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Poly(ADP-Ribose) Polymerase

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Cover of 'Poly(ADP-Ribose) Polymerase'

Table of Contents

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    Book Overview
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    Chapter 1 Quantitation of Poly(ADP-Ribose) by Isotope Dilution Mass Spectrometry
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    Chapter 2 Quantification of PARP Activity in Human Tissues: Ex Vivo Assays in Blood Cells and Immunohistochemistry in Human Biopsies
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    Chapter 3 Detecting and Quantifying pADPr In Vivo
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    Chapter 4 Compartment-Specific Poly-ADP-Ribose Formation as a Biosensor for Subcellular NAD Pools
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    Chapter 5 Cell Cycle Resolved Measurements of Poly(ADP-Ribose) Formation and DNA Damage Signaling by Quantitative Image-Based Cytometry
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    Chapter 6 Detecting Protein ADP-Ribosylation Using a Clickable Aminooxy Probe
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    Chapter 7 ADP-Ribosylated Peptide Enrichment and Site Identification: The Phosphodiesterase-Based Method
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    Chapter 8 Using Clickable NAD+ Analogs to Label Substrate Proteins of PARPs
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    Chapter 9 Identification of Protein Substrates of Specific PARP Enzymes Using Analog-Sensitive PARP Mutants and a “Clickable” NAD+ Analog
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    Chapter 10 Identification of ADP-Ribose Acceptor Sites on In Vitro Modified Proteins by Liquid Chromatography–Tandem Mass Spectrometry
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    Chapter 11 Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography–Tandem Mass Spectrometry
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    Chapter 12 Poly(ADP-Ribose)-Dependent Chromatin Remodeling in DNA Repair
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    Chapter 13 Methods to Assess the Role of Poly(ADP-Ribose) Polymerases in Regulating Mitochondrial Oxidation
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    Chapter 14 Approaches for Investigating Translational Regulation Controlled by PARP1: Biotin-Based UV Cross-Linking and Luciferase Reporter Assay
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    Chapter 15 Methodology to Identify Poly-ADP-Ribose Polymerase 1 (PARP1)–mRNA Targets by PAR-CLiP
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    Chapter 16 Biochemical and Biophysical Methods for Analysis of Poly(ADP-Ribose) Polymerase 1 and Its Interactions with Chromatin
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    Chapter 17 PARP-1 Interaction with and Activation by Histones and Nucleosomes
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    Chapter 18 Strategies Employed for the Development of PARP Inhibitors
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    Chapter 19 High-Throughput Colorimetric Assay for Identifying PARP-1 Inhibitors Using a Large Small-Molecule Collection
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    Chapter 20 Testing PARP Inhibitors Using a Murine Xenograft Model
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    Chapter 21 In Vitro Long-Term Proliferation Assays to Study Antiproliferative Effects of PARP Inhibitors on Cancer Cells
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    Chapter 22 Use of Inosine Monophosphate Dehydrogenase Activity Assay to Determine the Specificity of PARP-1 Inhibitors
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    Chapter 23 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
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    Chapter 24 Purification of Recombinant Human PARP-3
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    Chapter 25 Purification of Recombinant Human PARG and Activity Assays
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    Chapter 26 Studying Catabolism of Protein ADP-Ribosylation
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    Chapter 27 Purification of DNA Damage-Dependent PARPs from E. coli for Structural and Biochemical Analysis
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    Chapter 28 Identifying and Validating Tankyrase Binders and Substrates: A Candidate Approach
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    Chapter 29 Computational and Experimental Studies of ADP-Ribosylation
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    Chapter 30 Erratum to: Methodology to Identify Poly-ADP-Ribose Polymerase 1 (PARP1)–mRNA Targets by PAR-CLiP
Attention for Chapter 21: In Vitro Long-Term Proliferation Assays to Study Antiproliferative Effects of PARP Inhibitors on Cancer Cells
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Chapter title
In Vitro Long-Term Proliferation Assays to Study Antiproliferative Effects of PARP Inhibitors on Cancer Cells
Chapter number 21
Book title
Poly(ADP-Ribose) Polymerase
Published in
Methods in molecular biology, July 2017
DOI 10.1007/978-1-4939-6993-7_21
Pubmed ID
Book ISBNs
978-1-4939-6992-0, 978-1-4939-6993-7
Authors

Heike Keilhack, Paul Chang

Abstract

Cell proliferation assays are an important component of small molecule inhibitor screens for cancer therapies. An important but often overlooked variable involves the timing and timeframe of inhibitor treatment. Whereas many traditional chemotherapeutics kill or inhibit proliferation on the timeframe of hours or in a few days of treatment, more targeted therapies that affect other cancer-relevant pathways, including differentiation or cell stress responses, can take longer, often several days to weeks to impact cellular growth and survival. Many poly(ADP-ribose) polymerases (PARPs) are involved in cellular stress pathways; therefore, phenotypic effects of PARP inhibition are often only observed with long-term inhibitor treatment. Here we summarize several assays for analyzing long-term proliferation of both adherent and suspension cells, relying either on growth in two-dimensional tissue culture or on systems than enable growth in 3D.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 12 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 12 100%

Demographic breakdown

Readers by professional status Count As %
Student > Master 3 25%
Student > Bachelor 1 8%
Other 1 8%
Student > Ph. D. Student 1 8%
Student > Postgraduate 1 8%
Other 0 0%
Unknown 5 42%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 5 42%
Agricultural and Biological Sciences 2 17%
Unknown 5 42%