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Structure‐activity relationship and crystallographic studies on 4‐hydroxypyrimidine HIF prolyl hydroxylase domain inhibitors

DOI: 10.1002/cmdc.201900557 DOI Help

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

Open Access Open Access

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, Biology and Bio-materials, Medicine

Instruments: I03-Macromolecular Crystallography

Added On: 04/12/2019 14:05


Discipline Tags:

Health & Wellbeing Biochemistry Chemistry Structural biology Organic Chemistry Drug Discovery Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)