Abstract
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 ADP-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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Diphosphate Ribose / chemistry*
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Adenosine Diphosphate Ribose / genetics
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Adenosine Diphosphate Ribose / metabolism
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Aspartic Acid / chemistry*
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Aspartic Acid / metabolism
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Binding Sites
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DNA Damage
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Gene Knockdown Techniques
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Glutamic Acid / chemistry*
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Glutamic Acid / metabolism
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Glycoside Hydrolases / chemistry
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Glycoside Hydrolases / genetics
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Glycoside Hydrolases / metabolism
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HCT116 Cells
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Humans
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Hydrogen Peroxide / pharmacology
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Models, Molecular
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Poly (ADP-Ribose) Polymerase-1
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Poly(ADP-ribose) Polymerase Inhibitors
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Poly(ADP-ribose) Polymerases / chemistry*
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Poly(ADP-ribose) Polymerases / genetics
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Poly(ADP-ribose) Polymerases / metabolism
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Protein Conformation
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Protein Processing, Post-Translational
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Proteome / chemistry*
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Proteome / genetics
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Proteome / metabolism
Substances
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Poly(ADP-ribose) Polymerase Inhibitors
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Proteome
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Adenosine Diphosphate Ribose
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Aspartic Acid
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Glutamic Acid
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Hydrogen Peroxide
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PARP1 protein, human
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Poly (ADP-Ribose) Polymerase-1
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Poly(ADP-ribose) Polymerases
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Glycoside Hydrolases