Results 101 to 110 of about 8,445 (200)

A Comparison of Reversible Versus Irreversible Protein Glutathionylation

, 2014
Glutathionylation is generally a reversible posttranslational modification that occurs to cysteine residues that have been exposed to reactive oxygen species (P-SSG).
Arthur J.L. Cooper, Townsend, Danyelle, Volodymyr I. Lushchak, Cooper, Arthur J, Townsend, Danyelle M, Lushchak, Volodymyr I, Cooper, Arthur J L, Danyelle M. Townsend   +7 more
core   +1 more source

Glutathionylation assay with BIOGEE.

, 2019
Glutathionylated actin was detected as described in Methods. Densitometric analysis of the obtained bands revealed that actin S-glutathionylation significantly increased in cells treated with CdCl2 with respect to CTR.
Marianna Ranieri (330759), Graziana Difonzo (6495236), Mariangela Centrone (6495239), Annarita Di Mise (484678), Giovanna Valenti (330762), Tommaso Pellegrino (6495245), Maria Venneri (6495242), Annamaria Russo (6495248), Francesco Caponio (6495251), Grazia Tamma (330757), Maria Mastrodonato (478077)   +10 more
core   +1 more source

Evaluation of protein S-glutathionylation patterns.

, 2013
Evaluation of protein S-glutathionylation patterns was performed by 2D-immunoblotting with anti-GSH antibody: A) control cells. B) H-RasV12 expressing cells.
Carla Emiliani (184188), Lorena Urbanelli (293124), Francesca Magherini (293125), Giovanni Principato (293128), Alessandra Modesti (293127), Alessandro Magini (184184), Armanda Pugnaloni (293126), Francesco Piva (72402), Luisa Ercolani (293123), Tatiana Armeni (293122)   +9 more
core   +1 more source

Proteome-wide identification and quantification of S-glutathionylation targets in mouse liver

, 2015
Protein S-glutathionylation is a reversible post-translational modification regulating sulfhydryl homeostasis. However, little is known about the proteins and pathways regulated by S-glutathionylation in whole organisms and current approaches lack the ...
McGarry, David J., Chakravarty, Probir, Henderson, Colin J., Lamont, Douglas L., Chen, Wenzhang, Wolf, C. Roland   +5 more
core   +1 more source

Cytosolic Isocitrate Dehydrogenase from Arabidopsis thaliana Is Regulated by Glutathionylation

Antioxidants, 2019
NADP-dependent (Nicotinamide Adénine Dinucléotide Phosphate-dependent) isocitrate dehydrogenases (NADP-ICDH) are metabolic enzymes involved in 2-oxoglutarate biosynthesis, but they also supply cells with NADPH. Different NADP-ICDH genes are
Adnan Khan Niazi, Laetitia Bariat, Christophe Riondet, Christine Carapito, Amna Mhamdi, Graham Noctor, Jean-Philippe Reichheld   +6 more
doaj   +1 more source

Glutathionylation of Actin in the Dictyostelium Cytoskeleton

, 2015
Glutathione (GSH) is the most abundant antioxidant in living organisms. It is a small tripeptide composed of three amino acid residues; glutamate, cysteine and glycine.
Grosberg, Benjamin
core  

Actin S-glutathionylation: evidence against a thiol-disulphide exchange mechanism

, 2003
Many proteins, including actin, are targets for S-glutathionylation, the reversible formation of mixed disulphides between protein cysteinyl thiol groups and glutathione (GSH) that can be induced in cells by oxidative stress.
A. Milzani, D. Giustarini, Dalle Donne, I., Rossi, Ranieri, I. Dalle Donne, Giustarini, D., Milzani, A., R. Rossi, Colombo, R., R. Colombo   +9 more
core   +1 more source

Susceptibility of isolated myofibrils to in vitro glutathionylation: Potential relevance to muscle functions. [PDF]

, 2010
In this study we investigated the molecular mechanism of glutathionylation on isolated human cardiac myofibrils using several pro-glutathionylating agents.
Passarelli, Chiara, Pastore, Anna, Tesi, C, Bertini, E, Di Venere, A, Petrini, S, Pastore, A, Scellini, B, Scellini, Beatrice, Tesi, Chiara, Poggesi, C, Bertini, Enrico, Di Venere, Almerinda, Sale, Patrizio, Piemonte, F, Piroddi, N, Petrini, Stefania, Piroddi, Nicoletta, Passarelli, C, Poggesi, Corrado, Piemonte, Fiorella, Sale, P, Piemonte, F.   +22 more
core   +1 more source

S-glutathionylation regulates inflammatory activities of S100A9 [PDF]

, 2010
Reactive oxygen species generated by activated neutrophils can cause oxidative stress and tissue damage. S100A8 (A8) and S100A9 (A9), abundant in neutrophil cytoplasm, are exquisitely sensitive to oxidation, which may alter their functions.
Su Yin Lim, Mark J Raftery, Carolyn L Geczy, Jesse Goyette   +3 more
core  

Polysulfur-based bulking of dynamin-related protein 1 prevents ischemic sulfide catabolism and heart failure in mice

Nature Communications
The presence of redox-active molecules containing catenated sulfur atoms (supersulfides) in living organisms has led to a review of the concepts of redox biology and its translational strategy.
Akiyuki Nishimura, Seiryo Ogata, Xiaokang Tang, Kowit Hengphasatporn, Keitaro Umezawa, Makoto Sanbo, Masumi Hirabayashi, Yuri Kato, Yuko Ibuki, Yoshito Kumagai, Kenta Kobayashi, Yasunari Kanda, Yasuteru Urano, Yasuteru Shigeta, Takaaki Akaike, Motohiro Nishida   +15 more
doaj   +1 more source