New tools, new targets: Novel approaches for identifying and characterizing epigenetic modifications
Since the successful sequencing of the human genome, interest in the group of genes encoding proteins responsible for DNA remodeling has grown exponentially. Included in this group are enzymes that methylate and demethylate DNA, as well as those that modify histones by adding chemical groups through...
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Veröffentlicht in: | Science (American Association for the Advancement of Science) 2014-06, Vol.344 (6190), p.1415-1415 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Since the successful sequencing of the human genome, interest in the group of genes encoding proteins responsible for DNA remodeling has grown exponentially. Included in this group are enzymes that methylate and demethylate DNA, as well as those that modify histones by adding chemical groups through acetylation, methylation, and sumoylation reactions, amongst others. Epigenetic enzymes are now among the most important pharmaceutical targets due to their involvement in numerous key cellular processes and in the etiology of many devastating diseases including cancer, neurodegenerative disease, and developmental disorders. Significant efforts are under way in both academic and industrial laboratories to identify and validate new so-called reader, writer, and eraser enzymes as well as their histone substrates. Understanding the functions of these proteins may lead to a new generation of therapeutics. While various molecular biology techniques were initially used to identify and validate epigenetics enzymes and their substrates, novel approaches are now available to perform pharmacological characterization of histone-modifying enzymes. During this webinar, our expert panelists will describe these methods and present breakthrough research data obtained using novel experimental approaches, including immunoassays, microfluidics-based techniques, and high-content screening immunophenotypic assays.View the Webinar |
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ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.344.6190.1415-c |