Results 11 to 20 of about 17,263,040 (272)

The Barley Grain Thioredoxin System – an Update [PDF]

Frontiers in Plant Science, 2013
Thioredoxin reduces disulfide bonds and play numerous important functions in plants. In cereal seeds, cytosolic h-type thioredoxin facilitates the release of energy reserves during the germination process and is recycled by NADPH-dependent thioredoxin ...
Per eHägglund, Olof eBjörnberg, Nicolas eNavrot, Johanne eMørch Jensen, Kenji eMaeda, Kristine eKirkensgaard, Azar eShahpiri, Abida eSultan, Jakob eBunkenborg, Frank eGubler, José Maria Barrero, Anette eHenriksen, Christine eFinnie, Birte eSvensson   +13 more
doaj   +8 more sources

The Mitochondrial Thioredoxin System

Antioxidants & Redox Signaling, 2000
Eukaryotic organisms from yeast to human possess a mitochondrial thioredoxin system composed of thioredoxin and thioredoxin reductase, similar to the cytosolic thioredoxin system that exists in the same cells. Yeast and mammalian mitochondrial thioredoxins are monomers of approximately 12 kDa and contain the typical conserved active site WCGPC. However,
Miranda-Vizuete, Antonio, Damdimopoulos, Anastasios E., Spyrou, Giannis   +2 more
openaire   +4 more sources

The Mammalian Testis-Specific Thioredoxin System

Antioxidants & Redox Signaling, 2004
Redox control of cell physiology is one of the most important regulatory mechanisms in all living organisms. The thioredoxin system, composed of thioredoxin and thioredoxin reductase, has emerged as a key player in cellular redox-mediated reactions.
Miranda-Vizuete, Antonio, Sadek, Christine M., Jiménez, Alberto, Krause, William J., Sutovsky, Peter, Oko, Richard   +5 more
openaire   +4 more sources

Targeting the thioredoxin system as a novel strategy against B‐cell acute lymphoblastic leukemia [PDF]

Molecular Oncology, 2019
B‐cell precursor acute lymphoblastic leukemia (BCP‐ALL) is a genetically heterogeneous blood cancer characterized by abnormal expansion of immature B cells.
Klaudyna Fidyt, Agata Pastorczak, Agnieszka Goral, Kacper Szczygiel, Wojciech Fendler, Angelika Muchowicz, Marcin Adam Bartlomiejczyk, Joanna Madzio, Julia Cyran, Agnieszka Graczyk‐Jarzynka, Eugene Jansen, Elzbieta Patkowska, Ewa Lech‐Maranda, Deepali Pal, Helen Blair, Anna Burdzinska, Piotr Pedzisz, Eliza Glodkowska‐Mrowka, Urszula Demkow, Karolina Gawle‐Krawczyk, Michal Matysiak, Magdalena Winiarska, Przemyslaw Juszczynski, Wojciech Mlynarski, Olaf Heidenreich, Jakub Golab, Malgorzata Firczuk   +26 more
doaj   +2 more sources

The logic of kinetic regulation in the thioredoxin system [PDF]

BMC Systems Biology, 2011
The thioredoxin system consisting of NADP(H), thioredoxin reductase and thioredoxin provides reducing equivalents to a large and diverse array of cellular processes. Despite a great deal of information on the kinetics of individual thioredoxin-dependent reactions, the kinetic regulation of this system as an integrated whole is not known.
Ché S. Pillay, Jan-Hendrik S. Hofmeyr, Johann M. Rohwer   +2 more
openaire   +5 more sources

Molecular and Cellular Responses of DNA Methylation and Thioredoxin System to Heat Stress in Meat-Type Chickens [PDF]

Animals, 2021
Heat stress (HS) causes molecular dysfunction that adversely affects chicken performance and increases mortality. The responses of chickens to HS are extremely complex.
Walid S. Habashy, Marie C. Milfort, Romdhane Rekaya, Samuel E. Aggrey   +3 more
doaj   +2 more sources

Thioredoxin and Glutathione Systems

, 2021
Most cancer cells contain high levels of reactive oxygen species (ROS), which result in higher expression levels of the glutathione and thioredoxin reductase systems. These antioxidant systems convert ROS to nonharmful compounds and they also reduce disulfide bonds in oxidized proteins.
Yu, Yezhou, Di Trapani, Giovanna, Tonissen, Kathryn   +2 more
core   +5 more sources

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

Biochemistry, 2010
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 aspects related to this phenomenon remain elusive.
Oliveira, Marcos A., Discola, Karen F., Alves, Simone V., Medrano, Francisco J., Guimaraes, Beatriz G., Netto, Luis E. S.   +5 more
core   +5 more sources

Selenoproteins and the Thioredoxin System

, 2011
The thioredoxin system, comprising NADPH, flavoprotein thioredoxin reductase (TrxR), and 12 kDa thioredoxin (Trx) with a catalytic dithiol/disulfide, is the ubiquitous biological cellular disulfide reduction system with major functions in DNA synthesis, defense against oxidative stress, and thiol redox control. In mammalian cells Trx system activity is
Jun Lu, Arne Holmgren
openaire   +2 more sources

Antioxidant activity of the thioredoxin system. [PDF]

Biophys Rep, 2023
The thioredoxin system is composed of thioredoxin (Trx), thioredoxin reductase (TR) and reduced nicotinamide adenine dinucleotide phosphate. Trx is an important antioxidant molecule that can resist cell death caused by various stresses and plays a prominent role in redox reactions.
Liu Z.
europepmc   +3 more sources