Journal article
Lack of activity of recombinant HIF prolyl hydroxylases (PHDs) on reported non-HIF substrates
- Abstract:
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Human and other animal cells deploy three closely related dioxygenases (PHD 1, 2 and 3) to signal oxygen levels by catalysing oxygen regulated prolyl hydroxylation of the transcription factor HIF. The discovery of the HIF prolyl-hydroxylase (PHD) enzymes as oxygen sensors raises a key question as to the existence and nature of non-HIF substrates, potentially transducing other biological responses to hypoxia. Over 20 such substrates are reported. We therefore sought to characterise their react...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 4.0MB)
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- Publisher copy:
- 10.7554/eLife.46490.001
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Authors
Funding
Ludwig Institute for Cancer Research
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Bibliographic Details
- Publisher:
- eLife Sciences Publications Publisher's website
- Journal:
- eLife Journal website
- Volume:
- 8
- Issue:
- 2019
- Article number:
- e46490
- Publication date:
- 2019-09-10
- Acceptance date:
- 2019-07-22
- DOI:
- ISSN:
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2050-084X
- Source identifiers:
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1045731
Item Description
- Pubs id:
-
pubs:1045731
- UUID:
-
uuid:d8c7819e-9598-47d0-aed3-1751b8883f77
- Local pid:
- pubs:1045731
- Deposit date:
- 2019-08-20
Terms of use
- Copyright date:
- 2019
- Notes:
- This is an open access article distributed under the terms of the Creative Commons Attribution Licence
- Licence:
- CC Attribution (CC BY)
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