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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.

Abstract:

Activity of the hypoxia-inducible factor (HIF) complex is controlled by oxygen-dependent hydroxylation of prolyl and asparaginyl residues. Hydroxylation of specific prolyl residues by 2-oxoglutarate (2-OG)-dependent oxygenases mediates ubiquitinylation and proteasomal destruction of HIF-alpha. Hydroxylation of an asparagine residue in the C-terminal transactivation domain (CAD) of HIF-alpha abrogates interaction with p300, preventing transcriptional activation. Yeast two-hybrid assays recentl...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.c200273200

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
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Journal:
The Journal of biological chemistry
Volume:
277
Issue:
29
Pages:
26351-26355
Publication date:
2002-07-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:652ea231-c694-4457-ac8b-c9742164fc20
Source identifiers:
10301
Local pid:
pubs:10301

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