Results 71 to 80 of about 19,795 (176)

Substitution of the Thioredoxin System for Glutathione Reductase in Drosophila melanogaster

, 2001
The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals. These proteins maintain intracellular redox homeostasis to protect the organism from oxidative damage.
José Botella-Munoz, Katja Becker, Schneuwly, Stephan, R. Heiner Schirmer, Ulschmid, Julia K., Becker, Katja, Stefan M. Kanzok, Stephan Schneuwly, Müller, Hans-Michael, Bauer, Holger, Julia K. Ulschmid, Kanzok, Stefan M., Schirmer, R. Heiner, Anke Fechner, Botella-Munoz, José, Hans-Michael Müller, Holger Bauer, Fechner, Anke   +17 more
core   +1 more source

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

MedComm – 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, Azadeh Niknejad, Elaheh Amini   +2 more
wiley   +1 more source

Insights into the Specificity of Thioredoxin Reductase−Thioredoxin Interactions. A Structural and Functional Investigation of the Yeast Thioredoxin System

, 2016
The enzymatic activity of thioredoxin reductase enzymes is endowed by at least two redox centers: a flavin and a dithiol/disulfide CXXC motif. The interaction between thioredoxin reductase and thioredoxin is generally species-specific, but the molecular ...
Francisco J. Medrano (2119840), Beatriz G. Guimarães (2304772), Luis E. S. Netto (127450), Marcos A. Oliveira (2304778), Karen F. Discola (2304781), Simone V. Alves (2304775)   +5 more
core   +1 more source

Brain mitochondria from DJ-1 knockout mice show increased respiration-dependent hydrogen peroxide consumption

Redox Biology, 2014
Mutations in the DJ-1 gene have been shown to cause a rare autosomal-recessive genetic form of Parkinson’s disease (PD). The function of DJ-1 and its role in PD development has been linked to multiple pathways, however its exact role in the development ...
Pamela Lopert, Manisha Patel
doaj   +1 more source

Oxidative Stress and DNA Epigenetic Modifications in Cancer: Mechanisms and Targeted Therapeutics

MedComm – Oncology, Volume 5, Issue 2, June 2026.
Reactive oxygen species (ROS) modulate DNA methyltransferases (DNMTs), ten‐eleven translocation family proteins (TETs) and their cofactors, reshaping 5‐methylcytosine (5mC)/5‐hydroxymethylcytosine (5hmC)/5‐formylcytosine (5fC) landscapes and gene expression in cancer cells. In turn, epigenetic control of antioxidant and metabolic pathways feeds back on
Xishan Yang, Qitai Chen, YuJie Yu, Yi Zang, Rujia Zheng, Zhe Zhang, Shuaijun Lu, Li Zhou   +7 more
wiley   +1 more source

Thioredoxin and thioredoxin-reductase protein levels.

, 2016
Thioredoxin and thioredoxin-reductase protein levels.
Galina Zeltcer (2890028), Mordechai Chevion (119370), Benjamin Drenger (2890031), Hilbert Grievink (2890025), Eduard Berenshtein (119363)   +4 more
core   +1 more source

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

Nitroreductase reactions of Arabidopsis thaliana thioredoxin reductase

, 1998
Arabidopsisthaliana NADPH:thioredoxin reductase (TR, EC 1.6.4.5) catalyzed redox cycling of aromatic nitrocompounds, including the explosives 2,4,6-trinitrotoluene and tetryl, and the herbicide 3,5-dinitro-o-cresol.
Šarlauskas, Jonas, Miškinien≐, Vanda, Č≐nas, Narimantas, Jacquot, Jean-Pierre   +3 more
core   +1 more source

CydDC-mediated reductant export in Escherichia coli controls the transcriptional wiring of energy metabolism and combats nitrosative stress [PDF]

, 2016
The glutathione/cysteine exporter CydDC maintains redox balance in Escherichia coli. A cydD mutant strain was used to probe the influence of CydDC upon reduced thiol export, gene expression, metabolic perturbations, intracellular pH homeostasis, and ...
Sanguinetti, Guido, Holyoake, L.V., Rowe, Michelle L, Holyoake, Louise V, Howard, Mark J., Sanguinetti, G., Howard, Mark J, Rowe, M.L., Poole, Robert K, Poole, R.K., Hunt, Stuart, Cook, Gregory M, Hunt, S., Shepherd, M., Rowe, Michelle L., Shepherd, Mark, Howard, M.J., Cook, G.M.   +17 more
core   +1 more source

The competitive interplay of 12‐oxophytodienoic acid (OPDA), protein thiols, and glutathione

The FEBS Journal, Volume 293, Issue 12, Page 3683-3705, June 2026.
12‐Oxophytodienoic acid (OPDA) is a phytohormone involved in plant growth and stress defense. Due to its cyclopentenone moiety, OPDA can form Michael adducts with thiol‐containing compounds such as glutathione and cysteine residues of proteins, resulting in alterations of the cellular redox regulatory network.
Madita Knieper, Ruben Schwarz, Lara Vogelsang, Jens Sproß, Armağan Kaya, Maike Bittmann, Harald Gröger, Andrea Viehhauser, Karl‐Josef Dietz   +8 more
wiley   +1 more source