必应词典为您提供s-glutathionylation的释义,网络释义: 蛋白质谷胱甘肽化;蛋白质谷胱甘多胜化;
Xiong Y, Uys JD, Tew KD, and Townsend DM. S-Glu- tathionylation: from molecular mechanisms to health out- comes. Antioxid Redox Signal 15: 233-270, 2011.Xiong Y, Uys JD, Tew KD, et al. (2011). S-glutathionylation: from molecular mechanisms to health outcomes. Antiox...
Protein S‐glutathionylation (Pr‐SSG), the reversible formation of mixed disulfides between protein cysteinyl thiol groups and glutathione, is the most stable and abundant oxidative modification of proteins, and emerging as a critical redox signaling mechanism in cardiovascular diseases (CVD). However...
S-glutathionylation is a reversible posttranslational modification of proteins, achieved by the formation of disulfide bonds between cysteine motif in the protein and the cysteine in GSH, which can lead to change in protein function, localization, and stability. ...
Recently, we have identified another unique mechanism of redox regulation of eNOS through S-glutathionylation that was shown to be important in cell signaling and vascular disease. Herein, we briefly review the mechanisms of eNOS uncoupling as well as their interrelationships and the evidence for ...
Cysteine residues are critical for the maintenance of eNOS function; we therefore speculated that oxidative stress could alter eNOS activity through S-glutathionylation. Here we show that S-glutathionylation of eNOS reversibly decreases NOS activity with an increase in O(2)(-) generation primarily ...
S-glutathionylation, the reversible protein posttranslational modification (PTM) that generates a mixed disulfide bond between glutathione and cysteine residue, critically regulates protein activity, stability and redox regulation. Due to its importance in regulating oxidative/nitrosative stress and balance ...
Moreover, this provides the intriguing potential that Ox-PTMs such as S-glutathionylation may actually protect proteins from irreversible oxidation [9,12]. Predicting which cysteine residues are redox-sensitive is complex [13]; the reactivity of the cysteine depends on the redox milieu local to ...
S-glutathionylation Hsp90 Breast cancer Post-translational modification 1. Introduction Glutathione (GSH), the thiol-containing γGlu-Cys-Gly tripeptide, is mainly involved in the defense or rescue of various oxidative damage events [1], which represents a redox-dependent post-translational modificatio...
Protein S-glutathionylation (PSSG) is a posttranslational modification that involves the conjugation of the small antioxidant molecule glutathione to cysteine residues and is emerging as a critical mechanism of redox-based signaling. PSSG levels increase under conditions of oxidative stress and are contr...