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- W2024222023 endingPage "1357" @default.
- W2024222023 startingPage "1352" @default.
- W2024222023 abstract "Phenylalanine hydroxylase is regulated in a complex manner, including activation by phosphorylation. It is normally found as an equilibrium of dimeric and tetrameric species, with the tetramer thought to be the active form. We converted the protein to the dimeric form by deleting the C-terminal 24 residues and show that the truncated protein remains active and regulated by phosphorylation. This indicates that changes in the tetrameric quaternary structure of phenylalanine hydroxylase are not required for enzyme activation. Truncation also facilitates crystallization of both phosphorylated and dephosphorylated forms of the enzyme." @default.
- W2024222023 created "2016-06-24" @default.
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- W2024222023 date "1997-06-01" @default.
- W2024222023 modified "2023-10-11" @default.
- W2024222023 title "Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase" @default.
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- W2024222023 doi "https://doi.org/10.1002/pro.5560060626" @default.
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- W2024222023 hasPublicationYear "1997" @default.
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