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Chemical-biological exploration of the limits of the ras de- and repalmitoylating machinery

  • K. Görmer
  • , M. Bürger
  • , J.A. Kruijtzer
  • , I. Vetter
  • , N. Vartak
  • , L. Brunsveld
  • , P.I.H. Bastiaens
  • , R.M. Liskamp
  • , G. Triola
  • , H. Waldmann

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

A dynamic de-/repalmitoylation cycle determines localization and activity of H- and N-Ras. This combined cellular de- and repalmitoylation machinery has been shown to be substrate tolerant--it accepts variation of amino acid sequence, structure and configuration. Here, semisynthetic Ras-proteins in which the C-terminal amino acids are replaced by peptoid residues are used to reveal the first limitations of substrate recognition by the de- and repalmitoylating machinery.
Original languageEnglish
Pages (from-to)1017-1023
Number of pages7
JournalChemBioChem
Volume13
Issue number7
DOIs
Publication statusPublished - 2012

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