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Volumn 29, Issue 2, 2009, Pages 131-141

Histone arginine methylations: Their roles in chromatin dynamics and transcriptional regulation

Author keywords

Arginine demethylase; Cancer; Chromatin insulator; Histone cross talk; Protein arginine N methyltransferase (PRMT); Transcriptional regulation

Indexed keywords

ARGININE; HISTONE; PROTEIN ARGININE METHYLTRANSFERASE;

EID: 66349120902     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20080176     Document Type: Review
Times cited : (71)

References (68)
  • 1
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: An emerging regulator of protein function
    • Bedford, M. T. and Richard, S. (2005) Arginine methylation: an emerging regulator of protein function. Mol. Cell 18, 263-272
    • (2005) Mol. Cell , vol.18 , pp. 263-272
    • Bedford, M.1    Richard, S.2
  • 2
    • 33845896853 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: Evolution and assessment of their pharmacological and therapeutic potential
    • Krause, C. D., Yang, Z. H., Kim, Y. S., Lee, J. H., Cook, J. R. and Pestka, S. (2006) Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential. Pharmacol. Ther. 113, 50-87
    • (2006) Pharmacol. Ther. , vol.113 , pp. 50-87
    • Krause, C.D.1    Yang, Z.H.2    Kim, Y.S.3    Lee, J.H.4    Cook, J.R.5    Pestka, S.6
  • 3
    • 0035854372 scopus 로고    scopus 로고
    • State of the arg: Protein methylation at arginine comes of age
    • McBride, A. E. and Silver, P. A. (2001) State of the arg: protein methylation at arginine comes of age. Cell 106, 5-8
    • (2001) Cell , vol.106 , pp. 58
    • McBride, A.E.1    Silver, P.A.2
  • 4
    • 33751029979 scopus 로고    scopus 로고
    • The testis-specific factor ctcfl cooperates with the protein methyltransferase prmt7 in h19 imprinting control region methylation
    • Jelinic, P., Stehle, J.-C. and Shaw, P. (2006) The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation. PLoS Biol. 4, 1910-1922
    • (2006) PLoS Biol. , vol.4 , pp. 1910-1922
    • Jelinic, P.1    Stehle J.-C Shaw, P.2
  • 7
    • 33846581497 scopus 로고    scopus 로고
    • Loss of imprinting and cancer
    • Jelinic, P. and Shaw, P. (2007) Loss of imprinting and Cancer. J. Pathol. 211, 261-268
    • (2007) J. Pathol. , vol.211 , pp. 261-268
    • Jelinic, P.1    Shaw, P.2
  • 8
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early tis21 protein and the leukemia-associated btg1 protein interact with a protein-arginine n-methyltransferase
    • Lin, W. J., Gary, J. D., Yang, M. C., Clarke, S. and Herschman, H. R. (1996) The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J. Biol. Chem. 271, 15034-15044
    • (1996) J. Biol. Chem. , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 9
    • 0034733748 scopus 로고    scopus 로고
    • Protein-arginine methyltransferase i, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3
    • Tang, J., Kao, P. N. and Herschman, H. R. (2000) Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3. J. Biol. Chem. 275, 19866-19876
    • (2000) J. Biol. Chem. , vol.275 , pp. 19866-19876
    • Tang, J.1    Kao, P.N.2    Herschman, H.R.3
  • 10
    • 0034045559 scopus 로고    scopus 로고
    • Arginine n-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable
    • Pawlak, M. R., Scherer, C. A., Chen, J., Roshon, M. J. and Ruley, E. (2000) Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable. Mol. Cell. Biol. 20, 4859-4869
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4859-4869
    • Pawlak, M.R.1    Scherer, C.A.2    Chen, J.3    Roshon, M.J.4    Ruley, E.5
  • 11
    • 15444374342 scopus 로고    scopus 로고
    • Arginine methylation of mre11 by prmt1 is required for dna damage checkpoint control
    • Boisvert, F.-M., D́ery, U., Masson, J.-Y. and Richard, S. (2005) Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control. Genes Dev. 19, 671-676
    • (2005) Genes Dev. , vol.19 , pp. 671-676
    • Boisvert, F.-M.1    D́ery, U.2    Masson, J.-Y.3    Richard, S.4
  • 14
    • 23944435995 scopus 로고    scopus 로고
    • Methylation of histone h4 by arginine methyltransferase prmt1 is essential in vivo for many subsequent histone modifications
    • Huang, S., Litt, M. and Felsenfeld, G. (2005) Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications. Genes Dev. 19, 1885-1893
    • (2005) Genes Dev. , vol.19 , pp. 1885-1893
    • Huang, S.1    Litt, M.2    Felsenfeld, G.3
  • 15
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of prmt1, p300, and carm1 in transcriptional activation by p53
    • An, W., Kim, J. and Roeder, R. G. (2004) Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 117, 735-748
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 17
    • 45549102968 scopus 로고    scopus 로고
    • The protein arginine methyltransferases carm1 and prmt1 cooperate in gene regulation
    • Kleinschmidt, M. A., Streubel, G., Samans, B., Krause, M. and Bauer, U-M. (2008) The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation. Nucleic Acids Res. 36, 3202-3213
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3202-3213
    • Kleinschmidt, M.A.1    Streubel, G.2    Samans, B.3    Krause, M.4    Bauer, U.-M.5
  • 18
    • 33749664150 scopus 로고    scopus 로고
    • Two functional modes of a nuclear receptor-recruited arginine methyltransferases in transcriptional activation
    • Barrero, M. J. and Malik, S. (2006) Two functional modes of a nuclear receptor-recruited arginine methyltransferases in transcriptional activation. Mol. Cell 24, 233-243
    • (2006) Mol. Cell , vol.24 , pp. 233-243
    • Barrero, M.J.1    Malik, S.2
  • 21
    • 0037047399 scopus 로고    scopus 로고
    • Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor α
    • Qi, C., Chang, J., Zhu, Y., Yeldandi, A. V., Rao, S. M. and Zhu, Y. J. (2002) Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor α. J. Biol. Chem. 277, 28624-28630
    • (2002) J. Biol. Chem. , vol.277 , pp. 28624-28630
    • Qi, C.1    Chang, J.2    Zhu, Y.3    Yeldandi, A.V.4    Rao, S.M.5    Zhu, Y.J.6
  • 22
    • 0032479171 scopus 로고    scopus 로고
    • Prmt3, a type i protein arginine n-methyltransferase that differs from prmt1 in its oligomerization, suncellular localization, substrate specificity, and regulation
    • Tang, J., Gary, J. D., Clarke, S. and Herschman, H. R. (1998) PRMT3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, suncellular localization, substrate specificity, and regulation. J. Biol. Chem. 273, 16935-16945
    • (1998) J. Biol. Chem. , vol.273 , pp. 16935-16945
    • Tang, J.1    Gary, J.D.2    Clarke, S.3    Herschman, H.R.4
  • 23
    • 14244255860 scopus 로고    scopus 로고
    • Ribosomal protein s2 is a substrate for mammalian protein arginine methyltransferase 3 (prmt3)
    • Swiercz, R., Person, M. D. and Bedford, M. T. (2005) Ribosomal protein S2 is a substrate for mammalian protein arginine methyltransferase 3 (PRMT3). Biochem. J. 386, 85-91
    • (2005) Biochem. J. , vol.386 , pp. 85-91
    • Swiercz, R.1    Person, M.D.2    Bedford, M.T.3
  • 25
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities
    • Koh, S. S., Chen, D., Lee, Y. H. and Stallcup, M. R. (2001) Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. J. Biol. Chem. 276, 1089-1098
    • (2001) J. Biol. Chem. , vol.276 , pp. 1089-1098
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 26
    • 0037164736 scopus 로고    scopus 로고
    • Crosstalk between carm1 methylation and cbp acetylation on histone h3
    • Daujat, S., Bauer, U.-M., Shah, V., Turner, B., Berger, S. and Kouzarides, T. (2002) Crosstalk between CARM1 methylation and CBP acetylation on histone H3. Curr. Biol. 12, 2090-2097
    • (2002) Curr. Biol. , vol.12 , pp. 2090-2097
    • Daujat, S.1    Bauer, U.-M.2    Shah, V.3    Turner, B.4    Berger, S.5    Kouzarides, T.6
  • 27
    • 33846226977 scopus 로고    scopus 로고
    • Histone arginine methylation regulates pluripotency in the early mouse embryo
    • Torres-Padilla, M.-E., Parfitt, D.-E., Kouzarides, T. and Zernicka-Goetz, M. (2007) Histone arginine methylation regulates pluripotency in the early mouse embryo. Nature 445, 214-218
    • (2007) Nature , vol.445 , pp. 214-218
    • Torres-Padilla, M.-E.1    Parfitt, D.-E.2    Kouzarides, T.3    Zernicka-Goetz, M.4
  • 28
    • 0038313055 scopus 로고    scopus 로고
    • Specific protein methylation defects and gene expression perturbation in coactivator-associated arginine methyltransferase 1-deficient mice
    • Yadav, N., Lee, J., Kim, J., Hu, M. C., Aldaz, C. M. and Bedford, M. T. (2003) Specific protein methylation defects and gene expression perturbation in coactivator-associated arginine methyltransferase 1-deficient mice. Proc. Natl. Acad. Sci. U.S.A. 100, 6464-6468
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6464-6468
    • Yadav, N.1    Lee, J.2    Kim, J.3    Hu, M.C.4    Aldaz, C.M.5    Bedford, M.T.6
  • 31
    • 53549103598 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 5 suppresses the transcription of the rb family of tumor suppressors in leukemia and lymphoma cells
    • Wang, L., Pal, S. and Sif, S. (2008) Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells. Mol. Cell. Biol. 28, 6262-6277
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6262-6277
    • Wang, L.1    Pal, S.2    Sif, S.3
  • 32
    • 33845801596 scopus 로고    scopus 로고
    • The protein arginine methyltransferase prmt5 is required for myogenesis because it facilitates atp-dependent chromatin remodeling
    • Dacwag, C. S., Ohkawa, Y., Pal, S., Sif, S. and Imbalzano, A. N. (2007) The protein arginine methyltransferase prmt5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling. Mol. Cell. Biol. 27, 384-394
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 384-394
    • Dacwag, C.S.1    Ohkawa, Y.2    Pal, S.3    Sif, S.4    Imbalzano, A.N.5
  • 33
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein arginine n-methyltransferase prmt6 is a nuclear enzyme displaying unique substrate specificity
    • Frankel, A., Yadav, N., Lee, J., Branscombe, T. L., Clarke, S. and Bedford, M. T. (2002) The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277, 3527-3543
    • (2002) J. Biol. Chem. , vol.277 , pp. 3527-3543
    • Frankel, A.1    Yadav, N.2    Lee, J.3    Branscombe, T.L.4    Clarke, S.5    Bedford, M.T.6
  • 34
    • 34347355449 scopus 로고    scopus 로고
    • A mass spectrometric study on the in vitro methylation of hmga1a and hmga1b by prmts: Methylation specificity, the effect of binding to at-rich duplex dna, and the effect of c-terminal phosphorylation
    • Zou, Y., Webb, K., Perna, A. D., Zhang, Q., Clerke, S. and Wang, Y. (2007) A mass spectrometric study on the in vitro methylation of HMGA1a and HMGA1b by PRMTs: methylation specificity, the effect of binding to AT-rich duplex DNA, and the effect of C-terminal phosphorylation. Biochemistry 46, 7896-7906
    • (2007) Biochemistry , vol.46 , pp. 7896-7906
    • Zou, Y.1    Webb, K.2    Perna, A.D.3    Zhang, Q.4    Clerke, S.5    Wang, Y.6
  • 38
    • 25444463928 scopus 로고    scopus 로고
    • Prmt8, a new membrane-bound tissue-specific member of the protein methyltransferase family
    • Lee, J., Sayegh, J., Daniel, J., Clarke, S. and Bedford, M. T. (2005) PRMT8, a new membrane-bound tissue-specific member of the protein methyltransferase family. J. Biol. Chem. 280, 32890-32896
    • (2005) J. Biol. Chem. , vol.280 , pp. 32890-32896
    • Lee, J.1    Sayegh, J.2    Daniel, J.3    Clarke, S.4    Bedford, M.T.5
  • 41
    • 35349006314 scopus 로고    scopus 로고
    • Histone lysine demethylases: Emerging roles in development, physiology and disease
    • Shi, Y. (2007) Histone lysine demethylases: emerging roles in development, physiology and disease. Nat. Rev. Genet. 8, 829-833
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 829-833
    • Shi, Y.1
  • 42
    • 35348938519 scopus 로고    scopus 로고
    • Jmjd6 is a histone arginine demethylase
    • Chang, b., Chen, Y., Zhao, Y. and Bruick, R. K. (2007) JMJD6 is a histone arginine demethylase. Science 318, 444-447
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 43
    • 0345374586 scopus 로고    scopus 로고
    • Phosphatidylserine receptor is required for clearance of apoptotic cells
    • Li, M. O., Sarkisian, M. R., Mehal, W. Z., Rakic, P. and Flavell, R. A. (2003) Phosphatidylserine receptor is required for clearance of apoptotic cells. Science 302, 1560-1563
    • (2003) Science , vol.302 , pp. 1560-1563
    • Li, M.O.1    Sarkisian, M.R.2    Mehal, W.Z.3    Rakic, P.4    Flavell, R.A.5
  • 44
    • 1942489369 scopus 로고    scopus 로고
    • Defective fetal liver erythropoiesis and t lymphopoiesis in mice lacking the phosphatidylserine receptor
    • Kunisaki, Y., Masuko, S., Noda, M., Inayoshi, A., Sanui, T., Harada, M., Sasazuki, T. and Fukui, Y. (2004) Defective fetal liver erythropoiesis and T lymphopoiesis in mice lacking the phosphatidylserine receptor. Blood 103, 3362-3364
    • (2004) Blood , vol.103 , pp. 3362-3364
    • Kunisaki, Y.1    Masuko, S.2    Noda, M.3    Inayoshi, A.4    Sanui, T.5    Harada, M.6    Sasazuki, T.7    Fukui, Y.8
  • 45
    • 9444237436 scopus 로고    scopus 로고
    • Phosphatidylserine receptor is required for the engulfment of dead apoptotic cells and for normal embryonic development in zebrafish
    • Hong, J.-R., Lin, G.-H., Lin, C. J.-F., Wang, W.-P., Lee, C.-C., Lin, T.-L. and Wu, J.-L. (2004) Phosphatidylserine receptor is required for the engulfment of dead apoptotic cells and for normal embryonic development in zebrafish. Development 131, 5417-5427
    • (2004) Development , vol.131 , pp. 5417-5427
    • Hong, J.-R.1    Lin, G.-H.2    Lin, C.J.-F.3    Wang, W.-P.4    Lee, C.-C.5    Lin T.-L Wu, J.-L.6
  • 47
    • 7644222810 scopus 로고    scopus 로고
    • Dal-1/4.1b tumor suppressor interacts with protein arginine n-methyltransferase 3 (prmt3 and inhibits its ability to methylate substrates in vitro and in vivo
    • Singh, V., Miranda, T. B., Jing, W., Frankel, A., Roemer, M. E., Robb, V. A., Gutmann, D. H., Herschman, H. R., Clarke, S. and Newsham, I. F. (2004) DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3 and inhibits its ability to methylate substrates in vitro and in vivo. Oncogene 23, 7761-7771
    • (2004) Oncogene , vol.23 , pp. 7761-7771
    • Singh, V.1    Miranda, T.B.2    Jing, W.3    Frankel, A.4    Roemer, M.E.5    Robb, V.A.6    Gutmann, D.H.7    Herschman, H.R.8    Clarke, S.9    Newsham, I.F.10
  • 48
    • 14644444235 scopus 로고    scopus 로고
    • The tumor suppressor dal-1/4.1b modulates protein arginine n-methyltransferase 5 activity in a substrate-specific manner
    • Jiang, W., Roemer, M. E. and Newsham, I. F. (2005) The tumor suppressor DAL-1/4.1B modulates protein arginine N-methyltransferase 5 activity in a substrate-specific manner. Biochem. Biophys. Res. Commun. 329, 522-530
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 522-530
    • Jiang, W.1    Roemer, M.E.2    Newsham, I.F.3
  • 49
    • 43049084803 scopus 로고    scopus 로고
    • The histone-binding protein copr5 is required for nuclear functions of the protein arginine methyltransferase prmt5
    • Lacroix, M., El Messaoudi, S., Rodier, G., Cam, A. L., Sardet, C. and Fabbrizio, E. (2008) The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep. 9, 452-458
    • (2008) EMBO Rep. , vol.9 , pp. 452-458
    • Lacroix, M.1    El Messaoudi, S.2    Rodier, G.3    Cam, A.L.4    Sardet, C.5    Fabbrizio, E.6
  • 50
    • 25444455856 scopus 로고    scopus 로고
    • Dynamic combinatorial networks in nuclear receptor-mediated transcription
    • Rochette-Egly, C. (2005) Dynamic combinatorial networks in nuclear receptor-mediated transcription. J. Biol. Chem. 280, 32565-32568
    • (2005) J. Biol. Chem. , vol.280 , pp. 32565-32568
    • Rochette-Egly, C.1
  • 51
    • 14544280757 scopus 로고    scopus 로고
    • Transcriptional regulation and the role of diverse coactivators in animal cells
    • Roeder, R. G. (2005) Transcriptional regulation and the role of diverse coactivators in animal cells. FEBS Lett. 579, 909-915
    • (2005) FEBS Lett. , vol.579 , pp. 909-915
    • Roeder, R.G.1
  • 52
    • 17044392996 scopus 로고    scopus 로고
    • Role of protein methylation in regulation of transcription
    • Lee, D. Y., Teyssier, C., Strahl, B. D. and Stallcup, M. R. (2008) Role of protein methylation in regulation of transcription. Endocrinol. Rev. 26, 147-170
    • (2008) Endocrinol. Rev. , vol.26 , pp. 147-170
    • Lee, D.Y.1    Teyssier, C.2    Strahl, B.D.3    Stallcup, M.R.4
  • 53
    • 0035962649 scopus 로고    scopus 로고
    • Role of protein methylation in chromatin remodeling and transcriptional regulation
    • Stallcup, M. R. (2001) Role of protein methylation in chromatin remodeling and transcriptional regulation. Oncogene 20, 3014-3020
    • (2001) Oncogene , vol.20 , pp. 3014-3020
    • Stallcup, M.R.1
  • 55
    • 6344222803 scopus 로고    scopus 로고
    • Human swi/snf-associated prmt5 methylates histone h3 arginine 8 and negatively regulates expression of st7 and nm23 tumor suppressor genes
    • Pal, S., Vishwanath, S. N., Erdjument-Bromage, H., Tempst, P. and Sif, S. (2004) Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol. Cell. Biol. 24, 9630-9645
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9630-9645
    • Pal, S.1    Vishwanath, S.N.2    Erdjument-Bromage, H.3    Tempst, P.4    Sif, S.5
  • 56
    • 8644240108 scopus 로고    scopus 로고
    • Recruitment of histone modifications by usf proteins at a vertebrate barrier element
    • West, A. G., Huang, S., Gaszner, M., Litt, M. D. and Felsenfeld, G. (2004) Recruitment of histone modifications by USF proteins at a vertebrate barrier element. Mol. Cell 16, 453-463
    • (2004) Mol. Cell , vol.16 , pp. 453-463
    • West, A.G.1    Huang, S.2    Gaszner, M.3    Litt, M.D.4    Felsenfeld, G.5
  • 57
    • 36048976921 scopus 로고    scopus 로고
    • Usf1 recruits histone modification complexes and is critical for maintenance of a chromatin barrier
    • Huang, S., Li, X., Yusufzai, T. M., Qiu, Y. and and Felsenfeld, G. (2007) USF1 recruits histone modification complexes and is critical for maintenance of a chromatin barrier. Mol. Cell. Biol. 27, 7991-8002
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7991-8002
    • Huang, S.1    Li, X.2    Yusufzai, T.M.3    Qiu, Y.4    Felsenfeld, G.5
  • 58
    • 0034713375 scopus 로고    scopus 로고
    • Methylation of a ctcf-dependent boundary controls imprinted expression of the igf2 gene
    • Bell, A. C. and Felsenfeld, G. (2000) Methylation of a CTCF-dependent boundary controls imprinted expression of the Igf2 gene. Nature 405, 482-485
    • (2000) Nature , vol.405 , pp. 482-485
    • Bell, A.C.1    Felsenfeld, G.2
  • 59
    • 0034713275 scopus 로고    scopus 로고
    • Ctcf mediates methylation-sensitive enhancer-blocking activity at the h19/igf2 locus
    • Hank, A. T., Schoenherr, C. J., Katz, D. J., Ingram, R. S., Levorse, J. M. and Tilghman, S. M. (2000) CTCF mediates methylation-sensitive enhancer-blocking activity at the H19/Igf2 locus. Nature 405, 486-489
    • (2000) Nature , vol.405 , pp. 486-489
    • Hank, A.T.1    Schoenherr, C.J.2    Katz, D.J.3    Ingram, R.S.4    Levorse, J.M.5    Tilghman, S.M.6
  • 60
    • 35848951163 scopus 로고    scopus 로고
    • Covalent modifications of histones during development and disease pathogenesis
    • Bhaumik, S,R. and Shilatifard, A. (2007) Covalent modifications of histones during development and disease pathogenesis. Nat. Struct. Mol. Biol. 14, 1008-1016
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1008-1016
    • Bhaumik, S.R.1    Shilatifard, A.2
  • 61
    • 20744442981 scopus 로고    scopus 로고
    • Arginine methylation provides epigenetic transcription memory for retinoid-induced differentiation in myeloid cells
    • Balint, B. L., Szanto, A., Madi, A., Bauer, U. M., Gabor, P., Benko, S., Pusḱas, L. G., Davies, P. J. and Nagy, L. (2005) Arginine methylation provides epigenetic transcription memory for retinoid-induced differentiation in myeloid cells. Mol. Cell. Biol. 25, 5648-5663
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5648-5663
    • Balint, B.L.1    Szanto, A.2    Madi, A.3    Bauer, U.M.4    Gabor, P.5    Benko, S.6    Pusḱas, L.G.7    Davies, P.J.8    Nagy, L.9
  • 64
    • 30944469849 scopus 로고    scopus 로고
    • Estrogen carcinogenesis in breast cancer
    • Yager, J. D. and Davidson, N. E. (2006) Estrogen carcinogenesis in breast cancer. N. Engl. J. Med. 354, 270-282
    • (2006) N. Engl. J. Med. , vol.354 , pp. 270-282
    • Yager, J.D.1    Davidson, N.E.2
  • 66
    • 33748359520 scopus 로고    scopus 로고
    • Involvement of arginine methyltransferase carm1 in androgen receptor function and prostate cancer viability
    • Majumder, S., Liu, Y., Ford, O. H. III, Mohler, J. L. and Whang, Y. E. (2006) Involvement of arginine methyltransferase CARM1 in androgen receptor function and prostate cancer viability. Prostate 66, 1292-1301
    • (2006) Prostate , vol.66 , pp. 1292-1301
    • Majumder, S.1    Liu, Y.2    Ford III, O.H.3    Mohler, J.L.4    Whang, Y.E.5
  • 67
    • 0142123234 scopus 로고    scopus 로고
    • Msin3a/histone deacetylase 2- and prmt5-containing brg1 complex is involved in transcriptional repression of the myc target gene cad
    • Pal, S., Yun, R., Datta, A., Lacomis, L., Erdjument-Bromage, H., Kumar, J., Tempst, P. and Sif, S. (2003) mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad. Mol. Cell. Biol. 23, 7475-7487
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7475-7487
    • Pal, S.1    Yun, R.2    Datta, A.3    Lacomis, L.4    Erdjument-Bromage, H.5    Kumar, J.6    Tempst, P.7    Sif, S.8


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