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Found 2 results
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2012
F. - R. Wu, Liu, Y., Shang, M. - B., Yang, X. - X., Ding, B., Gao, J. - G., Wang, R., and Li, W. - Y., Differences in H3K4 trimethylation in in vivo and in vitro fertilization mouse preimplantation embryos, vol. 11, pp. 1099-1108, 2012.
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Nature 438: 1181-1185. http://dx.doi.org/10.1038/nature04290 PMid:16372014 Fleming TP, Kwong WY, Porter R, Ursell E, et al. (2004). The embryo and its future. Biol. Reprod. 71: 1046-1054. http://dx.doi.org/10.1095/biolreprod.104.030957 PMid:15215194 Glaser S, Lubitz S, Loveland KL, Ohbo K, et al. (2009). The histone 3 lysine 4 methyltransferase, Mll2, is only required briefly in development and spermatogenesis. Epigenetics Chromatin 2: 5. http://dx.doi.org/10.1186/1756-8935-2-5 Guillemette B, Drogaris P, Lin HH, Armstrong H, et al. (2011). H3 lysine 4 is acetylated at active gene promoters and is regulated by H3 lysine 4 methylation. PLoS Genet. 7: e1001354. http://dx.doi.org/10.1371/journal.pgen.1001354 PMid:21483810    PMCid:3069113 Hamatani T, Carter MG, Sharov AA and Ko MS (2004). Dynamics of global gene expression changes during mouse preimplantation development. Dev. Cell 6: 117-131. http://dx.doi.org/10.1016/S1534-5807(03)00373-3 Huang JC, Yan LY, Lei ZL, Miao YL, et al. (2007a). Changes in histone acetylation during postovulatory aging of mouse oocyte. Biol. Reprod. 77: 666-670. http://dx.doi.org/10.1095/biolreprod.107.062703 PMid:17582009 Huang JC, Lei ZL, Shi LH, Miao YL, et al. (2007b). Comparison of histone modifications in in vivo and in vitro fertilization mouse embryos. Biochem. Biophys. Res. Commun. 354: 77-83. http://dx.doi.org/10.1016/j.bbrc.2006.12.163 PMid:17210126 Kim JM, Ogura A, Nagata M and Aoki F (2002). Analysis of the mechanism for chromatin remodeling in embryos reconstructed by somatic nuclear transfer. Biol. Reprod. 67: 760-766. http://dx.doi.org/10.1095/biolreprod.101.000612 PMid:12193382 Kim JM, Liu H, Tazaki M, Nagata M, et al. (2003). Changes in histone acetylation during mouse oocyte meiosis. J. Cell Biol. 162: 37-46. http://dx.doi.org/10.1083/jcb.200303047 PMid:12835313    PMCid:2172711 Li L, Zheng P and Dean J (2010). Maternal control of early mouse development. 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Cross-talk between histone modifications in response to histone deacetylase inhibitors: MLL4 links histone H3 acetylation and histone H3K4 methylation. J. Biol. Chem. 282: 4408-4416. http://dx.doi.org/10.1074/jbc.M606773200 PMid:17166833 Ruthenburg AJ, Allis CD and Wysocka J (2007). Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Mol. Cell 25: 15-30. http://dx.doi.org/10.1016/j.molcel.2006.12.014 PMid:17218268 Shi X, Hong T, Walter KL, Ewalt M, et al. (2006). ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442: 96-99. PMid:16728974    PMCid:3089773 Shilatifard A (2008). Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation. Curr. Opin. Cell Biol. 20: 341-348. http://dx.doi.org/10.1016/j.ceb.2008.03.019 PMid:18508253    PMCid:2504688 Strömstedt M, Keeney DS, Waterman MR, Paria BC, et al. (1996). Preimplantation mouse blastocysts fail to express CYP genes required for estrogen biosynthesis. Mol. Reprod. Dev. 43: 428-436. http://dx.doi.org/10.1002/(SICI)1098-2795(199604)43:4<428::AID-MRD4>3.0.CO;2-R Wysocka J, Swigut T, Xiao H, Milne TA, et al. (2006). A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 442: 86-90. PMid:16728976 Yamanaka K, Sugimura S, Wakai T, Kawahara M, et al. (2009). Acetylation level of histone H3 in early embryonic stages affects subsequent development of miniature pig somatic cell nuclear transfer embryos. J. Reprod. Dev. 55: 638-644. http://dx.doi.org/10.1262/jrd.20245 PMid:19700928 Young LE and Fairburn HR (2000). Improving the safety of embryo technologies: possible role of genomic imprinting. Theriogenology 53: 627-648. http://dx.doi.org/10.1016/S0093-691X(99)00263-0 Zhao Z, Fan L and Frick KM (2010). Epigenetic alterations regulate estradiol-induced enhancement of memory consolidation. Proc. Natl. Acad. Sci. U. S. A. 107: 5605-5610. http://dx.doi.org/10.1073/pnas.0910578107 PMid:20212170    PMCid:2851775