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...
मुख्य लेखकों: | Flashman, E, Bagg, E, Chowdhury, R, Mecinović, J, Loenarz, C, McDonough, M, Hewitson, K, Schofield, C |
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स्वरूप: | Journal article |
भाषा: | English |
प्रकाशित: |
2008
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समान संसाधन
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Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases.
द्वारा: Chowdhury, R, और अन्य
प्रकाशित: (2009) -
2-Oxoglutarate analogue inhibitors of prolyl hydroxylase domain 2.
द्वारा: Mecinović, J, और अन्य
प्रकाशित: (2009) -
Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1)
द्वारा: Chowdhury, R, और अन्य
प्रकाशित: (2011) -
Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).
द्वारा: Chowdhury, R, और अन्य
प्रकाशित: (2011) -
Substrate selectivity of prolyl hydroxylases
द्वारा: McDonough, M
प्रकाशित: (2018)