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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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Journal:
The Journal of biological chemistry
Volume:
282
Issue:
33
Pages:
24027-24038
Publication date:
2007-08-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:74826a6b-6a38-4c6a-a6bd-6253c0621f10
Source identifiers:
18302
Local pid:
pubs:18302

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