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Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases

Abstract:

The response to hypoxia in animals involves the expression of multiple genes regulated by the αβ-hypoxia inducible transcription factors (HIFs). The hypoxia sensing mechanism involves oxygen limited hydroxylation of prolyl-residues in the N- and C-terminal oxygen dependent degradation domains (NODD and CODD) of HIFα isoforms, as catalyzed by prolyl hydroxylases (PHD 1-3). Prolyl hydroxylation promotes binding of HIFα to the von Hippel-Lindau protein (VHL)-elongin B/C comp...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1038/ncomms12673

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Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Department:
Oxford, MSD, NDM, Human Genetics Wt Centre
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Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Funding agency for:
Leung, I
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Funding agency for:
Leung, I
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Communications Journal website
Volume:
7
Pages:
12673
Publication date:
2016-08-26
Acceptance date:
2016-07-21
DOI:
ISSN:
2041-1723
Pubs id:
pubs:638965
URN:
uri:12cf6418-4abb-40c3-aeac-025d24c2d10d
UUID:
12cf6418-4abb-40c3-aeac-025d24c2d10d
Local pid:
pubs:638965

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