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Volumn 35, Issue 2, 2014, Pages 161-174

EZH2: Biology, disease, and structure-based drug discovery

Author keywords

[No Author keywords available]

Indexed keywords

DNA METHYLTRANSFERASE; HISTONE DEACETYLASE; POLYCOMB REPRESSIVE COMPLEX 2; TRANSCRIPTION FACTOR EZH2;

EID: 84893521949     PISSN: 16714083     EISSN: 17457254     Source Type: Journal    
DOI: 10.1038/aps.2013.161     Document Type: Review
Times cited : (175)

References (76)
  • 2
    • 69949148388 scopus 로고    scopus 로고
    • Protein methyltransferases as a target class for drug discovery
    • Copeland RA, Solomon ME, Richon VM. Protein methyltransferases as a target class for drug discovery. Nat Rev Drug Discov 2009; 8: 724-32.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 724-732
    • Copeland, R.A.1    Solomon, M.E.2    Richon, V.M.3
  • 3
    • 84864876023 scopus 로고    scopus 로고
    • Inner workings and regulatory inputs that control Polycomb repressive complex 2
    • O'Meara MM, Simon JA. Inner workings and regulatory inputs that control Polycomb repressive complex 2. Chromosoma 2012; 121: 221-34.
    • (2012) Chromosoma , vol.121 , pp. 221-234
    • O'Meara, M.M.1    Simon, J.A.2
  • 4
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 2002; 298: 1039-43.
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 5
    • 55949136562 scopus 로고    scopus 로고
    • Roles of the EZH2 histone methyltransferase in cancer epigenetics
    • Simon JA, Lange CA. Roles of the EZH2 histone methyltransferase in cancer epigenetics. Mutat Res 2008; 647: 21-9.
    • (2008) Mutat Res , vol.647 , pp. 21-29
    • Simon, J.A.1    Lange, C.A.2
  • 6
    • 20144363347 scopus 로고    scopus 로고
    • The murine polycomb group protein Eed is required for global histone H3 lysine-27 methylation
    • Montgomery ND, Yee D, Chen A, Kalantry S, Chamberlain SJ, Otte AP, et al. The murine polycomb group protein Eed is required for global histone H3 lysine-27 methylation. Curr Biol 2005; 15: 942-7.
    • (2005) Curr Biol , vol.15 , pp. 942-947
    • Montgomery, N.D.1    Yee, D.2    Chen, A.3    Kalantry, S.4    Chamberlain, S.J.5    Otte, A.P.6
  • 7
    • 36248930485 scopus 로고    scopus 로고
    • Molecular and functional mapping of EED motifs required for PRC2-dependent histone methylation
    • Montgomery ND, Yee D, Montgomery SA, Magnuson T. Molecular and functional mapping of EED motifs required for PRC2-dependent histone methylation. J Mol Biol 2007; 374: 1145-57.
    • (2007) J Mol Biol , vol.374 , pp. 1145-1157
    • Montgomery, N.D.1    Yee, D.2    Montgomery, S.A.3    Magnuson, T.4
  • 8
    • 8144230178 scopus 로고    scopus 로고
    • Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity
    • Pasini D, Bracken AP, Jensen MR, Lazzerini Denchi E, Helin K. Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity. EMBO J 2004; 23: 4061-71.
    • (2004) EMBO J , vol.23 , pp. 4061-4071
    • Pasini, D.1    Bracken, A.P.2    Jensen, M.R.3    Lazzerini Denchi, E.4    Helin, K.5
  • 9
    • 36349017912 scopus 로고    scopus 로고
    • A polycomb repression signature in metastatic prostate cancer predicts cancer outcome
    • Yu J, Yu J, Rhodes DR, Tomlins SA, Cao X, Chen G, et al. A polycomb repression signature in metastatic prostate cancer predicts cancer outcome. Cancer Res 2007; 67: 10657-63.
    • (2007) Cancer Res , vol.67 , pp. 10657-10663
    • Yu, J.1    Yu, J.2    Rhodes, D.R.3    Tomlins, S.A.4    Cao, X.5    Chen, G.6
  • 12
    • 32844459336 scopus 로고    scopus 로고
    • The Polycomb group protein EZH2 directly controls DNA methylation
    • Vire E, Brenner C, Deplus R, Blanchon L, Fraga M, Didelot C, et al. The Polycomb group protein EZH2 directly controls DNA methylation. Nature 2006; 439: 871-4.
    • (2006) Nature , vol.439 , pp. 871-874
    • Vire, E.1    Brenner, C.2    Deplus, R.3    Blanchon, L.4    Fraga, M.5    Didelot, C.6
  • 13
    • 0035141264 scopus 로고    scopus 로고
    • The drosophila polycomb group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3
    • Tie F, Furuyama T, Prasad-Sinha J, Jane E, Harte PJ. The drosophila polycomb group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3. Development 2001; 128: 275-86.
    • (2001) Development , vol.128 , pp. 275-286
    • Tie, F.1    Furuyama, T.2    Prasad-Sinha, J.3    Jane, E.4    Harte, P.J.5
  • 14
    • 0032751323 scopus 로고    scopus 로고
    • Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation
    • van der Vlag J, Otte AP. Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation. Nat Genet 1999; 23: 474-8.
    • (1999) Nat Genet , vol.23 , pp. 474-478
    • Van Der Vlag, J.1    Otte, A.P.2
  • 15
    • 75749124332 scopus 로고    scopus 로고
    • Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin
    • Morin RD, Johnson NA, Severson TM, Mungall AJ, An J, Goya R, et al. Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin. Nat Genet 2010; 42: 181-5.
    • (2010) Nat Genet , vol.42 , pp. 181-185
    • Morin, R.D.1    Johnson, N.A.2    Severson, T.M.3    Mungall, A.J.4    An, J.5    Goya, R.6
  • 16
    • 78650454078 scopus 로고    scopus 로고
    • Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas
    • Sneeringer CJ, Scott MP, Kuntz KW, Knutson SK, Pollock RM, Richon VM, et al. Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas. Proc Natl Acad Sci U S A 2010; 107: 20980-5.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20980-20985
    • Sneeringer, C.J.1    Scott, M.P.2    Kuntz, K.W.3    Knutson, S.K.4    Pollock, R.M.5    Richon, V.M.6
  • 17
    • 79952167230 scopus 로고    scopus 로고
    • Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation
    • Yap DB, Chu J, Berg T, Schapira M, Cheng SW, Moradian A, et al. Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation. Blood 2011; 117: 2451-9.
    • (2011) Blood , vol.117 , pp. 2451-2459
    • Yap, D.B.1    Chu, J.2    Berg, T.3    Schapira, M.4    Cheng, S.W.5    Moradian, A.6
  • 18
    • 84863165348 scopus 로고    scopus 로고
    • Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27)
    • McCabe MT, Graves AP, Ganji G, Diaz E, Halsey WS, Jiang Y, et al. Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27). Proc Natl Acad Sci U S A 2012; 109: 2989-94.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 2989-2994
    • McCabe, M.T.1    Graves, A.P.2    Ganji, G.3    Diaz, E.4    Halsey, W.S.5    Jiang, Y.6
  • 19
    • 80052222327 scopus 로고    scopus 로고
    • Context-specific regulation of NF-kappaB target gene expression by EZH2 in breast cancers
    • Lee ST, Li Z, Wu Z, Aau M, Guan P, Karuturi RK, et al. Context-specific regulation of NF-kappaB target gene expression by EZH2 in breast cancers. Mol Cell 2011; 43: 798-810.
    • (2011) Mol Cell , vol.43 , pp. 798-810
    • Lee, S.T.1    Li, Z.2    Wu, Z.3    Aau, M.4    Guan, P.5    Karuturi, R.K.6
  • 20
    • 34447544566 scopus 로고    scopus 로고
    • Integration of estrogen and Wnt signaling circuits by the polycomb group protein EZH2 in breast cancer cells
    • Shi B, Liang J, Yang X, Wang Y, Zhao Y, Wu H, et al. Integration of estrogen and Wnt signaling circuits by the polycomb group protein EZH2 in breast cancer cells. Mol Cell Biol 2007; 27: 5105-19.
    • (2007) Mol Cell Biol , vol.27 , pp. 5105-5119
    • Shi, B.1    Liang, J.2    Yang, X.3    Wang, Y.4    Zhao, Y.5    Wu, H.6
  • 21
    • 84871052080 scopus 로고    scopus 로고
    • EZH2 oncogenic activity in castration-resistant prostate cancer cells is Polycomb-independent
    • Xu K, Wu ZJ, Groner AC, He HH, Cai C, Lis RT, et al. EZH2 oncogenic activity in castration-resistant prostate cancer cells is Polycomb-independent. Science 2012; 338: 1465-9.
    • (2012) Science , vol.338 , pp. 1465-1469
    • Xu, K.1    Wu, Z.J.2    Groner, A.C.3    He, H.H.4    Cai, C.5    Lis, R.T.6
  • 22
    • 84877330098 scopus 로고    scopus 로고
    • Multifaceted role of EZH2 in breast and prostate tumorigenesis: Epigenetics and beyond
    • Deb G, Thakur VS, Gupta S. Multifaceted role of EZH2 in breast and prostate tumorigenesis: epigenetics and beyond. Epigenetics 2013; 8: 464-76.
    • (2013) Epigenetics , vol.8 , pp. 464-476
    • Deb, G.1    Thakur, V.S.2    Gupta, S.3
  • 23
    • 78650062951 scopus 로고    scopus 로고
    • EZH2-mediated epigenetic silencing in germinal center B cells contributes to proliferation and lymphomagenesis
    • Velichutina I, Shaknovich R, Geng H, Johnson NA, Gascoyne RD, Melnick AM, et al. EZH2-mediated epigenetic silencing in germinal center B cells contributes to proliferation and lymphomagenesis. Blood 2010; 116: 5247-55.
    • (2010) Blood , vol.116 , pp. 5247-5255
    • Velichutina, I.1    Shaknovich, R.2    Geng, H.3    Johnson, N.A.4    Gascoyne, R.D.5    Melnick, A.M.6
  • 24
    • 78049500122 scopus 로고    scopus 로고
    • Androgens suppress EZH2 expression via retinoblastoma (RB) and p130-dependent pathways: A potential mechanism of androgen-refractory progression of prostate cancer
    • Bohrer LR, Chen S, Hallstrom TC, Huang H. Androgens suppress EZH2 expression via retinoblastoma (RB) and p130-dependent pathways: a potential mechanism of androgen-refractory progression of prostate cancer. Endocrinology 2010; 151: 5136-45.
    • (2010) Endocrinology , vol.151 , pp. 5136-5145
    • Bohrer, L.R.1    Chen, S.2    Hallstrom, T.C.3    Huang, H.4
  • 26
    • 33644822360 scopus 로고    scopus 로고
    • EZH2 expression is associated with high proliferation rate and aggressive tumor subgroups in cutaneous melanoma and cancers of the endometrium, prostate, and breast
    • Bachmann IM, Halvorsen OJ, Collett K, Stefansson IM, Straume O, Haukaas SA, et al. EZH2 expression is associated with high proliferation rate and aggressive tumor subgroups in cutaneous melanoma and cancers of the endometrium, prostate, and breast. J Clin Oncol 2006; 24: 268-73.
    • (2006) J Clin Oncol , vol.24 , pp. 268-273
    • Bachmann, I.M.1    Halvorsen, O.J.2    Collett, K.3    Stefansson, I.M.4    Straume, O.5    Haukaas, S.A.6
  • 27
    • 0142105414 scopus 로고    scopus 로고
    • EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer
    • Bracken AP, Pasini D, Capra M, Prosperini E, Colli E, Helin K. EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer. EMBO J 2003; 22: 5323-35.
    • (2003) EMBO J , vol.22 , pp. 5323-5335
    • Bracken, A.P.1    Pasini, D.2    Capra, M.3    Prosperini, E.4    Colli, E.5    Helin, K.6
  • 28
    • 79952766783 scopus 로고    scopus 로고
    • Histone methyltransferase EZH2 induces Akt-dependent genomic instability and BRCA1 inhibition in breast cancer
    • Gonzalez ME, DuPrie ML, Krueger H, Merajver SD, Ventura AC, Toy KA, et al. Histone methyltransferase EZH2 induces Akt-dependent genomic instability and BRCA1 inhibition in breast cancer. Cancer Res 2011; 71: 2360-70.
    • (2011) Cancer Res , vol.71 , pp. 2360-2370
    • Gonzalez, M.E.1    DuPrie, M.L.2    Krueger, H.3    Merajver, S.D.4    Ventura, A.C.5    Toy, K.A.6
  • 30
    • 0141816752 scopus 로고    scopus 로고
    • EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells
    • Kleer CG, Cao Q, Varambally S, Shen R, Ota I, Tomlins SA, et al. EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells. Proc Natl Acad Sci U S A 2003; 100: 11606-11.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11606-11611
    • Kleer, C.G.1    Cao, Q.2    Varambally, S.3    Shen, R.4    Ota, I.5    Tomlins, S.A.6
  • 32
    • 0035877978 scopus 로고    scopus 로고
    • Coexpression of BMI-1 and EZH2 polycomb-group proteins is associated with cycling cells and degree of malignancy in B-cell non-Hodgkin lymphoma
    • van Kemenade FJ, Raaphorst FM, Blokzijl T, Fieret E, Hamer KM, Satijn DP, et al. Coexpression of BMI-1 and EZH2 polycomb-group proteins is associated with cycling cells and degree of malignancy in B-cell non-Hodgkin lymphoma. Blood 2001; 97: 3896-901.
    • (2001) Blood , vol.97 , pp. 3896-3901
    • Van Kemenade, F.J.1    Raaphorst, F.M.2    Blokzijl, T.3    Fieret, E.4    Hamer, K.M.5    Satijn, D.P.6
  • 33
    • 84890430327 scopus 로고    scopus 로고
    • Disruption of the MYC-miRNA-EZH2 loop to suppress aggressive B-cell lymphoma survival and clonogenicity
    • Zhao X, Lwin T, Zhang X, Huang A, Wang J, Marquez VE, et al. Disruption of the MYC-miRNA-EZH2 loop to suppress aggressive B-cell lymphoma survival and clonogenicity. Leukemia 2013; 27: 2341-50.
    • (2013) Leukemia , vol.27 , pp. 2341-2350
    • Zhao, X.1    Lwin, T.2    Zhang, X.3    Huang, A.4    Wang, J.5    Marquez, V.E.6
  • 34
    • 84880893647 scopus 로고    scopus 로고
    • EZH2 promotes E2F-Driven SCLC tumorigenesis through modulation of apoptosis and cell-cycle regulation
    • Hubaux R, Thu KL, Coe BP, Macaulay C, Lam S, Lam WL. EZH2 promotes E2F-Driven SCLC tumorigenesis through modulation of apoptosis and cell-cycle regulation. J Thorac Oncol 2013; 8: 1102-6.
    • (2013) J Thorac Oncol , vol.8 , pp. 1102-1106
    • Hubaux, R.1    Thu, K.L.2    Coe, B.P.3    Macaulay, C.4    Lam, S.5    Lam, W.L.6
  • 35
    • 84863041971 scopus 로고    scopus 로고
    • Cooperation between polycomb and androgen receptor during oncogenic transformation
    • Zhao JC, Yu J, Runkle C, Wu L, Hu M, Wu D, et al. Cooperation between polycomb and androgen receptor during oncogenic transformation. Genome Res 2012; 22: 322-31.
    • (2012) Genome Res , vol.22 , pp. 322-331
    • Zhao, J.C.1    Yu, J.2    Runkle, C.3    Wu, L.4    Hu, M.5    Wu, D.6
  • 38
    • 70349952171 scopus 로고    scopus 로고
    • Role of the polycomb protein EED in the propagation of repressive histone marks
    • Margueron R, Justin N, Ohno K, Sharpe ML, Son J, Drury WJ 3rd, et al. Role of the polycomb protein EED in the propagation of repressive histone marks. Nature 2009; 461: 762-7.
    • (2009) Nature , vol.461 , pp. 762-767
    • Margueron, R.1    Justin, N.2    Ohno, K.3    Sharpe, M.L.4    Son, J.5    Drury, W.J.6
  • 39
    • 78650613168 scopus 로고    scopus 로고
    • Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2)
    • Xu C, Bian C, Yang W, Galka M, Ouyang H, Chen C, et al. Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proc Natl Acad Sci U S A 2010; 107: 19266-71.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19266-19271
    • Xu, C.1    Bian, C.2    Yang, W.3    Galka, M.4    Ouyang, H.5    Chen, C.6
  • 40
    • 80053935847 scopus 로고    scopus 로고
    • Polycomb protein EZH2 regulates cancer cell fate decision in response to DNA damage
    • Wu Z, Lee ST, Qiao Y, Li Z, Lee PL, Lee YJ, et al. Polycomb protein EZH2 regulates cancer cell fate decision in response to DNA damage. Cell Death Differ 2011; 18: 1771-9.
    • (2011) Cell Death Differ , vol.18 , pp. 1771-1779
    • Wu, Z.1    Lee, S.T.2    Qiao, Y.3    Li, Z.4    Lee, P.L.5    Lee, Y.J.6
  • 41
    • 33947191081 scopus 로고    scopus 로고
    • The N terminus of Drosophila ESC binds directly to histone H3 and is required for E(Z)- dependent trimethylation of H3 lysine 27
    • Tie F, Stratton CA, Kurzhals RL, Harte PJ. The N terminus of Drosophila ESC binds directly to histone H3 and is required for E(Z)- dependent trimethylation of H3 lysine 27. Mol Cell Biol 2007; 27: 2014-26.
    • (2007) Mol Cell Biol , vol.27 , pp. 2014-2026
    • Tie, F.1    Stratton, C.A.2    Kurzhals, R.L.3    Harte, P.J.4
  • 42
    • 0031719427 scopus 로고    scopus 로고
    • The Drosophila Polycomb group proteins ESC and E(Z) bind directly to each other and co-localize at multiple chromosomal sites
    • Tie F, Furuyama T, Harte PJ. The Drosophila Polycomb group proteins ESC and E(Z) bind directly to each other and co-localize at multiple chromosomal sites. Development 1998; 125: 3483-96.
    • (1998) Development , vol.125 , pp. 3483-3496
    • Tie, F.1    Furuyama, T.2    Harte, P.J.3
  • 43
    • 23344450547 scopus 로고    scopus 로고
    • Subunit contributions to histone methyltransferase activities of fly and worm polycomb group complexes
    • Ketel CS, Andersen EF, Vargas ML, Suh J, Strome S, Simon JA. Subunit contributions to histone methyltransferase activities of fly and worm polycomb group complexes. Mol Cell Biol 2005; 25: 6857-68.
    • (2005) Mol Cell Biol , vol.25 , pp. 6857-6868
    • Ketel, C.S.1    Andersen, E.F.2    Vargas, M.L.3    Suh, J.4    Strome, S.5    Simon, J.A.6
  • 44
    • 1942502862 scopus 로고    scopus 로고
    • Dif ferent EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3
    • Kuzmichev A, Jenuwein T, Tempst P, Reinberg D. Dif ferent EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3. Mol Cell 2004; 14: 183-93.
    • (2004) Mol Cell , vol.14 , pp. 183-193
    • Kuzmichev, A.1    Jenuwein, T.2    Tempst, P.3    Reinberg, D.4
  • 45
    • 0347683447 scopus 로고    scopus 로고
    • Polycomb group suppressor of zeste 12 links heterochromatin protein 1alpha and enhancer of zeste 2
    • Yamamoto K, Sonoda M, Inokuchi J, Shirasawa S, Sasazuki T. Polycomb group suppressor of zeste 12 links heterochromatin protein 1alpha and enhancer of zeste 2. J Biol Chem 2004; 279: 401-6.
    • (2004) J Biol Chem , vol.279 , pp. 401-406
    • Yamamoto, K.1    Sonoda, M.2    Inokuchi, J.3    Shirasawa, S.4    Sasazuki, T.5
  • 47
    • 3042801308 scopus 로고    scopus 로고
    • SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex
    • Cao R, Zhang Y. SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol Cell 2004; 15: 57-67.
    • (2004) Mol Cell , vol.15 , pp. 57-67
    • Cao, R.1    Zhang, Y.2
  • 48
    • 17644410781 scopus 로고    scopus 로고
    • Nucleosome binding and histone methyltransferase activity of Drosophila PRC2
    • Nekrasov M, Wild B, Muller J. Nucleosome binding and histone methyltransferase activity of Drosophila PRC2. EMBO Rep 2005; 6: 348-53.
    • (2005) EMBO Rep , vol.6 , pp. 348-353
    • Nekrasov, M.1    Wild, B.2    Muller, J.3
  • 50
    • 78651380341 scopus 로고    scopus 로고
    • Insights into association of the NuRD complex with FOG-1 from the crystal structure of an RbAp48.FOG-1 complex
    • Lejon S, Thong SY, Murthy A, AlQarni S, Murzina NV, Blobel GA, et al. Insights into association of the NuRD complex with FOG-1 from the crystal structure of an RbAp48.FOG-1 complex. J Biol Chem 2011; 286: 1196-203.
    • (2011) J Biol Chem , vol.286 , pp. 1196-1203
    • Lejon, S.1    Thong, S.Y.2    Murthy, A.3    AlQarni, S.4    Murzina, N.V.5    Blobel, G.A.6
  • 51
    • 0030272047 scopus 로고    scopus 로고
    • Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
    • Verreault A, Kaufman PD, Kobayashi R, Stillman B. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 1996; 87: 95-104.
    • (1996) Cell , vol.87 , pp. 95-104
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 52
    • 0036829968 scopus 로고    scopus 로고
    • Structure of the SET domain histone lysine methyltransferase Clr4
    • Min J, Zhang X, Cheng X, Grewal SI, Xu RM. Structure of the SET domain histone lysine methyltransferase Clr4. Nat Struct Biol 2002; 9: 828-32.
    • (2002) Nat Struct Biol , vol.9 , pp. 828-832
    • Min, J.1    Zhang, X.2    Cheng, X.3    Grewal, S.I.4    Xu, R.M.5
  • 53
    • 0037020217 scopus 로고    scopus 로고
    • Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase
    • Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, et al. Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell 2002; 111: 117-27.
    • (2002) Cell , vol.111 , pp. 117-127
    • Zhang, X.1    Tamaru, H.2    Khan, S.I.3    Horton, J.R.4    Keefe, L.J.5    Selker, E.U.6
  • 54
    • 0037421847 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the human histone methyltransferase SET7/9
    • Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, et al. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature 2003; 421: 652-6.
    • (2003) Nature , vol.421 , pp. 652-656
    • Xiao, B.1    Jing, C.2    Wilson, J.R.3    Walker, P.A.4    Vasisht, N.5    Kelly, G.6
  • 57
    • 0042164227 scopus 로고    scopus 로고
    • Structural basis for the product specificity of histone lysine methyltransferases
    • Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, et al. Structural basis for the product specificity of histone lysine methyltransferases. Mol Cell 2003; 12: 177-85.
    • (2003) Mol Cell , vol.12 , pp. 177-185
    • Zhang, X.1    Yang, Z.2    Khan, S.I.3    Horton, J.R.4    Tamaru, H.5    Selker, E.U.6
  • 58
    • 44449162039 scopus 로고    scopus 로고
    • Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases
    • Zhang X, Bruice TC. Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases. Proc Natl Acad Sci U S A 2008; 105: 5728-32.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5728-5732
    • Zhang, X.1    Bruice, T.C.2
  • 59
    • 33646203168 scopus 로고    scopus 로고
    • Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase
    • Qian C, Wang X, Manzur K, Sachchidanand, Farooq A, Zeng L, et al. Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase. J Mol Biol 2006; 359: 86-96.
    • (2006) J Mol Biol , vol.359 , pp. 86-96
    • Qian, C.1    Wang, X.2    Manzur, K.3    Sachchidanand4    Farooq, A.5    Zeng, L.6
  • 60
    • 14044256546 scopus 로고    scopus 로고
    • In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases
    • Collins RE, Tachibana M, Tamaru H, Smith KM, Jia D, Zhang X, et al. In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases. J Biol Chem 2005; 280: 5563-70.
    • (2005) J Biol Chem , vol.280 , pp. 5563-5570
    • Collins, R.E.1    Tachibana, M.2    Tamaru, H.3    Smith, K.M.4    Jia, D.5    Zhang, X.6
  • 61
    • 59349115177 scopus 로고    scopus 로고
    • Chemical mechanisms of histone lysine and arginine modifications
    • Smith BC, Denu JM. Chemical mechanisms of histone lysine and arginine modifications. Biochim Biophys Acta 2009; 1789: 45-57.
    • (2009) Biochim Biophys Acta , vol.1789 , pp. 45-57
    • Smith, B.C.1    Denu, J.M.2
  • 62
    • 20544461679 scopus 로고    scopus 로고
    • Structural and sequence motifs of protein (histone) methylation enzymes
    • Cheng X, Collins RE, Zhang X. Structural and sequence motifs of protein (histone) methylation enzymes. Annu Rev Biophys Biomol Struct 2005; 34: 267-94.
    • (2005) Annu Rev Biophys Biomol Struct , vol.34 , pp. 267-294
    • Cheng, X.1    Collins, R.E.2    Zhang, X.3
  • 63
    • 34247625135 scopus 로고    scopus 로고
    • Pharmacologic disruption of polycomb-repressive complex 2-mediated gene repression selectively induces apoptosis in cancer cells
    • Tan J, Yang XJ, Zhuang L, Jiang X, Chen W, Lee PL, et al. Pharmacologic disruption of polycomb-repressive complex 2-mediated gene repression selectively induces apoptosis in cancer cells. Genes Dev 2007; 21: 1050-63.
    • (2007) Genes Dev , vol.21 , pp. 1050-1063
    • Tan, J.1    Yang, X.J.2    Zhuang, L.3    Jiang, X.4    Chen, W.5    Lee, P.L.6
  • 64
    • 73149085280 scopus 로고    scopus 로고
    • Combinatorial pharmacologic approaches target EZH2-mediated gene repression in breast cancer cells
    • Sun F, Chan E, Wu Z, Yang X, Marquez VE, Yu Q. Combinatorial pharmacologic approaches target EZH2-mediated gene repression in breast cancer cells. Mol Cancer Ther 2009; 8: 3191-202.
    • (2009) Mol Cancer Ther , vol.8 , pp. 3191-3202
    • Sun, F.1    Chan, E.2    Wu, Z.3    Yang, X.4    Marquez, V.E.5    Yu, Q.6
  • 65
    • 0034096583 scopus 로고    scopus 로고
    • Treatment of lethal Ebola virus infection in mice with a single dose of an S-adenosyl-L-homocysteine hydrolase inhibitor
    • Bray M, Driscoll J, Huggins JW. Treatment of lethal Ebola virus infection in mice with a single dose of an S-adenosyl-L-homocysteine hydrolase inhibitor. Antiviral Res 2000; 45: 135-47.
    • (2000) Antiviral Res , vol.45 , pp. 135-147
    • Bray, M.1    Driscoll, J.2    Huggins, J.W.3
  • 66
    • 0031934077 scopus 로고    scopus 로고
    • Biological effects of inhibitors of S-adenosylhomocysteine hydrolase
    • Chiang PK. Biological effects of inhibitors of S-adenosylhomocysteine hydrolase. Pharmacol Ther 1998; 77: 115-34.
    • (1998) Pharmacol Ther , vol.77 , pp. 115-134
    • Chiang, P.K.1
  • 67
    • 33745842198 scopus 로고    scopus 로고
    • Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases
    • Couture JF, Hauk G, Thompson MJ, Blackburn GM, Trievel RC. Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases. J Biol Chem 2006; 281: 19280-7.
    • (2006) J Biol Chem , vol.281 , pp. 19280-19287
    • Couture, J.F.1    Hauk, G.2    Thompson, M.J.3    Blackburn, G.M.4    Trievel, R.C.5
  • 69
    • 84879750981 scopus 로고    scopus 로고
    • An orally bioavailable chemical probe of the lysine methyltransferases EZH2 and EZH1
    • Konze KD, Ma A, Li F, Barsyte-Lovejoy D, Parton T, Macnevin CJ, et al. An orally bioavailable chemical probe of the lysine methyltransferases EZH2 and EZH1. ACS Chem Biol 2013; 8: 1324-34.
    • (2013) ACS Chem Biol , vol.8 , pp. 1324-1334
    • Konze, K.D.1    Ma, A.2    Li, F.3    Barsyte-Lovejoy, D.4    Parton, T.5    Macnevin, C.J.6
  • 70
    • 84870573126 scopus 로고    scopus 로고
    • EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations
    • McCabe MT, Ott HM, Ganji G, Korenchuk S, Thompson C, Van Aller GS, et al. EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations. Nature 2012; 492: 108-12.
    • (2012) Nature , vol.492 , pp. 108-112
    • McCabe, M.T.1    Ott, H.M.2    Ganji, G.3    Korenchuk, S.4    Thompson, C.5    Van Aller, G.S.6
  • 71
    • 84871841675 scopus 로고    scopus 로고
    • Selective inhibition of Ezh2 by a small molecule inhibitor blocks tumor cells proliferation
    • Qi W, Chan H, Teng L, Li L, Chuai S, Zhang R, et al. Selective inhibition of Ezh2 by a small molecule inhibitor blocks tumor cells proliferation. Proc Natl Acad Sci U S A 2012; 109: 21360-5.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 21360-21365
    • Qi, W.1    Chan, H.2    Teng, L.3    Li, L.4    Chuai, S.5    Zhang, R.6
  • 73
    • 84879580827 scopus 로고    scopus 로고
    • Convergent evolution of chromatin modification by structurally distinct enzymes: Comparative enzymology of histone H3 Lys27 methylation by human polycomb repressive complex 2 and vSET
    • Swalm BM, Hallenbeck KK, Majer CR, Jin L, Scott MP, Moyer MP, et al. Convergent evolution of chromatin modification by structurally distinct enzymes: comparative enzymology of histone H3 Lys27 methylation by human polycomb repressive complex 2 and vSET. Biochem J 2013; 453: 241-7.
    • (2013) Biochem J , vol.453 , pp. 241-247
    • Swalm, B.M.1    Hallenbeck, K.K.2    Majer, C.R.3    Jin, L.4    Scott, M.P.5    Moyer, M.P.6
  • 74
    • 78649890507 scopus 로고    scopus 로고
    • Dimerization of a viral SET protein endows its function
    • Wei H, Zhou MM. Dimerization of a viral SET protein endows its function. Proc Natl Acad Sci U S A 2010; 107: 18433-8.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18433-18438
    • Wei, H.1    Zhou, M.M.2
  • 75
    • 30644474460 scopus 로고    scopus 로고
    • Identification of a specific inhibitor of the histone methyltransferase SU(VAR) 3-9
    • Greiner D, Bonaldi T, Eskeland R, Roemer E, Imhof A. Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9. Nat Chem Biol 2005; 1: 143-5.
    • (2005) Nat Chem Biol , vol.1 , pp. 143-145
    • Greiner, D.1    Bonaldi, T.2    Eskeland, R.3    Roemer, E.4    Imhof, A.5
  • 76
    • 33846783261 scopus 로고    scopus 로고
    • Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase
    • Kubicek S, O'Sullivan RJ, August EM, Hickey ER, Zhang Q, Teodoro ML, et al. Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase. Mol Cell 2007; 25: 473-81.
    • (2007) Mol Cell , vol.25 , pp. 473-481
    • Kubicek, S.1    O'Sullivan, R.J.2    August, E.M.3    Hickey, E.R.4    Zhang, Q.5    Teodoro, M.L.6


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