Results 101 to 110 of about 6,885 (176)

Oxidative Stress in the Tumor Immune Microenvironment: Mechanisms and Therapeutic Perspectives

MedComm – Oncology, Volume 5, Issue 2, June 2026.
Oxidative stress is involved in several key processes in cancer, including redox regulation, DNA damage, post‐translational modifications, transcriptional regulation, epigenetic modifications, metabolic reprogramming, cell death, and immune modulation. These mechanisms collectively influence tumor progression, immune evasion, and therapeutic responses,
Zhen Wang, Bowen Li, Pan Tang, Fanchen Yan, Shuxin Wang, Guiying Leng, Panduo Dawa, Yuansi Chen, Yihan Guo, Pan Yang, Yi Li, Siyu Liu, Erdan Dong, Siyuan Qin, Zhoufeng Wang   +14 more
wiley   +1 more source

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

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

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

Regulated Cell Death in Idiopathic Pulmonary Fibrosis

The FASEB Journal, Volume 40, Issue 9, 15 May 2026.
This graphical abstract illustrates regulated cell death (RCD) across key pulmonary cell types—including alveolar epithelial cells, fibroblasts, macrophages, and endothelial cells—modulated through a dynamic death modulation network within the IPF microenvironment.
Xiaoyue Pan, Liu Yang, Man Zhao, Yanlin Zhou, Cong Xia, Huibing Liu, Yuqi Wang, Hui Lian, Bin Li, Lan Wang, Guoying Yu   +10 more
wiley   +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

The relationship between the amount of glutathionylation and the cellular thiol concentration.

, 2013
(A) Protein S-glutathionylation in BSO-treated cells. HEK 293 cells were incubated with 100 µM BSO overnight before treating with 0.5 mM diamide or 0.5 mM hydrogen peroxide.
Yuh-Cherng Chai (375282), Jasen Lee Gilge (375281), Michael Fisher (25505)   +2 more
core   +1 more source

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

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

Serum S-glutathionylated proteins as a potential biomarker of carotid artery stenosis

Clinical Biochemistry, 2012
As oxidative stress is known to be associated with the development of atherosclerosis, we investigated whether the serum S-glutathionylated proteins were increased in patients with carotid artery stenosis (CS).Fifty-four patients with CS and 20 age-matched non-CS patients were involved in this study.
Morito, Nakamoto, Makoto, Hirose, Miho, Kawakatsu, Toshiyuki, Nakayama, Yoshishige, Urata, Kensaku, Kamata, Makio, Kaminogo, Tao-Sheng, Li, Izumi, Nagata   +8 more
openaire   +2 more sources