Detecting protein ADP-ribosylation using a clickable aminooxy probe

Rory K. Morgan, Michael S. Cohen

Research output: Chapter in Book/Report/Conference proceedingChapter

6 Scopus citations


ADP-ribosylation, a posttranslational modification catalyzed by a family of enzymes known as poly(ADP-ribose) polymerases (PARPs, 17 in humans), regulates diverse cellular processes. To aid in understanding the functions of ADP-ribosylation in cells, we developed a clickable aminooxy probe, AO-alkyne, which detects ADP-ribosylation of acidic amino acids. AO-alkyne can be used to detect auto-ADP-ribosylation of PARP10 in cells following Cu-catalyzed click conjugation to an azide reporter. This method can be extended to other PARP family members that catalyze ADP-ribosylation on acidic amino acids, providing a convenient and direct readout of PARP activity in cells.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages7
StatePublished - 2017

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • ADP-ribosylation
  • Bioconjugation
  • Click chemistry
  • Oxime ligation
  • PARPs

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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