Results 61 to 70 of about 6,811 (158)

Microtubule S-glutathionylation as a potential approach for antimitotic agents

BMC Cancer, 2012
Background Microtubules have been one of the most effective targets for the development of anticancer agents. Cancer cells treated by these agents are characterized by cell arrest at G2/M phase.
Chen Wei, Seefeldt Teresa, Young Alan, Zhang Xiaoying, Zhao Yong, Ruffolo John, Kaushik Radhey S, Guan Xiangming   +7 more
doaj   +1 more source

Microbial Oxidative Stress in Food Fermentations: A Comprehensive Review

eFood, Volume 7, Issue 4, August 2026.
Oxidative stress has a dual role in food fermentations: low ROS supports adaptive signaling, whereas excessive ROS causes cellular damage and process inhibition. Managing redox state as a controllable process variable can improve fermentation robustness and final food quality.
Wanrong Hu, Manxi Wu, Hui Xu, Jiebiao Chen, Wen Cai, Han Yang, Hujing Cao, Xinlin Huang, Jinping Cao, Chongde Sun, Yue Wang, Dongliang Li   +11 more
wiley   +1 more source

S-Glutathionylation and Redox Protein Signaling in Drug Addiction [PDF]

, 2016
Drug addiction is a chronic relapsing disorder that comes at a high cost to individuals and society. Therefore understanding the mechanisms by which drugs exert their effects is of prime importance. Drugs of abuse increase the production of reactive oxygen and nitrogen species resulting in oxidative stress.
Jacqueline S, Womersley, Joachim D, Uys
openaire   +2 more sources

Glutathione S-transferase pi modulates NF-κB activation and pro-inflammatory responses in lung epithelial cells

Redox Biology, 2016
Nuclear Factor kappa B (NF-κB) is a transcription factor family critical in the activation of pro- inflammatory responses. The NF-κB pathway is regulated by oxidant-induced post-translational modifications. Protein S-glutathionylation, or the conjugation
Jane T. Jones, Xi Qian, Jos L.J. van der Velden, Shi Biao Chia, David H. McMillan, Stevenson Flemer, Sidra M. Hoffman, Karolyn G. Lahue, Robert W. Schneider, James D. Nolin, Vikas Anathy, Albert van der Vliet, Danyelle M. Townsend, Kenneth D. Tew, Yvonne M.W. Janssen-Heininger   +14 more
doaj   +1 more source

Glutathionyl Hemoglobin and Its Emerging Role as a Clinical Biomarker of Chronic Oxidative Stress

Antioxidants, 2023
Hemoglobin is one of the proteins that are more susceptible to S-glutathionylation and the levels of its modified form, glutathionyl hemoglobin (HbSSG), increase in several human pathological conditions.
Andrea Scirè, Giulia Casari, Brenda Romaldi, Lidia de Bari, Cinzia Antognelli, Tatiana Armeni   +5 more
doaj   +1 more source

The Circadian Oscillator Affects Both Glutathione Homeostasis and Its Response to Salt Stress in Arabidopsis thaliana

Plant, Cell &Environment, Volume 49, Issue 8, Page 5421-5434, August 2026.
ABSTRACT Glutathione, including reduced glutathione (GSH) and oxidized glutathione (GSSG), is the major non‐protein thiol‐based redox buffer. There are diurnal rhythms in total glutathione level and in this work, we investigate whether these oscillations might be indicative of circadian regulation of total glutathione homeostasis.
Desiré Cano‐Yelo, Raquel López‐Martínez, Francisca Sevilla, Alex A. R. Webb, Ana Jiménez, María Carmen Martí   +5 more
wiley   +1 more source

Origin of Elevated S-Glutathionylated GAPDH in Chronic Neurodegenerative Diseases

International Journal of Molecular Sciences, 2023
H2O2-oxidized glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalytic cysteine residues (Cc(SH) undergo rapid S-glutathionylation. Restoration of the enzyme activity is accomplished by thiol/disulfide SN2 displacement (directly or enzymatically) forming glutathione disulfide (G(SS)G) and active enzyme, a process that should be facile as Cc(SH ...
Paul A. Hyslop, Leonard N. Boggs, Michael O. Chaney   +2 more
openaire   +2 more sources

Cysteine Glutathionylation Acts as a Redox Switch in Endothelial Cells

Antioxidants, 2019
Oxidative post-translational modifications (oxPTM) of receptors, enzymes, ion channels and transcription factors play an important role in cell signaling.
Agathe Lermant, Colin E. Murdoch
doaj   +1 more source

Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility

Nature Communications, 2023
Protein-S-glutathionylation is a post-translational modification involving the conjugation of glutathione to protein thiols, which can modulate the activity and structure of key cellular proteins.
Elizabeth M. Corteselli, Mona Sharafi, Robert Hondal, Maximilian MacPherson, Sheryl White, Ying-Wai Lam, Clarissa Gold, Allison M. Manuel, Albert van der Vliet, Severin T. Schneebeli, Vikas Anathy, Jianing Li, Yvonne M. W. Janssen-Heininger   +12 more
doaj   +1 more source

Tricarboxylic Acid (TCA) Cycle Enzyme Alpha‐Ketoglutarate Dehydrogenase (KGDH) as a Nexus for the Regulation of Macrophage Polarization

Journal of Cellular Biochemistry, Volume 127, Issue 7, July 2026.
ABSTRACT Macrophage metabolism has been increasingly studied in recent years for its potential as a therapeutic target across multiple pathologies. In this article, we propose that the tricarboxylic acid (TCA) cycle enzyme alpha‐ketoglutarate (KG) dehydrogenase (KGDH) serves as a nexus for regulating macrophage polarization toward pro‐inflammatory (M1)
Meijing Li, Ryan J. Mailloux
wiley   +1 more source