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Volumn 6, Issue 7, 2011, Pages

Structural and functional profiling of the human histone methyltransferase SMYD3

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE SMYD1; HISTONE METHYLTRANSFERASE SMYD2; HISTONE METHYLTRANSFERASE SMYD3; HISTONE METHYLTRANSFERASE SMYD4; HISTONE METHYLTRANSFERASE SMYD5; UNCLASSIFIED DRUG; ADENOSINE; DRUG DERIVATIVE; HISTONE; HISTONE LYSINE METHYLTRANSFERASE; SINEFUNGIN; SMYD3 PROTEIN, HUMAN;

EID: 79960295875     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0022290     Document Type: Article
Times cited : (92)

References (66)
  • 1
    • 56449131444 scopus 로고    scopus 로고
    • Chromatin meets RNA polymerase II
    • Venters B, Pugh BF, (2007) Chromatin meets RNA polymerase II. Genome Biology 8: 319.
    • (2007) Genome Biology , vol.8 , pp. 319
    • Venters, B.1    Pugh, B.F.2
  • 2
    • 0022540321 scopus 로고
    • CpG-rich islands and the function of DNA methylation
    • Bird AP, (1986) CpG-rich islands and the function of DNA methylation. Nature 321: 209-213.
    • (1986) Nature , vol.321 , pp. 209-213
    • Bird, A.P.1
  • 3
    • 34547563511 scopus 로고    scopus 로고
    • Properties of RNA polymerase II elongation complexes before and after the P-TEFb-mediated transition into productive elongation
    • Cheng B, Price DH, (2007) Properties of RNA polymerase II elongation complexes before and after the P-TEFb-mediated transition into productive elongation. J Biol Chem 282: 21901-21912.
    • (2007) J Biol Chem , vol.282 , pp. 21901-21912
    • Cheng, B.1    Price, D.H.2
  • 4
    • 67449113768 scopus 로고    scopus 로고
    • Cancer DNA methylation: molecular mechanisms and clinical implications
    • McCabe MT, Brandes JC, Vertino PM, (2009) Cancer DNA methylation: molecular mechanisms and clinical implications. Clin Cancer Res 15: 3927-3937.
    • (2009) Clin Cancer Res , vol.15 , pp. 3927-3937
    • McCabe, M.T.1    Brandes, J.C.2    Vertino, P.M.3
  • 5
    • 4143074854 scopus 로고    scopus 로고
    • SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells
    • Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, et al. (2004) SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat Cell Biol 6: 731-740.
    • (2004) Nat Cell Biol , vol.6 , pp. 731-740
    • Hamamoto, R.1    Furukawa, Y.2    Morita, M.3    Iimura, Y.4    Silva, F.P.5
  • 7
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones PA, Baylin SB, (2007) The epigenomics of cancer. Cell 128: 683-692.
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 8
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones PA, Baylin SB, (2002) The fundamental role of epigenetic events in cancer. Nat Rev Genet 3: 415-428.
    • (2002) Nat Rev Genet , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 9
    • 33845211776 scopus 로고    scopus 로고
    • Epigenetic aberrations and cancer
    • Ducasse M, Brown MA, (2006) Epigenetic aberrations and cancer. Mol Cancer 5: 60.
    • (2006) Mol Cancer , vol.5 , pp. 60
    • Ducasse, M.1    Brown, M.A.2
  • 10
    • 34548827379 scopus 로고    scopus 로고
    • Suv4-20 h deficiency results in telomere elongation and derepression of telomere recombination
    • Benetti R, Gonzalo S, Jaco I, Schotta G, Klatt P, et al. (2007) Suv4-20 h deficiency results in telomere elongation and derepression of telomere recombination. J Cell Biol 178: 925-936.
    • (2007) J Cell Biol , vol.178 , pp. 925-936
    • Benetti, R.1    Gonzalo, S.2    Jaco, I.3    Schotta, G.4    Klatt, P.5
  • 11
    • 20144388146 scopus 로고    scopus 로고
    • Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
    • Fraga MF, Ballestar E, Villar-Garea A, Boix-Chornet M, Espada J, et al. (2005) Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nat Genet 37: 391-400.
    • (2005) Nat Genet , vol.37 , pp. 391-400
    • Fraga, M.F.1    Ballestar, E.2    Villar-Garea, A.3    Boix-Chornet, M.4    Espada, J.5
  • 12
    • 37549014575 scopus 로고    scopus 로고
    • Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle
    • Pesavento JJ, Yang H, Kelleher NL, Mizzen CA, (2008) Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle. Mol Cell Biol 28: 468-486.
    • (2008) Mol Cell Biol , vol.28 , pp. 468-486
    • Pesavento, J.J.1    Yang, H.2    Kelleher, N.L.3    Mizzen, C.A.4
  • 13
    • 2642542643 scopus 로고    scopus 로고
    • A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin
    • Schotta G, Lachner M, Sarma K, Ebert A, Sengupta R, et al. (2004) A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev 18: 1251-1262.
    • (2004) Genes Dev , vol.18 , pp. 1251-1262
    • Schotta, G.1    Lachner, M.2    Sarma, K.3    Ebert, A.4    Sengupta, R.5
  • 14
    • 48749102722 scopus 로고    scopus 로고
    • A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse
    • Schotta G, Sengupta R, Kubicek S, Malin S, Kauer M, et al. (2008) A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse. Genes Dev 22: 2048-2061.
    • (2008) Genes Dev , vol.22 , pp. 2048-2061
    • Schotta, G.1    Sengupta, R.2    Kubicek, S.3    Malin, S.4    Kauer, M.5
  • 15
    • 65249157999 scopus 로고    scopus 로고
    • The multiple facets of histone H4-lysine 20 methylation
    • Yang H, Mizzen CA, (2009) The multiple facets of histone H4-lysine 20 methylation. Biochem Cell Biol 87: 151-161.
    • (2009) Biochem Cell Biol , vol.87 , pp. 151-161
    • Yang, H.1    Mizzen, C.A.2
  • 16
    • 44349195470 scopus 로고    scopus 로고
    • Histone lysine methyltransferases and demethylases in Plasmodium falciparum
    • Cui L, Fan Q, Miao J, (2008) Histone lysine methyltransferases and demethylases in Plasmodium falciparum. Int J Parasitol 38: 1083-1097.
    • (2008) Int J Parasitol , vol.38 , pp. 1083-1097
    • Cui, L.1    Fan, Q.2    Miao, J.3
  • 17
    • 0037020032 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the histone methyltransferase SET7/9
    • Wilson JR, Jing C, Walker PA, Martin SR, Howell SA, et al. (2002) Crystal structure and functional analysis of the histone methyltransferase SET7/9. Cell 111: 105-115.
    • (2002) Cell , vol.111 , pp. 105-115
    • Wilson, J.R.1    Jing, C.2    Walker, P.A.3    Martin, S.R.4    Howell, S.A.5
  • 18
    • 0037020199 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of a SET domain protein methyltransferase
    • Trievel RC, Beach BM, Dirk LM, Houtz RL, Hurley JH, (2002) Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell 111: 91-103.
    • (2002) Cell , vol.111 , pp. 91-103
    • Trievel, R.C.1    Beach, B.M.2    Dirk, L.M.3    Houtz, R.L.4    Hurley, J.H.5
  • 19
    • 33746832077 scopus 로고    scopus 로고
    • Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex
    • Brown MA, Sims RJ, 3rd, Gottlieb PD, Tucker PW, (2006) Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol Cancer 5: 26.
    • (2006) Mol Cancer , vol.5 , pp. 26
    • Brown, M.A.1    Sims 3rd, R.J.2    Gottlieb, P.D.3    Tucker, P.W.4
  • 20
    • 0036578662 scopus 로고    scopus 로고
    • Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis
    • Gottlieb PD, Pierce SA, Sims RJ, Yamagishi H, Weihe EK, et al. (2002) Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis. Nat Genet 31: 25-32.
    • (2002) Nat Genet , vol.31 , pp. 25-32
    • Gottlieb, P.D.1    Pierce, S.A.2    Sims, R.J.3    Yamagishi, H.4    Weihe, E.K.5
  • 21
    • 33644542409 scopus 로고    scopus 로고
    • SmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos
    • Tan X, Rotllant J, Li H, De Deyne P, Du SJ, (2006) SmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos. Proc Natl Acad Sci U S A 103: 2713-2718.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2713-2718
    • Tan, X.1    Rotllant, J.2    Li, H.3    de Deyne, P.4    Du, S.J.5
  • 22
    • 42549095632 scopus 로고    scopus 로고
    • Enhanced methyltransferase activity of SMYD3 by the cleavage of its N-terminal region in human cancer cells
    • Silva FP, Hamamoto R, Kunizaki M, Tsuge M, Nakamura Y, et al. (2008) Enhanced methyltransferase activity of SMYD3 by the cleavage of its N-terminal region in human cancer cells. Oncogene 27: 2686-2692.
    • (2008) Oncogene , vol.27 , pp. 2686-2692
    • Silva, F.P.1    Hamamoto, R.2    Kunizaki, M.3    Tsuge, M.4    Nakamura, Y.5
  • 23
    • 33644929027 scopus 로고    scopus 로고
    • Enhanced SMYD3 expression is essential for the growth of breast cancer cells
    • Hamamoto R, Silva FP, Tsuge M, Nishidate T, Katagiri T, et al. (2006) Enhanced SMYD3 expression is essential for the growth of breast cancer cells. Cancer Sci 97: 113-118.
    • (2006) Cancer Sci , vol.97 , pp. 113-118
    • Hamamoto, R.1    Silva, F.P.2    Tsuge, M.3    Nishidate, T.4    Katagiri, T.5
  • 24
    • 27144496194 scopus 로고    scopus 로고
    • A variable number of tandem repeats polymorphism in an E2F-1 binding element in the 5′ flanking region of SMYD3 is a risk factor for human cancers
    • Tsuge M, Hamamoto R, Silva FP, Ohnishi Y, Chayama K, et al. (2005) A variable number of tandem repeats polymorphism in an E2F-1 binding element in the 5′ flanking region of SMYD3 is a risk factor for human cancers. Nat Genet 37: 1104-1107.
    • (2005) Nat Genet , vol.37 , pp. 1104-1107
    • Tsuge, M.1    Hamamoto, R.2    Silva, F.P.3    Ohnishi, Y.4    Chayama, K.5
  • 25
    • 41349105728 scopus 로고    scopus 로고
    • Association of the variable number of tandem repeats polymorphism in the promoter region of the SMYD3 gene with risk of esophageal squamous cell carcinoma in relation to tobacco smoking
    • Wang H, Liu Y, Tan W, Zhang Y, Zhao N, et al. (2008) Association of the variable number of tandem repeats polymorphism in the promoter region of the SMYD3 gene with risk of esophageal squamous cell carcinoma in relation to tobacco smoking. Cancer Sci 99: 787-791.
    • (2008) Cancer Sci , vol.99 , pp. 787-791
    • Wang, H.1    Liu, Y.2    Tan, W.3    Zhang, Y.4    Zhao, N.5
  • 26
    • 78650379579 scopus 로고    scopus 로고
    • Crystal Structure of Cardiac-specific Histone Methyltransferase SmyD1 Reveals Unusual Active Site Architecture
    • Sirinupong N, Brunzelle J, Ye J, Pirzada A, Nico L, et al. (2010) Crystal Structure of Cardiac-specific Histone Methyltransferase SmyD1 Reveals Unusual Active Site Architecture. Journal of Biological Chemistry 285: 40635-40644.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 40635-40644
    • Sirinupong, N.1    Brunzelle, J.2    Ye, J.3    Pirzada, A.4    Nico, L.5
  • 27
    • 79151470135 scopus 로고    scopus 로고
    • Structural Insights into the Autoinhibition and Posttranslational Activation of Histone Methyltransferase SmyD3
    • Sirinupong N, Brunzelle J, Doko E, Yang Z, (2011) Structural Insights into the Autoinhibition and Posttranslational Activation of Histone Methyltransferase SmyD3. Journal of Molecular Biology 406: 149-159.
    • (2011) Journal of Molecular Biology , vol.406 , pp. 149-159
    • Sirinupong, N.1    Brunzelle, J.2    Doko, E.3    Yang, Z.4
  • 28
    • 79961241001 scopus 로고    scopus 로고
    • Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding
    • Nucleic Acids Research
    • Xu S, Wu J, Sun B, Zhong C, Ding J, (2011) Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding. Nucleic Acids Research.
    • (2011)
    • Xu, S.1    Wu, J.2    Sun, B.3    Zhong, C.4    Ding, J.5
  • 29
    • 0037135616 scopus 로고    scopus 로고
    • m-Bop, a repressor protein essential for cardiogenesis, interacts with skNAC, a heart- and muscle-specific transcription factor
    • Sims RJ, 3rd, Weihe EK, Zhu L, O'Malley S, Harriss JV, et al. (2002) m-Bop, a repressor protein essential for cardiogenesis, interacts with skNAC, a heart- and muscle-specific transcription factor. J Biol Chem 277: 26524-26529.
    • (2002) J Biol Chem , vol.277 , pp. 26524-26529
    • Sims 3rd, R.J.1    Weihe, E.K.2    Zhu, L.3    O'Malley, S.4    Harriss, J.V.5
  • 32
    • 0037167839 scopus 로고    scopus 로고
    • Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1
    • Beisel C, Imhof A, Greene J, Kremmer E, Sauer F, (2002) Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1. Nature 419: 857-862.
    • (2002) Nature , vol.419 , pp. 857-862
    • Beisel, C.1    Imhof, A.2    Greene, J.3    Kremmer, E.4    Sauer, F.5
  • 33
    • 0037599617 scopus 로고    scopus 로고
    • NSD1 is essential for early post-implantation development and has a catalytically active SET domain
    • Rayasam GV, Wendling O, Angrand PO, Mark M, Niederreither K, et al. (2003) NSD1 is essential for early post-implantation development and has a catalytically active SET domain. EMBO J 22: 3153-3163.
    • (2003) EMBO J , vol.22 , pp. 3153-3163
    • Rayasam, G.V.1    Wendling, O.2    Angrand, P.O.3    Mark, M.4    Niederreither, K.5
  • 34
    • 0141816768 scopus 로고    scopus 로고
    • ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3
    • Byrd KN, Shearn A, (2003) ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3. Proc Natl Acad Sci U S A 100: 11535-11540.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11535-11540
    • Byrd, K.N.1    Shearn, A.2
  • 35
    • 34250820481 scopus 로고    scopus 로고
    • Trithorax-group protein ASH1 methylates histone H3 lysine 36
    • Tanaka Y, Katagiri Z, Kawahashi K, Kioussis D, Kitajima S, (2007) Trithorax-group protein ASH1 methylates histone H3 lysine 36. Gene 397: 161-168.
    • (2007) Gene , vol.397 , pp. 161-168
    • Tanaka, Y.1    Katagiri, Z.2    Kawahashi, K.3    Kioussis, D.4    Kitajima, S.5
  • 37
    • 79960305417 scopus 로고    scopus 로고
    • Protein Databank (PDB) accession ID
    • Protein Databank (PDB) accession ID 3RU0.
    • , vol.3 RU
  • 38
    • 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, et al. (2002) Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell 111: 117-127.
    • (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
  • 39
    • 0038419637 scopus 로고    scopus 로고
    • Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
    • Trievel RC, Flynn EM, Houtz RL, Hurley JH, (2003) Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT. Nat Struct Biol 10: 545-552.
    • (2003) Nat Struct Biol , vol.10 , pp. 545-552
    • Trievel, R.C.1    Flynn, E.M.2    Houtz, R.L.3    Hurley, J.H.4
  • 40
    • 0036829968 scopus 로고    scopus 로고
    • Structure of the SET domain histone lysine methyltransferase Clr4
    • Min J, Zhang X, Cheng X, Grewal SI, Xu RM, (2002) Structure of the SET domain histone lysine methyltransferase Clr4. Nat Struct Biol 9: 828-832.
    • (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
  • 41
    • 0037439085 scopus 로고    scopus 로고
    • Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet
    • Kwon T, Chang JH, Kwak E, Lee CW, Joachimiak A, et al. (2003) Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J 22: 292-303.
    • (2003) EMBO J , vol.22 , pp. 292-303
    • Kwon, T.1    Chang, J.H.2    Kwak, E.3    Lee, C.W.4    Joachimiak, A.5
  • 43
    • 22344454519 scopus 로고    scopus 로고
    • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
    • Couture JF, Collazo E, Brunzelle JS, Trievel RC, (2005) Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes Dev 19: 1455-1465.
    • (2005) Genes Dev , vol.19 , pp. 1455-1465
    • Couture, J.F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4
  • 44
    • 0037309997 scopus 로고    scopus 로고
    • Structure of SET domain proteins: a new twist on histone methylation
    • Marmorstein R, (2003) Structure of SET domain proteins: a new twist on histone methylation. Trends Biochem Sci 28: 59-62.
    • (2003) Trends Biochem Sci , vol.28 , pp. 59-62
    • Marmorstein, R.1
  • 45
    • 79960327339 scopus 로고    scopus 로고
    • SET domain protein lysine methyltransferases: Structure, specificity and catalysis
    • Zhou CQaM-M, (2006) SET domain protein lysine methyltransferases: Structure, specificity and catalysis. Cellular and Molecular Life Sciences 68: 9.
    • (2006) Cellular and Molecular Life Sciences , vol.68 , pp. 9
    • Zhou, CQaM-M.1
  • 46
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
    • Taverna SD, Li H, Ruthenburg AJ, Allis CD, Patel DJ, (2007) How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nat Struct Mol Biol 14: 1025-1040.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3    Allis, C.D.4    Patel, D.J.5
  • 47
    • 0036079307 scopus 로고    scopus 로고
    • DEAF-1 function is essential for the early embryonic development of Drosophila
    • Veraksa A, Kennison J, McGinnis W, (2002) DEAF-1 function is essential for the early embryonic development of Drosophila. Genesis 33: 67-76.
    • (2002) Genesis , vol.33 , pp. 67-76
    • Veraksa, A.1    Kennison, J.2    McGinnis, W.3
  • 49
    • 34249812945 scopus 로고    scopus 로고
    • Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity
    • Liu Y, Chen W, Gaudet J, Cheney MD, Roudaia L, et al. (2007) Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Cancer Cell 11: 483-497.
    • (2007) Cancer Cell , vol.11 , pp. 483-497
    • Liu, Y.1    Chen, W.2    Gaudet, J.3    Cheney, M.D.4    Roudaia, L.5
  • 50
    • 0026757174 scopus 로고
    • Identification of breakpoints in t(8;21) acute myelogenous leukemia and isolation of a fusion transcript, AML1/ETO, with similarity to Drosophila segmentation gene, runt
    • Erickson P, Gao J, Chang KS, Look T, Whisenant E, et al. (1992) Identification of breakpoints in t(8;21) acute myelogenous leukemia and isolation of a fusion transcript, AML1/ETO, with similarity to Drosophila segmentation gene, runt. Blood 80: 1825-1831.
    • (1992) Blood , vol.80 , pp. 1825-1831
    • Erickson, P.1    Gao, J.2    Chang, K.S.3    Look, T.4    Whisenant, E.5
  • 52
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL, (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 53
    • 77952692464 scopus 로고    scopus 로고
    • PR-Set7-mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression
    • Congdon LM, Houston SI, Veerappan CS, Spektor TM, Rice JC, (2010) PR-Set7-mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression. J Cell Biochem 110: 609-619.
    • (2010) J Cell Biochem , vol.110 , pp. 609-619
    • Congdon, L.M.1    Houston, S.I.2    Veerappan, C.S.3    Spektor, T.M.4    Rice, J.C.5
  • 54
    • 33645906532 scopus 로고    scopus 로고
    • Methylation of the ASC gene promoter is associated with aggressive prostate cancer
    • Collard RL, Harya NS, Monzon FA, Maier CE, O'Keefe DS, (2006) Methylation of the ASC gene promoter is associated with aggressive prostate cancer. Prostate 66: 687-695.
    • (2006) Prostate , vol.66 , pp. 687-695
    • Collard, R.L.1    Harya, N.S.2    Monzon, F.A.3    Maier, C.E.4    O'Keefe, D.S.5
  • 55
    • 0033676843 scopus 로고    scopus 로고
    • TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers
    • Conway KE, McConnell BB, Bowring CE, Donald CD, Warren ST, et al. (2000) TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers. Cancer Res 60: 6236-6242.
    • (2000) Cancer Res , vol.60 , pp. 6236-6242
    • Conway, K.E.1    McConnell, B.B.2    Bowring, C.E.3    Donald, C.D.4    Warren, S.T.5
  • 56
    • 1442277112 scopus 로고    scopus 로고
    • TMS1/ASC: the cancer connection
    • McConnell BB, Vertino PM, (2004) TMS1/ASC: the cancer connection. Apoptosis 9: 5-18.
    • (2004) Apoptosis , vol.9 , pp. 5-18
    • McConnell, B.B.1    Vertino, P.M.2
  • 57
    • 4644314826 scopus 로고    scopus 로고
    • Aberrant methylation and down-regulation of TMS1/ASC in human glioblastoma
    • Stone AR, Bobo W, Brat DJ, Devi NS, Van Meir EG, et al. (2004) Aberrant methylation and down-regulation of TMS1/ASC in human glioblastoma. Am J Pathol 165: 1151-1161.
    • (2004) Am J Pathol , vol.165 , pp. 1151-1161
    • Stone, A.R.1    Bobo, W.2    Brat, D.J.3    Devi, N.S.4    van Meir, E.G.5
  • 58
    • 53049099107 scopus 로고    scopus 로고
    • Role of hMOF-dependent histone H4 lysine 16 acetylation in the maintenance of TMS1/ASC gene activity
    • Kapoor-Vazirani P, Kagey JD, Powell DR, Vertino PM, (2008) Role of hMOF-dependent histone H4 lysine 16 acetylation in the maintenance of TMS1/ASC gene activity. Cancer Res 68: 6810-6821.
    • (2008) Cancer Res , vol.68 , pp. 6810-6821
    • Kapoor-Vazirani, P.1    Kagey, J.D.2    Powell, D.R.3    Vertino, P.M.4
  • 59
    • 79953131815 scopus 로고    scopus 로고
    • SUV420H2-Mediated H4K20 Trimethylation Enforces RNA Polymerase II Promoter-Proximal Pausing by Blocking hMOF-Dependent H4K16 Acetylation
    • Kapoor-Vazirani P, Kagey JD, Vertino PM, (2011) SUV420H2-Mediated H4K20 Trimethylation Enforces RNA Polymerase II Promoter-Proximal Pausing by Blocking hMOF-Dependent H4K16 Acetylation. Mol Cell Biol 31: 1594-1609.
    • (2011) Mol Cell Biol , vol.31 , pp. 1594-1609
    • Kapoor-Vazirani, P.1    Kagey, J.D.2    Vertino, P.M.3
  • 60
    • 0033212804 scopus 로고    scopus 로고
    • The Rossmann Fourier autoindexing algorithm in MOSFLM
    • Powell HR, (1999) The Rossmann Fourier autoindexing algorithm in MOSFLM. Acta Crystallogr D Biol Crystallogr 55: 1690-1695.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1690-1695
    • Powell, H.R.1
  • 61
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks C, Miller R, (1999) The design and implementation of SnB v2.0. J Appl Cryst 32: 120-124.
    • (1999) J Appl Cryst , vol.32 , pp. 120-124
    • Weeks, C.1    Miller, R.2
  • 62
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS, (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6: 458-463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 63
    • 79960319506 scopus 로고
    • Struct Biol
    • McRee D, (1993) Struct Biol 125: 156-165.
    • (1993) , vol.125 , pp. 156-165
    • McRee, D.1
  • 64
    • 0033039285 scopus 로고    scopus 로고
    • Preparation of nucleosome core particle from recombinant histones
    • Luger K, Rechsteiner TJ, Richmond TJ, (1999) Preparation of nucleosome core particle from recombinant histones. Methods Enzymol 304: 3-19.
    • (1999) Methods Enzymol , vol.304 , pp. 3-19
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 65
    • 0031587289 scopus 로고    scopus 로고
    • Characterization of nucleosome core particles containing histone proteins made in bacteria
    • Luger K, Rechsteiner TJ, Flaus AJ, Waye MM, Richmond TJ, (1997) Characterization of nucleosome core particles containing histone proteins made in bacteria. J Mol Biol 272: 301-311.
    • (1997) J Mol Biol , vol.272 , pp. 301-311
    • Luger, K.1    Rechsteiner, T.J.2    Flaus, A.J.3    Waye, M.M.4    Richmond, T.J.5
  • 66
    • 0039837085 scopus 로고    scopus 로고
    • Sequence motifs and free energies of selected natural and non-natural nucleosome positioning DNA sequences
    • Thastrom A, Lowary PT, Widlund HR, Cao H, Kubista M, et al. (1999) Sequence motifs and free energies of selected natural and non-natural nucleosome positioning DNA sequences. J Mol Biol 288: 213-229.
    • (1999) J Mol Biol , vol.288 , pp. 213-229
    • Thastrom, A.1    Lowary, P.T.2    Widlund, H.R.3    Cao, H.4    Kubista, M.5


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