期刊
BIOCHEMICAL JOURNAL
卷 367, 期 -, 页码 571-575出版社
PORTLAND PRESS
DOI: 10.1042/BJ20021162
关键词
asparagine hydroxylation; factor inhibiting hypoxia-inducible; factor-1 (FIH-1); hypoxia; oxygenase; oxygen sensing
Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo-isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro-isomer.
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