Results 21 to 30 of about 197,748 (297)

Thioredoxin VdTrx1, an unconventional secreted protein, is a virulence factor in Verticillium dahliae

Frontiers in Microbiology, 2023
Understanding how plant pathogenic fungi adapt to their hosts is of critical importance to securing optimal crop productivity. In response to pathogenic attack, plants produce reactive oxygen species (ROS) as part of a multipronged defense response ...
Li Tian, Jing Zhuang, Jing Zhuang, Jun-Jiao Li, He Zhu, Steven J. Klosterman, Xiao-Feng Dai, Xiao-Feng Dai, Jie-Yin Chen, Jie-Yin Chen, Krishna V. Subbarao, Dan-Dan Zhang, Dan-Dan Zhang   +12 more
doaj   +1 more source

Autonomous Non Antioxidant Roles for Fasciola hepatica Secreted Thioredoxin-1 and Peroxiredoxin-1

Frontiers in Cellular and Infection Microbiology, 2021
Trematode parasites of the genus Fasciola are the cause of liver fluke disease (fasciolosis) in humans and their livestock. Infection of the host involves invasion through the intestinal wall followed by migration in the liver that results in extensive ...
Amber Dorey, Krystyna Cwiklinski, James Rooney, Carolina De Marco Verissimo, Jesús López Corrales, Heather Jewhurst, Barbara Fazekas, Nichola Eliza Davies Calvani, Siobhán Hamon, Siobhán Gaughan, John P. Dalton, Richard Lalor   +11 more
doaj   +1 more source

Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity

Cell Reports, 2016
The thiol-disulfide oxidoreductase CXXC catalytic domain of thioredoxin contributes to antioxidant defense in phylogenetically diverse organisms. We find that although the oxidoreductase activity of thioredoxin-1 protects Salmonella enterica serovar ...
Miryoung Song, Ju-Sim Kim, Lin Liu, Maroof Husain, Andrés Vázquez-Torres   +4 more
doaj   +1 more source

A Redox-Sensitive Cysteine Is Required for PIN1At Function

Frontiers in Plant Science, 2021
Parvulins are ubiquitous peptidyl-prolyl isomerases (PPIases) required for protein folding and regulation. Among parvulin members, Arabidopsis PIN1At, human PIN1, and yeast ESS1 share a conserved cysteine residue but differ by the presence of an N ...
Benjamin Selles, Tiphaine Dhalleine, Alexis Boutilliat, Nicolas Rouhier, Jérémy Couturier, Jérémy Couturier   +5 more
doaj   +1 more source

Redox Regulation by Thioredoxin and Thioredoxin‐Binding Proteins [PDF]

IUBMB Life, 2001
AbstractRecent works have shown the importance of reduction/oxidation (redox) regulation in various biological phenomena. Thioredoxin is a 12‐kDa protein with redox‐active dithiol in the active site ‐Cys‐Gly‐Pro‐Cys‐ and constitutes a major thiol reducing system, the thioredoxin system.
A, Nishiyama, H, Masutani, H, Nakamura, Y, Nishinaka, J, Yodoi   +4 more
openaire   +2 more sources

The Barley Grain Thioredoxin System – an Update

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   +1 more source

Data on using single- and mixed-mode resins for capture chromatography of recombinant human thioredoxin from Escherichia coli

Data in Brief, 2020
This paper provides the data collected from screening chromatographic resins for their ability to bind and purify recombinant human thioredoxin from Escherichia coli lysate.
Ayswarya Ravi, Emma Foster, Zivko Nikolov   +2 more
doaj   +1 more source

Crystal structure of the human thioredoxin reductase–thioredoxin complex [PDF]

Nature Communications, 2011
Thioredoxin reductase 1 (TrxR1) is a homodimeric flavoprotein crucially involved in the regulation of cellular redox homeostasis, growth, and differentiation. Its importance in various diseases makes TrxR1 a highly interesting drug target. Here we present the first crystal structures of human TrxR1 in complex with its substrate thioredoxin (Trx).
Fritz-Wolf, K., Kehr, S., Stumpf, M., Rahlfs, S., Becker, K.   +4 more
openaire   +3 more sources

PLANT THIOREDOXIN SYSTEMS REVISITED [PDF]

Annual Review of Plant Physiology and Plant Molecular Biology, 2000
▪ Abstract  Thioredoxins, the ubiquitous small proteins with a redox active disulfide bridge, are important regulatory elements in plant metabolism. Initially recognized as regulatory proteins in the reversible light activation of key photosynthetic enzymes, they have subsequently been found in the cytoplasm and in mitochondria.
Schürmann, Peter, Jacquot, J.-P.
openaire   +2 more sources

Epigallocatechin-3-gallate enhances key enzymatic activities of hepatic thioredoxin and glutathione systems in selenium-optimal mice but activates hepatic Nrf2 responses in selenium-deficient mice

Redox Biology, 2016
Selenium participates in the antioxidant defense mainly through a class of selenoproteins, including thioredoxin reductase. Epigallocatechin-3-gallate (EGCG) is the most abundant and biologically active catechin in green tea.
Ruixia Dong, Dongxu Wang, Xiaoxiao Wang, Ke Zhang, Pingping Chen, Chung S. Yang, Jinsong Zhang   +6 more
doaj   +1 more source