Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation.
The asparaginyl hydroxylase, factor-inhibiting hypoxia-inducible factor (HIF), is central to the oxygen-sensing pathway that controls the activity of HIF. Factor-inhibiting HIF (FIH) also catalyzes the hydroxylation of a large set of proteins that share a structural motif termed the ankyrin repeat d...
Auteurs principaux: | Singleton, R, Trudgian, D, Fischer, R, Kessler, B, Ratcliffe, P, Cockman, M |
---|---|
Format: | Journal article |
Langue: | English |
Publié: |
2011
|
Documents similaires
-
Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation
par: Singleton, R, et autres
Publié: (2011) -
Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor.
par: Yang, M, et autres
Publié: (2011) -
Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
par: Cockman, M, et autres
Publié: (2009) -
Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
par: Coleman, M, et autres
Publié: (2007) -
Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
par: Yang, M, et autres
Publié: (2011)