Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory Domain

Family-wide chemical profiling and structural analysis of PARP and tankyrase inhibitors

(2012) Elisabet Wahlberg et al.   NATURE BIOTECHNOLOGY

PARP16/ARTD15 Is a Novel Endoplasmic-Reticulum-Associated Mono-ADP-Ribosyltransferase That Interacts with, and Modifies Karyopherin-ß1

(2012) Simone Di Paola et al.   PLoS One

Crystal Structure of the Catalytic Domain of Human PARP2 in Complex with PARP Inhibitor ABT-888

(2010) Tobias Karlberg et al.   BIOCHEMISTRY

Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes

(2010) Matteo Citarelli et al.   BMC EVOLUTIONARY BIOLOGY

The Zn3 Domain of Human Poly(ADP-ribose) Polymerase-1 (PARP-1) Functions in Both DNA-dependent Poly(ADP-ribose) Synthesis Activity and Chromatin Compaction

(2010) Marie-France Langelier et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Dali server: conservation mapping in 3D

(2010) Liisa Holm et al.   NUCLEIC ACIDS RESEARCH

Toward a unified nomenclature for mammalian ADP-ribosyltransferases

(2010) Michael O. Hottiger et al.   TRENDS IN BIOCHEMICAL SCIENCES

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

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

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