PARP-3 Is a Mono-ADP-ribosylase That Activates PARP-1 in the Absence of DNA

PARP is activated at stalled forks to mediate Mre11-dependent replication restart and recombination

(2009) Helen E Bryant et al.   EMBO JOURNAL

Assessment of PARP-3 Distribution in Tissues of Cynomolgous Monkeys

(2009) Michèle Rouleau et al.   JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY

Structural Basis for Inhibitor Specificity in Human Poly(ADP-ribose) Polymerase-3†

(2009) Lari Lehtiö et al.   JOURNAL OF MEDICINAL CHEMISTRY

Discovery of 2-{4-[(3S)-Piperidin-3-yl]phenyl}-2H-indazole-7-carboxamide (MK-4827): A Novel Oral Poly(ADP-ribose)polymerase (PARP) Inhibitor Efficacious in BRCA-1 and -2 Mutant Tumors

(2009) Philip Jones et al.   JOURNAL OF MEDICINAL CHEMISTRY

Identification of the ADP-Ribosylation Sites in the PARP-1 Automodification Domain: Analysis and Implications

(2009) Zhihua Tao et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites

(2009) Matthias Altmeyer et al.   NUCLEIC ACIDS RESEARCH

Domain C of Human Poly(ADP-ribose) Polymerase-1 Is Important for Enzyme Activity and Contains a Novel Zinc-Ribbon Motif†,‡

(2008) Zhihua Tao et al.   BIOCHEMISTRY

The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects’ Review Series

(2008) Antoinette Hakmé et al.   EMBO REPORTS

Substrate-Assisted Catalysis by PARP10 Limits Its Activity to Mono-ADP-Ribosylation

(2008) Henning Kleine et al.   MOLECULAR CELL

Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins

(2008) Ivan Ahel et al.   NATURE

The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases

(2007) Paul et al.   Frontiers in Bioscience-Landmark