A family of macrodomain proteins reverses cellular mono-ADP-ribosylation

Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element

(2012) In-Kwon Kim et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

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

Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase

(2012) Mark S. Dunstan et al.   Nature Communications

Orphan Macrodomain Protein (Human C6orf130) Is anO-Acyl-ADP-ribose Deacylase

(2011) Francis C. Peterson et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Identification of Macrodomain Proteins as NovelO-Acetyl-ADP-ribose Deacetylases

(2011) Dawei Chen et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Hydrolysis ofO-Acetyl-ADP-ribose Isomers by ADP-ribosylhydrolase 3

(2011) Atsushi Kasamatsu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

(2011) Dea Slade et al.   NATURE

XDS

(2010) Wolfgang Kabsch   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PARP1 ADP-ribosylates lysine residues of the core histone tails

(2010) Simon Messner et al.   NUCLEIC ACIDS RESEARCH

Substrate-assisted catalysis: Molecular basis and biological significance

(2010) William Dall'Acqua et al.   PROTEIN SCIENCE

MolProbity: all-atom structure validation for macromolecular crystallography

(2009) Vincent B. Chen et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Sensing NAD metabolites through macro domains

(2009) Susanne Till   Frontiers in Bioscience-Landmark

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

A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation

(2009) Gyula Timinszky et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

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

Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome

(2009) N. Dani et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Differential Activities of Cellular and Viral Macro Domain Proteins in Binding of ADP-Ribose Metabolites

(2008) Maarit Neuvonen et al.   JOURNAL OF MOLECULAR BIOLOGY

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

(2008) Henning Kleine et al.   MOLECULAR CELL

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