Journal article
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
Actions
Authors
Funding
+ Biotechnology and Biological Sciences Research Council
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Funding agency for:
Leung, I
+ Centre National de la Recherche Scientifique (CNRS)-Oxford Collaboration Scheme
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Funding agency for:
Leung, I
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Bibliographic Details
- 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
- Source identifiers:
-
638965
Item Description
- Pubs id:
-
pubs:638965
- UUID:
-
uuid:12cf6418-4abb-40c3-aeac-025d24c2d10d
- Local pid:
- pubs:638965
- Deposit date:
- 2016-08-17
Terms of use
- Copyright holder:
- Chowdhury et al
- Copyright date:
- 2016
- Notes:
- © The Author(s) 2016
- Licence:
- CC Attribution (CC BY)
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