Results 11 to 20 of about 161,743 (309)

Correlation of glutathione reductase activity distribution in the blood serum and tissues of white unborn rats

BIO Web of Conferences, 2020
It is known that the majority of pathological processes take place against the background of formation of active oxygen species and intensification of free radical oxidation of bio-substrates.
Boriskin Pavel, Gulenko Olga, Devyatkin Anatoly, Karimova Rufia, Leonov Victor, Pavlova Olga   +5 more
doaj   +1 more source

In vitro and in silico Evaluation of Some Natural Molecules as Potent Glutathione Reductase Inhibitors

International Journal of Secondary Metabolite, 2020
Glutathione reductase inhibitors are very popular antimalarial and anticancer agents. In this study, in vitro inhibition effects of β-sitosterol, stigmasterol, diosgenin and jervine which containing steroidal structure were determined against glutathione
Tuba Aydin
doaj   +1 more source

Exogenous salicylic acid enhances wheat drought tolerance by influence on the expression of genes related to ascorbate-glutathione cycle

Biologia Plantarum, 2013
Treatment with 0.5 mM salicylic acid (SA) significantly alleviated growth inhibition induced by drought in wheat seedlings, manifested by less decreassed fresh mass, dry mass, plant height, root length, and less increased lipid peroxidation.
G. Z. Kang, G. Z. Li, G. Q. Liu, W. Xu, X. Q. Peng, C. Y. Wang, Y. J. Zhu, T. C. Guo   +7 more
doaj   +1 more source

Effects of inhibiting antioxidant pathways on cellular hydrogen sulfide and polysulfide metabolism [PDF]

, 2019
Elaborate antioxidant pathways have evolved to minimize the threat of excessive reactive oxygen species (ROS) and to regulate ROS as signaling entities.
Gao, Yan, Olson, Kenneth R.
core   +1 more source

Catalytic oxidant scavenging by selenium-containing compounds: Reduction of selenoxides and N-chloramines by thiols and redox enzymes

Redox Biology, 2017
Myeloperoxidase produces strong oxidants during the immune response to destroy invading pathogens. However, these oxidants can also cause tissue damage, which contributes to the development of numerous inflammatory diseases. Selenium containing compounds,
Luke Carroll, David I. Pattison, Shanlin Fu, Carl H. Schiesser, Michael J. Davies, Clare L. Hawkins   +5 more
doaj   +1 more source

Fragment-based discovery of a regulatory site in thioredoxin glutathione reductase acting as "doorstop" for NADPH entry [PDF]

, 2018
Members of the FAD/NAD-linked reductase family are recognized as crucial targets in drug development for cancers, inflammatory disorders, and infectious diseases.
Angelucci, Francesco, Ardini, Matteo, Arner, Elias S. J., Bellelli, Andrea, Boumis, Giovanna, Chen, Qing, Fata, Francesca, Ippoliti, Rodolfo, Jadhav, Ajit, Lea, Wendy A., Lyu, Haining, Miele, Adriana E., Petukhov, Pavel A., Silvestri, Ilaria, Simeonov, Anton, Thatcher, Gregory R. J., Williams, David L.   +16 more
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Characterizing roles for the glutathione reductase, thioredoxin reductase and thioredoxin peroxidase-encoding genes of Magnaporthe oryzae during rice blast disease. [PDF]

PLoS ONE, 2014
Understanding how pathogenic fungi adapt to host plant cells is of major concern to securing global food production. The hemibiotrophic rice blast fungus Magnaporthe oryzae, cause of the most serious disease of cultivated rice, colonizes leaf cells ...
Jessie Fernandez, Richard A Wilson
doaj   +1 more source

How are proteins reduced in the endoplasmic reticulum? [PDF]

, 2018
The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for protein folding, degradation, chaperone function, and the ER stress response. Our understanding of this process is generally poor but progress has been made.
Bulleid, Neil, Ellgaard, Lars, Sevier, Carolyn S.   +2 more
core   +2 more sources

Selenoprotein gene nomenclature [PDF]

, 2016
The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These proteins are involved in a variety of functions, most notably redox homeostasis.
Arn\ue9r, Elias S., Berry, Marla J., Bruford, Elspeth A., Burk, Raymond F., Carlson, Bradley A., Castellano, Sergi, Chavatte, Laurent, Conrad, Marcus, Copeland, Paul R., Diamond, Alan M., Driscoll, Donna M., Ferreiro, Ana, Floh\ue9, Leopold, Gladyshev, Vadim N, Green, Fiona R., Guig\uf3, Roderic, Handy, Diane E., Hatfield, Dolph L., Hesketh, John, Hoffmann, Peter R., Holmgren, Arne, Hondal, Robert J., Howard, Michael T., Huang, Kaixun, K\uf6hrle, Josef, Kim, Hwa Young, Kim, Ick Young, Krol, Alain, Kryukov, Gregory V., Lee, Byeong Jae, Lee, Byung Cheon, Lei, Xin Gen, Lescure, Alain, Liu, Qiong, Lobanov, Alexei V., Loscalzo, Joseph, Maiorino, Matilde, Mariotti, Marco, Prabhu, K. Sandeep, Rayman, Margaret P., Regina, Brigelius Floh\ue9, Rozovsky, Sharon, Salinas, Gustavo, Schmidt, Edward E., Schomburg, Lutz, Schweizer, Ulrich, Simonovi\u107, Miljan, Sunde, Roger A., Tsuji, Petra A., Tweedie, Susan, Ursini, Fulvio, Whanger, Philip D., Zhang, Yan   +52 more
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Arabidopsis thaliana dehydroascorbate reductase 2 : conformational flexibility during catalysis [PDF]

, 2017
Dehydroascorbate reductase (DHAR) catalyzes the glutathione (GSH)-dependent reduction of dehydroascorbate and plays a direct role in regenerating ascorbic acid, an essential plant antioxidant vital for defense against oxidative stress.
Bodra, Nandita, De Proft, Frank, Huang, Jingjing, Messens, Joris, Pallo, Anna, Rosado, Leonardo Astolfi, Van Breusegem, Frank, Wahni, Khadija, Young, David   +8 more
core   +1 more source