Эпигенетика

Odegard V.H., Kim S.T., Anderson S.M., Shlomchik M.J., and Schatz D.G., 2005. Histone modifications associated with somatic hypermutation. Immunity 23: 101-110.

Ogata N., Ueda K., Kagamiyama H., and Hayaishi O., 1980. ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites. J. Biol. Chem. 255: 7616-7620.

Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., andNakatani Y., 2002. A complex with chromatin modifiers that occupies E2F-and Myc-responsive genes in G₀ cells. Science 296: 1132-1136.

Ogawa Y., Ono T., Wakata Y.. Okawa K.. Tagami H.. and Shibahara K.I., 2005. Histone variant macroH2Al.2 is mono-ubiquitinated at its histone domain. Biochem. Biophys. Res. Commun. 336: 204-209.

Pantazis P. and Bonner W.M., 1981. Quantitative determination of histone modification. H2A acetylation and phosphoiylation. J. Biol. Chem. 256: 4669-4675.

Parthun M.R., Widom J., and Gottschling D.E., 1996. The major cytoplasmic histone acetyltransferase in yeast: Links to chromatin replication and histone metabolism. Cell 87: 85-94.

Peters A.H., O’Carroll D., Scherthan H., Mechtler K., Sauer S., Schofer C, Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A., et al., 2001. Loss of the Suv39h histone methyl-transferases impairs mammalian heterochromatin and genome stability. Cell 107: 323-337.

Pham A.D. and Sauer F., 2000. Ubiquitin-activating/conjugating activity of TAF_n250, a mediator of activation of gene expression in Drosophila. Science 289: 2357-2360.

Polioudaki H., Markaki Y.. Kourmouli N., Dialynas G., Theodoro-poulos P.A., Singh P.B., and Georgatos S.D., 2004. Mitotic phosphorylation of histone H3 at threonine 3. FEES Lett. 560: 39-44.

Preuss U., Landsberg G., and Scheidtmann K.H., 2003. Novel mitosis-specific phosphorylation of histone H3 atThrl 1 mediated by Dlk/ZIP kinase Nucleic Acids Res. 31: 878-885.

Puerta C., Hernandez F., Lopez-Alarcon L., and Palacian E., 1995. Acetylation of histone H2A.H2B dimers facilitates transcription. Biochem. Biophys. Res. Cotnmun. 210: 409-416.

Rea S., Eisenhaber F., O’Carroll D., Strahl B.D., Sun Z.W., Schmid M., Opravil S., Mechtler K., Ponting C.P., Allis C.D., and Jenuwein T., 2000. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406: 593-599.

Redon C., Pilch D.R., Rogakou E.P., Orr A.H., Lowndes N.F., and Bonner W.M., 2003. Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damage. EMBO Rep. A: 678-684.

Rice J.C., Nishioka K., Sarma K., Steward R., Reinberg D., and Allis C.D., 2002. Mitotic-specific methylation of histone H4 Lys, 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes. Genes Dev. 16: 2225-2230.

Robzyk K., Recht ]., and Osley M.A., 2000. Rad6-dependent ubiquitina-tion of histone H2B in yeast. Science 287: 501-504.

Rogakou E.P., Boon C., Redon C., and Bonner W.M., 1999. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J. Cell Biol. 146: 905-916.

Rogakou E.R, Pilch D.R., Orr A.H., Ivanova VS., and Bonner W.M., 1998. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 273: 5858-5868.

Roguev A., Schaft D., Shevchenko A., Pijnappel W.W., Wilm M., Aasland R., and Stewart A.F., 2001. The Saccharomyces cerevisiae Setl complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J., 20: 7137-7148.

Rouleau M., Aubin R.A., and Poirier G.G., 2004. Poly(ADP-ribosyl) ated chromatin domains: Access granted. J. Cell Sci. 117: 815-825.

Ruiz-Carrillo A., Wangh L.J., and Allfrey V.G., 1975. Processing of newly synthesized histone molecules. Science, 190: 117-128.

Sanchez-Eisner T., Gou D., Kremmer E., and Sauer F., 2006. Noncoding RNAs of trithorax response elements recruit Drosophila Ashl to Ultrabithorax. Science 311: 1118-1123.

Santos-Rosa H., Schneider R., Bannister A. J., SherriffJ., Bernstein B.E., Emre N.C., Schreiber S.L., Mellor J., and Kouzarides T., 2002. Active genes are tri-methylated at K4 of histone H3. Nature 419: 407-411.

Sarg B., Helliger W., Talasz H., Forg B., and Lindner H.H., 2006. Histone HI phosphorylation occurs site-specifically during interphase and mitosis: Identification of a novel phosphorylation site on histone HI. /. Biol. Chem. 281: 6573-6580

Sassone-Corsi P., Mizzen C.A., Cheung P., Crosio C, Monaco L., Jacquot S., Hanauer A., and Allis C.D., 1999. Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3. Science 285: 886-891.