ADP-ribosylation and NAD+ Utilizing Enzymes : Methods and Protocols /

Detalles Bibliográficos
Autor Corporativo: SpringerLink (Online service)
Otros Autores: Chang, Paul. (Editor )
Formato: eBook
Lenguaje:English
Publicado: New York, NY : Springer New York : Imprint: Humana, 2018.
Edición:1st ed. 2018.
Colección:Methods in Molecular Biology, 1813
Materias:
Tabla de Contenidos:
  • Vitamin B3 in Health and Disease: Toward the Second Century of Discovery
  • Monitoring Poly(ADP-Ribosyl)ation in Response to DNA Damage in Live Cells Using Fluorescently-Tagged Macrodomains
  • In Vitro Techniques for ADP-Ribosylated Substrate Identification
  • Assessment of Intracellular Auto-Modification Levels of ARTD10 using Mono-ADP-Ribose-Specific Macrodomains 2 and 3 of Murine Artd8
  • Biochemical and Biophysical Assays of PAR-WWE Domain Interactions and Production of iso-ADPr for PAR Binding Analysis
  • Assays for NAD-Dependent Reactions and NAD Metabolites
  • Generating Protein-Linked and Protein-Free Mono-, Oligo-, and Poly(ADP-Ribose) In Vitro
  • Methods to Study TCDD-Inducible Poly-ADP-Ribose Polymerase (TIPARP) Mono-ADP-Ribosyltransferase Activity
  • Dictyostelium as a Model to Assess Site-Specific ADP-Ribosylation Events
  • Mono-ADP-Ribosylation Catalyzed by Arginine-Specific ADP-Ribosyltransferases
  • Monitoring Expression and Enzyme Activity of Ecto-ARTCs
  • ADP-Ribosyl-Acceptor Hydrolase Activities Catalyzed by the ARH Family of Proteins
  • Mono-ADP-Ribosylhydrolase Assays
  • Hydrolysis of ADP-Ribosylation by Macrodomains
  • HPLC-Based Enzyme Assays for Sirtuins
  • Small Molecule Screening Assay for Mono-ADP-Ribosyltransferases
  • A Simple, Sensitive, and Generalizable Plate Assay for Screening PARP Inhibitors
  • Non-Localized Searching of HCD Data for Fast and Sensitive Identification of ADP-Ribosylated Peptides
  • Quantitative Determination of MAR Hydrolase Residue Specificity In Vitro by Tandem Mass Spectrometry
  • Detection of ADP-Ribosylating Bacterial Toxins
  • Preparation of Recombinant Alphaviruses for Functional Studies of ADP-Ribosylation
  • Monitoring the Sensitivity of T Cell Populations towards NAD+ Released during Cell Preparation
  • Identifying Target RNAs of PARPs
  • ADPr-Peptide Synthesis
  • Identifying Genomic Sites of ADP-Ribosylation Mediated by Specific Nuclear PARP Enzymes Using Click-ChIP
  • Methods for Using a Genetically-Encoded Fluorescent Biosensor to Monitor Nuclear NAD+.