- Abstract:
- We describe covalently binding modulators of the activity of human prolyl hydroxylase domain 2 (PHD2) and studies towards a strategy for photocapture of PHD2 substrates. Reversible active site binding of electrophile bearing compounds enables susbsequent covalent reaction with a lysine residue (K408) in the flexible C-terminal region of PHD2 to give a modified protein that retains catalytic activity.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's Version
- Files:
-
-
(pdf, 4.2MB)
-
- Publisher copy:
- 10.1039/C8CC07706A
-
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- Publisher:
- Royal Society of Chemistry Publisher's website
- Journal:
- Chemical Communications Journal website
- Volume:
- 55
- Issue:
- 8
- Pages:
- 1020-1023
- Publication date:
- 2018-11-19
- Acceptance date:
- 2018-11-01
- DOI:
- EISSN:
-
1364-548X
- ISSN:
-
1359-7345
- Pubs id:
-
pubs:936513
- URN:
-
uri:3fcef202-cb23-4209-8d01-7298411b874a
- UUID:
-
uuid:3fcef202-cb23-4209-8d01-7298411b874a
- Local pid:
- pubs:936513
- Copyright holder:
- The Royal Society of Chemistry
- Copyright date:
- 2018
- Notes:
- © The Royal Society of Chemistry 2018. Open Access Article. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence
Journal article
Small-molecules that covalently react with a human prolyl hydroxylase – towards activity modulation and substrate capture
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