组蛋白甲基转移酶 (Chinese Wikipedia)

Analysis of information sources in references of the Wikipedia article "组蛋白甲基转移酶" in Chinese language version.

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14doi.org

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12nih.gov

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doi.org

Wood A. Posttranslational Modifications of Histones by Methylation. Conaway JW, Conaway RC (编). Proteins in eukaryotic transcription. Advances in Protein Chemistry 67. Amsterdam: Elsevier Academic Press. 2004: 201–222. ISBN 0-12-034267-7. doi:10.1016/S0065-3233(04)67008-2.
Trievel RC, Beach BM, Dirk LM, Houtz RL, Hurley JH. Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell. October 2002, 111 (1): 91–103. PMID 12372303. doi:10.1016/S0092-8674(02)01000-0.
Min J, Feng Q, Li Z, Zhang Y, Xu RM. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell. March 2003, 112 (5): 711–23. PMID 12628190. doi:10.1016/S0092-8674(03)00114-4.
Chen D, Ma H, Hong H, Koh SS, Huang SM, Schurter BT, Aswad DW, Stallcup MR. Regulation of transcription by a protein methyltransferase. Science. June 1999, 284 (5423): 2174–7. PMID 10381882. doi:10.1126/science.284.5423.2174.
Gary JD, Lin WJ, Yang MC, Herschman HR, Clarke S. The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. J. Biol. Chem. May 1996, 271 (21): 12585–94. PMID 8647869. doi:10.1074/jbc.271.21.12585.
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. February 2000, 275 (5): 3128–36. PMID 10652296. doi:10.1074/jbc.275.5.3128.
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. February 2000, 275 (5): 3128–36. PMID 10652296. doi:10.1074/jbc.275.5.3128.
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. February 2000, 275 (5): 3128–36. PMID 10652296. doi:10.1074/jbc.275.5.3128.
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. February 2000, 275 (5): 3128–36. PMID 10652296. doi:10.1074/jbc.275.5.3128.
McBride AE, Silver PA. State of the arg: protein methylation at arginine comes of age. Cell. July 2001, 106 (1): 5–8. PMID 11461695. doi:10.1016/S0092-8674(01)00423-8.
Fersht AR, Sperling J. The charge relay system in chymotrypsin and chymotrypsinogen. J. Mol. Biol. February 1973, 74 (2): 137–49. PMID 4689953. doi:10.1016/0022-2836(73)90103-4.
Chen F, Kan H, Castranova V. Methylation of Lysine 9 of Histone H3: Role of Heterochromatin Modulation and Tumorigenesis. Tollefsbol TO (编). Handbook of Epigenetics: The New Molecular and Medical Genetics. Boston: Academic Press. 2010: 149–157. ISBN 0-12-375709-6. doi:10.1016/B978-0-12-375709-8.00010-1.
Espino PS, Drobic B, Dunn KL, Davie JR. Histone modifications as a platform for cancer therapy. J. Cell. Biochem. April 2005, 94 (6): 1088–102. PMID 15723344. doi:10.1002/jcb.20387.
Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M, Yagyu R, Nakamura Y. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat. Cell Biol. August 2004, 6 (8): 731–40. PMID 15235609. doi:10.1038/ncb1151.

nih.gov

ncbi.nlm.nih.gov

Trievel RC, Beach BM, Dirk LM, Houtz RL, Hurley JH. Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell. October 2002, 111 (1): 91–103. PMID 12372303. doi:10.1016/S0092-8674(02)01000-0.
Min J, Feng Q, Li Z, Zhang Y, Xu RM. Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell. March 2003, 112 (5): 711–23. PMID 12628190. doi:10.1016/S0092-8674(03)00114-4.
Chen D, Ma H, Hong H, Koh SS, Huang SM, Schurter BT, Aswad DW, Stallcup MR. Regulation of transcription by a protein methyltransferase. Science. June 1999, 284 (5423): 2174–7. PMID 10381882. doi:10.1126/science.284.5423.2174.
Gary JD, Lin WJ, Yang MC, Herschman HR, Clarke S. The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae. J. Biol. Chem. May 1996, 271 (21): 12585–94. PMID 8647869. doi:10.1074/jbc.271.21.12585.
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. February 2000, 275 (5): 3128–36. PMID 10652296. doi:10.1074/jbc.275.5.3128.
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. February 2000, 275 (5): 3128–36. PMID 10652296. doi:10.1074/jbc.275.5.3128.
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. February 2000, 275 (5): 3128–36. PMID 10652296. doi:10.1074/jbc.275.5.3128.
McBride AE, Weiss VH, Kim HK, Hogle JM, Silver PA. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. J. Biol. Chem. February 2000, 275 (5): 3128–36. PMID 10652296. doi:10.1074/jbc.275.5.3128.
McBride AE, Silver PA. State of the arg: protein methylation at arginine comes of age. Cell. July 2001, 106 (1): 5–8. PMID 11461695. doi:10.1016/S0092-8674(01)00423-8.
Fersht AR, Sperling J. The charge relay system in chymotrypsin and chymotrypsinogen. J. Mol. Biol. February 1973, 74 (2): 137–49. PMID 4689953. doi:10.1016/0022-2836(73)90103-4.
Espino PS, Drobic B, Dunn KL, Davie JR. Histone modifications as a platform for cancer therapy. J. Cell. Biochem. April 2005, 94 (6): 1088–102. PMID 15723344. doi:10.1002/jcb.20387.
Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M, Yagyu R, Nakamura Y. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat. Cell Biol. August 2004, 6 (8): 731–40. PMID 15235609. doi:10.1038/ncb1151.