@inbook{4653929c1d714d5c82ac73ea2aea4508,
title = "Methods for Purification of Proteins Associated with Cellular Poly(ADP-Ribose) and PARP-Specific Poly(ADP-Ribose)",
abstract = "Poly(ADP-ribose) (pADPr) is a posttranslational modification that regulates protein function through two major mechanisms: covalent modification of acceptor proteins and noncovalent binding of proteins to pADPr. pADPr is synthesized by a family of enzymes called poly(ADP-ribose) polymerases (PARPs) that are themselves major targets of pADPr modification. Here, we outline two methods for the purification of pADPr-binding proteins via pADPr purification under native conditions: purification of cellular pADPr and pADPr covalently linked to specific PARPs. Together, these methods provide complementary approaches to the identification of noncovalent pADPr–protein interactions in the cell.",
keywords = "Boronate affinity, Immunoprecipitation, PARP, Poly(ADP-ribose), Poly(ADP-ribose) acceptor protein, Poly(ADP-ribose) associated protein, Poly(ADP-ribose) polymerase, Poly(ADP-ribose) purification, cis-diol",
author = "Rood, {Jennifer E.} and Leung, {Anthony K.L.} and Paul Chang",
note = "Publisher Copyright: {\textcopyright} 2011, Springer Science+Business Media, LLC.",
year = "2011",
doi = "10.1007/978-1-61779-270-0_10",
language = "English (US)",
isbn = "9781617792694",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "153--164",
booktitle = "Poly(ADP-ribose) Polymerase",
}