Understanding the rules governing NCX1 palmitoylation

Fiona Plain, Dionne Turnbull, Niall J. Fraser, William Fuller (Lead / Corresponding author)

Research output: Contribution to journalComment/debatepeer-review

6 Citations (Scopus)
148 Downloads (Pure)


The ability to identify sites of post-translational modification in proteins is central to understanding the molecular details of pathways regulating their activity. Through recent advances in mass spectrometry, many of the phosphorylation sites in the human proteome have been experimentally determined, and the kinases responsible predicted according to well-established consensus sequence motifs. However, what of other post-translational modifications? Can we predict these with as much certainty as we can phosphorylation?
Although the palmitoyl proteomes of many different tissues have been determined, reliable palmitoylation site prediction has thus far eluded us.
Original languageEnglish
Pages (from-to)377-379
Number of pages3
Issue number5
Early online date15 Jun 2017
Publication statusPublished - 10 Jul 2017


  • Acylation
  • Post-translational modification
  • Sodium
  • Calcium
  • Secondary structure
  • Substrate recognition


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