Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Niina Nyberg"'
Autor:
Sanna Niinivehmas, Pekka A. Postila, Sanna Rauhamäki, Elangovan Manivannan, Sami Kortet, Mira Ahinko, Pasi Huuskonen, Niina Nyberg, Pasi Koskimies, Sakari Lätti, Elina Multamäki, Risto O. Juvonen, Hannu Raunio, Markku Pasanen, Juhani Huuskonen, Olli T. Pentikäinen
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 743-754 (2018)
A comprehensive set of 3-phenylcoumarin analogues with polar substituents was synthesised for blocking oestradiol synthesis by 17-β-hydroxysteroid dehydrogenase 1 (HSD1) in the latter part of the sulphatase pathway. Five analogues produced ≥62% HS
Externí odkaz:
https://doaj.org/article/ca9ca7ff4f1a4f61961e932f9fb13641
Autor:
Sanna Rauhamäki, Pekka A. Postila, Sanna Niinivehmas, Sami Kortet, Emmi Schildt, Mira Pasanen, Elangovan Manivannan, Mira Ahinko, Pasi Koskimies, Niina Nyberg, Pasi Huuskonen, Elina Multamäki, Markku Pasanen, Risto O. Juvonen, Hannu Raunio, Juhani Huuskonen, Olli T. Pentikäinen
Publikováno v:
Frontiers in Chemistry, Vol 6 (2018)
Monoamine oxidase B (MAO-B) catalyzes deamination of monoamines such as neurotransmitters dopamine and norepinephrine. Accordingly, small-molecule MAO-B inhibitors potentially alleviate the symptoms of dopamine-linked neuropathologies such as depress
Externí odkaz:
https://doaj.org/article/7ce7e89c445b4b708ee76689792f6021
Autor:
Pekka A. Postila, Elina Multamäki, Sanna Niinivehmas, Markku Pasanen, Juhani Huuskonen, Risto O. Juvonen, Pasi Koskimies, Niina Nyberg, Sakari Lätti, Pasi Huuskonen, Hannu Raunio, Sami Kortet, Olli T. Pentikäinen, Mira Ahinko, Elangovan Manivannan, Sanna Rauhamäki
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 743-754 (2018)
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 743-754 (2018)
A comprehensive set of 3-phenylcoumarin analogues with polar substituents was synthesised for blocking oestradiol synthesis by 17-b-hydroxysteroid dehydrogenase 1 (HSD1) in the latter part of the sulphatase pathway. Five analogues produced 62% HSD1 i