메뉴 건너뛰기




Volumn 45, Issue 8, 2012, Pages 470-475

The role of protein arginine-methyltransferase 1 in gliomagenesis

Author keywords

Glioma; H4R3diMe; Posttranslational modification; PRMT1; Tumorgenesis

Indexed keywords

HISTONE; PRMT1 PROTEIN, HUMAN; PROTEIN ARGININE METHYLTRANSFERASE; REPRESSOR PROTEIN; SMALL INTERFERING RNA;

EID: 84866616994     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2012.45.8.022     Document Type: Article
Times cited : (38)

References (22)
  • 1
    • 66149108467 scopus 로고    scopus 로고
    • Human protein arginine methyltransferases in vivo-distinct properties of eight canonical members of the PRMT family
    • Herrmann, F., Pably, P., Eckerich, C., Bedford, M. T. and Fackelmayer, F. O. (2009) Human protein arginine methyltransferases in vivo-distinct properties of eight canonical members of the PRMT family. J. Cell. Sci. 122, 667-677.
    • (2009) J. Cell. Sci. , vol.122 , pp. 667-677
    • Herrmann, F.1    Pably, P.2    Eckerich, C.3    Bedford, M.T.4    Fackelmayer, F.O.5
  • 2
    • 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.T.1    Richard, S.2
  • 3
    • 64749109224 scopus 로고    scopus 로고
    • Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation
    • Lee, Y. H. and Stallcup, M. R. (2009) Minireview: protein arginine methylation of nonhistone proteins in transcriptional regulation. Mol. Endocrinol. 23, 425-433.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 425-433
    • Lee, Y.H.1    Stallcup, M.R.2
  • 4
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: who, what, and why
    • Bedford, M. T. and Clarke, S. G. (2009) Protein arginine methylation in mammals: who, what, and why. Mol. Cell. 33, 1-13.
    • (2009) Mol. Cell. , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 6
    • 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. (2007) Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential. Pharmacol. Ther. 113, 50-87.
    • (2007) 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
  • 7
    • 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, H. 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, H.E.5
  • 8
    • 66349133369 scopus 로고    scopus 로고
    • A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation
    • Yu, Z., Chen, T., Hebert, J., Li, E. and Richard, S. (2009) A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation. Mol. Cell Biol. 29, 2982-2996.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 2982-2996
    • Yu, Z.1    Chen, T.2    Hebert, J.3    Li, E.4    Richard, S.5
  • 9
    • 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
  • 11
    • 4744344066 scopus 로고    scopus 로고
    • Epigenetics and cancer
    • Lund, A. H. and van Lohuizen, M. (2004) Epigenetics and cancer. Genes Dev. 18, 2315-2335.
    • (2004) Genes Dev , vol.18 , pp. 2315-2335
    • Lund, A.H.1    Van Lohuizen, M.2
  • 12
    • 70350084477 scopus 로고    scopus 로고
    • The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation
    • Nicholson, T. B., Chen, T. and Richard, S. (2009) The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation. Pharmacol. Res. 60, 466-474.
    • (2009) Pharmacol. Res. , vol.60 , pp. 466-474
    • Nicholson, T.B.1    Chen, T.2    Richard, S.3
  • 14
    • 84859598555 scopus 로고    scopus 로고
    • Arginine methylation-dependent regulation of ASK1 signaling by PRMT1
    • Cho, J. H., Lee, M. K., Yoon, K. W., Lee, J., Cho, S. G. and Choi, E. J. (2011) Arginine methylation-dependent regulation of ASK1 signaling by PRMT1. Cell Death. Differ. 19, 859-870.
    • (2011) Cell Death. Differ. , vol.19 , pp. 859-870
    • Cho, J.H.1    Lee, M.K.2    Yoon, K.W.3    Lee, J.4    Cho, S.G.5    Choi, E.J.6
  • 15
    • 21744457108 scopus 로고    scopus 로고
    • Global histone modification patterns predict risk of prostate cancer recurrence
    • Seligson, D. B., Horvath, S., Shi, T., Yu, H., Tze, S., Grunstein, M. and Kurdistani, S. K. (2005) Global histone modification patterns predict risk of prostate cancer recurrence. Nature 435, 1262-1266.
    • (2005) Nature , vol.435 , pp. 1262-1266
    • Seligson, D.B.1    Horvath, S.2    Shi, T.3    Yu, H.4    Tze, S.5    Grunstein, M.6    Kurdistani, S.K.7
  • 18
    • 67649968054 scopus 로고    scopus 로고
    • The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans
    • Wolf, S. S. (2009) The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans. Cell Mol. Life Sci. 66, 2109-2121.
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 2109-2121
    • Wolf, S.S.1
  • 21
    • 77950390899 scopus 로고    scopus 로고
    • H4R3 methylation facilitates -globin transcription by regulating histone acetyltransferase binding and H3 acetylation
    • Li, X., Hu, X., Patel, B., Zhou, Z., Liang, S., Ybarra, R., Qiu, Y., Felsenfeld, G., Bungert, J. and Huang, S. (2010) H4R3 methylation facilitates -globin transcription by regulating histone acetyltransferase binding and H3 acetylation. Blood 115, 2028-2037.
    • (2010) Blood , vol.115 , pp. 2028-2037
    • Li, X.1    Hu, X.2    Patel, B.3    Zhou, Z.4    Liang, S.5    Ybarra, R.6    Qiu, Y.7    Felsenfeld, G.8    Bungert, J.9    Huang, S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.