Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.
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 pr...
Main Authors: | McNeill, L, Hewitson, K, Claridge, T, Seibel, J, Horsfall, L, Schofield, C |
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Format: | Journal article |
Sprog: | English |
Udgivet: |
2002
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Lignende værker
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Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
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Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
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Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family.
af: Hewitson, K, et al.
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FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
af: Cockman, M, et al.
Udgivet: (2009) -
Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
af: Yang, M, et al.
Udgivet: (2011)