A simple, sensitive, and generalizable plate assay for screening PARP inhibitors

Ilsa T. Kirby, Rory K. Morgan, Michael Cohen

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations

Abstract

Poly-ADP-ribose polymerases (also known as ADP-ribosyltransferases or ARTDs) are a family of 17 enzymes in humans that catalyze the reversible posttranslational modification known as ADP-ribosylation. PARPs are implicated in diverse cellular processes, from DNA repair to the unfolded protein response. Small-molecule inhibitors of PARPs have improved our understanding of PARP-mediated biology and, in some cases, have emerged as promising treatments for cancers and other human diseases. However these advancements are hindered, in part, by a poor understanding of inhibitor selectivity across the PARP family. Here, we describe a simple, sensitive, and generalizable plate assay to test the potency and selectivity of small molecules against several PARP enzymes in vitro. In principle, this assay can be extended to all active PARPs, providing a convenient and direct comparison of inhibitors across the entire PARP enzyme family.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages245-252
Number of pages8
DOIs
StatePublished - Jan 1 2018

Publication series

NameMethods in Molecular Biology
Volume1813
ISSN (Print)1064-3745

Keywords

  • 6-a-NAD
  • ADP-ribosylation
  • ARTDs
  • Click chemistry
  • PARPs
  • Screen
  • Small-molecule inhibitor

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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