Journal article
Structural basis for binding of the renal carcinoma target hypoxia-inducible factor 2α to prolyl hydroxylase domain 2
- Abstract:
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The hypoxia-inducible factor (HIF) prolyl-hydroxylases (human PHD1-3) catalyze prolyl hydroxylation in oxygen-dependent degradation (ODD) domains of HIFα isoforms, modifications that signal for HIFα proteasomal degradation in an oxygen-dependent manner. PHD inhibitors are used for treatment of anemia in kidney disease. Increased erythropoietin (EPO) in patients with familial/idiopathic erythrocytosis and pulmonary hypertension is associated with mutations in EGLN1 (PHD2) and EPAS1 (HIF2α); a ...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 4.0MB, Terms of use)
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- Publisher copy:
- 10.1002/prot.26541
Authors
Funding
+ Biotechnology and Biological Sciences Research Council
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Grant:
BB/J001694/2
BB/L000121/1
BB/R013829/1
Bibliographic Details
- Publisher:
- Wiley
- Journal:
- Proteins More from this journal
- Volume:
- 91
- Issue:
- 11
- Pages:
- 1510-1524
- Place of publication:
- United States
- Publication date:
- 2023-07-14
- Acceptance date:
- 2023-06-08
- DOI:
- EISSN:
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1097-0134
- ISSN:
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0887-3585
- Pmid:
-
37449559
Item Description
- Language:
-
English
- Keywords:
- Pubs id:
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1496097
- Local pid:
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pubs:1496097
- Deposit date:
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2023-08-07
Terms of use
- Copyright holder:
- Figg et al
- Copyright date:
- 2023
- Rights statement:
- © 2023 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
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