@inbook{69b52abbfe914b8c9edd0c87ee8f1f54,
title = "Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry",
abstract = "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.",
keywords = "ADP-ribosylation, Cancer, DNA damage response, NAD + metabolism, PARP",
author = "Peng Li and Yuanli Zhen and Yonghao Yu",
note = "Funding Information: This work was supported in part by grants from the Welch Foundation (I-1800 to Y.Y.) and NIH (GM122932 to Y.Y.). Publisher Copyright: {\textcopyright} 2019 Elsevier Inc.",
year = "2019",
doi = "10.1016/bs.mie.2019.06.024",
language = "English (US)",
isbn = "9780128186695",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "301--321",
editor = "Garcia, {Benjamin A.}",
booktitle = "Post-translational Modifications That Modulate Enzyme Activity",
}