Poly(ADP-Ribose) Polymerase

Quantitation of Poly(ADP-ribose) by Isotope Dilution Mass Spectrometry.- Quantification of PARP Activity in Human Tissues: Ex Vivo Assays in Blood Cells and Immunohistochemistry in Human Biopsies.- Detecting and Quantifying pADPr In Vivo.- Compartment-Specific Poly-ADP-Ribose Formation as a Biosensor for Subcellular NAD Pools.- Cell Cycle Resolved Measurements of Poly(ADP-ribose) Formation and DNA Damage Signaling by Quantitative Image-Based Cytometry.- Detecting Protein ADP-Ribosylation Using a Clickable Aminooxy Probe.- ADP-Ribosylated Peptide Enrichment and Site Identification: The Phosphodiesterase-Based Method.- Using Clickable NAD+ Analogues to Label Substrate Proteins of PARPs.- Identification of Protein Substrates of Specific PARP Enzymes Using Analog-Sensitive PARP Mutants and a 'Clickable' NAD+ Analog.- Identification of ADP-Ribose Acceptor Sites on In Vitro Modified Proteins by Liquid Chromatography - Tandem Mass Spectrometry.- Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography -Tandem Mass Spectrometry.- Poly(ADP-Ribose)-Dependent Chromatin Remodeling in DNA Repair.- Methods to Assess the Role of Poly(ADP-Ribose) Polymerases in Regulating Mitochondrial Oxidative Function.- Approaches for Investigating Translational Regulation Controlled by PARP1: Biotin-Based UV-Crosslinking and Luciferase Reporter Assay.- Methodology to Identify Poly-ADP-Ribose Polymerase 1 (PARP1) - mRNA Targets by PAR-CLiP.- Biochemical and Biophysical Methods for Analysis of Poly(ADP-Ribose) Polymerase 1 and Its Interactions with Chromatin.- PARP-1 Interaction with and Activation by Histones and Nucleosomes.- Strategies Employed for the Development of PARP Inhibitors.- High-Throughput Colorimetric Assay for Identifying PARP-1 Inhibitors Using a Large Small-Molecule Collection.- Testing PARP Inhibitors Using a Subcutaneous Murine Xenograft Model.- In Vitro Long Term Proliferation Assays to Study Antiproliferative Effectsof PARP Inhibitors on