Structural Basis of Prolyl Hydroxylase Domain Inhibition by Molidustat-Reference-Cited by-同舟云学术

Structural Basis of Prolyl Hydroxylase Domain Inhibition by Molidustat

Published:2021-04-09 Issue: Volume: Page:
ISSN:1860-7179
Container-title:ChemMedChem
language:en
Short-container-title:ChemMedChem

Author:

Figg William D.¹^ORCID,McDonough Michael A.¹^ORCID,Chowdhury Rasheduzzaman¹²^ORCID,Nakashima Yu¹³,Zhang Zhihong¹,Holt‐Martyn James P.¹,Krajnc Alen¹^ORCID,Schofield Christopher J.¹^ORCID

Affiliation:

1. Department of Chemistry University of Oxford 12 Mansfield Road Oxford OX1 3TA UK

2. Cardiovascular Research Institute University of California, San Francisco 555 Mission Bay Blvd. San Francisco CA 94158 USA

3. Institute of Natural Medicine University of Toyama 2630 Sugitani Toyama 930–0194 Japan

Funder

Wellcome Trust

Cancer Research UK

Publisher

Wiley

Subject

Organic Chemistry,General Pharmacology, Toxicology and Pharmaceutics,Molecular Medicine,Drug Discovery,Biochemistry,Pharmacology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.202100133

Reference29 articles.

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2. The von Hippel–Lindau tumour suppressor protein: O2 sensing and cancer

3. A Conserved Family of Prolyl-4-Hydroxylases That Modify HIF

4. Hypoxia-inducible Factor (HIF) Asparagine Hydroxylase Is Identical to Factor Inhibiting HIF (FIH) and Is Related to the Cupin Structural Family

5. Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803

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