Journal article
Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
- Abstract:
-
The stability and activity of hypoxia-inducible factor (HIF) are regulated by the post-translational hydroxylation of specific prolyl and asparaginyl residues. We show that the HIF asparaginyl hydroxylase, factor inhibiting HIF (FIH), also catalyzes hydroxylation of highly conserved asparaginyl residues within ankyrin repeat (AR) domains (ARDs) of endogenous Notch receptors. AR hydroxylation decreases the extent of ARD binding to FIH while not affecting signaling through the canonical Notch p...
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- Publication status:
- Published
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- Publisher copy:
- 10.1074/jbc.m704102200
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Authors
Bibliographic Details
- Journal:
- Journal of biological chemistry
- Volume:
- 282
- Issue:
- 33
- Pages:
- 24027-24038
- Publication date:
- 2007-08-01
- DOI:
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- Source identifiers:
-
18302
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:18302
- UUID:
-
uuid:74826a6b-6a38-4c6a-a6bd-6253c0621f10
- Local pid:
- pubs:18302
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2007
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