Results 121 to 130 of about 6,811 (158)

Vimentin S-glutathionylation at Cys328 inhibits filament elongation and induces severing of mature filaments in vitro. [PDF]

FEBS J, 2020
Kaus-Drobek M, Mücke N, Szczepanowski RH, Wedig T, Czarnocki-Cieciura M, Polakowska M, Herrmann H, Wysłouch-Cieszyńska A, Dadlez M.   +8 more
europepmc   +1 more source

Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells. [PDF]

FASEB J, 2020
Watanabe Y, Watanabe K, Fujioka D, Nakamura K, Nakamura T, Uematsu M, Bachschmid MM, Matsui R, Kugiyama K.   +8 more
europepmc   +1 more source

Implication of <i>S</i>-d-Lactoylglutathione in the Spontaneous Cysteine <i>S</i>-Glutathionylation and Lysine <i>N</i>-Lactoylation of <i>Arabidopsis thaliana</i> NAD-Dependent Glyceraldehyde-3-Phosphate Dehydrogenase. [PDF]

Int J Mol Sci
Clément C, Dorion S, Bykova NV, Fetterley V, Branchini E, Boutin C, Cappadocia L, Rivoal J.   +7 more
europepmc   +1 more source

Is there a role for S-glutathionylation of proteins in human disease?

, 2005
DALLE DONNE I, ROSSI, RANIERI, GIUSTARINI D, COLOMBO R, AND MILZANI A.   +4 more
openaire   +2 more sources

S-Glutathionylation signaling in cell biology: Progress and prospects

European Journal of Pharmaceutical Sciences, 2012
S-Glutathionylation is a mechanism of signal transduction by which cells respond effectively and reversibly to redox inputs. The glutathionylation regulates most cellular pathways. It is involved in oxidative cellular response to insult by modulating the transcription factor Nrf2 and inducing the expression of antioxidant genes (ARE); it contributes to
Anna Pastore, Fiorella Piemonte
exaly   +3 more sources

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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., Rossi, Ranieri, Giustarini, D., Colombo, R., MilzaniI, A.   +4 more
openaire   +5 more sources

First Proteomic Study of S-Glutathionylation in Cyanobacteria

Journal of Proteome Research, 2014
Glutathionylation, the reversible post-translational formation of a mixed disulfide between a cysteine residue and glutathione (GSH), is a crucial mechanism for signal transduction and regulation of protein function. Until now this reversible redox modification was studied mainly in eukaryotic cells.
Chardonnet, Solenne, Sakr, Samer, Cassier-Chauvat, Corinne, Le Maréchal, Pierre, Chauvat, Franck, Lemaire, Stéphane D, Decottignies, Paulette   +6 more
openaire   +3 more sources

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, Roberta, Galeazzi, Luca, Massaccesi, Raffaele, Spaccini, M Luisa, Caniglia, Giovanni, Principato, Tatiana, Armeni   +6 more
openaire   +2 more sources

S-glutathionylation regulates GTP-binding of Rac2

Biochemical and Biophysical Research Communications, 2012
Phagocyte NADPH oxidase catalyzes the reduction of molecular oxygen to superoxide and is essential for defense against microbes. Rac2 is a low molecular weight GTP-binding protein that has been implicated in the regulation of phagocyte NADPH oxidase. Here we report that Cys(157) of Rac2 is a target of S-glutathionylation and that this modification is ...
In Sup, Kil, Seoung Woo, Shin, Jeen-Woo, Park   +2 more
openaire   +2 more sources