Results 91 to 100 of about 24,013,578 (179)

S-glutathionylation modification of proteins and the association with cellular death (Review)

Medicine International
S-glutathionylation (SSG), a redox-sensitive post-translational modification mediated by glutathione, regulates protein structure and function through reversible disulfide bond formation at cysteine residues. Glutaredoxins (GRXs), pivotal antioxidant enzymes, catalyze SSG dynamics to maintain thiol homeostasis.
Sun, Xiongxing, Xie, Le, Wang, Shiliang, Zeng, Shanshan, Wu, Lingying, Tang, Xukun, Zhu, Jiajian, Lin, Shigao, Hu, Tenghui, Jia, Lin, Li, Xia, Zhang, Songqing, Deng, Jun, Wu, Dahua   +13 more
openaire   +2 more sources

Characterization of the impact of glutaredoxin-2 (GRX2) deficiency on superoxide/hydrogen peroxide release from cardiac and liver mitochondria

Redox Biology, 2018
Mitochondria are critical sources of hydrogen peroxide (H2O2), an important secondary messenger in mammalian cells. Recent work has shown that O2•-/H2O2 emission from individual sites of production in mitochondria is regulated by protein S ...
Julia Chalker, Danielle Gardiner, Nidhi Kuksal, Ryan J. Mailloux   +3 more
doaj   +1 more source

Dietary glycine supplementation enhances growth, feed utilization, and antioxidant capacity of large yellow croaker Larimichthys crocea

Journal of the World Aquaculture Society, Volume 57, Issue 5, October 2026.
Abstract Glycine is a dispensable and functional amino acid that promotes fish growth, however, the optimal glycine content in fish diets is not known. This study assessed the effect of dietary glycine content on growth, feed utilization, and antioxidant capacity of large yellow croaker (LYC) Larimichthys crocea.
Mingtao Lei, Jieliang Fan, Pingding Liu, Peng Li, Yan Wang   +4 more
wiley   +1 more source

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

A cross‐species post‐translational modification profiling of histones by LC‐MS/MS revealed conserved oxidative modifications in plants

New Phytologist, Volume 252, Issue 2, Page 538-545, October 2026.
Conservation of post‐translational modifications (PTMs) in histones across six plant species.
Sau‐Shan Cheng, Wai‐Ching Sin, Yuen‐Yi Chau, Hon‐Ming Lam   +3 more
wiley   +1 more source

S-Glutathionylation: Indicator of Cell Stress and Regulator of the Unfolded Protein Response [PDF]

Molecular Interventions, 2007
The specific posttranslational modification of protein cysteine residues by the addition of the tripeptide glutathione is termed S-glutathionylation. This process is promoted by oxidative and nitrosative stress but also occurs in unstressed cells. Altered levels of S-glutathionylation in some proteins have been associated with numerous pathologies ...
openaire   +2 more sources

Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase

Redox Biology, 2016
2-Oxoglutarate dehydrogenase (Ogdh) is an important mitochondria redox sensor that can undergo S-glutathionylation following an increase in H2O2 levels.
Ryan J. Mailloux, D. Craig Ayre, Sherri L. Christian   +2 more
doaj   +1 more source

Serum Levels of S-Glutathionylated Proteins as a Risk-Marker for Arteriosclerosis Obliterans

Circulation Journal, 2007
Oxidative stress plays a role in the development of chronic peripheral arterial disease (PAD) because under these conditions redox regulation is impaired, inducing the S-glutathionylation of proteins. A method of estimating the levels of S-glutathionylated proteins has been developed using biotinylated glutathione S-transferase, which allows the study ...
Nonaka, Kazuki, Kume, Noriaki, Urata, Yoshishige, Seto, Shinji, Kohno, Takaaki, Honda, Sumihisa, Ikeda, Soji, Muroya, Takahiro, Ikeda, Yosihiko, Ihara, Yoshito, Kita, Toru, Kondo, Takahito   +11 more
openaire   +3 more sources

Protein phosphatase PP2Cα S-glutathionylation regulates cell migration

Journal of Biological Chemistry
Redox signaling is a fundamental mechanism that controls all major biological processes partly via protein cysteine oxidations, including S-glutathionylation. Despite over 2000 cysteines identified to form S-glutathionylation in databases, the identification of redox cysteines functionally linked to a biological process of interest remains challenging.
Dhanushika S.K. Kukulage, Kusal T.G. Samarasinghe, Nadee N.J. Matarage Don, Madhu C. Shivamadhu, Kyosuke Shishikura, William Schiff, Faezeh Mashhadi Ramezani, Rayavarapu Padmavathi, Megan L. Matthews, Young-Hoon Ahn   +9 more
openaire   +2 more sources

S-glutathionylation of buccal cell proteins as biomarkers of exposure to hydrogen peroxide

BBA Clinical, 2014
Exogenous or endogenous hydrogen peroxide (H2O2) is a reactive oxygen species (ROS) that can lead to oxidation of cellular nucleophiles, particularly cysteines in proteins. Commercial mouthwashes containing H2O2 provide the opportunity to determine clinically whether changes in S-glutathionylation of susceptible proteins in buccal mucosa cells can be ...
Grek, Christina L., Reyes, Leticia, Townsend, Danyelle M., Tew, Kenneth D.   +3 more
openaire   +2 more sources