Small-molecules that covalently react with a human prolyl hydroxylase – towards activity modulation and substrate capture
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...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Published: |
Royal Society of Chemistry
2018
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