Results 21 to 30 of about 8,996 (206)

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

Glutathionylation mediates angiotensin II-induced eNOS uncoupling, amplifying NADPH oxidase-dependent endothelial dysfunction. [PDF]

, 2023
BACKGROUND: Glutathionylation of endothelial nitric oxide synthase (eNOS) "uncouples" the enzyme, switching its function from nitric oxide (NO) to O2(•-) generation.
Kok, C, Nunez, A, Fry, NAS, Hawkins, CL, Davies, MJ, Rasmussen, HH, Liu, C-C, Figtree, GA, Galougahi, KK, Garcia, A, Gentile, C   +10 more
core   +1 more source

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

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

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

Post-translational S-glutathionylation of cofilin increases actin cycling during cocaine seeking.

PLoS ONE, 2019
Neuronal defense against oxidative damage is mediated primarily by the glutathione redox system. Traditionally considered a mechanism to protect proteins from irreversible oxidation, mounting evidence supports a role for protein S-glutathionylation in ...
Anna Kruyer, Lauren E Ball, Danyelle M Townsend, Peter W Kalivas, Joachim D Uys   +4 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

Novel control of cardiac myofilament response to calcium by S-glutahionylation at specific sites of myosin binding protein C

Frontiers in Physiology, 2013
Our previous studies demonstrated a relation between glutathionylation of cardiac myosin binding protein C and diastolic dysfunction in a hypertensive mouse model stressed by treatment with salt, deoxycorticosterone acetate, and unilateral nephrectomy.
Bindiya G Patel, Tanganyika eWilder, R. John Solaro   +2 more
doaj   +1 more source

Conditions Conducive to the Glutathionylation of Complex I Subunit NDUFS1 Augment ROS Production following the Oxidation of Ubiquinone Linked Substrates, Glycerol-3-Phosphate and Proline

Antioxidants, 2022
Mitochondrial complex I can produce large quantities of reactive oxygen species (ROS) by reverse electron transfer (RET) from the ubiquinone (UQ) pool.
Kevin Wang, Jonathan Hirschenson, Amanda Moore, Ryan J. Mailloux   +3 more
doaj   +1 more source

Peroxiredoxin promotes longevity and H2O2-resistance in yeast through redox-modulation of protein kinase A

eLife, 2020
Peroxiredoxins are H2O2 scavenging enzymes that also carry out H2O2 signaling and chaperone functions. In yeast, the major cytosolic peroxiredoxin, Tsa1 is required for both promoting resistance to H2O2 and extending lifespan upon caloric restriction. We
Friederike Roger, Cecilia Picazo, Wolfgang Reiter, Marouane Libiad, Chikako Asami, Sarah Hanzén, Chunxia Gao, Gilles Lagniel, Niek Welkenhuysen, Jean Labarre, Thomas Nyström, Morten Grøtli, Markus Hartl, Michel B Toledano, Mikael Molin   +14 more
doaj   +1 more source