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008			170710s2017 xxu| o |||| 0|eng d
020			_a9781493969937
024	7		_a10.1007/978-1-4939-6993-7 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQP606 .P76 _b2017 EB
245	0	0	_aPoly(ADP-Ribose) Polymerase : _bMethods and Protocols _cedited by Alexei V. Tulin
250			_a2nd edition 2017
264		1	_aNew York, NY _bSpringer International Publishing _c2017
300			_a1 recurso en línea (XV, 528 páginas) _b82 ilustraciones, 47 ilustraciones a color
336			_atexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
347			_aarchivo de texto _bPDF
490	0		_aMethods in Molecular Biology _x1940-6029 _v1608
505	0		_aQuantitation 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.
520			_aThis 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.
988			_aSpringer_Protocols_2017
650		7	_2embne _9510854 _aProteína cinasas _vManuales de laboratorio
776	0	8	_iPrinted edition: _z9781493969920
776	0	8	_iPrinted edition: _z9781493969944
776	0	8	_iPrinted edition: _z9781493983612
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-4939-6993-7 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b11/2023 _dz _eu _zSI