Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases.
Hydroxylation of two conserved prolyl residues in the N- and C-terminal oxygen-dependent degradation domains (NODD and CODD) of the alpha-subunit of hypoxia-inducible factor (HIF) signals for its degradation via the ubiquitin-proteasome pathway. In human cells, three prolyl hydroxylases (PHDs 1-3) b...
المؤلفون الرئيسيون: | Flashman, E, Bagg, E, Chowdhury, R, Mecinović, J, Loenarz, C, McDonough, M, Hewitson, K, Schofield, C |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2008
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مواد مشابهة
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Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases.
حسب: Chowdhury, R, وآخرون
منشور في: (2009) -
2-Oxoglutarate analogue inhibitors of prolyl hydroxylase domain 2.
حسب: Mecinović, J, وآخرون
منشور في: (2009) -
Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1)
حسب: Chowdhury, R, وآخرون
منشور في: (2011) -
Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).
حسب: Chowdhury, R, وآخرون
منشور في: (2011) -
Substrate selectivity of prolyl hydroxylases
حسب: McDonough, M
منشور في: (2018)