- Abstract:
- Prolyl hydroxylation of hypoxia inducible factor (HIF)-α, as catalysed by the Fe(II)/2-oxoglutarate (2OG)-dependent prolyl hydroxylase domain (PHD) enzymes, has a hypoxia sensing role in animals. We report that binding of prolyl-hydroxylated HIF-α to PHD2 is ~50 fold hindered by prior 2OG binding; thus, when 2OG is limiting, HIF-α degradation might be inhibited by PHD binding
- Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 2.2mb)
-
- Publisher copy:
- 10.1039/C8CC00387D
-
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- Publisher:
- Royal Society of Chemistry Publisher's website
- Journal:
- Chemical Communications Journal website
- Volume:
- 54
- Issue:
- 25
- Pages:
- 3130-3133
- Publication date:
- 2018-03-09
- Acceptance date:
- 2018-01-31
- DOI:
- EISSN:
-
1364-548X
- ISSN:
-
1359-7345
- Pubs id:
-
pubs:821941
- URN:
-
uri:3ac24af1-3ca0-4ba4-9c27-f26f64a0b7eb
- UUID:
-
uuid:3ac24af1-3ca0-4ba4-9c27-f26f64a0b7eb
- Local pid:
- pubs:821941
- Copyright date:
- 2018
- Notes:
- This article is licensed under a Creative Commons Attribution 3.0 Unported Licence
Journal article
2-oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2
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