Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1)
The hypoxic response in animals is mediated via the transcription factor hypoxia-inducible factor (HIF). An oxygen-sensing component of the HIF system is provided by Fe(II) and 2-oxoglutarate-dependent oxygenases that catalyse the posttranslational hydroxylation of the HIF-α subunit. It is proposed...
Main Authors: | Chowdhury, R, Flashman, E, Mecinović, J, Kramer, H, Kessler, B, Frapart, Y, Boucher, J, Clifton, I, McDonough, M, Schofield, C |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2011
|
Similar Items
-
Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).
by: Chowdhury, R, et al.
Published: (2011) -
Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases.
by: Chowdhury, R, et al.
Published: (2009) -
BIOL 56-ESI-MS studies on prolyl hydroxylase domain 2
by: Mecinovic, J, et al.
Published: (2008) -
Mutation Analysis of HIF-prolyl hydroxylases (PHD/EGLN) in Inherited Phaeochromocytoma and Renal Cell Carcinoma
by: Astuti, D, et al.
Published: (2010) -
Use of mass spectrometry to probe the nucleophilicity of cysteinyl residues of prolyl hydroxylase domain 2.
by: Mecinović, J, et al.
Published: (2009)