Results 21 to 30 of about 8,445 (200)

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, Yefim Manevich, Kenneth D. Tew, Danyelle M. Townsend   +3 more
doaj   +2 more sources

The emerging roles of protein glutathionylation in chloroplasts

Plant Science, 2012
Reactive oxygen species play important roles in redox signaling mainly through a set of reversible post-translational modifications of cysteine thiol residues in proteins, including glutathionylation and dithiol/disulfide exchange. Protein glutathionylation has been extensively studied in mammals but emerging evidence suggests that it can play ...
ZAFFAGNINI, MIRKO, Bedhomme M., Lemaire S. D., TROST, PAOLO BERNARDO   +3 more
openaire   +3 more sources

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, Bedhomme M., Marchand C. H., Morisse S., TROST, PAOLO BERNARDO, Lemaire S. D.   +5 more
openaire   +4 more sources

Glutathionylation in photosynthetic organisms

, 2009
Protein glutathionylation is a reversible posttranslational modification promoted by oxidative and nitrosative stresses and consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue. This modification can protect specific cysteines from irreversible oxidation but can also modulate protein activities, either ...
Gao XG, Bedhomme M, Michelet L, ZAFFAGNINI, MIRKO, Lemaire S.D.   +4 more
openaire   +2 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   +4 more sources

Protein Glutathionylation in Erythrocytes [PDF]

Clinical Chemistry, 2003
Analysis of antioxidant molecules is potentially important to understanding the role of oxidative stress (1)(2)(3)(4)(5)(6) in disease, as oxidative damage is accompanied or preceded by their depletion. Reduced glutathione (GSH) is ubiquitous and abundant; it can be oxidized to its disulfide form (GSSG) in response to an oxidative perturbation ...
Giustarini, D., Dalle Donne, I., Colombo, R., Petralia, S., Giampaoletti, S., Milzani, A., Rossi, Ranieri   +6 more
openaire   +3 more sources

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, Milzani, Aldo, Dalle-Donne, Isabella, Rossi, Ranieri   +3 more
openaire   +5 more sources

Protein kinase function and glutathionylation [PDF]

Biochemical Journal, 2004
Intracellular reactive oxygen species are generated as a by-product of normal metabolic processes and can both damage cellular constituents and function as important signalling species. This signalling often involves changes in the thiol redox balance.
Anthony N, Anselmo, Melanie H, Cobb
openaire   +2 more sources

The redox mechanism for vascular barrier dysfunction associated with metabolic disorders: Glutathionylation of Rac1 in endothelial cells

Redox Biology, 2016
Background: Oxidative stress is implicated in increased vascular permeability associated with metabolic disorders, but the underlying redox mechanism is poorly defined.
Jingyan Han, Robert M. Weisbrod, Di Shao, Yosuke Watanabe, Xiaoyan Yin, Markus M. Bachschmid, Francesca Seta, Yvonne M.W. Janssen-Heininger, Reiko Matsui, Mengwei Zang, Naomi M. Hamburg, Richard A. Cohen   +11 more
doaj   +1 more source

Alcohol Binge Drinking Selectively Stimulates Protein S-Glutathionylation in Aorta and Liver of ApoE−/− Mice

Frontiers in Cardiovascular Medicine, 2021
Background: Binge drinking has become the most common and deadly pattern of excessive alcohol use in the United States, especially among younger adults. It is closely related to the increased risk of cardiovascular disease.
Kerstin Seidel, Xueping Wan, Mo Zhang, Yuxiang Zhou, Mengwei Zang, Mengwei Zang, Jingyan Han   +6 more
doaj   +1 more source