- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1074/jbc.c200273200
-
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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
- Language:
- English
- Keywords:
- Copyright date:
- 2002
Journal article
Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family.
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