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...
Những tác giả chính: | Cockman, M, Webb, J, Ratcliffe, P |
---|---|
Định dạng: | Journal article |
Ngôn ngữ: | English |
Được phát hành: |
2009
|
Những quyển sách tương tự
-
Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
Bằng: Cockman, M, et al.
Được phát hành: (2009) -
Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
Bằng: Cockman, M, et al.
Được phát hành: (2006) -
Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
Bằng: Coleman, M, et al.
Được phát hành: (2007) -
Asparaginyl beta-hydroxylation of proteins containing ankyrin repeat domains influences their stability and function.
Bằng: Hardy, A, et al.
Được phát hành: (2009) -
Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
Bằng: Yang, M, et al.
Được phát hành: (2011)