Zobrazeno 1 - 10
of 626
pro vyhledávání: '"Flohé, L"'
Publikováno v:
In Redox Biology July 2020 34
Publikováno v:
Journal of Cheminformatics, Vol 2, Iss Suppl 1, p P24 (2010)
Externí odkaz:
https://doaj.org/article/660994b0325041778f5f715fe552206b
Publikováno v:
In Journal of Biotechnology 2004 108(1):31-39
Publikováno v:
Redox Report. 2003, Vol. 8 Issue 5, p256-264. 9p. 3 Diagrams, 1 Chart.
Publikováno v:
In Free Radical Biology and Medicine 1999 27(9):966-984
Autor:
Orian, Laura, BOSELLO TRAVAIN, Valentina, Flohé, L., Maiorino, Matilde, Miotto, Giovanni, Polimeno, Antonino, Roveri, Antonella, Toppo, Stefano, Ursini, Fulvio, Zaccarin, Mattia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3657::fb03477bb0e66b0db6f1a21290517cea
http://hdl.handle.net/11577/3166516
http://hdl.handle.net/11577/3166516
Autor:
Flohé L
Publikováno v:
Ciba Foundation Symposium 65 - Oxygen Free Radicals and Tissue Damage
The present knowledge of glutathione (GSH) peroxidase is briefly reviewed: GSH peroxidase has a molecular weight of about 85,000, consists of four apparently-identical subunits and contains four g atom of selenium/mol. The enzyme-bound selenium can u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::094ce512be313cdc1fe50c9f64834e29
https://doi.org/10.1002/9780470715413.ch7
https://doi.org/10.1002/9780470715413.ch7
Autor:
Flohé L
Publikováno v:
Medizinische Klinik. 92:5-7
Out of the growing number of so far known mammalian selenoproteins four are peroxidases. Their common catalytic mechanism involves redox shuttling of a selenocysteine residue in the active site, where it forms a characteristic catalytic triad with hy