Results 11 to 20 of about 8,996 (206)
Cell Reports, 2017 Reactive oxygen species (ROS)-induced cysteine S-glutathionylation is an important posttranslational modification (PTM) that controls a wide range of intracellular protein activities.
Xue Zhang +23 more
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S-Glutathionylation of metallothioneins by nitrosative/oxidative stress
Experimental Gerontology, 2008 Cystein residues within metallothionein (MT) structure have been shown to be particularly prone to S-nitrosylation. The objective of this study was to examine the possibility that MTs undergo S-glutathionylation under nitrosative/oxidative stress. MT from rabbit liver was treated with different concentrations of GSNO, diamide plus GSH or H(2)O(2) plus ...
CASADEI M +4 more
core +7 more sources
Detection of Protein Glutathionylation
, 2009 Recent studies indicate that protein glutathionylation is an important regulatory mechanism. The develop-ment of redox proteomics techniques to identify proteins undergoing glutathionylation has a key role in defining the importance of this post-translational modification, although the available methods are not yet comparable to those for the study of ...
E. Gianazza, I. Eberini, P. Ghezzi
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S-Glutathionylation of Protein Disulfide Isomerase Regulates Estrogen Receptor α Stability and Function [PDF]
International Journal of Cell Biology, 2012 S-Glutathionylation of cysteine residues within target proteins is a posttranslational modification that alters structure and function. We have shown that S-glutathionylation of protein disulfide isomerase (PDI) disrupts protein folding and leads to the ...
Ying Xiong +3 more
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S-glutathionylation in protein redox regulation
Free Radical Biology and Medicine, 2007 Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and low-pKa cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative stress, but also occurs under basal (physiological) conditions. S-glutathionylation has now emerged as a potential mechanism for dynamic, posttranslational regulation
Dalle Donne, I. +4 more
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Glutathionylation pathways in drug response
Current Opinion in Pharmacology, 2007 Regulation of protein function through post-translational modifications (PTM) can be important pharmacological target, and there are drugs developed to modulate specific PTM such as protein kinase or histone deacetylase inhibitors. We are still far behind in considering protein glutathionylation as pharmacological target as the biological consequences ...
Ghezzi, Pietro, Di Simplicio, Paolo
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Glyoxalase II promotes "in vitro" S-glutathionylation
Free Radical Biology and Medicine, 2014 S-glutathionylation involves the reversible formation of a mix disulphide-bridge between specific cysteine and a molecule of glutathione, the major non-protein antioxidant compound in the cell. Mechanisms of protein S-glutathionylation are far to be completely understood and several reactions can promote it, either spontaneously or catalyzed.
Laura, Cianfruglia +6 more
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Glutathionylation of dengue and Zika NS5 proteins affects guanylyltransferase and RNA dependent RNA polymerase activities. [PDF]
PLoS ONE, 2018 It has been estimated for dengue infection that the global population at risk is 3.5 billion people, which makes dengue an important public health problem. The causative agents of dengue are dengue viruses.
Chonticha Saisawang +4 more
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A novel approach for predicting protein S-glutathionylation [PDF]
BMC Bioinformatics, 2020 Background S-glutathionylation is the formation of disulfide bonds between the tripeptide glutathione and cysteine residues of the protein, protecting them from irreversible oxidation and in some cases causing change in their functions.
Anastasia A. Anashkina +6 more
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Redox Regulation in Photosynthetic Organisms: Focus on Glutathionylation
Antioxidants & Redox Signaling, 2012 In photosynthetic organisms, besides the well-established disulfide/dithiol exchange reactions specifically controlled by thioredoxins (TRXs), protein S-glutathionylation is emerging as an alternative redox modification occurring under stress conditions.
ZAFFAGNINI, MIRKO +5 more
openaire +4 more sources