Results 41 to 50 of about 8,445 (200)

Glutathionyl systems and metabolic dysfunction in obesity [PDF]

Nutrition Reviews, 2015
Oxidative stress is associated with obesity. However, glutathione (GSH), one of the body's most abundant antioxidants, plays dual and seemingly contradictory roles in the development of obesity and its comorbidities. Glutathione has complex metabolic and biochemical fates and is a cofactor for several enzymes that function in modifying obesity-related ...
Matthew J, Picklo, Eric K, Long, Emilie E, Vomhof-DeKrey   +2 more
openaire   +2 more sources

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, Atichat Kuadkitkan, Prasert Auewarakul, Duncan R Smith, Albert J Ketterman   +4 more
doaj   +1 more source

Causes and Consequences of Cysteine S-Glutathionylation [PDF]

Journal of Biological Chemistry, 2013
Post-translational S-glutathionylation occurs through the reversible addition of a proximal donor of glutathione to thiolate anions of cysteines in target proteins, where the modification alters molecular mass, charge, and structure/function and/or prevents degradation from sulfhydryl overoxidation or proteolysis.
Christina L, Grek, Jie, Zhang, Yefim, Manevich, Danyelle M, Townsend, Kenneth D, Tew   +4 more
openaire   +2 more sources

Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300

mBio, 2021
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent for coronavirus disease 2019 (COVID-19), encodes two proteases required for replication.
David A. Davis, Haydar Bulut, Prabha Shrestha, Amulya Yaparla, Hannah K. Jaeger, Shin-ichiro Hattori, Paul T. Wingfield, John J. Mieyal, Hiroaki Mitsuya, Robert Yarchoan   +9 more
doaj   +1 more source

Regulation of Annexin A2 by Reversible Glutathionylation [PDF]

Journal of Biological Chemistry, 2004
The annexin A2-S100A10 heterotetramer (AIIt) is a multifunctional Ca(2+)-dependent, phospholipid-binding, and F-actin-binding phosphoprotein composed of two annexin A2 subunits and two S100A10 subunits. It was reported previously that oxidative stress from exogenous hydrogen peroxide or generated in response to tumor necrosis factor-alpha results in ...
Jennifer F, Caplan, Nolan R, Filipenko, Sandra L, Fitzpatrick, David M, Waisman   +3 more
openaire   +2 more sources

A novel approach for predicting protein S-glutathionylation

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, Yuri M. Poluektov, Vladimir A. Dmitriev, Eugene N. Kuznetsov, Vladimir A. Mitkevich, Alexander A. Makarov, Irina Yu. Petrushanko   +6 more
doaj   +1 more source

Glutathionyl‐hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones [PDF]

FEBS Letters, 2014
Glutathionyl‐hydroquinone reductases (GHRs) catalyze the deglutathionylation of quinones via a catalytic cysteine. The two GHR genes in the Populus trichocarpa genome, Pt‐GHR1 and Pt‐GHR2, are primarily expressed in reproductive organs. Both proteins are localized in plastids. More specifically, Pt‐GHR2 localizes in nucleoids.
Lallement, Pierre-Alexandre, Meux, Edgar, Gualberto, José M., Dumarcay, Stéphane, Favier, Frédérique, Didierjean, Claude, Saul, Frederick, Haouz, Ahmed, Rouhier, Mélanie, Gelhaye, Éric, Rouhier, Nicolas, Hecker, Arnaud   +11 more
openaire   +4 more sources

Cysteine-based redox regulation and signalling in plants

Frontiers in Plant Science, 2013
Living organisms are subjected to oxidative stress conditions which are characterized by the production of reactive oxygen (ROS), nitrogen (RNS) and sulfur (RSS) species.
Jérémy eCouturier, Kamel eChibani, Jean-Pierre eJacquot, Nicolas eRouhier   +3 more
doaj   +1 more source

Protein Glutathionylation and Glutaredoxin: Role in Neurodegenerative Diseases

Antioxidants, 2022
Oxidative stress has been implicated in the pathogenesis and progression of many neurodegenerative disorders including Parkinson’s disease and Alzheimer’s disease. One of the major enzyme systems involved in the defense against reactive oxygen species are the tripeptide glutathione and oxidoreductase glutaredoxin.
Haseena P. A., Latha Diwakar, Vijayalakshmi Ravindranath   +2 more
openaire   +3 more sources

Protein S-glutathionylation: a regulatory device from bacteria to humans

, 2009
S-Glutathionylation is the specific post-translational modification of protein cysteine residues by the addition of the tripeptide glutathione, the most abundant and important low-molecular-mass thiol within most cell types.
A. Milzani, D. Giustarini, G. Colombo, I. Dalle Donne, R. Rossi   +4 more
core   +2 more sources