@inbook{99cb09d9bb4443058a8c1fa5a13a66fd,
title = "Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography-Tandem Mass Spectrometry",
abstract = "ADP-ribosylation is a posttranslational modification (PTM) that affects a variety of cellular processes. In recent years, mass spectrometry (MS)-based proteomics has become a valuable tool for studying ADP-ribosylation. However, studying this PTM in vivo in an unbiased and sensitive manner has remained a difficult challenge. Here, we describe a detailed protocol for unbiased analysis of ADP-ribosylated proteins and their ADP-ribose acceptor sites under physiological conditions. The method relies on the enrichment of mono-ADP-ribosylated peptides using the macrodomain Af1521 in combination with liquid chromatography-high-resolution tandem MS (LC-MS/MS). The 5-day protocol explains the step-by-step enrichment and identification of ADP-ribosylated peptides from cell culture stage all the way through to data processing using the MaxQuant software suite.",
keywords = "Journal Article",
author = "Larsen, {Sara C} and Mario Leutert and Vera Bilan and Rita Martello and Stephanie Jungmichel and Clifford Young and Hottiger, {Michael O} and Nielsen, {Michael L}",
year = "2017",
doi = "10.1007/978-1-4939-6993-7_11",
language = "English",
isbn = "978-1-4939-6992-0",
volume = "1608",
series = "Methods in molecular biology (Clifton, N.J.)",
publisher = "Humana Press",
pages = "149--162",
editor = "Tulin, {Alexei V.}",
booktitle = "Poly(ADP-Ribose) Polymerase",
address = "United States",
}