Poly(ADP-Ribose) Polymerase : Methods and Protocols / edited by Alexei V. Tulin.

Format:

Book

Contributor:

Tulin, Alexei V., editor.

SpringerLink (Online service)

Series:

Methods in molecular biology 1064-3745 ; 1608.

Springer Protocols (Springer-12345)

Methods in Molecular Biology, 1064-3745 ; 1608

Language:

English

Subjects (All):

Life sciences.

Proteins.

Life Sciences.

Protein Science.

Local Subjects:

Life Sciences.

Protein Science.

Physical Description:

1 online resource (XV, 528 pages) : 82 illustrations, 47 illustrations in color.

Edition:

Second edition 2017.

Contained In:

Springer eBooks

Place of Publication:

New York, NY : Springer New York : Imprint: Humana Press, 2017.

System Details:

text file PDF

Summary:

This book presents multiple new and classical methods for studying the vital poly-ADP-ribose (pADPr) pathway. Beginning with techniques for the detection and quantification of the product of poly(ADP-ribose) polymerase (PARP) enzymatic activity and detection of variation in pADPr production during the cell cycle, the volume continues with sections on the identification of pADPr protein acceptors, methods focusing on studying molecular mechanisms of PARP functions in eukaryotic cells, particularly those involved in control of DNA repair and oxidative stress, as well as in expression regulation, approaches to the in vitro reconstitution of PARP-1 interaction with chromatin, the development and testing of small molecule PARP inhibitors, and the functions of understudied members of PARP family. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Poly(ADP-Ribose) Polymerase: Methods and Protocols, Second Edition serves as an ideal companion to the first edition for scientists whose investigations involve this important pathway. The chapter 'Identifying and Validating Tankyrase Binders and Substrates: A Candidate Approach' is published open access under a CC BY 4.0 license.

Contents:

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 Effects of PARP Inhibitors on Cancer Cells

Use of Inosine Monophosphate Dehydrogenase Activity Assay to Determine the Specificity of PARP-1 Inhibitors

The Use of PARP Inhibitors in Cancer Therapy: Use as Adjuvant with Chemotherapy or Radiotherapy, Use as a Single Agent in Susceptible Patients, and Techniques Used to Identify Susceptible Patients

Purification of Recombinant Human PARP-3

Purification of Recombinant Human PARG and Activity Assays

Studying Catabolism of Protein ADP-Ribosylation

Purification of DNA Damage-Dependent PARPs from E. coli for Structural and Biochemical Analysis

Identifying and Validating Tankyrase Binders and Substrates: A Candidate Approach

Computational and Experimental Studies of ADP-Ribosylation.

Other Format:

Printed edition:

ISBN:

9781493969937

Access Restriction:

Restricted for use by site license.