathionylation in the Zebrafish (Danio rerio) Embryo [PDF]
AntioxidantsActivation of Nrf2—the master regulator of antioxidative response—at different stages of embryonic development has been shown to result in changes in gene expression, but the tissue-specific and downstream effects of Nrf2 activation during development ...
Emily S. Marques +4 more
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Dicarbonyl Stress and S-Glutathionylation in Cerebrovascular Diseases: A Focus on Cerebral Cavernous Malformations [PDF]
Antioxidants, 2020 Dicarbonyl stress is a dysfunctional state consisting in the abnormal accumulation of reactive α-oxaldehydes leading to increased protein modification.
Cinzia Antognelli +4 more
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Redox regulation of the proteasome via S-glutathionylation
Redox Biology, 2014 The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis.
Marilene Demasi +9 more
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Fusaric acid-mediated S-glutathionylation of MaAKT1 channel confers the virulence of Foc TR4 to banana. [PDF]
PLoS PathogensOur previous studies have demonstrated that the phytotoxin fusaric acid (FSA), secreted by several Fusarium species, acts as a key factor in the development of plant diseases; however, the underlying mechanism remains unknown.
Jun Zhang +7 more
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Protein S-glutathionylation confers cellular resistance to ferroptosis induced by glutathione depletion [PDF]
Redox BiologyFerroptosis is one of the most critical biological consequences of glutathione depletion. Excessive oxidative stress, indicated by an elevated oxidized glutathione (GSSG)/reduced glutathione (GSH) ratio, is recognized as a key driver of ferroptosis ...
Yi Ju +20 more
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Measurement of S-glutathionylated proteins by HPLC [PDF]
Amino Acids, 2021 AbstractS-glutathionylated proteins (GSSP), i.e., protein-mixed disulfides with glutathione (GSH), are considered a suitable biomarker of oxidative stress. In fact, they occur within cells at low level and their concentration increases markedly under pro-oxidant conditions.
Giustarini, Daniela +3 more
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Oxidized GAPDH transfers S-glutathionylation to a nuclear protein Sirtuin-1 leading to apoptosis [PDF]
Free Radical Biology and Medicine, 2021 Syed Husain Mustafa Rizvi +2 more
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