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Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena

โœ Scribed by Strahl, B. D.; Ohba, R.; Cook, R. G.; Allis, C. D.


Book ID
126916855
Publisher
National Academy of Sciences
Year
1999
Tongue
English
Weight
193 KB
Volume
96
Category
Article
ISSN
0027-8424

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Methylation of histone H3 at lysine 4 is
โœ Strahl, B. D.; Ohba, R.; Cook, R. G.; Allis, C. D. ๐Ÿ“‚ Article ๐Ÿ“… 1999 ๐Ÿ› National Academy of Sciences ๐ŸŒ English โš– 193 KB

Studies into posttranslational modifications of histones, notably acetylation, have yielded important insights into the dynamic nature of chromatin structure and its fundamental role in gene expression. The roles of other covalent histone modifications remain poorly understood. To gain further insig