Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
Post-translational hydroxylation has been considered an unusual modification on intracellular proteins. However, following the recognition that oxygen-sensitive prolyl and asparaginyl hydroxylation are central to the regulation of the transcription factor hypoxia-inducible factor (HIF), interest has...
প্রধান লেখক: | Cockman, M, Webb, J, Kramer, H, Kessler, B, Ratcliffe, P |
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বিন্যাস: | Journal article |
ভাষা: | English |
প্রকাশিত: |
2009
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অনুরূপ উপাদানগুলি
অনুরূপ উপাদানগুলি
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FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.
অনুযায়ী: Cockman, M, অন্যান্য
প্রকাশিত: (2009) -
Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH).
অনুযায়ী: Cockman, M, অন্যান্য
প্রকাশিত: (2006) -
Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
অনুযায়ী: Coleman, M, অন্যান্য
প্রকাশিত: (2007) -
Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
অনুযায়ী: Yang, M, অন্যান্য
প্রকাশিত: (2011) -
Factor inhibiting HIF can catalyse two asparaginyl-hydroxylations in VNVN motifs of ankyrin fold proteins
অনুযায়ী: Leissing, TM, অন্যান্য
প্রকাশিত: (2022)