Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry

Peng Li, Yuanli Zhen, Yonghao Yu

Research output: Chapter in Book/Report/Conference proceedingChapter

7 Scopus citations


ADP-ribosylation is a protein post-translational modification that is critically involved in a wide array of biological processes connected to cell stress responses. Enzymes known as poly-ADP-ribose polymerases (PARPs) catalyze the addition of the ADP-ribose units to amino acids with various side chain chemistries. In particular, the PARP family member PARP1 is responsible for the modification of a large number of proteins and is involved in initiation of the DNA damage response, although the mechanisms through which PARP1 functions are still incompletely understood. The analysis of protein ADP-ribosylation is challenging because PARylation is a low-abundance, labile and heterogeneous protein modification. Recently, we developed an integrative proteomic platform for the site-specific analysis of protein ADP-ribosylation on Asp and Glu residues. Herein, we describe the method, and demonstrate its utility in quantitative characterization of the human Asp- and Glu-ADP-ribosylated proteome.

Original languageEnglish (US)
Title of host publicationPost-translational Modifications That Modulate Enzyme Activity
EditorsBenjamin A. Garcia
PublisherAcademic Press Inc.
Number of pages21
ISBN (Print)9780128186695
StatePublished - 2019

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


  • ADP-ribosylation
  • Cancer
  • DNA damage response
  • NAD + metabolism
  • PARP

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry'. Together they form a unique fingerprint.

Cite this