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Quantitative Proteomic Approaches to Studying Histone Modifications

Histone post-translational modifications (PTMs) positively and negatively regulate gene expression, and are consequently a vital influence on the genomic profile of all eukaryotic species. The study of histone PTMs using classical methods in molecular biology, such as immunofluorescence and Western...

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Detalles Bibliográficos
Autores principales: Zee, Barry M, Young, Nicolas L, Garcia, Benjamin A
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Bentham Open 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3178935/
https://www.ncbi.nlm.nih.gov/pubmed/21966350
http://dx.doi.org/10.2174/1875397301005010106
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author Zee, Barry M
Young, Nicolas L
Garcia, Benjamin A
author_facet Zee, Barry M
Young, Nicolas L
Garcia, Benjamin A
author_sort Zee, Barry M
collection PubMed
description Histone post-translational modifications (PTMs) positively and negatively regulate gene expression, and are consequently a vital influence on the genomic profile of all eukaryotic species. The study of histone PTMs using classical methods in molecular biology, such as immunofluorescence and Western blotting, is challenging given the technical issues of the approaches, and chemical diversity and combinatorial patterns of the modifications. In light of these many technical limitations, mass spectrometry (MS) is emerging as the most unbiased and rigorous experimental platform to identify and quantify histone PTMs in a high-throughput manner. This review covers the latest developments in mass spectrometry for the analysis of histone PTMs, with the hope of inspiring the continued integration of proteomic, genomic and epigenetic research.
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spelling pubmed-31789352011-09-30 Quantitative Proteomic Approaches to Studying Histone Modifications Zee, Barry M Young, Nicolas L Garcia, Benjamin A Curr Chem Genomics Article Histone post-translational modifications (PTMs) positively and negatively regulate gene expression, and are consequently a vital influence on the genomic profile of all eukaryotic species. The study of histone PTMs using classical methods in molecular biology, such as immunofluorescence and Western blotting, is challenging given the technical issues of the approaches, and chemical diversity and combinatorial patterns of the modifications. In light of these many technical limitations, mass spectrometry (MS) is emerging as the most unbiased and rigorous experimental platform to identify and quantify histone PTMs in a high-throughput manner. This review covers the latest developments in mass spectrometry for the analysis of histone PTMs, with the hope of inspiring the continued integration of proteomic, genomic and epigenetic research. Bentham Open 2011-08-22 /pmc/articles/PMC3178935/ /pubmed/21966350 http://dx.doi.org/10.2174/1875397301005010106 Text en © Zee et al.; Licensee Bentham Open. http://creativecommons.org/licenses/by-nc/3.0/ This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
spellingShingle Article
Zee, Barry M
Young, Nicolas L
Garcia, Benjamin A
Quantitative Proteomic Approaches to Studying Histone Modifications
title Quantitative Proteomic Approaches to Studying Histone Modifications
title_full Quantitative Proteomic Approaches to Studying Histone Modifications
title_fullStr Quantitative Proteomic Approaches to Studying Histone Modifications
title_full_unstemmed Quantitative Proteomic Approaches to Studying Histone Modifications
title_short Quantitative Proteomic Approaches to Studying Histone Modifications
title_sort quantitative proteomic approaches to studying histone modifications
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3178935/
https://www.ncbi.nlm.nih.gov/pubmed/21966350
http://dx.doi.org/10.2174/1875397301005010106
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