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  One, two, three: how histone methylation is read.

Fischle, W. (2012). One, two, three: how histone methylation is read. Epigenomics, 4(6), 641-653. doi:10.2217/epi.12.56.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-7251-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C854-C
Genre: Journal Article

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1587582.pdf (Publisher version), 3MB
 
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 Creators:
Fischle, W.1, Author              
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1Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578604              

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Free keywords: Arginine; binding; chromatin; domains; epigenetic; histone; lysine; methylation; modules
 Abstract: Methylation of histone lysine and arginine residues constitutes a highly complex control system directing diverse functions of the genome. Owing to their immense signaling potential with distinct sites of methylation and defined methylation states of mono-, di- or trimethylation as well as their higher biochemical stability compared with other histone modifications, these marks are thought to be part of epigenetic regulatory networks. Biological principles of how histone methylation is read and translated have emerged over the last few years. Only very few methyl marks directly impact chromatin. Conversely, a large number of histone methylation binding proteins has been identified. These contain specialized modules that are recruited to chromatin in a methylation site- and state-specific manner. Besides the molecular mechanisms of interaction, patterns of regulation of the binding proteins are becoming evident.

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Language(s): eng - English
 Dates: 2012-12
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.2217/epi.12.56
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Title: Epigenomics
Source Genre: Journal
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Pages: - Volume / Issue: 4 (6) Sequence Number: - Start / End Page: 641 - 653 Identifier: -