Nuclear and nucleolar activity of linker histone variant H1.0
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://link.springer.com/content/pdf/10.1186/s11658-016-0014-0
Reference67 articles.
1. Happel N, Doenecke D. Histone H1 and its isoforms: contribution to chromatin structure and function. Gene. 2009;431:1–12.
2. Kowalski A. Abundance of intrinsic structural disorder in the histone H1 subtypes. Comp Biol Chem. 2015;59:16–27.
3. Hansen J, Lu X, Ross ED, Woody RW. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J Biol Chem. 2006;281:1853–6.
4. Carerino TL, Hayes JJ. Structure of the H1 C-terminal domain and function in chromatin condensation. Biochem Cell Biol. 2011;89:35–44.
5. Lu X, Hansen JC. Identification of specific functional subdomains within the linker histone H1° C-terminal domain. J Biol Chem. 2004;279:8701–7.
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