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pro vyhledávání: '"Karin Anestål"'
Publikováno v:
PLoS ONE, Vol 3, Iss 4, p e1846 (2008)
BackgroundSecTRAPs (selenium compromised thioredoxin reductase-derived apoptotic proteins) can be formed from the selenoprotein thioredoxin reductase (TrxR) by targeting of its selenocysteine (Sec) residue with electrophiles, or by its removal throug
Externí odkaz:
https://doaj.org/article/fa2cadde54034892ad8c477ccacbeaa3
Publikováno v:
PLoS ONE
PLoS ONE, Vol 3, Iss 4, p e1846 (2008)
PLoS ONE, Vol 3, Iss 4, p e1846 (2008)
BackgroundSecTRAPs (selenium compromised thioredoxin reductase-derived apoptotic proteins) can be formed from the selenoprotein thioredoxin reductase (TrxR) by targeting of its selenocysteine (Sec) residue with electrophiles, or by its removal throug
Publikováno v:
Free radical biologymedicine. 39(5)
Mammalian thioredoxin reductase (TrxR) is important for cell proliferation, antioxidant defense, and redox signaling. Together with glutathione reductase (GR) it is the main enzyme providing reducing equivalents to many cellular processes. GR and Trx
Autor:
Karin Anestål, Elias S.J. Arnér
Publikováno v:
The Journal of biological chemistry. 278(18)
Mammalian thioredoxin reductases are selenoproteins. For native catalytic activity, these enzymes utilize a C-terminal -Gly-Cys-Sec-Gly-COOH sequence (where Sec is selenocysteine) forming a redox active selenenylsulfide/selenolthiol motif. A range of