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Volumn 42, Issue 10, 2014, Pages 6168-6182

KDM4C (GASC1) lysine demethylase is associated with mitotic chromatin and regulates chromosome segregation during mitosis

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; HISTONE H3; PROTEIN KDM4A; PROTEIN KDM4B; PROTEIN KDM4C; UNCLASSIFIED DRUG;

EID: 84903155824     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku253     Document Type: Article
Times cited : (34)

References (92)
  • 2
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • Berger, S.L. (2007) The complex language of chromatin regulation during transcription. Nature, 447, 407-412.
    • (2007) Nature , vol.447 , pp. 407-412
    • Berger, S.L.1
  • 3
    • 84878282462 scopus 로고    scopus 로고
    • Histone variants in pluripotency and disease
    • Skene, P.J. and Henikoff, S. (2013) Histone variants in pluripotency and disease. Development, 140, 2513-2524.
    • (2013) Development , vol.140 , pp. 2513-2524
    • Skene, P.J.1    Henikoff, S.2
  • 4
    • 84875149194 scopus 로고    scopus 로고
    • Regulation of nucleosome dynamics by histone modifications
    • Zentner, G.E. and Henikoff, S. (2013) Regulation of nucleosome dynamics by histone modifications. Nat. Struct. Mol. Biol., 20, 259-266.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 259-266
    • Zentner, G.E.1    Henikoff, S.2
  • 5
    • 79952111963 scopus 로고    scopus 로고
    • Nucleosome dynamics and histone variants
    • Ray-Gallet, D. and Almouzni, G. (2010) Nucleosome dynamics and histone variants. Essays Biochem., 48, 75-87.
    • (2010) Essays Biochem. , vol.48 , pp. 75-87
    • Ray-Gallet, D.1    Almouzni, G.2
  • 6
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li, B., Carey, M. and Workman, J.L. (2007) The role of chromatin during transcription. Cell, 128, 707-719.
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 7
    • 0037010187 scopus 로고    scopus 로고
    • The complexity of chromatin remodeling and its links to cancer
    • Neely, K.E. and Workman, J.L. (2002) The complexity of chromatin remodeling and its links to cancer. Biochim. Biophys. Acta., 1603, 19-29.
    • (2002) Biochim. Biophys. Acta. , vol.1603 , pp. 19-29
    • Neely, K.E.1    Workman, J.L.2
  • 8
    • 34548544648 scopus 로고    scopus 로고
    • Chromatin remodeling and cancer, Part II: ATP-dependent chromatin remodeling
    • Wang, G.G., Allis, C.D. and Chi, P. (2007) Chromatin remodeling and cancer, Part II: ATP-dependent chromatin remodeling. Trends Mol. Med., 13, 373-380.
    • (2007) Trends Mol. Med. , vol.13 , pp. 373-380
    • Wang, G.G.1    Allis, C.D.2    Chi, P.3
  • 9
    • 84875424617 scopus 로고    scopus 로고
    • Emerging roles for chromatin as a signal integration and storage platform
    • Badeaux, A.I. and Shi, Y. (2013) Emerging roles for chromatin as a signal integration and storage platform. Nat. Rev. Mol. Cell Biol., 14, 211-224.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 211-224
    • Badeaux, A.I.1    Shi, Y.2
  • 10
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007) Chromatin modifications and their function. Cell, 128, 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 11
    • 84874116331 scopus 로고    scopus 로고
    • Chromatin: Receiver and quarterback for cellular signals
    • Johnson, D.G. and Dent, S.Y. (2013) Chromatin: receiver and quarterback for cellular signals. Cell, 152, 685-689.
    • (2013) Cell , vol.152 , pp. 685-689
    • Johnson, D.G.1    Dent, S.Y.2
  • 12
    • 79954416946 scopus 로고    scopus 로고
    • Readers of histone modifications
    • Yun, M., Wu, J., Workman, J.L. and Li, B. (2011) Readers of histone modifications. Cell Res., 21, 564-578.
    • (2011) Cell Res. , vol.21 , pp. 564-578
    • Yun, M.1    Wu, J.2    Workman, J.L.3    Li, B.4
  • 13
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin, C. and Zhang, Y. (2005) The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol., 6, 838-849.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 14
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. (1997) Histone acetylation in chromatin structure and transcription. Nature, 389, 349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 15
    • 53549088904 scopus 로고    scopus 로고
    • Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin
    • Li, F., Huarte, M., Zaratiegui, M., Vaughn, M.W., Shi, Y., Martienssen, R. and Cande, W.Z. (2008) Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Cell, 135, 272-283.
    • (2008) Cell , vol.135 , pp. 272-283
    • Li, F.1    Huarte, M.2    Zaratiegui, M.3    Vaughn, M.W.4    Shi, Y.5    Martienssen, R.6    Cande, W.Z.7
  • 16
    • 77949678340 scopus 로고    scopus 로고
    • Chromatin structure and the inheritance of epigenetic information
    • Margueron, R. and Reinberg, D. (2010) Chromatin structure and the inheritance of epigenetic information. Nat. Rev. Genet., 11, 285-296.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 285-296
    • Margueron, R.1    Reinberg, D.2
  • 17
    • 0037154972 scopus 로고    scopus 로고
    • Epigenetic codes for heterochromatin formation and silencing: Rounding up the usual suspects
    • Richards, E.J. and Elgin, S.C. (2002) Epigenetic codes for heterochromatin formation and silencing: rounding up the usual suspects. Cell, 108, 489-500.
    • (2002) Cell , vol.108 , pp. 489-500
    • Richards, E.J.1    Elgin, S.C.2
  • 21
    • 84870375316 scopus 로고    scopus 로고
    • Histone lysine methylation dynamics: Establishment, regulation, and biological impact
    • Black, J.C., Van Rechem, C. and Whetstine, J.R. (2012) Histone lysine methylation dynamics: establishment, regulation, and biological impact. Mol. Cell, 48, 491-507.
    • (2012) Mol. Cell , vol.48 , pp. 491-507
    • Black, J.C.1    Van Rechem, C.2    Whetstine, J.R.3
  • 23
    • 84859893371 scopus 로고    scopus 로고
    • Histone methylation: A dynamic mark in health, disease and inheritance
    • Greer, E.L. and Shi, Y. (2012) Histone methylation: a dynamic mark in health, disease and inheritance. Nat. Rev. Genet., 13, 343-357.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 343-357
    • Greer, E.L.1    Shi, Y.2
  • 25
    • 78049286684 scopus 로고    scopus 로고
    • Histone demethylases in development and disease
    • Pedersen, M.T. and Helin, K. (2010) Histone demethylases in development and disease. Trends Cell Biol., 20, 662-671.
    • (2010) Trends Cell Biol. , vol.20 , pp. 662-671
    • Pedersen, M.T.1    Helin, K.2
  • 26
    • 36849084465 scopus 로고    scopus 로고
    • Linking the epigenetic 'language' of covalent histone modifications to cancer
    • Hake, S.B., Xiao, A. and Allis, C.D. (2007) Linking the epigenetic 'language' of covalent histone modifications to cancer. Br. J. Cancer, 96 Suppl, R31-R39.
    • (2007) Br. J. Cancer , vol.96 , Issue.SUPPL.
    • Hake, S.B.1    Xiao, A.2    Allis, C.D.3
  • 27
    • 4644220954 scopus 로고    scopus 로고
    • MLL: A histone methyltransferase disrupted in leukemia
    • Hess, J.L. (2004) MLL: a histone methyltransferase disrupted in leukemia. Trends Mol. Med., 10, 500-507.
    • (2004) Trends Mol. Med. , vol.10 , pp. 500-507
    • Hess, J.L.1
  • 29
    • 0036683308 scopus 로고    scopus 로고
    • Unsafe SETs: Histone lysine methyltransferases and cancer
    • Schneider, R., Bannister, A.J. and Kouzarides, T. (2002) Unsafe SETs: histone lysine methyltransferases and cancer. Trends Biochem. Sci., 27, 396-402.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 396-402
    • Schneider, R.1    Bannister, A.J.2    Kouzarides, T.3
  • 33
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose, R.J., Kallin, E.M. and Zhang, Y. (2006) JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet., 7, 715-727.
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 36
    • 33846025127 scopus 로고    scopus 로고
    • Dynamic regulation of histone lysine methylation by demethylases
    • Shi, Y. and Whetstine, J.R. (2007) Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell, 25, 1-14.
    • (2007) Mol. Cell , vol.25 , pp. 1-14
    • Shi, Y.1    Whetstine, J.R.2
  • 39
    • 33745847680 scopus 로고    scopus 로고
    • The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
    • Klose, R.J., Yamane, K., Bae, Y., Zhang, D., Erdjument-Bromage, H., Tempst, P., Wong, J. and Zhang, Y. (2006) The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature, 442, 312-316.
    • (2006) Nature , vol.442 , pp. 312-316
    • Klose, R.J.1    Yamane, K.2    Bae, Y.3    Zhang, D.4    Erdjument-Bromage, H.5    Tempst, P.6    Wong, J.7    Zhang, Y.8
  • 40
    • 57349135504 scopus 로고    scopus 로고
    • The JMJD2 members of histone demethylase revisited
    • Tan, H., Wu, S., Wang, J. and Zhao, Z.K. (2008) The JMJD2 members of histone demethylase revisited. Mol. Biol. Rep., 35, 551-556.
    • (2008) Mol. Biol. Rep. , vol.35 , pp. 551-556
    • Tan, H.1    Wu, S.2    Wang, J.3    Zhao, Z.K.4
  • 41
    • 33846132573 scopus 로고    scopus 로고
    • Diversity within the JMJD2 histone demethylase family
    • Shin, S. and Janknecht, R. (2007) Diversity within the JMJD2 histone demethylase family. Biochem. Biophys. Res. Commun., 353, 973-977.
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 973-977
    • Shin, S.1    Janknecht, R.2
  • 43
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • Horton, J.R., Upadhyay, A.K., Qi, H.H., Zhang, X., Shi, Y. and Cheng, X. (2010) Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nat. Struct. Mol. Biol., 17, 38-43.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.6
  • 45
    • 80053132089 scopus 로고    scopus 로고
    • Deciphering arginine methylation: Tudor tells the tale
    • Chen, C., Nott, T.J., Jin, J. and Pawson, T. (2011) Deciphering arginine methylation: Tudor tells the tale. Nat. Rev. Mol. Cell Biol., 12, 629-642.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 629-642
    • Chen, C.1    Nott, T.J.2    Jin, J.3    Pawson, T.4
  • 47
    • 77957849604 scopus 로고    scopus 로고
    • Tudor domain
    • Lasko, P. (2010) Tudor domain. Curr. Biol., 20, R666-667.
    • (2010) Curr. Biol. , vol.20
    • Lasko, P.1
  • 48
    • 77950488501 scopus 로고    scopus 로고
    • How does the royal family of Tudor rule the PIWI-interacting RNA pathway?
    • Siomi, M.C., Mannen, T. and Siomi, H. (2010) How does the royal family of Tudor rule the PIWI-interacting RNA pathway? Genes Dev., 24, 636-646.
    • (2010) Genes Dev. , vol.24 , pp. 636-646
    • Siomi, M.C.1    Mannen, T.2    Siomi, H.3
  • 49
    • 84861980264 scopus 로고    scopus 로고
    • Tudor domain proteins in development
    • Pek, J.W., Anand, A. and Kai, T. (2012) Tudor domain proteins in development. Development, 139, 2255-2266.
    • (2012) Development , vol.139 , pp. 2255-2266
    • Pek, J.W.1    Anand, A.2    Kai, T.3
  • 51
    • 34250168304 scopus 로고    scopus 로고
    • Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D
    • Shin, S. and Janknecht, R. (2007) Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D. Biochem. Biophys. Res. Commun., 359, 742-746.
    • (2007) Biochem. Biophys. Res. Commun. , vol.359 , pp. 742-746
    • Shin, S.1    Janknecht, R.2
  • 52
    • 22544465244 scopus 로고    scopus 로고
    • 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)
    • Zhang, D., Yoon, H.G. and Wong, J. (2005) 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). Mol. Cell Biol., 25, 6404-6414.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 6404-6414
    • Zhang, D.1    Yoon, H.G.2    Wong, J.3
  • 53
    • 84870463217 scopus 로고    scopus 로고
    • JMJD2A promotes cellular transformation by blocking cellular senescence through transcriptional repression of the tumor suppressor CHD5
    • Mallette, F.A. and Richard, S. (2012) JMJD2A promotes cellular transformation by blocking cellular senescence through transcriptional repression of the tumor suppressor CHD5. Cell Rep., 2, 1233-1243.
    • (2012) Cell Rep. , vol.2 , pp. 1233-1243
    • Mallette, F.A.1    Richard, S.2
  • 54
    • 84859725611 scopus 로고    scopus 로고
    • Regulation of tumor suppressor p53 and HCT116 cell physiology by histone demethylase JMJD2D/KDM4D
    • Kim, T.D., Oh, S., Shin, S. and Janknecht, R. (2012) Regulation of tumor suppressor p53 and HCT116 cell physiology by histone demethylase JMJD2D/KDM4D. PLoS One, 7, e34618.
    • (2012) PLoS One , vol.7
    • Kim, T.D.1    Oh, S.2    Shin, S.3    Janknecht, R.4
  • 56
    • 84859895529 scopus 로고    scopus 로고
    • RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites
    • Mallette, F.A., Mattiroli, F., Cui, G., Young, L.C., Hendzel, M.J., Mer, G., Sixma, T.K. and Richard, S. (2012) RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. Embo. J., 31, 1865-1878.
    • (2012) Embo. J. , vol.31 , pp. 1865-1878
    • Mallette, F.A.1    Mattiroli, F.2    Cui, G.3    Young, L.C.4    Hendzel, M.J.5    Mer, G.6    Sixma, T.K.7    Richard, S.8
  • 57
    • 77957821048 scopus 로고    scopus 로고
    • Drosophila p53 is required to increase the levels of the dKDM4B demethylase after UV induced DNA damage to demethylate histone H3-lysine 9
    • Palomera-Sanchez, Z., Bucio-Mendez, A., Valadez-Graham, V., Reynaud, E. and Zurita, M. (2010) Drosophila p53 is required to increase the levels of the dKDM4B demethylase after UV induced DNA damage to demethylate histone H3-lysine 9. J. Biol. Chem, 285, 31370-31379.
    • (2010) J. Biol. Chem , vol.285 , pp. 31370-31379
    • Palomera-Sanchez, Z.1    Bucio-Mendez, A.2    Valadez-Graham, V.3    Reynaud, E.4    Zurita, M.5
  • 58
    • 84880557003 scopus 로고    scopus 로고
    • Kdm4b histone demethylase Is a DNA damage response protein and confers a survival advantage following gamma-Irradiation
    • Young, L.C., McDonald, D.W. and Hendzel, M.J. (2013) Kdm4b histone demethylase Is a DNA damage response protein and confers a survival advantage following gamma-Irradiation. J. Biol. Chem., 288, 21376-21388.
    • (2013) J. Biol. Chem. , vol.288 , pp. 21376-21388
    • Young, L.C.1    McDonald, D.W.2    Hendzel, M.J.3
  • 59
    • 35348982301 scopus 로고    scopus 로고
    • Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cells
    • Loh, Y.H., Zhang, W., Chen, X., George, J. and Ng, H.H. (2007) Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cells. Genes Dev., 21, 2545-2557.
    • (2007) Genes Dev. , vol.21 , pp. 2545-2557
    • Loh, Y.H.1    Zhang, W.2    Chen, X.3    George, J.4    Ng, H.H.5
  • 60
    • 72449133771 scopus 로고    scopus 로고
    • The histone demethylase Dmel\Kdm4A controls genes required for life span and male-specific sex determination in Drosophila
    • Lorbeck, M.T., Singh, N., Zervos, A., Dhatta, M., Lapchenko, M., Yang, C. and Elefant, F. (2010) The histone demethylase Dmel\Kdm4A controls genes required for life span and male-specific sex determination in Drosophila. Gene, 450, 8-17.
    • (2010) Gene , vol.450 , pp. 8-17
    • Lorbeck, M.T.1    Singh, N.2    Zervos, A.3    Dhatta, M.4    Lapchenko, M.5    Yang, C.6    Elefant, F.7
  • 61
    • 84903155987 scopus 로고    scopus 로고
    • Histone lysine demethylase (KDM) subfamily 4: Structures, functions and therapeutic potential
    • Labbe, R.M., Holowatyj, A. and Yang, Z.Q. (2013) Histone lysine demethylase (KDM) subfamily 4: structures, functions and therapeutic potential. Am. J. Transl. Res., 6, 1-15.
    • (2013) Am. J. Transl. Res. , vol.6 , pp. 1-15
    • Labbe, R.M.1    Holowatyj, A.2    Yang, Z.Q.3
  • 63
    • 84877861510 scopus 로고    scopus 로고
    • KDM4/JMJD2 histone demethylases: Epigenetic regulators in cancer cells
    • Berry, W.L. and Janknecht, R. (2013) KDM4/JMJD2 histone demethylases: epigenetic regulators in cancer cells. Cancer Res., 73, 2936-2942.
    • (2013) Cancer Res. , vol.73 , pp. 2936-2942
    • Berry, W.L.1    Janknecht, R.2
  • 65
    • 0034282790 scopus 로고    scopus 로고
    • Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines
    • Yang, Z.Q., Imoto, I., Fukuda, Y., Pimkhaokham, A., Shimada, Y., Imamura, M., Sugano, S., Nakamura, Y. and Inazawa, J. (2000) Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines. Cancer Res., 60, 4735-4739.
    • (2000) Cancer Res. , vol.60 , pp. 4735-4739
    • Yang, Z.Q.1    Imoto, I.2    Fukuda, Y.3    Pimkhaokham, A.4    Shimada, Y.5    Imamura, M.6    Sugano, S.7    Nakamura, Y.8    Inazawa, J.9
  • 66
    • 33644670527 scopus 로고    scopus 로고
    • Comprehensive genomic analysis of desmoplastic medulloblastomas: Identification of novel amplified genes and separate evaluation of the different histological components
    • Ehrbrecht, A., Muller, U., Wolter, M., Hoischen, A., Koch, A., Radlwimmer, B., Actor, B., Mincheva, A., Pietsch, T., Lichter, P. et al. (2006) Comprehensive genomic analysis of desmoplastic medulloblastomas: identification of novel amplified genes and separate evaluation of the different histological components. J. Pathol., 208, 554-563.
    • (2006) J. Pathol. , vol.208 , pp. 554-563
    • Ehrbrecht, A.1    Muller, U.2    Wolter, M.3    Hoischen, A.4    Koch, A.5    Radlwimmer, B.6    Actor, B.7    Mincheva, A.8    Pietsch, T.9    Lichter, P.10
  • 67
    • 84870608916 scopus 로고    scopus 로고
    • Histone demethylase JMJD2C is a coactivator for hypoxia-inducible factor 1 that is required for breast cancer progression
    • Luo, W., Chang, R., Zhong, J., Pandey, A. and Semenza, G.L. (2012) Histone demethylase JMJD2C is a coactivator for hypoxia-inducible factor 1 that is required for breast cancer progression. Proc. Natl. Acad. Sci. U. S. A., 109, E3367-3376.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109
    • Luo, W.1    Chang, R.2    Zhong, J.3    Pandey, A.4    Semenza, G.L.5
  • 68
    • 72449186524 scopus 로고    scopus 로고
    • Genomic amplification and oncogenic properties of the GASC1 histone demethylase gene in breast cancer
    • Liu, G., Bollig-Fischer, A., Kreike, B., van de Vijver, M.J., Abrams, J., Ethier, S.P. and Yang, Z.Q. (2009) Genomic amplification and oncogenic properties of the GASC1 histone demethylase gene in breast cancer. Oncogene, 28, 4491-4500.
    • (2009) Oncogene , vol.28 , pp. 4491-4500
    • Liu, G.1    Bollig-Fischer, A.2    Kreike, B.3    Van De-Vijver, M.J.4    Abrams, J.5    Ethier, S.P.6    Yang, Z.Q.7
  • 70
    • 84855876194 scopus 로고    scopus 로고
    • Histone demethylase JMJD2B is required for tumor cell proliferation and survival and is overexpressed in gastric cancer
    • Li, W., Zhao, L., Zang, W., Liu, Z., Chen, L., Liu, T., Xu, D. and Jia, J. (2011) Histone demethylase JMJD2B is required for tumor cell proliferation and survival and is overexpressed in gastric cancer. Biochem. Biophys. Res. Commun., 416, 372-378.
    • (2011) Biochem. Biophys. Res. Commun. , vol.416 , pp. 372-378
    • Li, W.1    Zhao, L.2    Zang, W.3    Liu, Z.4    Chen, L.5    Liu, T.6    Xu, D.7    Jia, J.8
  • 71
    • 79952800100 scopus 로고    scopus 로고
    • Histone demethylase JMJD2B functions as a co-factor of estrogen receptor in breast cancer proliferation and mammary gland development
    • Kawazu, M., Saso, K., Tong, K.I., McQuire, T., Goto, K., Son, D.O., Wakeham, A., Miyagishi, M., Mak, T.W. and Okada, H. (2011) Histone demethylase JMJD2B functions as a co-factor of estrogen receptor in breast cancer proliferation and mammary gland development. PLoS One, 6, e17830.
    • (2011) PLoS One , vol.6
    • Kawazu, M.1    Saso, K.2    Tong, K.I.3    McQuire, T.4    Goto, K.5    Son, D.O.6    Wakeham, A.7    Miyagishi, M.8    Mak, T.W.9    Okada, H.10
  • 72
    • 79956291600 scopus 로고    scopus 로고
    • Histone demethylase JMJD2B coordinates H3K4/H3K9 methylation and promotes hormonally responsive breast carcinogenesis
    • Shi, L., Sun, L., Li, Q., Liang, J., Yu, W., Yi, X., Yang, X., Li, Y., Han, X., Zhang, Y. et al. (2011) Histone demethylase JMJD2B coordinates H3K4/H3K9 methylation and promotes hormonally responsive breast carcinogenesis. Proc. Natl. Acad. Sci. U. S. A., 108, 7541-7546.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 7541-7546
    • Shi, L.1    Sun, L.2    Li, Q.3    Liang, J.4    Yu, W.5    Yi, X.6    Yang, X.7    Li, Y.8    Han, X.9    Zhang, Y.10
  • 73
    • 84878239632 scopus 로고    scopus 로고
    • Heat shock protein 90 (Hsp90) selectively regulates the stability of KDM4B/JMJD2B histone demethylase
    • Ipenberg, I., Guttmann-Raviv, N., Khoury, H.P., Kupershmit, I. and Ayoub, N. (2013) Heat shock protein 90 (Hsp90) selectively regulates the stability of KDM4B/JMJD2B histone demethylase. J. Biol. Chem., 288, 14681-14687.
    • (2013) J. Biol. Chem. , vol.288 , pp. 14681-14687
    • Ipenberg, I.1    Guttmann-Raviv, N.2    Khoury, H.P.3    Kupershmit, I.4    Ayoub, N.5
  • 76
    • 84894367244 scopus 로고    scopus 로고
    • PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair
    • Khoury, H., Guttmann-Raviv, N., Ipenberg, I., Huggins, D., Jeyasekharan, A. D. and Nabieh Ayoub,. (2014) PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair. PNAS Plus, 111, E728-E737.
    • (2014) PNAS Plus , vol.111
    • Khoury, H.1    Guttmann-Raviv, N.2    Ipenberg, I.3    Huggins, D.4    Jeyasekharan, A.D.5    Ayoub, N.6
  • 77
    • 0032871844 scopus 로고    scopus 로고
    • Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells
    • Minc, E., Allory, Y., Worman, H.J., Courvalin, J.C. and Buendia, B. (1999) Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells. Chromosoma, 108, 220-234.
    • (1999) Chromosoma , vol.108 , pp. 220-234
    • Minc, E.1    Allory, Y.2    Worman, H.J.3    Courvalin, J.C.4    Buendia, B.5
  • 79
    • 77954244593 scopus 로고    scopus 로고
    • Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation
    • Nozawa, R.S., Nagao, K., Masuda, H.T., Iwasaki, O., Hirota, T., Nozaki, N., Kimura, H. and Obuse, C. (2010) Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation. Nat. Cell Biol., 12, 719-727.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 719-727
    • Nozawa, R.S.1    Nagao, K.2    Masuda, H.T.3    Iwasaki, O.4    Hirota, T.5    Nozaki, N.6    Kimura, H.7    Obuse, C.8
  • 80
    • 0032101295 scopus 로고    scopus 로고
    • Differential subcellular localization of protein phosphatase-1 alpha, gamma1, and delta isoforms during both interphase and mitosis in mammalian cells
    • Andreassen, P.R., Lacroix, F.B., Villa-Moruzzi, E. and Margolis, R.L. (1998) Differential subcellular localization of protein phosphatase-1 alpha, gamma1, and delta isoforms during both interphase and mitosis in mammalian cells. J. Cell Biol., 141, 1207-1215.
    • (1998) J. Cell Biol. , vol.141 , pp. 1207-1215
    • Andreassen, P.R.1    Lacroix, F.B.2    Villa-Moruzzi, E.3    Margolis, R.L.4
  • 81
    • 52949122554 scopus 로고    scopus 로고
    • TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules
    • Goulet, I., Boisvenue, S., Mokas, S., Mazroui, R. and Cote, J. (2008) TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules. Hum. Mol. Genet., 17, 3055-3074.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3055-3074
    • Goulet, I.1    Boisvenue, S.2    Mokas, S.3    Mazroui, R.4    Cote, J.5
  • 82
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan, M.V., Lee, J., Ward, I.M., Kim, J.E., Thompson, J.R., Chen, J. and Mer, G. (2006) Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell, 127, 1361-1373.
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5    Chen, J.6    Mer, G.7
  • 83
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang, Y., Fang, J., Bedford, M.T., Zhang, Y. and Xu, R.M. (2006) Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science, 312, 748-751.
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 84
    • 37849015924 scopus 로고    scopus 로고
    • Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
    • Lee, J., Thompson, J.R., Botuyan, M.V. and Mer, G. (2008) Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nat. Struct. Mol. Biol., 15, 109-111.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 109-111
    • Lee, J.1    Thompson, J.R.2    Botuyan, M.V.3    Mer, G.4
  • 87
    • 0037018844 scopus 로고    scopus 로고
    • Inhibition of aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis
    • Kallio, M.J., McCleland, M.L., Stukenberg, P.T. and Gorbsky, G.J. (2002) Inhibition of aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis. Curr. Biol., 12, 900-905.
    • (2002) Curr. Biol. , vol.12 , pp. 900-905
    • Kallio, M.J.1    McCleland, M.L.2    Stukenberg, P.T.3    Gorbsky, G.J.4
  • 88
    • 20144379551 scopus 로고    scopus 로고
    • Chromosome segregation: Aurora B gets Tousled
    • Richie, C.T. and Golden, A. (2005) Chromosome segregation: Aurora B gets Tousled. Curr. Biol., 15, R379-382.
    • (2005) Curr. Biol. , vol.15
    • Richie, C.T.1    Golden, A.2
  • 89
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Kagey, M.H., Melhuish, T.A. and Wotton, D. (2003) The polycomb protein Pc2 is a SUMO E3. Cell, 113, 127-137.
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 91
    • 33646824163 scopus 로고    scopus 로고
    • Dynamic changes in histone H3 lysine 9 methylations: Identification of a mitosis-specific function for dynamic methylation in chromosome congression and segregation
    • McManus, K.J., Biron, V.L., Heit, R., Underhill, D.A. and Hendzel, M.J. (2006) Dynamic changes in histone H3 lysine 9 methylations: identification of a mitosis-specific function for dynamic methylation in chromosome congression and segregation. J. Biol. Chem., 281, 8888-8897.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8888-8897
    • McManus, K.J.1    Biron, V.L.2    Heit, R.3    Underhill, D.A.4    Hendzel, M.J.5


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