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Structure‐activity relationship and crystallographic studies on 4‐hydroxypyrimidine HIF prolyl hydroxylase domain inhibitors
Authors:
James P.
Holt‐martyn
(University of Oxford)
,
Rasheduzzaman
Chowdhury
(University of Oxford)
,
Anthony
Tumber
(University of Oxford)
,
Tzu‐lan
Yeh
(University of Oxford)
,
Martine I.
Abboud
(University of Oxford)
,
Kerstin
Lippl
(University of Oxford)
,
Christopher T.
Lohans
(University of Oxford)
,
Gareth W.
Langley
(University of Oxford)
,
William
Figg
(University of Oxford)
,
Michael A.
Mcdonough
(University of Oxford)
,
Christopher W.
Pugh
(University of Oxford)
,
Peter J.
Ratcliffe
(University of Oxford)
,
Christopher J.
Schofield
(University of Oxford)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Chemmedchem
, VOL 13
State:
Published (Approved)
Published:
December 2019
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.
Journal Keywords: anaemia; hypoxia; prolyl hydroxylases; structure-activity relationships
Subject Areas:
Chemistry
Instruments:
I03-Macromolecular Crystallography
Discipline Tags:
Technical Tags: