The modification and variants of histone
Author:
Publisher
Pleiades Publishing Ltd
Subject
Structural Biology,Biophysics
Link
http://link.springer.com/content/pdf/10.1134/S0026893307030028.pdf
Reference112 articles.
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2. Mario F., Ballestar E., Villar-Garea A., et al. 2005. Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nature Genet. 37, 391–400.
3. Jürgen C.B., Selma U., Eva-Bettina B., David S., Roland H. 2006. New therapeutic approaches for solid tumors: Histone deacetylase, methyltransferase and proteasome inhibitors. J. Dtsch. Dermatol. Ges. 4, 108–115.
4. Turner B.M., Birley A.J., Lavender J. 1992. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell. 69, 375–384.
5. Strahl B.D., Allis C.D. 2000. The language of covalent histone modifications. Nature. 403, 41–45.
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