메뉴 건너뛰기




Volumn , Issue , 2013, Pages 189-226

Histone methyltransferases: Opportunities in cancer drug discovery

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84929535203     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-642-38404-2_9     Document Type: Chapter
Times cited : (1)

References (184)
  • 1
    • 41549133493 scopus 로고    scopus 로고
    • The tale of two domains: Proteomics and genomics analysis of SMYD2, a new histone methyltransferase
    • Abu-Farha M et al (2008) The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase. Mol Cell Proteomics 7(3):560-572
    • (2008) Mol Cell Proteomics , vol.7 , Issue.3 , pp. 560-572
    • Abu-Farha, M.1
  • 2
    • 65249151919 scopus 로고    scopus 로고
    • Structure and function of histone methylation binding proteins
    • Adams-Cioaba MA, Min J (2009) Structure and function of histone methylation binding proteins. Biochem Cell Biol 87(1):93-105
    • (2009) Biochem Cell Biol , vol.87 , Issue.1 , pp. 93-105
    • Adams-Cioaba, M.A.1    Min, J.2
  • 3
    • 77957966270 scopus 로고    scopus 로고
    • Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase
    • Aggarwal P et al (2010) Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase. Cancer Cell 18(4):329-340
    • (2010) Cancer Cell , vol.18 , Issue.4 , pp. 329-340
    • Aggarwal, P.1
  • 4
    • 35148867907 scopus 로고    scopus 로고
    • UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development
    • Agger K et al (2007) UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development. Nature 449(7163):731-734
    • (2007) Nature , vol.449 , Issue.7163 , pp. 731-734
    • Agger, K.1
  • 5
    • 59649090382 scopus 로고    scopus 로고
    • N-Benzyl-1-heteroaryl-3-(trifl uoromethyl)-1H-pyrazole-5-carboxamides as inhibitors of co-activator associated arginine methyltransferase 1 (CARM1)
    • Allan M et al (2009) N-Benzyl-1-heteroaryl-3-(trifl uoromethyl)-1H-pyrazole-5-carboxamides as inhibitors of co-activator associated arginine methyltransferase 1 (CARM1). Bioorg Med Chem Lett 19(4):1218-1223
    • (2009) Bioorg Med Chem Lett , vol.19 , Issue.4 , pp. 1218-1223
    • Allan, M.1
  • 6
    • 77956810338 scopus 로고    scopus 로고
    • MLL2 is required in oocytes for bulk histone 3 lysine 4 trimethylation and transcriptional silencing
    • Andreu-Vieyra CV et al (2010) MLL2 is required in oocytes for bulk histone 3 lysine 4 trimethylation and transcriptional silencing. PLoS Biol 8(8):e1000453
    • (2010) PLoS Biol , vol.8 , Issue.8 , pp. e1000453
    • Andreu-Vieyra, C.V.1
  • 7
    • 0035872769 scopus 로고    scopus 로고
    • NSD3, a new SET domain-containing gene, maps to 8p12 and is ampli-fi ed in human breast cancer cell lines
    • Angrand PO et al (2001) NSD3, a new SET domain-containing gene, maps to 8p12 and is ampli-fi ed in human breast cancer cell lines. Genomics 74(1):79-88
    • (2001) Genomics , vol.74 , Issue.1 , pp. 79-88
    • Angrand, P.O.1
  • 8
    • 34250320926 scopus 로고    scopus 로고
    • Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases
    • Barrett A et al (2007) Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases. Int J Cancer 121(2):265-275
    • (2007) Int J Cancer , vol.121 , Issue.2 , pp. 265-275
    • Barrett, A.1
  • 9
    • 77949563562 scopus 로고    scopus 로고
    • Targeting DOT1L action and interactions in leukemia: The role of DOT1L in transformation and development
    • Barry ER, Corry GN, Rasmussen TP (2010) Targeting DOT1L action and interactions in leukemia: the role of DOT1L in transformation and development. Expert Opin Ther Targets 14(4):405-418
    • (2010) Expert Opin Ther Targets , vol.14 , Issue.4 , pp. 405-418
    • Barry, E.R.1    Corry, G.N.2    Rasmussen, T.P.3
  • 10
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profi ling of histone methylations in the human genome
    • Barski A et al (2007) High-resolution profi ling of histone methylations in the human genome. Cell 129(4):823-837
    • (2007) Cell , vol.129 , Issue.4 , pp. 823-837
    • Barski, A.1
  • 11
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: An emerging regulator of protein function
    • Bedford MT, 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
  • 12
    • 19944430797 scopus 로고    scopus 로고
    • Genomic maps and comparative analysis of histone modifi cations in human and mouse
    • Bernstein BE et al (2005) Genomic maps and comparative analysis of histone modifi cations in human and mouse. Cell 120(2):169-181
    • (2005) Cell , vol.120 , Issue.2 , pp. 169-181
    • Bernstein, B.E.1
  • 13
    • 33646070846 scopus 로고    scopus 로고
    • A bivalent chromatin structure marks key developmental genes in embryonic stem cells
    • Bernstein BE et al (2006) A bivalent chromatin structure marks key developmental genes in embryonic stem cells. Cell 125(2):315-326
    • (2006) Cell , vol.125 , Issue.2 , pp. 315-326
    • Bernstein, B.E.1
  • 14
    • 33846522525 scopus 로고    scopus 로고
    • The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling
    • Bitoun E, Oliver PL, Davies KE (2007) The mixed-lineage leukemia fusion partner AF4 stimulates RNA polymerase II transcriptional elongation and mediates coordinated chromatin remodeling. Hum Mol Genet 16(1):92-106
    • (2007) Hum Mol Genet , vol.16 , Issue.1 , pp. 92-106
    • Bitoun, E.1    Oliver, P.L.2    Davies, K.E.3
  • 15
    • 15444374342 scopus 로고    scopus 로고
    • Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control
    • Boisvert FM et al (2005a) Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control. Genes Dev 19(6):671-676
    • (2005) Genes Dev , vol.19 , Issue.6 , pp. 671-676
    • Boisvert, F.M.1
  • 16
    • 29244456155 scopus 로고    scopus 로고
    • The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity
    • Boisvert FM et al (2005b) The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity. Cell Cycle 4(12):1834-1841
    • (2005) Cell Cycle , vol.4 , Issue.12 , pp. 1834-1841
    • Boisvert, F.M.1
  • 17
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specifi c recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan MV et al (2006) Structural basis for the methylation state-specifi c recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127(7):1361-1373
    • (2006) Cell , vol.127 , Issue.7 , pp. 1361-1373
    • Botuyan, M.V.1
  • 18
    • 25144525014 scopus 로고    scopus 로고
    • Core transcriptional regulatory circuitry in human embryonic stem cells
    • Boyer LA et al (2005) Core transcriptional regulatory circuitry in human embryonic stem cells. Cell 122(6):947-956
    • (2005) Cell , vol.122 , Issue.6 , pp. 947-956
    • Boyer, L.A.1
  • 19
    • 33646882068 scopus 로고    scopus 로고
    • Polycomb complexes repress developmental regulators in murine embryonic stem cells
    • Boyer LA et al (2006) Polycomb complexes repress developmental regulators in murine embryonic stem cells. Nature 441(7091):349-353
    • (2006) Nature , vol.441 , Issue.7091 , pp. 349-353
    • Boyer, L.A.1
  • 20
    • 0142105414 scopus 로고    scopus 로고
    • EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplifi ed in cancer
    • Bracken AP et al (2003) EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplifi ed in cancer. EMBO J 22(20):5323-5335
    • (2003) EMBO J , vol.22 , Issue.20 , pp. 5323-5335
    • Bracken, A.P.1
  • 21
    • 33746832077 scopus 로고    scopus 로고
    • Identifi cation and characterization of Smyd2: A split SET/MYND domaincontaining histone H3 lysine 36-specifi c methyltransferase that interacts with the Sin3 histone deacetylase complex
    • Brown MA et al (2006) Identifi cation and characterization of Smyd2: a split SET/MYND domaincontaining histone H3 lysine 36-specifi c methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol Cancer 5:26
    • (2006) Mol Cancer , vol.5 , pp. 26
    • Brown, M.A.1
  • 22
    • 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 (2004a) SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol Cell 15(1):57-67
    • (2004) Mol Cell , vol.15 , Issue.1 , pp. 57-67
    • Cao, R.1    Zhang, Y.2
  • 23
    • 1942503942 scopus 로고    scopus 로고
    • The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3
    • Cao R, Zhang Y (2004b) The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3. Curr Opin Genet Dev 14(2):155-164
    • (2004) Curr Opin Genet Dev , vol.14 , Issue.2 , pp. 155-164
    • Cao, R.1    Zhang, Y.2
  • 24
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao R et al (2002) Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298(5595):1039-1043
    • (2002) Science , vol.298 , Issue.5595 , pp. 1039-1043
    • Cao, R.1
  • 25
    • 40749126138 scopus 로고    scopus 로고
    • Role of hPHF1 in H3K27 methylation and Hox gene silencing
    • Cao R et al (2008a) Role of hPHF1 in H3K27 methylation and Hox gene silencing. Mol Cell Biol 28(5):1862-1872
    • (2008) Mol Cell Biol , vol.28 , Issue.5 , pp. 1862-1872
    • Cao, R.1
  • 26
    • 57649124289 scopus 로고    scopus 로고
    • Repression of E-cadherin by the polycomb group protein EZH2 in cancer
    • Cao Q et al (2008b) Repression of E-cadherin by the polycomb group protein EZH2 in cancer. Oncogene 27(58):7274-7284
    • (2008) Oncogene , vol.27 , Issue.58 , pp. 7274-7284
    • Cao, Q.1
  • 27
    • 79953056443 scopus 로고    scopus 로고
    • The histone methyltransferase SETDB1 is recurrently amplifi ed in melanoma and accelerates its onset
    • Ceol CJ et al (2011) The histone methyltransferase SETDB1 is recurrently amplifi ed in melanoma and accelerates its onset. Nature 471(7339):513-517
    • (2011) Nature , vol.471 , Issue.7339 , pp. 513-517
    • Ceol, C.J.1
  • 28
    • 62049083789 scopus 로고    scopus 로고
    • Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294
    • Chang Y et al (2009) Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294. Nat Struct Mol Biol 16(3):312-317
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.3 , pp. 312-317
    • Chang, Y.1
  • 29
    • 77953691195 scopus 로고    scopus 로고
    • Adding a lysine mimic in the design of potent inhibitors of histone lysine methyltransferases
    • Chang Y et al (2010) Adding a lysine mimic in the design of potent inhibitors of histone lysine methyltransferases. J Mol Biol 400(1):1-7
    • (2010) J Mol Biol , vol.400 , Issue.1 , pp. 1-7
    • Chang, Y.1
  • 30
    • 0033603396 scopus 로고    scopus 로고
    • Regulation of transcription by a protein methyltransferase
    • Chen D et al (1999) Regulation of transcription by a protein methyltransferase. Science 284(5423):2174-2177
    • (1999) Science , vol.284 , Issue.5423 , pp. 2174-2177
    • Chen, D.1
  • 31
    • 77950678085 scopus 로고    scopus 로고
    • Coordinated chromatin control: Structural and functional linkage of DNA and histone methylation
    • Cheng X, Blumenthal RM (2010) Coordinated chromatin control: structural and functional linkage of DNA and histone methylation. Biochemistry 49(14):2999-3008
    • (2010) Biochemistry , vol.49 , Issue.14 , pp. 2999-3008
    • Cheng, X.1    Blumenthal, R.M.2
  • 32
    • 0032212243 scopus 로고    scopus 로고
    • The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts
    • Chesi M et al (1998) The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts. Blood 92(9):3025-3034
    • (1998) Blood , vol.92 , Issue.9 , pp. 3025-3034
    • Chesi, M.1
  • 33
    • 34848865728 scopus 로고    scopus 로고
    • Protein arginine-methyltransferase-dependent oncogenesis
    • Cheung N et al (2007) Protein arginine-methyltransferase-dependent oncogenesis. Nat Cell Biol 9(10):1208-1215
    • (2007) Nat Cell Biol , vol.9 , Issue.10 , pp. 1208-1215
    • Cheung, N.1
  • 34
    • 33746332412 scopus 로고    scopus 로고
    • The putative oncogene GASC1 demethylates tri-and dimethylated lysine 9 on histone H3
    • Cloos PA et al (2006) The putative oncogene GASC1 demethylates tri-and dimethylated lysine 9 on histone H3. Nature 442(7100):307-311
    • (2006) Nature , vol.442 , Issue.7100 , pp. 307-311
    • Cloos, P.A.1
  • 35
    • 14044256546 scopus 로고    scopus 로고
    • In vitro and in vivo analyses of a Phe/Tyr switch controlling product speci-fi city of histone lysine methyltransferases
    • Collins RE et al (2005) In vitro and in vivo analyses of a Phe/Tyr switch controlling product speci-fi city of histone lysine methyltransferases. J Biol Chem 280(7):5563-5570
    • (2005) J Biol Chem , vol.280 , Issue.7 , pp. 5563-5570
    • Collins, R.E.1
  • 36
    • 69949148388 scopus 로고    scopus 로고
    • Protein methyltransferases as a target class for drug discovery
    • Copeland RA, Solomon ME, Richon VM (2009) Protein methyltransferases as a target class for drug discovery. Nat Rev Drug Discov 8(9):724-732
    • (2009) Nat Rev Drug Discov , vol.8 , Issue.9 , pp. 724-732
    • Copeland, R.A.1    Solomon, M.E.2    Richon, V.M.3
  • 37
    • 79960058024 scopus 로고    scopus 로고
    • Selective killing of mixed lineage leukemia cells by a potent small-molecule DOT1L inhibitor
    • Daigle SR et al (2011) Selective killing of mixed lineage leukemia cells by a potent small-molecule DOT1L inhibitor. Cancer Cell 20(1):53-65
    • (2011) Cancer Cell , vol.20 , Issue.1 , pp. 53-65
    • Daigle, S.R.1
  • 38
    • 0037164736 scopus 로고    scopus 로고
    • Crosstalk between CARM1 methylation and CBP acetylation on histone H3
    • Daujat S et al (2002) Crosstalk between CARM1 methylation and CBP acetylation on histone H3. Curr Biol 12(24):2090-2097
    • (2002) Curr Biol , vol.12 , Issue.24 , pp. 2090-2097
    • Daujat, S.1
  • 39
    • 77957770113 scopus 로고    scopus 로고
    • SET7/9 catalytic mutants reveal the role of active site water molecules in lysine multiple methylation
    • Del Rizzo PA et al (2010) SET7/9 catalytic mutants reveal the role of active site water molecules in lysine multiple methylation. J Biol Chem 285(41):31849-31858
    • (2010) J Biol Chem , vol.285 , Issue.41 , pp. 31849-31858
    • Del Rizzo, P.A.1
  • 40
    • 79959829510 scopus 로고    scopus 로고
    • Histone arginine methylation
    • Di Lorenzo A, Bedford MT (2011) Histone arginine methylation. FEBS Lett 585(13):2024-2031
    • (2011) FEBS Lett , vol.585 , Issue.13 , pp. 2024-2031
    • Di Lorenzo, A.1    Bedford, M.T.2
  • 41
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: Protein lysine methyltransferases
    • Dillon SC et al (2005) The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol 6(8):227
    • (2005) Genome Biol , vol.6 , Issue.8 , pp. 227
    • Dillon, S.C.1
  • 42
    • 33947615716 scopus 로고    scopus 로고
    • Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases
    • Dirk LM et al (2007) Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases. Biochemistry 46(12):3905-3915
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3905-3915
    • Dirk, L.M.1
  • 43
    • 76949107741 scopus 로고    scopus 로고
    • Histone H3 lysine 4 (H3K4) methylation in development and differentiation
    • Eissenberg JC, Shilatifard A (2010) Histone H3 lysine 4 (H3K4) methylation in development and differentiation. Dev Biol 339(2):240-249
    • (2010) Dev Biol , vol.339 , Issue.2 , pp. 240-249
    • Eissenberg, J.C.1    Shilatifard, A.2
  • 44
    • 33748624090 scopus 로고    scopus 로고
    • Coactivator-associated arginine methyltransferase 1 (CARM1) is a positive regulator of the Cyclin E1 gene
    • El Messaoudi S et al (2006) Coactivator-associated arginine methyltransferase 1 (CARM1) is a positive regulator of the Cyclin E1 gene. Proc Natl Acad Sci USA 103(36):13351-13356
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.36 , pp. 13351-13356
    • El Messaoudi, S.1
  • 45
    • 33645132331 scopus 로고    scopus 로고
    • G9a-mediated irreversible epigenetic inactivation of Oct-3/4 during early embryogenesis
    • Feldman N et al (2006) G9a-mediated irreversible epigenetic inactivation of Oct-3/4 during early embryogenesis. Nat Cell Biol 8(2):188-194
    • (2006) Nat Cell Biol , vol.8 , Issue.2 , pp. 188-194
    • Feldman, N.1
  • 46
    • 0036850549 scopus 로고    scopus 로고
    • Different HATS of the ING1 gene family
    • Feng X, Hara Y, Riabowol K (2002) Different HATS of the ING1 gene family. Trends Cell Biol 12(11):532-538
    • (2002) Trends Cell Biol , vol.12 , Issue.11 , pp. 532-538
    • Feng, X.1    Hara, Y.2    Riabowol, K.3
  • 47
    • 33750342491 scopus 로고    scopus 로고
    • Signaling within a coactivator complex: Methylation of SRC-3/AIB1 is a molecular switch for complex disassembly
    • Feng Q et al (2006) Signaling within a coactivator complex: methylation of SRC-3/AIB1 is a molecular switch for complex disassembly. Mol Cell Biol 26(21):7846-7857
    • (2006) Mol Cell Biol , vol.26 , Issue.21 , pp. 7846-7857
    • Feng, Q.1
  • 48
    • 0015935205 scopus 로고
    • The charge relay system in chymotrypsin and chymotrypsinogen
    • Fersht AR, Sperling J (1973) The charge relay system in chymotrypsin and chymotrypsinogen. J Mol Biol 74(2):137-149
    • (1973) J Mol Biol , vol.74 , Issue.2 , pp. 137-149
    • Fersht, A.R.1    Sperling, J.2
  • 49
    • 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 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(4):391-400
    • (2005) Nat Genet , vol.37 , Issue.4 , pp. 391-400
    • Fraga, M.F.1
  • 50
    • 39149092383 scopus 로고    scopus 로고
    • CARM1 regulates estrogen-stimulated breast cancer growth through upregulation of E2F1
    • Frietze S et al (2008) CARM1 regulates estrogen-stimulated breast cancer growth through upregulation of E2F1. Cancer Res 68(1):301-306
    • (2008) Cancer Res , vol.68 , Issue.1 , pp. 301-306
    • Frietze, S.1
  • 51
    • 78650081714 scopus 로고    scopus 로고
    • ZNF274 recruits the histone methyltransferase SETDB1 to the 3 ends of ZNF genes
    • Frietze S et al (2010) ZNF274 recruits the histone methyltransferase SETDB1 to the 3 ends of ZNF genes. PLoS One 5(12):e15082
    • (2010) PLoS One , vol.5 , Issue.12 , pp. e15082
    • Frietze, S.1
  • 52
    • 62249127449 scopus 로고    scopus 로고
    • DOT1: A distinct class of histone lysine methyltransferase
    • Gao WL, Liu HL (2007) DOT1: a distinct class of histone lysine methyltransferase. Yi Chuan 29(12):1449-1454
    • (2007) Yi Chuan , vol.29 , Issue.12 , pp. 1449-1454
    • Gao, W.L.1    Liu, H.L.2
  • 53
    • 77956194960 scopus 로고    scopus 로고
    • Methylation of the tumor suppressor protein, BRCA1, infl uences its transcriptional cofactor function
    • Guendel I et al (2010) Methylation of the tumor suppressor protein, BRCA1, infl uences its transcriptional cofactor function. PLoS One 5(6):e11379
    • (2010) PLoS One , vol.5 , Issue.6 , pp. e11379
    • Guendel, I.1
  • 54
    • 34547433238 scopus 로고    scopus 로고
    • Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specifi city
    • Guo HB, Guo H (2007) Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specifi city. Proc Natl Acad Sci USA 104(21):8797-8802
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.21 , pp. 8797-8802
    • Guo, H.B.1    Guo, H.2
  • 55
    • 65549091962 scopus 로고    scopus 로고
    • Methylation-state-specifi c recognition of histones by the MBT repeat protein L3MBTL2
    • Guo Y et al (2009) Methylation-state-specifi c recognition of histones by the MBT repeat protein L3MBTL2. Nucleic Acids Res 37(7):2204-2210
    • (2009) Nucleic Acids Res , vol.37 , Issue.7 , pp. 2204-2210
    • Guo, Y.1
  • 56
    • 77951118936 scopus 로고    scopus 로고
    • Long non-coding RNA HOTAIR reprograms chromatin state to promote cancer metastasis
    • Gupta RA et al (2010) Long non-coding RNA HOTAIR reprograms chromatin state to promote cancer metastasis. Nature 464(7291):1071-1076
    • (2010) Nature , vol.464 , Issue.7291 , pp. 1071-1076
    • Gupta, R.A.1
  • 57
    • 4143074854 scopus 로고    scopus 로고
    • SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells
    • Hamamoto R et al (2004) SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat Cell Biol 6(8):731-740
    • (2004) Nat Cell Biol , vol.6 , Issue.8 , pp. 731-740
    • Hamamoto, R.1
  • 58
    • 33644929027 scopus 로고    scopus 로고
    • Enhanced SMYD3 expression is essential for the growth of breast cancer cells
    • Hamamoto R et al (2006) Enhanced SMYD3 expression is essential for the growth of breast cancer cells. Cancer Sci 97(2):113-118
    • (2006) Cancer Sci , vol.97 , Issue.2 , pp. 113-118
    • Hamamoto, R.1
  • 59
    • 13544272858 scopus 로고    scopus 로고
    • Mechanisms of transformation by MLL
    • Hess JL (2004) Mechanisms of transformation by MLL. Crit Rev Eukaryot Gene Expr 14(4):235-254
    • (2004) Crit Rev Eukaryot Gene Expr , vol.14 , Issue.4 , pp. 235-254
    • Hess, J.L.1
  • 60
    • 34547644685 scopus 로고    scopus 로고
    • Phosphorylation-mediated inactivation of coactivator-associated arginine methyltransferase 1
    • Higashimoto K et al (2007) Phosphorylation-mediated inactivation of coactivator-associated arginine methyltransferase 1. Proc Natl Acad Sci USA 104(30):12318-12323
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.30 , pp. 12318-12323
    • Higashimoto, K.1
  • 61
    • 3042536209 scopus 로고    scopus 로고
    • Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status
    • Hong H et al (2004) Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status. Cancer 101(1):83-89
    • (2004) Cancer , vol.101 , Issue.1 , pp. 83-89
    • Hong, H.1
  • 62
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specifi city of a family of jumonji histone lysine demethylases
    • Horton JR et al (2010) Enzymatic and structural insights for substrate specifi city of a family of jumonji histone lysine demethylases. Nat Struct Mol Biol 17(1):38-43
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.1 , pp. 38-43
    • Horton, J.R.1
  • 63
    • 43249086048 scopus 로고    scopus 로고
    • The LIM protein AJUBA recruits protein arginine methyltransferase 5 to mediate SNAIL-dependent transcriptional repression
    • Hou Z et al (2008) The LIM protein AJUBA recruits protein arginine methyltransferase 5 to mediate SNAIL-dependent transcriptional repression. Mol Cell Biol 28(10):3198-3207
    • (2008) Mol Cell Biol , vol.28 , Issue.10 , pp. 3198-3207
    • Hou, Z.1
  • 64
    • 73149118652 scopus 로고    scopus 로고
    • Novel oligoamine analogues inhibit lysine-specifi c demethylase 1 and induce reexpression of epigenetically silenced genes
    • Huang Y et al (2009) Novel oligoamine analogues inhibit lysine-specifi c demethylase 1 and induce reexpression of epigenetically silenced genes. Clin Cancer Res 15(23):7217-7228
    • (2009) Clin Cancer Res , vol.15 , Issue.23 , pp. 7217-7228
    • Huang, Y.1
  • 65
    • 77951233574 scopus 로고    scopus 로고
    • G9a and Glp methylate lysine 373 in the tumor suppressor p53
    • Huang J et al (2010) G9a and Glp methylate lysine 373 in the tumor suppressor p53. J Biol Chem 285(13):9636-9641
    • (2010) J Biol Chem , vol.285 , Issue.13 , pp. 9636-9641
    • Huang, J.1
  • 66
    • 65549130422 scopus 로고    scopus 로고
    • Optimization of pyrazole inhibitors of Coactivator Associated Arginine Methyltransferase 1 (CARM1)
    • Huynh T et al (2009) Optimization of pyrazole inhibitors of Coactivator Associated Arginine Methyltransferase 1 (CARM1). Bioorg Med Chem Lett 19(11):2924-2927
    • (2009) Bioorg Med Chem Lett , vol.19 , Issue.11 , pp. 2924-2927
    • Huynh, T.1
  • 67
    • 0035883090 scopus 로고    scopus 로고
    • A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia
    • Jaju RJ et al (2001) A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia. Blood 98(4):1264-1267
    • (2001) Blood , vol.98 , Issue.4 , pp. 1264-1267
    • Jaju, R.J.1
  • 68
    • 57049087451 scopus 로고    scopus 로고
    • Arginine methylation regulates the p53 response
    • Jansson M et al (2008) Arginine methylation regulates the p53 response. Nat Cell Biol 10(12):1431-1439
    • (2008) Nat Cell Biol , vol.10 , Issue.12 , pp. 1431-1439
    • Jansson, M.1
  • 69
    • 77951167356 scopus 로고    scopus 로고
    • Phosphorylation of serine-10 of histone H3 shields modifi ed lysine-9 selectively during mitosis
    • Jeong YS et al (2010) Phosphorylation of serine-10 of histone H3 shields modifi ed lysine-9 selectively during mitosis. Genes Cells 15(3):181-192
    • (2010) Genes Cells , vol.15 , Issue.3 , pp. 181-192
    • Jeong, Y.S.1
  • 70
    • 47549087904 scopus 로고    scopus 로고
    • Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1
    • Kalakonda N et al (2008) Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1. Oncogene 27(31):4293-4304
    • (2008) Oncogene , vol.27 , Issue.31 , pp. 4293-4304
    • Kalakonda, N.1
  • 71
    • 35348914451 scopus 로고    scopus 로고
    • Association of the SUV39H1 histone methyltransferase with the DNA methyltransferase 1 at mRNA expression level in primary colorectal cancer
    • Kang MY et al (2007) Association of the SUV39H1 histone methyltransferase with the DNA methyltransferase 1 at mRNA expression level in primary colorectal cancer. Int J Cancer 121(10):2192-2197
    • (2007) Int J Cancer , vol.121 , Issue.10 , pp. 2192-2197
    • Kang, M.Y.1
  • 72
    • 78650964531 scopus 로고    scopus 로고
    • Recognition and specifi city determinants of the human cbx chromodomains
    • Kaustov L et al (2011) Recognition and specifi city determinants of the human cbx chromodomains. J Biol Chem 286(1):521-529
    • (2011) J Biol Chem , vol.286 , Issue.1 , pp. 521-529
    • Kaustov, L.1
  • 73
    • 67749114645 scopus 로고    scopus 로고
    • Requirement of histone methyltransferase SMYD3 for estrogen receptormediated transcription
    • Kim H et al (2009) Requirement of histone methyltransferase SMYD3 for estrogen receptormediated transcription. J Biol Chem 284(30):19867-19877
    • (2009) J Biol Chem , vol.284 , Issue.30 , pp. 19867-19877
    • Kim, H.1
  • 74
    • 78149244916 scopus 로고    scopus 로고
    • Identifi cation of non-peptide malignant brain tumor (MBT) repeat antagonists by virtual screening of commercially available compounds
    • Kireev D et al (2010) Identifi cation of non-peptide malignant brain tumor (MBT) repeat antagonists by virtual screening of commercially available compounds. J Med Chem 53(21):7625-7631
    • (2010) J Med Chem , vol.53 , Issue.21 , pp. 7625-7631
    • Kireev, D.1
  • 75
    • 0141576562 scopus 로고    scopus 로고
    • Identifi cation of the polycomb group protein SU(Z)12 as a potential molecular target for human cancer therapy
    • Kirmizis A, Bartley SM, Farnham PJ (2003) Identifi cation of the polycomb group protein SU(Z)12 as a potential molecular target for human cancer therapy. Mol Cancer Ther 2(1):113-121
    • (2003) Mol Cancer Ther , vol.2 , Issue.1 , pp. 113-121
    • Kirmizis, A.1    Bartley, S.M.2    Farnham, P.J.3
  • 76
    • 0141816752 scopus 로고    scopus 로고
    • EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells
    • Kleer CG et al (2003) EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells. Proc Natl Acad Sci USA 100(20):11606-11611
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.20 , pp. 11606-11611
    • Kleer, C.G.1
  • 77
    • 33745847680 scopus 로고    scopus 로고
    • The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
    • Klose RJ et al (2006) The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature 442(7100):312-316
    • (2006) Nature , vol.442 , Issue.7100 , pp. 312-316
    • Klose, R.J.1
  • 78
    • 19344375746 scopus 로고    scopus 로고
    • A chromosomal memory triggered by Xist regulates histone methylation in X inactivation
    • Kohlmaier A et al (2004) A chromosomal memory triggered by Xist regulates histone methylation in X inactivation. PLoS Biol 2(7):E171
    • (2004) PLoS Biol , vol.2 , Issue.7 , pp. E171
    • Kohlmaier, A.1
  • 79
    • 66349097033 scopus 로고    scopus 로고
    • Type i arginine methyltransferases PRMT1 and PRMT-3 Act distributively
    • Kolbel K et al (2009) Type I arginine methyltransferases PRMT1 and PRMT-3 Act distributively. J Biol Chem 284(13):8274-8282
    • (2009) J Biol Chem , vol.284 , Issue.13 , pp. 8274-8282
    • Kolbel, K.1
  • 80
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifi cations and their function
    • Kouzarides T (2007) Chromatin modifi cations and their function. Cell 128(4):693-705
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 81
    • 78751610660 scopus 로고    scopus 로고
    • Structure and function of histone H3 lysine 9 methyltransferases and demethylases
    • Krishnan S, Horowitz S, Trievel RC (2011) Structure and function of histone H3 lysine 9 methyltransferases and demethylases. Chembiochem 12(2):254-263
    • (2011) Chembiochem , vol.12 , Issue.2 , pp. 254-263
    • Krishnan, S.1    Horowitz, S.2    Trievel, R.C.3
  • 82
    • 35548934558 scopus 로고    scopus 로고
    • MLL translocations, histone modifi cations and leukaemia stem-cell development
    • Krivtsov AV, Armstrong SA (2007) MLL translocations, histone modifi cations and leukaemia stem-cell development. Nat Rev Cancer 7(11):823-833
    • (2007) Nat Rev Cancer , vol.7 , Issue.11 , pp. 823-833
    • Krivtsov, A.V.1    Armstrong, S.A.2
  • 83
    • 54549083228 scopus 로고    scopus 로고
    • H3K79 methylation profi les defi ne murine and human MLL-AF4 leukemias
    • Krivtsov AV et al (2008) H3K79 methylation profi les defi ne murine and human MLL-AF4 leukemias. Cancer Cell 14(5):355-368
    • (2008) Cancer Cell , vol.14 , Issue.5 , pp. 355-368
    • Krivtsov, A.V.1
  • 84
    • 33846783261 scopus 로고    scopus 로고
    • Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase
    • Kubicek S et al (2007) Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase. Mol Cell 25(3):473-481
    • (2007) Mol Cell , vol.25 , Issue.3 , pp. 473-481
    • Kubicek, S.1
  • 85
    • 34547793043 scopus 로고    scopus 로고
    • Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression
    • Lan F et al (2007) Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression. Nature 448(7154):718-722
    • (2007) Nature , vol.448 , Issue.7154 , pp. 718-722
    • Lan, F.1
  • 86
    • 38349087546 scopus 로고    scopus 로고
    • The multiple myeloma associated MMSET gene contributes to cellular adhesion, clonogenic growth, and tumorigenicity
    • Lauring J et al (2008) The multiple myeloma associated MMSET gene contributes to cellular adhesion, clonogenic growth, and tumorigenicity. Blood 111(2):856-864
    • (2008) Blood , vol.111 , Issue.2 , pp. 856-864
    • Lauring, J.1
  • 87
    • 29144525954 scopus 로고    scopus 로고
    • The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair
    • Lee SH et al (2005) The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair. Proc Natl Acad Sci USA 102(50): 18075-18080
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.50 , pp. 18075-18080
    • Lee, S.H.1
  • 88
    • 0036340237 scopus 로고    scopus 로고
    • The core of the polycomb repressive complex is compositionally and functionally conserved in fl ies and humans
    • Levine SS et al (2002) The core of the polycomb repressive complex is compositionally and functionally conserved in fl ies and humans. Mol Cell Biol 22(17):6070-6078
    • (2002) Mol Cell Biol , vol.22 , Issue.17 , pp. 6070-6078
    • Levine, S.S.1
  • 89
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specifi c read-out of histone H3K4me3 by the BPTF PHD fi nger of NURF
    • Li H et al (2006) Molecular basis for site-specifi c read-out of histone H3K4me3 by the BPTF PHD fi nger of NURF. Nature 442(7098):91-95
    • (2006) Nature , vol.442 , Issue.7098 , pp. 91-95
    • Li, H.1
  • 90
    • 71749121455 scopus 로고    scopus 로고
    • The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate
    • Li Y et al (2009) The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate. J Biol Chem 284(49):34283-34295
    • (2009) J Biol Chem , vol.284 , Issue.49 , pp. 34283-34295
    • Li, Y.1
  • 91
    • 77950390899 scopus 로고    scopus 로고
    • H4R3 methylation facilitates beta-globin transcription by regulating histone acetyltransferase binding and H3 acetylation
    • Li X et al (2010) H4R3 methylation facilitates beta-globin transcription by regulating histone acetyltransferase binding and H3 acetylation. Blood 115(10):2028-2037
    • (2010) Blood , vol.115 , Issue.10 , pp. 2028-2037
    • Li, X.1
  • 92
    • 77956636685 scopus 로고    scopus 로고
    • Epigenetic regulation of cancer growth by histone demethylases
    • Lim S et al (2010a) Epigenetic regulation of cancer growth by histone demethylases. Int J Cancer 127(9):1991-1998
    • (2010) Int J Cancer , vol.127 , Issue.9 , pp. 1991-1998
    • Lim, S.1
  • 93
    • 77950868547 scopus 로고    scopus 로고
    • Lysine-specifi c demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology
    • Lim S et al (2010b) Lysine-specifi c demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology. Carcinogenesis 31(3):512-520
    • (2010) Carcinogenesis , vol.31 , Issue.3 , pp. 512-520
    • Lim, S.1
  • 94
    • 34047272162 scopus 로고    scopus 로고
    • The telomerase reverse transcriptase (hTERT) gene is a direct target of the histone methyltransferase SMYD3
    • Liu C et al (2007) The telomerase reverse transcriptase (hTERT) gene is a direct target of the histone methyltransferase SMYD3. Cancer Res 67(6):2626-2631
    • (2007) Cancer Res , vol.67 , Issue.6 , pp. 2626-2631
    • Liu, C.1
  • 95
    • 73249124141 scopus 로고    scopus 로고
    • Discovery of a 2, 4-diamino-7-aminoalkoxyquinazoline as a potent and selective inhibitor of histone lysine methyltransferase G9a
    • Liu F et al (2009a) Discovery of a 2, 4-diamino-7-aminoalkoxyquinazoline as a potent and selective inhibitor of histone lysine methyltransferase G9a. J Med Chem 52(24):7950-7953
    • (2009) J Med Chem , vol.52 , Issue.24 , pp. 7950-7953
    • Liu, F.1
  • 96
    • 72449186524 scopus 로고    scopus 로고
    • Genomic amplifi cation and oncogenic properties of the GASC1 histone demethylase gene in breast cancer
    • Liu G et al (2009b) Genomic amplifi cation and oncogenic properties of the GASC1 histone demethylase gene in breast cancer. Oncogene 28(50):4491-4500
    • (2009) Oncogene , vol.28 , Issue.50 , pp. 4491-4500
    • Liu, G.1
  • 97
    • 77955363182 scopus 로고    scopus 로고
    • Protein lysine methyltransferase G9a inhibitors: Design, syn thesis, and structure activity relationships of 2, 4-diamino-7-aminoalkoxy-quinazolines
    • Liu F et al (2010) Protein lysine methyltransferase G9a inhibitors: design, synthesis, and structure activity relationships of 2, 4-diamino-7-aminoalkoxy-quinazolines. J Med Chem 53(15):5844-5857
    • (2010) J Med Chem , vol.53 , Issue.15 , pp. 5844-5857
    • Liu, F.1
  • 98
    • 67650096728 scopus 로고    scopus 로고
    • The HP1alpha-CAF1-SetDB1-containing complex provides H3K9me1 for Suv39-mediated K9me3 in pericentric heterochromatin
    • Loyola A et al (2009) The HP1alpha-CAF1-SetDB1-containing complex provides H3K9me1 for Suv39-mediated K9me3 in pericentric heterochromatin. EMBO Rep 10(7):769-775
    • (2009) EMBO Rep , vol.10 , Issue.7 , pp. 769-775
    • Loyola, A.1
  • 99
    • 69449099439 scopus 로고    scopus 로고
    • Effects of SMYD3 overexpression on transformation, serum dependence, and apoptosis sensitivity in NIH3T3 cells
    • Luo XG et al (2009) Effects of SMYD3 overexpression on transformation, serum dependence, and apoptosis sensitivity in NIH3T3 cells. IUBMB Life 61(6):679-684
    • (2009) IUBMB Life , vol.61 , Issue.6 , pp. 679-684
    • Luo, X.G.1
  • 100
    • 33748359520 scopus 로고    scopus 로고
    • Involvement of arginine methyltransferase CARM1 in androgen receptor function and prostate cancer cell viability
    • Majumder S et al (2006) Involvement of arginine methyltransferase CARM1 in androgen receptor function and prostate cancer cell viability. Prostate 66(12):1292-1301
    • (2006) Prostate , vol.66 , Issue.12 , pp. 1292-1301
    • Majumder, S.1
  • 101
    • 55949132133 scopus 로고    scopus 로고
    • Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms
    • Margueron R et al (2008) Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol Cell 32(4):503-518
    • (2008) Mol Cell , vol.32 , Issue.4 , pp. 503-518
    • Margueron, R.1
  • 102
    • 0037310947 scopus 로고    scopus 로고
    • The Tudor domain 'Royal Family': Tudor, plant Agenet, Chromo, PWWP and MBT domains
    • Maurer-Stroh S et al (2003) The Tudor domain 'Royal Family': Tudor, plant Agenet, Chromo, PWWP and MBT domains. Trends Biochem Sci 28(2):69-74
    • (2003) Trends Biochem Sci , vol.28 , Issue.2 , pp. 69-74
    • Maurer-Stroh, S.1
  • 103
    • 0344837759 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase
    • Min J et al (2003) Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell 112(5):711-723
    • (2003) Cell , vol.112 , Issue.5 , pp. 711-723
    • Min, J.1
  • 104
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specifi city
    • Miranda TB et al (2004) PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specifi city. J Biol Chem 279(22):22902-22907
    • (2004) J Biol Chem , vol.279 , Issue.22 , pp. 22902-22907
    • Miranda, T.B.1
  • 105
    • 75749124332 scopus 로고    scopus 로고
    • Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin
    • Morin RD et al (2010) Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin. Nat Genet 42(2):181-185
    • (2010) Nat Genet , vol.42 , Issue.2 , pp. 181-185
    • Morin, R.D.1
  • 106
    • 33845789120 scopus 로고    scopus 로고
    • The activity and stability of the transcriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation
    • Naeem H et al (2007) The activity and stability of the transcriptional coactivator p/CIP/SRC-3 are regulated by CARM1-dependent methylation. Mol Cell Biol 27(1):120-134
    • (2007) Mol Cell Biol , vol.27 , Issue.1 , pp. 120-134
    • Naeem, H.1
  • 107
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng HH et al (2002a) Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev 16(12):1518-1527
    • (2002) Genes Dev , vol.16 , Issue.12 , pp. 1518-1527
    • Ng, H.H.1
  • 108
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for effi cient Dot1-mediated methylation of histone H3 lysine 79
    • Ng HH et al (2002b) Ubiquitination of histone H2B by Rad6 is required for effi cient Dot1-mediated methylation of histone H3 lysine 79. J Biol Chem 277(38):34655-34657
    • (2002) J Biol Chem , vol.277 , Issue.38 , pp. 34655-34657
    • Ng, H.H.1
  • 109
    • 64749106929 scopus 로고    scopus 로고
    • Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development
    • Oda H et al (2009) Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development. Mol Cell Biol 29(8):2278-2295
    • (2009) Mol Cell Biol , vol.29 , Issue.8 , pp. 2278-2295
    • Oda, H.1
  • 110
    • 17444375685 scopus 로고    scopus 로고
    • HDOT1L links histone methylation to leukemogenesis
    • Okada Y et al (2005) hDOT1L links histone methylation to leukemogenesis. Cell 121(2):167-178
    • (2005) Cell , vol.121 , Issue.2 , pp. 167-178
    • Okada, Y.1
  • 111
    • 34547725157 scopus 로고    scopus 로고
    • DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA
    • Ooi SK et al (2007) DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA. Nature 448(7154):714-717
    • (2007) Nature , vol.448 , Issue.7154 , pp. 714-717
    • Ooi, S.K.1
  • 112
    • 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 et al (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(21):9630-9645
    • (2004) Mol Cell Biol , vol.24 , Issue.21 , pp. 9630-9645
    • Pal, S.1
  • 113
    • 34547741040 scopus 로고    scopus 로고
    • Low levels of miR-92b/96 induce PRMT5 translation and H3R8/H4R3 methylation in mantle cell lymphoma
    • Pal S et al (2007) Low levels of miR-92b/96 induce PRMT5 translation and H3R8/H4R3 methylation in mantle cell lymphoma. EMBO J 26(15):3558-3569
    • (2007) EMBO J , vol.26 , Issue.15 , pp. 3558-3569
    • Pal, S.1
  • 114
    • 37549014575 scopus 로고    scopus 로고
    • Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle
    • Pesavento JJ et al (2008) Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle. Mol Cell Biol 28(1):468-486
    • (2008) Mol Cell Biol , vol.28 , Issue.1 , pp. 468-486
    • Pesavento, J.J.1
  • 115
    • 9144268924 scopus 로고    scopus 로고
    • Partitioning and plasticity of repressive histone methylation states in mammalian chromatin
    • Peters AH et al (2003) Partitioning and plasticity of repressive histone methylation states in mammalian chromatin. Mol Cell 12(6):1577-1589
    • (2003) Mol Cell , vol.12 , Issue.6 , pp. 1577-1589
    • Peters, A.H.1
  • 116
    • 47849115661 scopus 로고    scopus 로고
    • Pyrazole inhibitors of coactivator associated arginine methyltransferase 1 (CARM1)
    • Purandare AV et al (2008) Pyrazole inhibitors of coactivator associated arginine methyltransferase 1 (CARM1). Bioorg Med Chem Lett 18(15):4438-4441
    • (2008) Bioorg Med Chem Lett , vol.18 , Issue.15 , pp. 4438-4441
    • Purandare, A.V.1
  • 117
    • 27144458417 scopus 로고    scopus 로고
    • Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide
    • Rao B et al (2005) Dimethylation of histone H3 at lysine 36 demarcates regulatory and nonregulatory chromatin genome-wide. Mol Cell Biol 25(21):9447-9459
    • (2005) Mol Cell Biol , vol.25 , Issue.21 , pp. 9447-9459
    • Rao, B.1
  • 118
    • 43749093216 scopus 로고    scopus 로고
    • Protein lysine methyltransferase G9a acts on non-histone targets
    • Rathert P et al (2008) Protein lysine methyltransferase G9a acts on non-histone targets. Nat Chem Biol 4(6):344-346
    • (2008) Nat Chem Biol , vol.4 , Issue.6 , pp. 344-346
    • Rathert, P.1
  • 119
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specifi c histone H3 methyltransferases
    • Rea S et al (2000) Regulation of chromatin structure by site-specifi c histone H3 methyltransferases. Nature 406(6796):593-599
    • (2000) Nature , vol.406 , Issue.6796 , pp. 593-599
    • Rea, S.1
  • 120
    • 79960367903 scopus 로고    scopus 로고
    • Chemogenetic analysis of human protein methyltransferases
    • Richon VM et al (2011) Chemogenetic analysis of human protein methyltransferases. Chem Biol Drug Des 78(2):199-210
    • (2011) Chem Biol Drug des , vol.78 , Issue.2 , pp. 199-210
    • Richon, V.M.1
  • 121
    • 0037093259 scopus 로고    scopus 로고
    • NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15)
    • Rosati R et al (2002) NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15). Blood 99(10):3857-3860
    • (2002) Blood , vol.99 , Issue.10 , pp. 3857-3860
    • Rosati, R.1
  • 122
    • 33846019277 scopus 로고    scopus 로고
    • Methylation of lysine 4 on histone H3: Intricacy of writing and reading a single epigenetic mark
    • Ruthenburg AJ, Allis CD, Wysocka J (2007) Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Mol Cell 25(1):15-30
    • (2007) Mol Cell , vol.25 , Issue.1 , pp. 15-30
    • Ruthenburg, A.J.1    Allis, C.D.2    Wysocka, J.3
  • 123
    • 8844248619 scopus 로고    scopus 로고
    • Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage
    • Sanders SL et al (2004) Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. Cell 119(5):603-614
    • (2004) Cell , vol.119 , Issue.5 , pp. 603-614
    • Sanders, S.L.1
  • 124
    • 0037179716 scopus 로고    scopus 로고
    • Active genes are tri-methylated at K4 of histone H3
    • Santos-Rosa H et al (2002) Active genes are tri-methylated at K4 of histone H3. Nature 419(6905):407-411
    • (2002) Nature , vol.419 , Issue.6905 , pp. 407-411
    • Santos-Rosa, H.1
  • 125
    • 42149149895 scopus 로고    scopus 로고
    • Ezh2 requires PHF1 to effi ciently catalyze H3 lysine 27 trimethylation in vivo
    • Sarma K et al (2008) Ezh2 requires PHF1 to effi ciently catalyze H3 lysine 27 trimethylation in vivo. Mol Cell Biol 28(8):2718-2731
    • (2008) Mol Cell Biol , vol.28 , Issue.8 , pp. 2718-2731
    • Sarma, K.1
  • 126
    • 33846649587 scopus 로고    scopus 로고
    • Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer
    • Schlesinger Y et al (2007) Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat Genet 39(2):232-236
    • (2007) Nat Genet , vol.39 , Issue.2 , pp. 232-236
    • Schlesinger, Y.1
  • 127
    • 1342268289 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation patterns in higher eukaryotic genes
    • Schneider R et al (2004) Histone H3 lysine 4 methylation patterns in higher eukaryotic genes. Nat Cell Biol 6(1):73-77
    • (2004) Nat Cell Biol , vol.6 , Issue.1 , pp. 73-77
    • Schneider, R.1
  • 128
    • 2642542643 scopus 로고    scopus 로고
    • A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin
    • Schotta G et al (2004) A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev 18(11):1251-1262
    • (2004) Genes Dev , vol.18 , Issue.11 , pp. 1251-1262
    • Schotta, G.1
  • 129
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • Schubert HL, Blumenthal RM, Cheng X (2003) Many paths to methyltransfer: a chronicle of convergence. Trends Biochem Sci 28(6):329-335
    • (2003) Trends Biochem Sci , vol.28 , Issue.6 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 130
    • 62449197931 scopus 로고    scopus 로고
    • Lysine-specifi c demethylase 1 is strongly expressed in poorly differentiated neuroblastoma: Implications for therapy
    • Schulte JH et al (2009) Lysine-specifi c demethylase 1 is strongly expressed in poorly differentiated neuroblastoma: implications for therapy. Cancer Res 69(5):2065-2071
    • (2009) Cancer Res , vol.69 , Issue.5 , pp. 2065-2071
    • Schulte, J.H.1
  • 131
    • 0037089626 scopus 로고    scopus 로고
    • SETDB1: A novel KAP-1-associated histone H3, lysine 9-specifi c methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-fi nger proteins
    • Schultz DC et al (2002) SETDB1: a novel KAP-1-associated histone H3, lysine 9-specifi c methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-fi nger proteins. Genes Dev 16(8):919-932
    • (2002) Genes Dev , vol.16 , Issue.8 , pp. 919-932
    • Schultz, D.C.1
  • 132
    • 22544461653 scopus 로고    scopus 로고
    • Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1
    • Shahbazian MD, Zhang K, Grunstein M (2005) Histone H2B ubiquitylation controls processive methylation but not monomethylation by Dot1 and Set1. Mol Cell 19(2):271-277
    • (2005) Mol Cell , vol.19 , Issue.2 , pp. 271-277
    • Shahbazian, M.D.1    Zhang, K.2    Grunstein, M.3
  • 133
    • 33846025127 scopus 로고    scopus 로고
    • Dynamic regulation of histone lysine methylation by demethylases
    • Shi Y, Whetstine JR (2007) Dynamic regulation of histone lysine methylation by demethylases. Mol Cell 25(1):1-14
    • (2007) Mol Cell , vol.25 , Issue.1 , pp. 1-14
    • Shi, Y.1    Whetstine, J.R.2
  • 134
    • 33745868054 scopus 로고    scopus 로고
    • ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
    • Shi X et al (2006) ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442(7098):96-99
    • (2006) Nature , vol.442 , Issue.7098 , pp. 96-99
    • Shi, X.1
  • 135
    • 84861494738 scopus 로고    scopus 로고
    • PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential
    • Shia WJ et al (2012) PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential. Blood 119(21):4953-4962
    • (2012) Blood , vol.119 , Issue.21 , pp. 4953-4962
    • Shia, W.J.1
  • 136
    • 44649139771 scopus 로고    scopus 로고
    • Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation
    • Shilatifard A (2008) Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation. Curr Opin Cell Biol 20(3):341-348
    • (2008) Curr Opin Cell Biol , vol.20 , Issue.3 , pp. 341-348
    • Shilatifard, A.1
  • 137
    • 55949136562 scopus 로고    scopus 로고
    • Roles of the EZH2 histone methyltransferase in cancer epigenetics
    • Simon JA, Lange CA (2008) Roles of the EZH2 histone methyltransferase in cancer epigenetics. Mutat Res 647(1-2):21-29
    • (2008) Mutat Res , vol.647 , Issue.1-2 , pp. 21-29
    • Simon, J.A.1    Lange, C.A.2
  • 138
    • 33751116960 scopus 로고    scopus 로고
    • Histone H3 Lys 4 methylation: Caught in a bind
    • Sims RJ 3rd, Reinberg D (2006) Histone H3 Lys 4 methylation: caught in a bind Genes Dev 20(20):2779-2786
    • (2006) Genes Dev , vol.20 , Issue.20 , pp. 2779-2786
    • Sims, R.J.1    Reinberg, D.2
  • 139
    • 0031658303 scopus 로고    scopus 로고
    • Identifi cation of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae
    • Singer MS et al (1998) Identifi cation of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae. Genetics 150(2):613-632
    • (1998) Genetics , vol.150 , Issue.2 , pp. 613-632
    • Singer, M.S.1
  • 140
    • 67650770689 scopus 로고    scopus 로고
    • The molecular biology of mixed lineage leukemia
    • Slany RK (2009) The molecular biology of mixed lineage leukemia. Haematologica 94(7): 984-993
    • (2009) Haematologica , vol.94 , Issue.7 , pp. 984-993
    • Slany, R.K.1
  • 141
    • 78650454078 scopus 로고    scopus 로고
    • Coordinated activities of wild-type plus mutant EZH2 drive tumorassociated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas
    • Sneeringer CJ et al (2010) Coordinated activities of wild-type plus mutant EZH2 drive tumorassociated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas. Proc Natl Acad Sci USA 107(49):20980-20985
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.49 , pp. 20980-20985
    • Sneeringer, C.J.1
  • 142
    • 33745604636 scopus 로고    scopus 로고
    • Suz12 binds to silenced regions of the genome in a cell-type-specifi c manner
    • Squazzo SL et al (2006) Suz12 binds to silenced regions of the genome in a cell-type-specifi c manner. Genome Res 16(7):890-900
    • (2006) Genome Res , vol.16 , Issue.7 , pp. 890-900
    • Squazzo, S.L.1
  • 143
    • 0031779421 scopus 로고    scopus 로고
    • WHSC1, a 90 kb SET domain-containing gene, expressed in early development and homologous to a Drosophila dysmorphy gene maps in the Wolf-Hirschhorn syndrome critical region and is fused to IgH in t(4;14) multiple myeloma
    • Stec I et al (1998) WHSC1, a 90 kb SET domain-containing gene, expressed in early development and homologous to a Drosophila dysmorphy gene maps in the Wolf-Hirschhorn syndrome critical region and is fused to IgH in t(4;14) multiple myeloma. Hum Mol Genet 7(7):1071-1082
    • (1998) Hum Mol Genet , vol.7 , Issue.7 , pp. 1071-1082
    • Stec, I.1
  • 144
    • 42149146774 scopus 로고    scopus 로고
    • DOT1L/KMT4 recruitment and H3K79 methylation are ubiquitously coupled with gene transcription in mammalian cells
    • Steger DJ et al (2008) DOT1L/KMT4 recruitment and H3K79 methylation are ubiquitously coupled with gene transcription in mammalian cells. Mol Cell Biol 28(8):2825-2839
    • (2008) Mol Cell Biol , vol.28 , Issue.8 , pp. 2825-2839
    • Steger, D.J.1
  • 145
    • 0033592999 scopus 로고    scopus 로고
    • Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena
    • Strahl BD et al (1999) Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena. Proc Natl Acad Sci USA 96(26): 14967-14972
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.26 , pp. 14967-14972
    • Strahl, B.D.1
  • 146
    • 0037099413 scopus 로고    scopus 로고
    • G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
    • Tachibana M et al (2002) G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev 16(14):1779-1791
    • (2002) Genes Dev , vol.16 , Issue.14 , pp. 1779-1791
    • Tachibana, M.1
  • 147
    • 20144388930 scopus 로고    scopus 로고
    • Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9
    • Tachibana M et al (2005) Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. Genes Dev 19(7):815-826
    • (2005) Genes Dev , vol.19 , Issue.7 , pp. 815-826
    • Tachibana, M.1
  • 148
    • 33644542409 scopus 로고    scopus 로고
    • SmyD1, a histone methyltransferase, is required for myofi bril organization and muscle contraction in zebrafi sh embryos
    • Tan X et al (2006) SmyD1, a histone methyltransferase, is required for myofi bril organization and muscle contraction in zebrafi sh embryos. Proc Natl Acad Sci USA 103(8):2713-2718
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.8 , pp. 2713-2718
    • Tan, X.1
  • 149
    • 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 PN, Herschman HR (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(26):19866-19876
    • (2000) J Biol Chem , vol.275 , Issue.26 , pp. 19866-19876
    • Tang, J.1    Kao, P.N.2    Herschman, H.R.3
  • 150
    • 71749083438 scopus 로고    scopus 로고
    • 1, 2-Diamines as inhibitors of co-activator associated arginine methyltransferase 1 (CARM1)
    • Therrien E et al (2009) 1, 2-Diamines as inhibitors of co-activator associated arginine methyltransferase 1 (CARM1). Bioorg Med Chem Lett 19(23):6725-6732
    • (2009) Bioorg Med Chem Lett , vol.19 , Issue.23 , pp. 6725-6732
    • Therrien, E.1
  • 151
    • 35348916034 scopus 로고    scopus 로고
    • Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains
    • Troffer-Charlier N et al (2007) Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains. EMBO J 26(20):4391-4401
    • (2007) EMBO J , vol.26 , Issue.20 , pp. 4391-4401
    • Troffer-Charlier, N.1
  • 152
    • 32544452237 scopus 로고    scopus 로고
    • Loss of DNA methylation and histone H4 lysine 20 trimethylation in human breast cancer cells is associated with aberrant expression of DNA methyltransferase 1 Suv4-20h2 histone methyltransferase and methyl-binding proteins
    • Tryndyak VP, Kovalchuk O, Pogribny IP (2006) Loss of DNA methylation and histone H4 lysine 20 trimethylation in human breast cancer cells is associated with aberrant expression of DNA methyltransferase 1, Suv4-20h2 histone methyltransferase and methyl-binding proteins. Cancer Biol Ther 5(1):65-70
    • (2006) Cancer Biol Ther , vol.5 , Issue.1 , pp. 65-70
    • Tryndyak, V.P.1    Kovalchuk, O.2    Pogribny, I.P.3
  • 153
    • 58149329023 scopus 로고    scopus 로고
    • Loss of histone H4K20 trimethylation occurs in preneoplasia and infl uences prognosis of non-small cell lung cancer
    • Van Den Broeck A et al (2008) Loss of histone H4K20 trimethylation occurs in preneoplasia and infl uences prognosis of non-small cell lung cancer. Clin Cancer Res 14(22):7237-7245
    • (2008) Clin Cancer Res , vol.14 , Issue.22 , pp. 7237-7245
    • Van Den Broeck, A.1
  • 154
    • 67349203626 scopus 로고    scopus 로고
    • Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer
    • van Haaften G et al (2009) Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer. Nat Genet 41(5):521-523
    • (2009) Nat Genet , vol.41 , Issue.5 , pp. 521-523
    • Van Haaften, G.1
  • 155
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F, Gafken PR, Gottschling DE (2002) Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 109(6):745-756
    • (2002) Cell , vol.109 , Issue.6 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 156
    • 18644382388 scopus 로고    scopus 로고
    • The polycomb group protein EZH2 is involved in progression of prostate cancer
    • Varambally S et al (2002) The polycomb group protein EZH2 is involved in progression of prostate cancer. Nature 419(6907):624-629
    • (2002) Nature , vol.419 , Issue.6907 , pp. 624-629
    • Varambally, S.1
  • 157
    • 79960493567 scopus 로고    scopus 로고
    • A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells
    • Vedadi M et al (2011) A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells. Nat Chem Biol 7(8):566-574
    • (2011) Nat Chem Biol , vol.7 , Issue.8 , pp. 566-574
    • Vedadi, M.1
  • 158
    • 38549179917 scopus 로고    scopus 로고
    • G9a histone methyltransferase contributes to imprinting in the mouse placenta
    • Wagschal A et al (2008) G9a histone methyltransferase contributes to imprinting in the mouse placenta. Mol Cell Biol 28(3):1104-1113
    • (2008) Mol Cell Biol , vol.28 , Issue.3 , pp. 1104-1113
    • Wagschal, A.1
  • 159
    • 68449090273 scopus 로고    scopus 로고
    • Benzo[d]imidazole inhibitors of Coactivator Associated Arginine Methyltransferase 1 (CARM1)-Hit to Lead studies
    • Wan H et al (2009) Benzo[d]imidazole inhibitors of Coactivator Associated Arginine Methyltransferase 1 (CARM1)-Hit to Lead studies. Bioorg Med Chem Lett 19(17): 5063-5066
    • (2009) Bioorg Med Chem Lett , vol.19 , Issue.17 , pp. 5063-5066
    • Wan, H.1
  • 160
    • 0141992115 scopus 로고    scopus 로고
    • MAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression
    • Wang H et al (2003) mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Mol Cell 12(2):475-487
    • (2003) Mol Cell , vol.12 , Issue.2 , pp. 475-487
    • Wang, H.1
  • 161
    • 34347392874 scopus 로고    scopus 로고
    • NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis
    • Wang GG et al (2007) NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis. Nat Cell Biol 9(7):804-812
    • (2007) Nat Cell Biol , vol.9 , Issue.7 , pp. 804-812
    • Wang, G.G.1
  • 162
    • 43249122483 scopus 로고    scopus 로고
    • Knockdown of SMYD3 by RNA interference inhibits cervical carcinoma cell growth and invasion in vitro
    • Wang SZ et al (2008a) Knockdown of SMYD3 by RNA interference inhibits cervical carcinoma cell growth and invasion in vitro. BMB Rep 41(4):294-299
    • (2008) BMB Rep , vol.41 , Issue.4 , pp. 294-299
    • Wang, S.Z.1
  • 163
    • 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, Sif S (2008b) Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells. Mol Cell Biol 28(20):6262-6277
    • (2008) Mol Cell Biol , vol.28 , Issue.20 , pp. 6262-6277
    • Wang, L.1    Pal, S.2    Sif, S.3
  • 164
    • 71949107301 scopus 로고    scopus 로고
    • Global analysis of H3K4 methylation defi nes MLL family member targets and points to a role for MLL1-mediated H3K4 methylation in the regulation of transcriptional initiation by RNA polymerase II
    • Wang P et al (2009) Global analysis of H3K4 methylation defi nes MLL family member targets and points to a role for MLL1-mediated H3K4 methylation in the regulation of transcriptional initiation by RNA polymerase II. Mol Cell Biol 29(22):6074-6085
    • (2009) Mol Cell Biol , vol.29 , Issue.22 , pp. 6074-6085
    • Wang, P.1
  • 165
    • 56649103900 scopus 로고    scopus 로고
    • Deregulation of histone lysine methyltransferases contributes to oncogenic transformation of human bronchoepithelial cells
    • Watanabe H et al (2008) Deregulation of histone lysine methyltransferases contributes to oncogenic transformation of human bronchoepithelial cells. Cancer Cell Int 8:15
    • (2008) Cancer Cell Int , vol.8 , pp. 15
    • Watanabe, H.1
  • 166
    • 0028791842 scopus 로고
    • Pharmacokinetic and pharmacodynamic properties and therapeutic use of bunazosin in hypertension A review
    • Weidinger G (1995) Pharmacokinetic and pharmacodynamic properties and therapeutic use of bunazosin in hypertension. A review. Arzneimittelforschung 45(11):1166-1171
    • (1995) Arzneimittelforschung , vol.45 , Issue.11 , pp. 1166-1171
    • Weidinger, G.1
  • 167
    • 77949351403 scopus 로고    scopus 로고
    • Screening for inhibitors of low-affi nity epigenetic peptide-protein interactions: An AlphaScreen-based assay for antagonists of methyl-lysine binding proteins
    • Wigle TJ et al (2010) Screening for inhibitors of low-affi nity epigenetic peptide-protein interactions: an AlphaScreen-based assay for antagonists of methyl-lysine binding proteins. J Biomol Screen 15(1):62-71
    • (2010) J Biomol Screen , vol.15 , Issue.1 , pp. 62-71
    • Wigle, T.J.1
  • 168
    • 77952488976 scopus 로고    scopus 로고
    • Structural biology of human H3K9 methyltransferases
    • Wu H et al (2010) Structural biology of human H3K9 methyltransferases. PLoS One 5(1):e8570
    • (2010) PLoS One , vol.5 , Issue.1 , pp. e8570
    • Wu, H.1
  • 169
    • 33745839365 scopus 로고    scopus 로고
    • A PHD fi nger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
    • Wysocka J et al (2006) A PHD fi nger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 442(7098):86-90
    • (2006) Nature , vol.442 , Issue.7098 , pp. 86-90
    • Wysocka, J.1
  • 170
    • 37649023563 scopus 로고    scopus 로고
    • JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer
    • Xiang Y et al (2007) JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer. Proc Natl Acad Sci USA 104(49):19226-19231
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.49 , pp. 19226-19231
    • Xiang, Y.1
  • 171
    • 22344455665 scopus 로고    scopus 로고
    • Specifi city and mechanism of the histone methyltransferase Pr-Set7
    • Xiao B et al (2005) Specifi city and mechanism of the histone methyltransferase Pr-Set7. Genes Dev 19(12):1444-1454
    • (2005) Genes Dev , vol.19 , Issue.12 , pp. 1444-1454
    • Xiao, B.1
  • 172
    • 0038003140 scopus 로고    scopus 로고
    • Role of histone methyltransferase G9a in CpG methylation of the Prader-Willi syndrome imprinting center
    • Xin Z et al (2003) Role of histone methyltransferase G9a in CpG methylation of the Prader-Willi syndrome imprinting center. J Biol Chem 278(17):14996-15000
    • (2003) J Biol Chem , vol.278 , Issue.17 , pp. 14996-15000
    • Xin, Z.1
  • 173
    • 0942290543 scopus 로고    scopus 로고
    • A methylation-mediator complex in hormone signaling
    • Xu W et al (2004) A methylation-mediator complex in hormone signaling. Genes Dev 18(2):144-156
    • (2004) Genes Dev , vol.18 , Issue.2 , pp. 144-156
    • Xu, W.1
  • 174
    • 78650613168 scopus 로고    scopus 로고
    • Binding of different histone marks differentially regulates the activity and specifi city of polycomb repressive complex 2 (PRC2)
    • Xu C et al (2010) Binding of different histone marks differentially regulates the activity and specifi city of polycomb repressive complex 2 (PRC2). Proc Natl Acad Sci USA 107(45):19266-19271
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.45 , pp. 19266-19271
    • Xu, C.1
  • 175
    • 0034282790 scopus 로고    scopus 로고
    • Identifi cation of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines
    • Yang ZQ et al (2000) Identifi cation of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines. Cancer Res 60(17):4735-4739
    • (2000) Cancer Res , vol.60 , Issue.17 , pp. 4735-4739
    • Yang, Z.Q.1
  • 176
    • 45549088504 scopus 로고    scopus 로고
    • Preferential dimethylation of histone H4 lysine 20 by Suv4-20
    • Yang H et al (2008) Preferential dimethylation of histone H4 lysine 20 by Suv4-20. J Biol Chem 283(18):12085-12092
    • (2008) J Biol Chem , vol.283 , Issue.18 , pp. 12085-12092
    • Yang, H.1
  • 177
    • 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 et al (2011) Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation. Blood 117(8):2451-2459
    • (2011) Blood , vol.117 , Issue.8 , pp. 2451-2459
    • Yap, D.B.1
  • 178
    • 67650120109 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein L Is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo
    • Yuan W et al (2009) Heterogeneous nuclear ribonucleoprotein L Is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo. J Biol Chem 284(23):15701-15707
    • (2009) J Biol Chem , vol.284 , Issue.23 , pp. 15701-15707
    • Yuan, W.1
  • 179
    • 35348861410 scopus 로고    scopus 로고
    • Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase
    • Yue WW et al (2007) Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase. EMBO J 26(20):4402-4412
    • (2007) EMBO J , vol.26 , Issue.20 , pp. 4402-4412
    • Yue, W.W.1
  • 180
    • 37349096313 scopus 로고    scopus 로고
    • Histone lysine methyltransferase SET7/9: Formation of a water channel precedes each methyl transfer
    • Zhang X, Bruice TC (2007) Histone lysine methyltransferase SET7/9: formation of a water channel precedes each methyl transfer. Biochemistry 46(51):14838-14844
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 14838-14844
    • Zhang, X.1    Bruice, T.C.2
  • 181
    • 44449162039 scopus 로고    scopus 로고
    • Enzymatic mechanism and product specifi city of SET-domain protein lysine methyltransferases
    • Zhang X, Bruice TC (2008) Enzymatic mechanism and product specifi city of SET-domain protein lysine methyltransferases. Proc Natl Acad Sci USA 105(15):5728-5732
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.15 , pp. 5728-5732
    • Zhang, X.1    Bruice, T.C.2
  • 182
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • Zhang X, Cheng X (2003) Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure 11(5):509-520
    • (2003) Structure , vol.11 , Issue.5 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 183
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • Zhang X, Zhou L, Cheng X (2000) Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. EMBO J 19(14):3509-3519
    • (2000) EMBO J , vol.19 , Issue.14 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3
  • 184
    • 62049086288 scopus 로고    scopus 로고
    • PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing
    • Zhao Q et al (2009) PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing. Nat Struct Mol Biol 16(3):304-311
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.3 , pp. 304-311
    • Zhao, Q.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.