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...
Váldodahkkit: | Cockman, M, Webb, J, Ratcliffe, P |
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Materiálatiipa: | Journal article |
Giella: | English |
Almmustuhtton: |
2009
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Geahča maid
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Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
Dahkki: Cockman, M, et al.
Almmustuhtton: (2009) -
Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
Dahkki: Cockman, M, et al.
Almmustuhtton: (2006) -
Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
Dahkki: Coleman, M, et al.
Almmustuhtton: (2007) -
Asparaginyl beta-hydroxylation of proteins containing ankyrin repeat domains influences their stability and function.
Dahkki: Hardy, A, et al.
Almmustuhtton: (2009) -
Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
Dahkki: Yang, M, et al.
Almmustuhtton: (2011)