Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Trond-André Kråkenes"'
Autor:
María Teresa Bueno-Carrasco, Jorge Cuéllar, Marte I. Flydal, César Santiago, Trond-André Kråkenes, Rune Kleppe, José R. López-Blanco, Miguel Marcilla, Knut Teigen, Sara Alvira, Pablo Chacón, Aurora Martinez, José M. Valpuesta
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the catecholamine neurotransmitters and hormones dopamine (DA), adrenaline and noradrenaline. Here, the authors present the cryo-EM structures of full-length human TH in t
Externí odkaz:
https://doaj.org/article/3b54c91d09444b37ba25ca02cc815dcd
Autor:
Trond-André Kråkenes, Mary Dayne S. Tai, Marte I. Flydal, Aurora Martinez, Knut Teigen, Maria P.A. Tran
Publikováno v:
Biochimie. 183:126-132
Tyrosine hydroxylase (TH) catalyses the (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4)-dependent conversion of L-tyrosine to L-3,4-dihydroxyphenylalanine (L-Dopa), which is the rate-limiting step in the synthesis of dopamine and other catecholamine
Autor:
Aurora Martinez, Maria Teresa Bezem, Fredrik Gullaksen Johannessen, Michael J. Sailor, Trond-André Kråkenes
Publikováno v:
Molecular Pharmaceutics
Tyrosine hydroxylase (TH) is the enzyme catalyzing the rate-limiting step in the synthesis of dopamine in the brain. Developing enzyme replacement therapies using TH could therefore be beneficial to patient groups with dopamine deficiency, and the us
Autor:
Knut Teigen, José Ramón López-Blanco, Pablo Chacón, Jorge Cuéllar, Rune Kleppe, Aurora Martinez, César Santiago, Marte I. Flydal, José M. Valpuesta, Trond-André Kråkenes, Sara Alvira, Teresa Bueno-Carrasco
Tyrosine hydroxylase (TH) is a highly regulated enzyme that catalyses the rate-limiting step in the biosynthesis of dopamine (DA) and other catecholamines. Mutations and dysfunction in this enzyme lead to DA deficiency and parkinsonisms of different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::03a8c8befef21a868f87c0a99aa3f0d4
https://doi.org/10.21203/rs.3.rs-64971/v1
https://doi.org/10.21203/rs.3.rs-64971/v1