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

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

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bcbb0397431d45b6a10192b43d152868

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

About this item

Full title

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

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2016-08, Vol.7 (1), p.12673-12673, Article 12673

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The response to hypoxia in animals involves the expression of multiple genes regulated by the αβ-hypoxia-inducible transcription factors (HIFs). The hypoxia-sensing mechanism involves oxygen limited hydroxylation of prolyl residues in the N- and C-terminal oxygen-dependent degradation domains (NODD and CODD) of HIFα isoforms, as catalysed by prolyl...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_bcbb0397431d45b6a10192b43d152868

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bcbb0397431d45b6a10192b43d152868

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms12673

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