Inhibition of the Catalytic Activity of Hypoxia-Inducible Factor-1α-Prolyl-Hydroxylase 2 by a MYND-Type Zinc Finger-Reference-Cited by-同舟云学术

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Inhibition of the Catalytic Activity of Hypoxia-Inducible Factor-1α-Prolyl-Hydroxylase 2 by a MYND-Type Zinc Finger

Published:2005-09-09 Issue:6 Volume:68 Page:1803-1809
ISSN:0026-895X
Container-title:Molecular Pharmacology
language:en
Short-container-title:Mol Pharmacol

Author:

Choi Kyung-Ok,Lee Taekyong,Lee Naery,Kim Ji-Hyun,Yang Eun Gyeong,Yoon Jung Min,Kim Jin Hwan,Lee Tae Gyu,Park Hyunsung

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference30 articles.

1. The Conserved Mynd Domain of BS69 Binds Cellular and Oncoviral Proteins through a Common PXLXP Motif

2. Differential Function of the Prolyl Hydroxylases PHD1, PHD2, and PHD3 in the Regulation of Hypoxia-inducible Factor

3. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1 in normoxia

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

5. Role of Prolyl Hydroxylation in Oncogenically Stabilized Hypoxia-inducible Factor-1α

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1. The Pro-Oncogenic Adaptor CIN85 Acts as an Inhibitory Binding Partner of Hypoxia-Inducible Factor Prolyl Hydroxylase 2;Cancer Research;2019-05-29

2. The conservation and functionality of the oxygen-sensing enzyme Factor Inhibiting HIF (FIH) in non-vertebrates;PLOS ONE;2019-04-29

3. The pro-oncogenic adaptor CIN85 inhibits hypoxia-inducible factor prolyl hydroxylase-2;2018-11-09

4. Loss-of-function zinc finger mutation in the EGLN1 gene associated with erythrocytosis;Blood;2018-09-27

5. The Zinc Finger of Prolyl Hydroxylase Domain Protein 2 Is Essential for Efficient Hydroxylation of Hypoxia-Inducible Factor α;Molecular and Cellular Biology;2016-09-15

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