Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro.

@article{MurrayRust2006PurifiedRH,
  title={Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro.},
  author={Thomas A Murray-Rust and Neil J Oldham and Kirsty S. Hewitson and Christopher J. Schofield},
  journal={FEBS letters},
  year={2006},
  volume={580 8},
  pages={1911-8}
}
In humans, many responses to hypoxia including angiogenesis and erythropoiesis are mediated by the alpha/beta-heterodimeric transcription factor hypoxia inducible factor (HIF). The stability and/or activity of human HIF-1alpha are modulated by post-translational modifications including prolyl and asparaginyl hydroxylation, phosphorylation, and reportedly by acetylation of the side-chain of Lys532 by ARD1 (arrest defective protein 1 homologue), an acetyltransferase. Using purified recombinant… CONTINUE READING

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