Results 51 to 60 of about 24,013,578 (179)

Nitrosative Stress-Induced S-Glutathionylation of Protein Disulfide Isomerase [PDF]

, 2011
Oxidative and nitrosative stress result in the accumulation of reactive oxygen and nitrogen species (ROS/RNS) which trigger redox-mediated signaling cascades through posttranslational modifications on cysteine residues, including S-nitrosylation (P-SNO) and S-glutathionylation (P-SSG). Protein disulfide isomerase (PDI) is the most abundant chaperone in
Joachim D, Uys, Ying, Xiong, Danyelle M, Townsend   +2 more
openaire   +2 more sources

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

Protein-Protein Interaction between Glyoxalase II and Specific Redox Dependent Proteins through S-Glutathionylation Modification

, 2020
S-glutathionylation, the reversible formation of a mixed disulfide bridge between a specific cysteine and a glutathione molecule, can occur spontaneously or be catalyzed by enzymes. Glyoxalase II (GloII), using its natural substrate SLG can form specific
Andrea Scirè, Tatiana Armeni, Laura Cianfruglia, Cristina Minnelli   +3 more
core   +1 more source

S-nitrosation vs. S-glutathionylation of protein sulfhydryl groups by S-nitrosoglutathione

, 2005
S-Nitrosation of protein sulfhydryl groups is an established response to oxidative/nitrosative stress. The transient nature and reversibility of S-nitrosation, as well as its specificity, render this posttranslational modification an attractive mechanism
G. Aldini, D. Giustarini, R. Rossi, A.D.G. Milzani, I. Dalle-Donne, M. Carini   +5 more
core   +2 more sources

OTUD6A‐Mediated Deubiquitination of PRDX1 Protects Against Oral Ulcer by Restoring Mitochondrial Function

Advanced Science, EarlyView.
In human oral keratinocytes, OTUD6A promoted cell migration by deubiquitinating and stabilizing PRDX1. Conversely, OTUD6A deficiency reduced PRDX1 stability, triggering mitochondrial dysfunction and aggravating OU progression. ABSTRACT Oral ulcers (OU), as the most highly prevalent and recurrent oral mucosal lesion, have an unclear pathogenesis that ...
Xiaoyu Sun, Ruiwei Jia, Xingbei Pan, Rui Huang, Jiahong Chen, Ziyi Yao, Lei Yin, Jun Ma, Hongjieliang Wang, Xinyu Huang, Yilin Ma, Yifan Ping, Yuanyuan Chen, Huining Wang, Shengbin Huang, Guang Liang   +15 more
wiley   +1 more source

Glyoxalase II promotes "in vitro" S-glutathionylation.

, 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.
M., Caniglia, Luisa, ARMENI, Tatiana, Cianfruglia, Laura, MASSACCESI, LUCA, GALEAZZI, ROBERTA, SPACCINI, Raffaele, PRINCIPATO, GIOVANNI   +7 more
core   +1 more source

Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences [PDF]

Cardiovascular Research, 2007
The role of nitric oxide in several signalling routes has been clearly established. In recent years increasing attention has been paid to its ability to produce covalent protein post-translational modifications in conjunction with other reactive oxygen and nitrogen species.
Martínez Ruiz, Antonio, Lamas, Santiago
openaire   +3 more sources

S-glutathionylation reactions in mitochondrial function and disease

Frontiers in Cell and Developmental Biology, 2014
Mitochondria are highly efficient energy-transforming organelles that convert energy stored in carbon bonds into the universal energy currency ATP. The production of ATP by mitochondria is dependent on oxidation of nutrients and coupling of exergonic ...
Ryan J. Mailloux, William G. Willmore
doaj   +1 more source

Glutaredoxins Rapidly Reduce Glutathione Hydroper‐ and Polysulfides

Angewandte Chemie International Edition, EarlyView.
Glutaredoxins (Grx) rapidly reduce glutathione polysulfides (GSSnSG) to glutathione hydroper/polysulfides (GSSnH) or GSSnH to hydrogen (poly)sulfides (H2Sn). Reduction of glutathionylated glutaredoxins by reduced glutathione (GSH) yields glutathione disulfide (GSSG).
Philipp Reinert, Seiryo Ogata, Laura Leiskau, Sernur Sena Yildiz, Takaaki Akaike, Uladzimir Barayeu, Marcel Deponte   +6 more
wiley   +1 more source

Membrane skeletal protein S-glutathionylation and hemolysis in human red blood cells.

, 2006
In this work, protein-glutathione mixed disulfide formation in human red blood cells (RBCs) was evaluated in vitro by using the thiol-specific reagent diamide. We investigated what mechanism could lead to S-glutathionylation of membrane skeletal proteins,
D. Giustarini, A. Milzani, Rossi, Ranieri, Dalle Donne, I., I. Dalle Donne, Giustarini, D., Milzani, A., R. Rossi   +7 more
core   +1 more source