Journal
NATURE METHODS
Volume 10, Issue 10, Pages 981-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nmeth.2603
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Funding
- UT Southwestern Medical Center Endowed Scholar Program
- Cancer Prevention and Research Institute of Texas [CPRIT R1103]
- Welch Foundation [I-1800]
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Poly(ADP-ribosyl)ation is catalyzed by a family of enzymes known as PARPs. We describe a method to characterize the human aspartic acid- and glutamic acid-ADP-ribosylated proteome. We identified 1,048 ADADP-ribosylation sites on 340 proteins involved in a wide array of nuclear functions; among these were many previously unknown PARP downstream targets whose ADP-ribosylation was sensitive to PARP inhibitor treatment. We also confirmed that iniparib had a negligible effect on PARP activity in intact cells.
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