Results 91 to 100 of about 8,445 (200)

Redox Regulation of cAMP-Dependent Protein Kinase and Its Role in Health and Disease

open access: yesLife
Protein kinase A (PKA) is a key regulator of cellular signaling that regulates key physiological processes such as metabolism, cell proliferation, and neuronal function.
Ese S. Ekhator   +2 more
doaj   +1 more source

Redox Regulation and Oxidative Stress in Health and Disease: Mechanisms and Therapeutic Targeting

open access: yesMedComm – Future Medicine, Volume 5, Issue 2, June 2026.
Reactive species serve crucial roles which are tightly regulated in both physiological as well as disease states. At physiological levels, these species are integral to redox signaling, while uncontrolled redox promotes disease pathology. This review examines the dysregulation of these processes.
Mohammad Hossein Azadi   +2 more
wiley   +1 more source

Glutathionylation of UCP2 sensitizes drug resistant leukemia cells to chemotherapeutics

open access: yes, 2013
Uncoupling protein-2 (UCP2) is used by cells to control reactive oxygen species (ROS) production by mitochondria. This ability depends on the glutathionylation state of UCP2. UCP2 is often overexpressed in drug resistant cancer cells and therein controls
Adjeitey, Cyril Nii-Klu   +3 more
core   +1 more source

Activation of Nrf2 at Critical Windows of Development Alters Tissue-Specific Protein S-Glutathionylation in the Zebrafish (Danio rerio) Embryo

open access: yesAntioxidants
Activation of Nrf2—the master regulator of antioxidative response—at different stages of embryonic development has been shown to result in changes in gene expression, but the tissue-specific and downstream effects of Nrf2 activation during development ...
Emily S. Marques   +4 more
doaj   +1 more source

Structural Basis for Redox Regulation of Cytoplasmic and Chloroplastic Triosephosphate Isomerases from Arabidopsis thaliana

open access: yesFrontiers in Plant Science, 2016
In plants triosephosphate isomerase (TPI) interconverts glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) during glycolysis, gluconeogenesis, and the Calvin-Benson cycle.
Laura Margarita López-Castillo   +7 more
doaj   +1 more source

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

open access: yesMedComm – 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   +14 more
wiley   +1 more source

Detection of ROS Induced Proteomic Signatures by Mass Spectrometry

open access: yesFrontiers in Physiology, 2017
Reversible and irreversible post-translational modifications (PTMs) induced by endogenously generated reactive oxygen species (ROS) in regulatory enzymes and proteins plays an essential role in cellular signaling.
Brian McDonagh
doaj   +1 more source

Regulated Cell Death in Idiopathic Pulmonary Fibrosis

open access: yesThe 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   +10 more
wiley   +1 more source

Microtubule S-glutathionylation as a potential approach for antimitotic agents [PDF]

open access: yes, 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.
Young, A.   +15 more
core   +1 more source

Glutathionylspermidine in the Modification of Protein SH Groups: The Enzymology and Its Application to Study Protein Glutathionylation

open access: yesMolecules, 2015
Cysteine is very susceptible to reactive oxygen species. In response; posttranslational thiol modifications such as reversible disulfide bond formation have arisen as protective mechanisms against undesired in vivo cysteine oxidation.
Jason Ching-Yao Lin   +6 more
doaj   +1 more source

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