Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Anne J. Stokka"'
Publikováno v:
FEBS Open Bio, Vol 7, Iss 7, Pp 1026-1036 (2017)
Mammalian phenylalanine hydroxylase (PAH) is a key enzyme in l‐phenylalanine (l‐Phe) metabolism and is active as a homotetramer. Biochemical and biophysical work has demonstrated that it cycles between two states with a variably low and a high ac
Externí odkaz:
https://doaj.org/article/42c8efbce0d54fe8ac7f5f75f891e932
Publikováno v:
FEBS Open Bio
Mammalian phenylalanine hydroxylase (PAH) is a key enzyme in l‐phenylalanine (l‐Phe) metabolism and is active as a homotetramer. Biochemical and biophysical work has demonstrated that it cycles between two states with a variably low and a high ac
Autor:
Silje A, Solheim, Evangelia, Petsalaki, Anne J, Stokka, Robert B, Russell, Kjetil, Taskén, Torunn, Berge
Publikováno v:
The FEBS journal. 275(19)
Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched domains is a transmembrane adaptor protein primarily involved in negative regulation of T-cell activation by recruitment of C-terminal Src kinase (Csk), a protein tyrosine
Publikováno v:
European journal of biochemistry. 270(5)
The catalytic activity of phenylalanine hydroxylase (PAH, phenylalanine 4-monooxygenase EC 1.14.16.1) is regulated by three main mechanisms, i.e. substrate (l-phenylalanine, L-Phe) activation, pterin cofactor inhibition and phosphorylation of a singl