ADP-ribosylation and NAD+ Utilizing Enzymes

Preface...Table of Contents...Contributing Authors...Part I Introduction1. Vitamin B3 in Health and Disease: Toward the Second Century of DiscoveryMyron K. Jacobson and Elaine L. JacobsonPart II ADPribose Binding Domains as Tools2.Monitoring Poly(ADP-Ribosyl)ation in Response to DNA Damage in Live Cells Using Fluorescently-Tagged MacrodomainsRebecca Smith and Gyula Timinszky3.In Vitro Techniques for ADP-Ribosylated Substrate IdentificationGiovanna Grimaldi, Giulianan Catara, Carmen Valente, and Daniela Corda4.Assessment of Intracellular Auto-Modification Levels of ARTD10 using Mono-ADP-Ribose-Specific Macrodomains 2 and 3 of Murine Artd8Mareike Bütepage, Sarah Krieg, laura Eckei, Jinyu Li, Giulia Rossetti, Patricia Verheugd, and Bernhard Lüscher5.Biochemical and Biophysical Assays of PAR-WWE Domain Interactions and Production of iso-ADPr for PAR Binding AnalysisZhizhi Wang and Wenqing XuPart III Enzymatic Assays of NAD+ Utilizing Enzymes6.Assays for NAD-Dependent Reactions and NAD MetabolitesMichael B. Schultz, Yuancheng Lu, Nady Braidy, and David A Sinclair7.Generating Protein-Linked and Protein-Free Mono-, Oligo-, and Poly(ADP-Ribose) In VitroKen Y. Lin, Dan Huang, and W. Lee Kraus8.Methods to Study TCDD-Inducible Poly-ADP-Ribose Polymerase (TIPARP) Mono-ADP-Ribosyltransferase ActivityDavid Hutin, Giulia Grimaldi, and Jason Matthews9.Dictyostelium as a Model to Assess Site-Specific ADP-Ribosylation EventsAnna-Lena Kolb, Duen-Wei Hsu, Ana B.A. Wallis, Seiji Ura, Alina Rakhimova, Catherine J. Pears, and Nicholas D. Lakin10.Mono-ADP-Ribosylation Catalyzed by Arginine-Specific ADP-RibosyltransferasesLinda A. Stevens and Joel Moss11.Monitoring Expression and Enzyme Activity of Ecto-ARTCsStephan Menzel, Sahil Abriouch, Peter Bannas, Friedrich Haag, and Friedrich Koch-Nolte12.ADP-Ribosyl-Acceptor Hydrolase Activities Catalyzed by the ARH Family of ProteinsMasato Mashimo and Joel Moss13.Mono-ADP-Ribosylhydrolase AssaysJeannette Abplanalp, Ann-Katrin Hopp, and Michael O. Hottiger14.Hydrolysis of ADP-Ribosylation by MacrodomainsMelanija Posavec Marjanovic, Gytis Jankevicius, and Ivan Ahel15.HPLC-Based Enzyme Assays for SirtuinsJun Young Hong, Xiaoyu Zhang, and Hening LinPart IV Small Molecule Screening Assays of NAD+ Utilizing Enzymes16.Small Molecule Screening Assay for Mono-ADP-RibosyltransferasesHaikarainen Teemu, Murphy Sudarshan, Maksimainen Mirko, and Lari Lehtiö17.¬A Simple, Sensitive, and Generalizable Plate Assay for Screening PARP InhibitorsIlsa T. Kirby, Rory K. Morgan, and Michael S. CohenPart V Mass Spectrometry Techniques for Detection of Mono-ADP-Ribosylation18.Non-Localized Searching of HCD Data for Fast and Sensitive Identification of ADP-Ribosylated PeptidesThomas Colby, Juan José Bonfiglio, and Ivan Matic19.Quantitative Determination of MAR Hydrolase Residue Specificity In Vitro by Tandem Mass SpectrometryRobert Lyle Mcpherson, Shao-En Ong, and Anthony K.L. LeungPart VI Mono-ADP-Ribose and Disease20.Detection of ADP-Ribosylating Bacterial ToxinsChen Chen and Joseph T. Barbieri21.Preparation of Recombinant Alphaviruses for Functional Studies of ADP-RibosylationRachy Abraham, Robert L. McPherson, Easwaran Sreekumar, Anthony K.L. Leung, and Diane E. Griffin22.Monitoring the Sensitivity of T Cell Populations towards NAD+ Released during Cell PreparationBjörn Rissiek, Marco Lukowiak, Friedrich Haag, Tim Magnus, and Friedrich Koch-Nolte23.Identifying Target RNAs of PARPsFlorian J. Bock and Paul ChangPart VII NAD+ Analogue Approaches and Chemical Synthesis24.ADPr-Peptide SynthesisHans A.V. Kistemaker, Jim Voorneveld, and Dmitri V. Filippov25.Identifying Genomic Sites of ADP-Ribosylation Mediated by Specific Nuclear PARP Enzymes Using Click-ChIPRyan A. Rogge, Bryan A. Gibson, and W. Lee KrausPart VIII NAD+ Sensors26.Methods for Using a Genetically-Encoded Fluorescent Biosensor to Monitor Nuclear NAD+Michael S. Cohen, Melissa L. Stewart, Richard H. Goodman, and Xiaolu A. Cambronne... Mehr