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- W1966092511 abstract "Histones form the protein core around which genomic DNA is wrapped in eukaryotic chromatin. Numerous genetic studies have established that the structure and transcriptional state of chromatin are closely related to histone post-translational modifications. Further elucidation of the precise mechanistic roles for individual histone modifications requires the ability to isolate and study homogeneously modified histones. However, the highly heterogeneous nature of histone modifications in vivo poses a significant challenge for such studies. Chemical tools that have enabled biochemical and biophysical studies of site-specifically modified histones are the focus of this minireview." @default.
- W1966092511 created "2016-06-24" @default.
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- W1966092511 date "2010-04-01" @default.
- W1966092511 modified "2023-10-09" @default.
- W1966092511 title "Chemical Approaches for Studying Histone Modifications" @default.
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- W1966092511 doi "https://doi.org/10.1074/jbc.r109.080291" @default.
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