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Structure‐Activity Relationship and Crystallographic Studies on 4‐Hydroxypyrimidine HIF Prolyl Hydroxylase Domain Inhibitors
Author(s) -
HoltMartyn James P.,
Chowdhury Rasheduzzaman,
Tumber Anthony,
Yeh TzuLan,
Abboud Martine I.,
Lippl Kerstin,
Lohans Christopher T.,
Langley Gareth W.,
Figg William,
McDonough Michael A.,
Pugh Christopher W.,
Ratcliffe Peter J.,
Schofield Christopher J.
Publication year - 2020
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201900557
Subject(s) - chemistry , stereochemistry , domain (mathematical analysis) , mathematics , mathematical analysis
Abstract The 2‐oxoglutarate‐dependent hypoxia inducible factor prolyl hydroxylases (PHDs) are targets for treatment of a variety of diseases including anaemia. One PHD inhibitor is approved for use for the treatment of renal anaemia and others are in late stage clinical trials. The number of reported templates for PHD inhibition is limited. We report structure–activity relationship and crystallographic studies on a promising class of 4‐hydroxypyrimidine‐containing PHD inhibitors.