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020 _a9781071624814
024 7 _a10.1007/978-1-0716-2481-4
_2doi
040 _aES-MaUEC
_bspa
_cES-MaUEC
_dES-MaUEC
050 4 _aQP552 .H5
_b2022 EB
245 0 0 _aHistone Methyltransferases :
_bMethods and Protocols
_cedited by Raphaël Margueron, Daniel Holoch
250 _a1st edition 2022
264 1 _aNew York, NY
_bSpringer International Publising
_c2022
300 _a1 recurso en línea (XVII, 495 páginas)
_b72 ilustraciones, 53 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
_v2529
505 0 _aNot all is SET for methylation: Evolution of eukaryotic protein methyltransferases -- Detection and quantification of histone methyltransferase activity in vitro -- In Vitro Histone Demethylase Assays -- Preparation and characterization of chromatin templates for histone methylation assays -- Techniques to study automethylation of histone methyltransferases and its functional impact -- Rodriguez Profiling the regulation of histone methylation and demethylation by metabolites and metals -- Determination of histone methyltransferase structure by crystallography -- Determination of histone methyltransferase structures in complex with the nucleosome by cryogenic electron microscopy -- Development and validation of antibodies targeting site-specific histone methylation -- Genetic, genomic and imaging approaches to dissect the role of Polycomb group epigenetic regulators in mice -- Profiling histone methylation in low numbers of cells -- Automated CUT&RUN using the KingFisher Duo Prime -- Bioinformatics methods for ChIP-seq histone analysis -- Characterization of SET-domain histone lysine methyltransferase substrates using a cofactor S-adenosyl-L-methionine surrogate -- Specificity analysis of protein methyltransferases and discovery of novel substrates using SPOT peptide arrays -- Identifying specific protein interactors of nucleosomes carrying methylated histones using mass spectrometr -- Investigating mitotic inheritance of histone post-translational modifications by triple pSILAC coupled to Nascent Chromatin Capture -- Investigating mitotic inheritance of histone modifications using tethering -- Investigating histone modification dynamics by mechanistic computational modelling -- Screening for small molecule inhibitors of histone methyltransferases.
520 _aThis volume provides methods used to investigate histone methyltransferase function. Chapters guide readers through a comprehensive set of approaches that detail phylogenetic diversity, histone demethylase activities in vitro, generating chromatin substrates, auto-methylation, quantification of metabolites, protein purification, crystallization, X-ray structure, cryogenic electron microscopy, assessing genome-wide patterns, CUT&Tag in mouse embryonic tissues, chemical biology approaches, peptide SPOT arrays, nascent chromatin capture, ectopic protein tethering, computational models, and development of methyltransferase inhibitors. Written in the format of the highly successful Methods in Molecular Biology series, each chapter includes an introduction to the topic, lists necessary materials and reagents, includes tips on troubleshooting and known pitfalls, and step-by-step, readily reproducible protocols. Authoritative and cutting-edge, Histone Methyltransferases: Methods and Protocols aims to be a useful and practical guide to new researchers and experts looking to expand their knowledge.
988 _aSpringer_Protocols_2022
650 7 _2embne
_9145787
_aHistonas
_vManuales de laboratorio
776 0 8 _iPrinted edition:
_z9781071624807
776 0 8 _iPrinted edition:
_z9781071624821
776 0 8 _iPrinted edition:
_z9781071624838
856 4 0 _uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-0716-2481-4
_zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942 _2lcc
_cLE
998 _b07/2023
_dz
_eu
_zSI