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170710s2017 xxu| s |||| 0|eng d |
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|a 9781493969937
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|a 10.1007/978-1-4939-6993-7
|2 doi
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| 040 |
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|a Sistema de Bibliotecas del Tecnológico de Costa Rica
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| 245 |
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|a Poly(ADP-Ribose) Polymerase :
|b Methods and Protocols /
|c edited by Alexei V. Tulin.
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| 250 |
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|a 2nd ed. 2017.
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| 260 |
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|a New York, NY :
|b Springer New York :
|b Imprint: Humana,
|c 2017.
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| 300 |
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|a XV, 528 p. 82 illus., 47 illus. in color. :
|b online resource.
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| 336 |
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|a text
|b txt
|2 rdacontent
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|a computer
|b c
|2 rdamedia
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|a online resource
|b cr
|2 rdacarrier
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|a Methods in Molecular Biology,
|v 1608
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| 505 |
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|a 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.
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| 650 |
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|a Proteins .
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| 650 |
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|a Protein Science.
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| 700 |
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|a Tulin, Alexei V.
|e editor.
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| 710 |
2 |
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|a SpringerLink (Online service)
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| 773 |
0 |
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|t Springer eBooks
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