Copyright © 2011 Tomohiro Hayakawa and Jun-ichi Nakayama. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

1. B. D. Strahl and C. D. Allis, “The language of covalent histone modifications,” Nature, vol. 403, no. 6765, pp. 41–45, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
2. T. Kouzarides, “Chromatin modifications and their function,” Cell, vol. 128, no. 4, pp. 693–705, 2007. View at Publisher · View at Google Scholar · View at PubMed
3. J. B. Rayman, Y. Takahashi, and Y. Takahashi, “E2F mediates cell cycle-dependent transcriptional repression in vivo by recruitment of an HDAC1/mSin3B corepressor complex,” Genes and Development, vol. 16, no. 8, pp. 933–947, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
4. E. Balciunaite, A. Spektor, and A. Spektor, “Pocket protein complexes are recruited to distinct targets in quiescent and proliferating cells,” Molecular and Cellular Biology, vol. 25, no. 18, pp. 8166–8178, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
5. J. Liang, M. Wan, and M. Wan, “Nanog and Oct4 associate with unique transcriptional repression complexes in embryonic stem cells,” Nature Cell Biology, vol. 10, no. 6, pp. 731–739, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
6. Y. Shi, F. Lan, and F. Lan, “Histone demethylation mediated by the nuclear amine oxidase homolog LSD1,” Cell, vol. 119, no. 7, pp. 941–953, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
7. R. J. Klose, Q. Yan, and Q. Yan, “The retinoblastoma binding protein RBP2 is an H3K4 demethylase,” Cell, vol. 128, no. 5, pp. 889–900, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
8. P. A. C. Cloos, J. Christensen, and J. Christensen, “The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3,” Nature, vol. 442, no. 7100, pp. 307–311, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
9. K. Agger, P. A. C. Cloos, and P. A. C. Cloos, “UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development,” Nature, vol. 449, no. 7163, pp. 731–734, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
10. F. Lan, P. E. Bayliss, and P. E. Bayliss, “A histone H3 lysine 27 demethylase regulates animal posterior development,” Nature, vol. 449, no. 7163, pp. 689–694, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
11. R. J. Klose and Y. Zhang, “Regulation of histone methylation by demethylimination and demethylation,” Nature Reviews Molecular Cell Biology, vol. 8, no. 4, pp. 307–318, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
12. Y. Zhang, R. Iratni, H. Erdjument-Bromage, P. Tempst, and D. Reinberg, “Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex,” Cell, vol. 89, no. 3, pp. 357–364, 1997. View at Publisher · View at Google Scholar · View at Scopus
13. Y. Zhang, Z.-W. Sun, R. Iratni, H. Erdjument-Bromage, P. Tempst, M. Hampsey, and D. Reinberg, “SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex,” Molecular Cell, vol. 1, no. 7, pp. 1021–1031, 1998. View at Scopus
14. Y. Zhang, G. LeRoy, H.-P. Seelig, W. S. Lane, and D. Reinberg, “The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities,” Cell, vol. 95, no. 2, pp. 279–289, 1998. View at Publisher · View at Google Scholar · View at Scopus
15. J.-H. Dannenberg, G. David, S. Zhong, J. Van Der Torre, W. H. Wong, and R. A. DePinho, “mSin3A corepressor regulates diverse transcriptional networks governing normal and neoplastic growth and survival,” Genes and Development, vol. 19, no. 13, pp. 1581–1595, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
16. G. David, K. B. Grandinetti, P. M. Finnerty, N. Simpson, G. C. Chu, and R. A. DePinho, “Specific requirement of the chromatin modifier mSin3B in cell cycle exit and cellular differentiation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 11, pp. 4168–4172, 2008. View at Publisher · View at Google Scholar · View at PubMed
17. M. J. Carrozza, B. Li, and B. Li, “Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription,” Cell, vol. 123, no. 4, pp. 581–592, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
18. M.-C. Keogh, S. K. Kurdistani, and S. K. Kurdistani, “Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex,” Cell, vol. 123, no. 4, pp. 593–605, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
19. M. L. Youdell, K. O. Kizer, E. Kisseleva-Romanova, S. M. Fuchs, E. Duro, B. D. Strahl, and J. Mellor, “Roles for Ctk1 and Spt6 in regulating the different methylation states of histone H3 lysine 36,” Molecular and Cellular Biology, vol. 28, no. 16, pp. 4915–4926, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
20. B. Sun, J. Hong, P. Zhang, X. Dong, X. Shen, D. Lin, and J. Ding, “Molecular basis of the interaction of Saccharomyces cerevisiae Eaf3 chromo domain with methylated H3K36,” Journal of Biological Chemistry, vol. 283, no. 52, pp. 36504–36512, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
21. C. Xu, G. Cui, M. V. Botuyan, and G. Mer, “Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S,” Structure, vol. 16, no. 11, pp. 1740–1750, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
22. B. Li, M. Gogol, M. Carey, D. Lee, C. Seidel, and J. L. Workman, “Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin,” Science, vol. 316, no. 5827, pp. 1050–1054, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
23. M. J. Bertram, N. G. Bérubé, X. H. Swanson, and O. M. Pereira-Smith, “Assembly of a BAC contig of the complementation group B cell senescence gene candidate region at 4q33-q34.1 and identification of expressed sequences,” Genomics, vol. 56, no. 3, pp. 353–354, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
24. M. J. Bertram and O. M. Pereira-Smith, “Conservation of the MORF4 related gene family: identification of a new chromo domain subfamily and novel protein motif,” Gene, vol. 266, no. 1-2, pp. 111–121, 2001. View at Publisher · View at Google Scholar · View at Scopus
25. G. S. Yochum and D. E. Ayer, “Role for the mortality factors MORF4, MRGX, and MRG15 in transcriptional repression via associations with Pf1, mSin3A, and transducin-like enhancer of split,” Molecular and Cellular Biology, vol. 22, no. 22, pp. 7868–7876, 2002. View at Publisher · View at Google Scholar · View at Scopus
26. T. Hayakawa, Y. Ohtani, N. Hayakawa, K. Shinmyozu, M. Saito, F. Ishikawa, and J.-C. Nakayama, “RBP2 is an MRG15 complex component and down-regulates intragenic histone H3 lysine 4 methylation,” Genes to Cells, vol. 12, no. 6, pp. 811–826, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
27. Y. Cai, J. Jin, and J. Jin, “Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex,” Journal of Biological Chemistry, vol. 278, no. 44, pp. 42733–42736, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
28. Y. Doyon, W. Selleck, W. S. Lane, S. Tan, and J. Côté, “Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans,” Molecular and Cellular Biology, vol. 24, no. 5, pp. 1884–1896, 2004. View at Publisher · View at Google Scholar · View at Scopus
29. T. Hayakawa, F. Zhang, N. Hayakawa, Y. Ohtani, K. Shinmyozu, J. -I. Nakayama, and P. R. Andreassen, “MRG15 binds directly to PALB2 and stimulates homology-directed repair of chromosomal breaks,” Journal of Cell Science, vol. 123, no. 7, pp. 1124–1130, 2010. View at Publisher · View at Google Scholar · View at PubMed
30. S. M.-H. Sy, M. S. Y. Huen, and J. Chen, “MRG15 is a novel PALB2-interacting factor involved in homologous recombination,” Journal of Biological Chemistry, vol. 284, no. 32, pp. 21127–21131, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
31. J.-I. Nakayama, G. Xiao, and G. Xiao, “Alp13, an MRG family protein, is a component of fission yeast Clr6 histone deacetylase required for genomic integrity,” EMBO Journal, vol. 22, no. 11, pp. 2776–2787, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
32. T. Kusch, L. Florens, and L. Florens, “Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions,” Science, vol. 306, no. 5704, pp. 2084–2087, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
33. S. N. Garcia, B. M. Kirtane, A. J. Podlutsky, O. M. Pereira-Smith, and K. Tominaga, “Mrg15 null and heterozygous mouse embryonic fibroblasts exhibit DNA-repair defects post exposure to gamma ionizing radiation,” FEBS Letters, vol. 581, no. 27, pp. 5275–5281, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
34. C. van Oevelen, J. Wang, P. Asp, Q. Yan, W. G. Kaelin Jr., Y. Kluger, and B. D. Dynlacht, “A role for mammalian Sin3 in permanent gene silencing,” Molecular Cell, vol. 32, no. 3, pp. 359–370, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
35. N. Lee, H. Erdjument-Bromage, P. Tempst, R. S. Jones, and Y. Zhang, “The H3K4 demethylase lid associates with and inhibits histone deacetylase Rpd3,” Molecular and Cellular Biology, vol. 29, no. 6, pp. 1401–1410, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
36. Y. M. Moshkin, T. W. Kan, and T. W. Kan, “Histone chaperones ASF1 and NAP1 differentially modulate removal of active histone marks by LID-RPD3 complexes during NOTCH silencing,” Molecular Cell, vol. 35, no. 6, pp. 782–793, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
37. S. J. Bray, “Notch signalling: a simple pathway becomes complex,” Nature Reviews Molecular Cell Biology, vol. 7, no. 9, pp. 678–689, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
38. U. Koch and F. Radtke, “Notch and cancer: a double-edged sword,” Cellular and Molecular Life Sciences, vol. 64, no. 21, pp. 2746–2762, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
39. R. Liefke, F. Oswald, and F. Oswald, “Histone demethylase KDM5A is an integral part of the core Notch-RBP-J repressor complex,” Genes and Development, vol. 24, no. 6, pp. 590–601, 2010. View at Publisher · View at Google Scholar · View at PubMed
40. L. A. Pile, P. T. Spellman, R. J. Katzenberger, and D. A. Wassarman, “The SIN3 deacetylase complex represses genes encoding mitochondrial proteins: implications for the regulation of energy metabolism,” Journal of Biological Chemistry, vol. 278, no. 39, pp. 37840–37848, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
41. N. Lopez-Bigas, T. A. Kisiel, and T. A. Kisiel, “Genome-wide analysis of the H3K4 histone demethylase RBP2 reveals a transcriptional program controlling differentiation,” Molecular Cell, vol. 31, no. 4, pp. 520–530, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
42. J. K. Tong, C. A. Hassig, G. R. Schnitzler, R. E. Kingston, and S. L. Schreiber, “Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex,” Nature, vol. 395, no. 6705, pp. 917–921, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
43. Y. Xue, J. Wong, G. T. Moreno, M. K. Young, J. Côté, and W. Wang, “NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities,” Molecular Cell, vol. 2, no. 6, pp. 851–861, 1998. View at Scopus
44. Q. Ge, D. S. Nilasena, C. A. O'Brien, M. B. Frank, and I. N. Targoff, “Molecular analysis of a major antigenic region of the 240-kD protein of Mi-2 autoantigen,” Journal of Clinical Investigation, vol. 96, no. 4, pp. 1730–1737, 1995. View at Scopus
45. M. Saito and F. Ishikawa, “The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2,” Journal of Biological Chemistry, vol. 277, no. 38, pp. 35434–35439, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
46. B. Hendrich and A. Bird, “Identification and characterization of a family of mammalian methyl-CpG binding proteins,” Molecular and Cellular Biology, vol. 18, no. 11, pp. 6538–6547, 1998. View at Scopus
47. Y. Zhang, H.-H. Ng, H. Erdjument-Bromage, P. Tempst, A. Bird, and D. Reinberg, “Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation,” Genes and Development, vol. 13, no. 15, pp. 1924–1935, 1999. View at Scopus
48. X. Le Guezennec, M. Vermeulen, A. B. Brinkman, W. A. M. Hoeijmakers, A. Cohen, E. Lasonder, and H. G. Stunnenberg, “MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties,” Molecular and Cellular Biology, vol. 26, no. 3, pp. 843–851, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
49. B. Hendrich, J. Guy, B. Ramsahoye, V. A. Wilson, and A. Bird, “Closely related proteins MBD2 and MBD3 play distinctive but interacting roles in mouse development,” Genes and Development, vol. 15, no. 6, pp. 710–723, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
50. R. Kumar, R.-A. Wang, and R.-A. Wang, “A naturally occurring MTA1 variant sequesters oestrogen receptor-α in the cytoplasm,” Nature, vol. 418, no. 6898, pp. 654–657, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
51. N. Fujita, D. L. Jaye, M. Kajita, C. Geigerman, C. S. Moreno, and P. A. Wade, “MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer,” Cell, vol. 113, no. 2, pp. 207–219, 2003. View at Publisher · View at Google Scholar · View at Scopus
52. Y. Toh, E. Oki, and E. Oki, “Overexpression of the MTA1 gene in gastrointestinal carcinomas: correlation with invasion and metastasis,” International Journal of Cancer, vol. 74, no. 4, pp. 459–463, 1997. View at Publisher · View at Google Scholar · View at Scopus
53. Y. Toh, H. Kuwano, M. Mori, G. L. Nicolson, and K. Sugimachi, “Overexpression of metastasis-associated MTA1 mRNA in invasive oesophageal carcinomas,” British Journal of Cancer, vol. 79, no. 11-12, pp. 1723–1726, 1999. View at Scopus
54. A. Mazumdar, R.-A. Wang, and R.-A. Wang, “Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor,” Nature Cell Biology, vol. 3, no. 1, pp. 30–37, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
55. K. Kaji, I. M. Caballero, R. MacLeod, J. Nichols, V. A. Wilson, and B. Hendrich, “The NuRD component Mbd3 is required for pluripotency of embryonic stem cells,” Nature Cell Biology, vol. 8, no. 3, pp. 285–292, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
56. K. Kaji, J. Nichols, B. Hendrich, and B. Hendrich, “Mbd3, a component of the NuRD co-repressor complex, is reqiured for development of pluripotent cells,” Development, vol. 134, no. 6, pp. 1123–1132, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
57. M. Brackertz, Z. Gong, J. Leers, and R. Renkawitz, “p66α and p66β of the Mi-2/NuRD complex mediate MBD2 and histone interaction,” Nucleic Acids Research, vol. 34, no. 2, pp. 397–406, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
58. S. Marino and R. Nusse, “Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic lethal,” PloS One, vol. 2, no. 6, article e519, 2007.
59. I. Chambers and A. Smith, “Self-renewal of teratocarcinoma and embryonic stem cells,” Oncogene, vol. 23, no. 43, pp. 7150–7160, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
60. Y. Wang, H. Zhang, and H. Zhang, “LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer,” Cell, vol. 138, no. 4, pp. 660–672, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
61. M. E. Andres, C. Burger, and C. Burger, “CoREST: a functional corepressor required for regulation of neural- specific gene expression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 17, pp. 9873–9878, 1999. View at Publisher · View at Google Scholar · View at Scopus
62. A. You, J. K. Tong, C. M. Grozinger, and S. L. Schreiber, “CoREST is an integral component of the CoREST-human histone deacetylase complex,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 4, pp. 1454–1458, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
63. R. Aasland, A. F. Stewart, and T. Gibson, “The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB,” Trends in Biochemical Sciences, vol. 21, no. 3, pp. 87–88, 1996. View at Publisher · View at Google Scholar · View at Scopus
64. Y.-J. Shi, C. Matson, F. Lan, S. Iwase, T. Baba, and Y. Shi, “Regulation of LSD1 histone demethylase activity by its associated factors,” Molecular Cell, vol. 19, no. 6, pp. 857–864, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
65. J. Yu, Y. Li, T. Ishizuka, M. G. Guenther, and M. A. Lazar, “A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation,” EMBO Journal, vol. 22, no. 13, pp. 3403–3410, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
66. J. J. M. Cowger, Q. Zhao, M. Isovic, and J. Torchia, “Biochemical characterization of the zinc-finger protein 217 transcriptional repressor complex: identification of a ZNF217 consensus recognition sequence,” Oncogene, vol. 26, no. 23, pp. 3378–3386, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
67. Y. Shi, J.-I. Sawada, and J.-I. Sawada, “Coordinated histone modifications mediated by a CtBP co-repressor complex,” Nature, vol. 422, no. 6933, pp. 735–738, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
68. Y. Lin, Y. Wu, and Y. Wu, “The SNAG domain of snail1 functions as a molecular hook for recruiting lysine-specific demethylase 1,” EMBO Journal, vol. 29, no. 11, pp. 1803–1816, 2010. View at Publisher · View at Google Scholar · View at PubMed
69. S. Saleque, J. Kim, H. M. Rooke, and S. H. Orkin, “Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1,” Molecular Cell, vol. 27, no. 4, pp. 562–572, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
70. P. Ordentlich, M. Downes, W. Xie, A. Genin, N. B. Spinner, and R. M. Evans, “Unique forms of human and mouse nuclear receptor corepressor SMRT,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 6, pp. 2639–2644, 1999. View at Publisher · View at Google Scholar · View at Scopus
71. O. Hermanson, K. Jepsen, and M. G. Rosenfeld, “N-CoR controls differentiation of neural stem cells into astrocytes,” Nature, vol. 419, no. 6910, pp. 934–939, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
72. K. Jepsen, D. Solum, and D. Solum, “SMRT-mediated repression of an H3K27 demethylase in progression from neural stem cell to neuron,” Nature, vol. 450, no. 7168, pp. 415–419, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
73. V. Perissi, K. Jepsen, C. K. Glass, and M. G. Rosenfeld, “Deconstructing repression: evolving models of co-repressor action,” Nature Reviews Genetics, vol. 11, no. 2, pp. 109–123, 2010. View at Publisher · View at Google Scholar · View at PubMed
74. W. Fischle, F. Dequiedt, M. J. Hendzel, M. G. Guenther, M. A. Lazar, W. Voelter, and E. Verdin, “Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR,” Molecular Cell, vol. 9, no. 1, pp. 45–57, 2002. View at Publisher · View at Google Scholar · View at Scopus
75. C. K. Glass and M. G. Rosenfeld, “The coregulator exchange in transcriptional functions of nuclear receptors,” Genes and Development, vol. 14, no. 2, pp. 121–141, 2000. View at Scopus
76. K. Jepsen, O. Hermanson, and O. Hermanson, “Combinatorial roles of the nuclear receptor corepressor in transcription and development,” Cell, vol. 102, no. 6, pp. 753–763, 2000. View at Scopus
77. H.-G. Yoon, D. W. Chan, A. B. Reynolds, J. Qin, and J. Wong, “N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso,” Molecular Cell, vol. 12, no. 3, pp. 723–734, 2003. View at Publisher · View at Google Scholar · View at Scopus
78. D. Zhang, H.-G. Yoon, and J. Wong, “JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2),” Molecular and Cellular Biology, vol. 25, no. 15, pp. 6404–6414, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
79. S. S. Ng, K. L. Kavanagh, and K. L. Kavanagh, “Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity,” Nature, vol. 448, no. 7149, pp. 87–91, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
80. P. Trojer, J. Zhang, M. Yonezawa, A. Schmidt, H. Zheng, T. Jenuwein, and D. Reinberg, “Dynamic histone H1 isotype 4 methylation and demethylation by histone lysine methyltransferase G9a/KMT1C and the jumonji domain-containing JMJD2/KDM4 proteins,” Journal of Biological Chemistry, vol. 284, no. 13, pp. 8395–8405, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
81. A. Tzschach, S. Lenzner, and S. Lenzner, “Novel JARID1C/SMCX mutations in patients with X-linked mental retardation,” Human Mutation, vol. 27, no. 4, p. 389, 2006. View at Scopus
82. A. Adegbola, H. Gao, S. Sommer, and M. Browning, “A novel mutation in JARID1C/SMCX in a patient with autism spectrum disorder (ASD),” American Journal of Medical Genetics A, vol. 146, no. 4, pp. 505–511, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
83. L. R. Jensen, M. Amende, and M. Amende, “Mutations in the JARID1C gene, which is involved in transcriptional regulation and chromatin remodeling, cause X-linked mental retardation,” American Journal of Human Genetics, vol. 76, no. 2, pp. 227–236, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
84. M. Tahiliani, P. Mei, and P. Mei, “The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation,” Nature, vol. 447, no. 7144, pp. 601–605, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
85. J. M. Coulson, “Transcriptional regulation: cancer, neurons and the REST,” Current Biology, vol. 15, no. 17, pp. R665–R668, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
86. J. J. Abrajano, I. A. Qureshi, S. Gokhan, D. Zheng, A. Bergman, and M. F. Mehler, “Differential deployment of REST and CoREST promotes glial subtype specification and oligodendrocyte lineage maturation,” PLoS One, vol. 4, no. 11, Article ID e7665, 2009. View at Publisher · View at Google Scholar · View at PubMed