Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases

The response to hypoxia involves multiple genes regulated by the hypoxia inducible transcription factors (HIFs), whose stability is regulated by prolyl hydroxylation. Here the authors provide a molecular basis for the substrate selectivity of the HIF prolyl hydroxylases that can be altered in erythr...

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Autores principales:	Rasheduzzaman Chowdhury, Ivanhoe K. H. Leung, Ya-Min Tian, Martine I. Abboud, Wei Ge, Carmen Domene, François-Xavier Cantrelle, Isabelle Landrieu, Adam P. Hardy, Christopher W. Pugh, Peter J. Ratcliffe, Timothy D. W. Claridge, Christopher J. Schofield
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/bcbb0397431d45b6a10192b43d152868
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spelling	oai:doaj.org-article:bcbb0397431d45b6a10192b43d1528682021-12-02T17:32:53ZStructural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases10.1038/ncomms126732041-1723https://doaj.org/article/bcbb0397431d45b6a10192b43d1528682016-08-01T00:00:00Zhttps://doi.org/10.1038/ncomms12673https://doaj.org/toc/2041-1723The response to hypoxia involves multiple genes regulated by the hypoxia inducible transcription factors (HIFs), whose stability is regulated by prolyl hydroxylation. Here the authors provide a molecular basis for the substrate selectivity of the HIF prolyl hydroxylases that can be altered in erythrocytosis and cancer.Rasheduzzaman ChowdhuryIvanhoe K. H. LeungYa-Min TianMartine I. AbboudWei GeCarmen DomeneFrançois-Xavier CantrelleIsabelle LandrieuAdam P. HardyChristopher W. PughPeter J. RatcliffeTimothy D. W. ClaridgeChristopher J. SchofieldNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Rasheduzzaman Chowdhury Ivanhoe K. H. Leung Ya-Min Tian Martine I. Abboud Wei Ge Carmen Domene François-Xavier Cantrelle Isabelle Landrieu Adam P. Hardy Christopher W. Pugh Peter J. Ratcliffe Timothy D. W. Claridge Christopher J. Schofield Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases
description	The response to hypoxia involves multiple genes regulated by the hypoxia inducible transcription factors (HIFs), whose stability is regulated by prolyl hydroxylation. Here the authors provide a molecular basis for the substrate selectivity of the HIF prolyl hydroxylases that can be altered in erythrocytosis and cancer.
format	article
author	Rasheduzzaman Chowdhury Ivanhoe K. H. Leung Ya-Min Tian Martine I. Abboud Wei Ge Carmen Domene François-Xavier Cantrelle Isabelle Landrieu Adam P. Hardy Christopher W. Pugh Peter J. Ratcliffe Timothy D. W. Claridge Christopher J. Schofield
author_facet	Rasheduzzaman Chowdhury Ivanhoe K. H. Leung Ya-Min Tian Martine I. Abboud Wei Ge Carmen Domene François-Xavier Cantrelle Isabelle Landrieu Adam P. Hardy Christopher W. Pugh Peter J. Ratcliffe Timothy D. W. Claridge Christopher J. Schofield
author_sort	Rasheduzzaman Chowdhury
title	Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases
title_short	Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases
title_full	Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases
title_fullStr	Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases
title_full_unstemmed	Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases
title_sort	structural basis for oxygen degradation domain selectivity of the hif prolyl hydroxylases
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/bcbb0397431d45b6a10192b43d152868
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Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases

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