FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.

FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.

Studies on hypoxia-sensitive pathways have identified a series of Fe(II)-dependent dioxygenases that regulate hypoxia-inducible factor (HIF) by prolyl and asparaginyl hydroxylation. The asparaginyl hydroxylase factor inhibiting HIF (FIH) targets a conserved asparaginyl residue in the C-terminal tran...

Deskribapen osoa

Xehetasun bibliografikoak
Egile Nagusiak:	Cockman, M, Webb, J, Ratcliffe, P
Formatua:	Journal article
Hizkuntza:	English
Argitaratua:	2009

Antzeko izenburuak

Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
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Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
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Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
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Factor inhibiting HIF can catalyse two asparaginyl-hydroxylations in VNVN motifs of ankyrin fold proteins
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Asparagine beta-hydroxylation stabilizes the ankyrin repeat domain fold.
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Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.
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Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes [corrected].
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Signalling cross talk of the HIF system: involvement of the FIH protein.
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Studies on FIH interactions
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HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O(2) levels.
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Poxviral Ankyrin Proteins
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