Results 1 to 10 of about 10,696 (83)

Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]

, 2017
Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio, Tokatlidis, Konstantinos   +1 more
core   +1 more source

Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space [PDF]

, 2016
Mitochondria are organelles that play a central role in cellular metabolism, as they are responsible for processes such as iron/sulfur cluster biogenesis, respiration and apoptosis.
MacPherson, Lisa, Manganas, Phanee, Tokatlidis, Kostas   +2 more
core   +1 more source

Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State [PDF]

, 2016
The mitochondrial thioredoxin system (NADPH, thioredoxin reductase, thioredoxin) is a major redox regulator. Here we have investigated the redox correlation between this system and the mitochondrial enzyme cyclophilin D.
Bindoli, Alberto, Cali', Tito, Citta, Anna, Folda, Alessandra, Rigobello, MARIA PIA, Scalcon, Valeria, Scutari, Guido, Zonta, Francesco   +7 more
core   +1 more source

Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER [PDF]

, 2017
Folding of proteins entering the secretory pathway in mammalian cells frequently requires the insertion of disulfide bonds. Disulfide insertion can result in covalent linkages found in the native structure as well as those that are not, so‐called non ...
Elias SJ Arnér, Fourie AM, Greg J Poet, Marcel Lith, Marie Anne Pringle, Neil J Bulleid, Ojore BV Oka, Philip J Robinson, Zhenbo Cao   +8 more
core   +2 more sources

Review

, 2020
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R, Arai K, Baskakov IV, Creighton TE, Dittmer K, Du Vigneaud V, Janeček J, Metanis N, Musiol HJ, Muttenthaler M, Nygard B, O'Donnell ME, Welch M, Yang F   +13 more
core   +1 more source

Paradoxical roles of antioxidant enzymes:Basic mechanisms and health implications [PDF]

, 2015
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) are generated from aerobic metabolism, as a result of accidental electron leakage as well as regulated enzymatic processes.
Amit R. Reddi, Arne Holmgren, Chan PH, Chen EP, Chu FF, Daiber A, Elias S. J. Arnér, Geismann C, Hogan B, Jaarsma D, Jian-Hong Zhu, Jin R, Leitzmann C, Li JJ, Li JJ, Lu YP, Makino N, Miranda-Vizuete A, Mirochnitchenko O, Motoori S, Mulder DW, Ogata M, Oury TD, Papaioannou V, Radi R, Sandbach JM, Takahara S, Thimmulappa RK, Tome ME, Vogel U, Wang F, Wen JK, Wen-Hsing Cheng, Wispe JR, Woychik RP, Xin Gen Lei, Ye-Shih Ho, Yongping Bao, Yoshida T   +38 more
core   +1 more source

The role of peroxiredoxins in cancer [PDF]

, 2017
Peroxiredoxins (PRDXs) are a ubiquitously expressed family of small (22-27 kDa) non-seleno peroxidases that catalyze the peroxide reduction of H2O2, organic hydroperoxides and peroxynitrite.
CAPALBO, CARLO, COPPA, Anna, D'INZEO, SONIA, GIANNINI, Giuseppe, NICOLUSSI, Arianna   +4 more
core   +1 more source

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
core   +3 more sources

The barley grain thioredoxin system - an update. [PDF]

, 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 ...
Barrero, José Maria, Björnberg, Olof, Bunkenborg, Jakob, Finnie, Christine, Gubler, Frank, Henriksen, Anette, Hägglund, Per, Kirkensgaard, Kristine Groth, Maeda, Kenji, Mørch Jensen, Johanne, Navrot, Nicolas, Shahpiri, Azar, Sultan, Abida, Svensson, Birte   +13 more
core   +4 more sources

Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation [PDF]

, 2014
Typical 2-cys peroxiredoxins are required to remove hydrogen peroxide from several different cellular compartments. Their activity can be regulated by hyperoxidation and consequent inactivation of the active site peroxidatic cysteine.
Bulleid, Neil J., Cao, Zhenbo, Subramaniam, Suraj   +2 more
core   +1 more source