메뉴 건너뛰기




Volumn 67, Issue , 2011, Pages 107-124

Dynamics of histone lysine methylation: Structures of methyl writers and erasers

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; BIX 01294; HISTONE; HISTONE DEACETYLASE; HISTONE LYSINE METHYLTRANSFERASE; HISTONE LYSINE SPECIFIC DEMETHYLASE; JUMONJI DOMAIN CONTAINING HISTONE DEMETHYLASE 1; KIAA1718 PROTEIN; METHYLTRANSFERASE INHIBITOR; PROTEIN JMJD2A; PROTEIN PHF8; UNCLASSIFIED DRUG; HISTONE DEMETHYLASE; LYSINE;

EID: 79952112943     PISSN: 0071786X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-7643-8989-5_6     Document Type: Article
Times cited : (47)

References (104)
  • 2
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • DOI 10.1038/nrg1945, PII NRG1945
    • Klose RJ, Kallin EM, Zhang Y (2006) JmjC-domain-containing proteins and histone demethylation. Nat Rev Genet 7:715-727 (Pubitemid 44260007)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.9 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 3
    • 35349006314 scopus 로고    scopus 로고
    • Histone lysine demethylases: Emerging roles in development, physiology and disease
    • DOI 10.1038/nrg2218, PII NRG2218
    • Shi Y (2007) Histone lysine demethylases: emerging roles in development, physiology and disease. Nat Rev Genet 8:829-833 (Pubitemid 47609092)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.11 , pp. 829-833
    • Shi, Y.1
  • 4
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • DOI 10.1038/nature04802, PII NATURE04802
    • Li H, Ilin S, Wang W, Duncan EM, Wysocka J, Allis CD, Patel DJ (2006) Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442:91-95 (Pubitemid 44064215)
    • (2006) Nature , vol.442 , Issue.7098 , pp. 91-95
    • Li, H.1    Ilin, S.2    Wang, W.3    Duncan, E.M.4    Wysocka, J.5    Allis, C.D.6    Patel, D.J.7
  • 7
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • DOI 10.1038/35065132
    • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (2001) Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410:116-120 (Pubitemid 32225847)
    • (2001) Nature , vol.410 , Issue.6824 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 10
    • 41649092299 scopus 로고    scopus 로고
    • Roles of the Clr4 methyltransferase complex in nucleation, spreading and maintenance of heterochromatin
    • DOI 10.1038/nsmb.1406, PII NSMB1406
    • Zhang K, Mosch K, Fischle W, Grewal SI (2008) Roles of the Clr4 methyltransferase complex in nucleation, spreading and maintenance of heterochromatin. Nat Struct Mol Biol 15:381-388 (Pubitemid 351483395)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.4 , pp. 381-388
    • Zhang, K.1    Mosch, K.2    Fischle, W.3    Grewal, S.I.S.4
  • 11
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • DOI 10.1038/nrm1761, PII N1761
    • Martin C, Zhang Y (2005) The diverse functions of histone lysine methylation. Nat Rev Mol Cell Biol 6:838-849 (Pubitemid 41568733)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.11 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 13
    • 0036683308 scopus 로고    scopus 로고
    • Unsafe SETs: Histone lysine methyltransferases and cancer
    • DOI 10.1016/S0968-0004(02)02141-2, PII S0968000402021412
    • Schneider R, Bannister AJ, Kouzarides T (2002) Unsafe SETs: histone lysine methyltransferases and cancer. Trends Biochem Sci 27:396-402 (Pubitemid 34874749)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.8 , pp. 396-402
    • Schneider, R.1    Bannister, A.J.2    Kouzarides, T.3
  • 14
    • 70349780606 scopus 로고    scopus 로고
    • The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors
    • Spannhoff A, Hauser AT, Heinke R, Sippl W, Jung M (2009) The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors. ChemMedChem 4:1568-1582
    • (2009) ChemMedChem , vol.4 , pp. 1568-1582
    • Spannhoff, A.1    Hauser, A.T.2    Heinke, R.3    Sippl, W.4    Jung, M.5
  • 15
    • 55949109901 scopus 로고    scopus 로고
    • Cancer treatment of the future: Inhibitors of histone methyltransferases
    • Spannhoff A, Sippl W, Jung M (2009) Cancer treatment of the future: inhibitors of histone methyltransferases. Int J Biochem Cell Biol 41:4-11
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 4-11
    • Spannhoff, A.1    Sippl, W.2    Jung, M.3
  • 16
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • DOI 10.1016/S0092-8674(02)00759-6
    • van Leeuwen F, Gafken PR, Gottschling DE (2002) Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 109:745-756 (Pubitemid 34727348)
    • (2002) Cell , vol.109 , Issue.6 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 17
    • 0344837759 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human Dot1L, a non-SET domain nucleosomal histone methyltransferase
    • DOI 10.1016/S0092-8674(03)00114-4
    • Min J, Feng Q, Li Z, Zhang Y, Xu RM (2003) Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell 112:711-723 (Pubitemid 36331782)
    • (2003) Cell , vol.112 , Issue.5 , pp. 711-723
    • Min, J.1    Feng, Q.2    Li, Z.3    Zhang, Y.4    Xu, R.-M.5
  • 18
    • 5644261221 scopus 로고    scopus 로고
    • Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase
    • DOI 10.1074/jbc.M405902200
    • Sawada K, Yang Z, Horton JR, Collins RE, Zhang X, Cheng X (2004) Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase. J Biol Chem 279:43296-43306 (Pubitemid 39372225)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 43296-43306
    • Sawada, K.1    Yang, Z.2    Horton, J.R.3    Collins, R.E.4    Zhang, X.5    Cheng, X.6
  • 20
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: Protein lysine methyltransferases
    • Dillon SC, Zhang X, Trievel RC, Cheng X (2005) The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol 6:227
    • (2005) Genome Biol , vol.6 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3    Cheng, X.4
  • 21
    • 33845487512 scopus 로고    scopus 로고
    • SET domain protein lysine methyltransferases: Structure, specificity and catalysis
    • DOI 10.1007/s00018-006-6274-5
    • Qian C, Zhou MM (2006) SET domain protein lysine methyltransferases: structure, specificity and catalysis. Cell Mol Life Sci 63:2755-2763 (Pubitemid 44913316)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.23 , pp. 2755-2763
    • Qian, C.1    Zhou, M.-M.2
  • 22
    • 34247493994 scopus 로고    scopus 로고
    • Histone-modifying enzymes: Encrypting an enigmatic epigenetic code
    • DOI 10.1016/j.sbi.2006.10.002, PII S0959440X06001746, Catalysis and Regulation / Proteins
    • Couture JF, Trievel RC (2006) Histone-modifying enzymes: encrypting an enigmatic epigenetic code. Curr Opin Struct Biol 16:753-760 (Pubitemid 44827726)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.6 , pp. 753-760
    • Couture, J.-F.1    Trievel, R.C.2
  • 23
    • 34147149505 scopus 로고    scopus 로고
    • Structural dynamics of protein lysine methylation and demethylation
    • DOI 10.1016/j.mrfmmm.2006.05.041, PII S0027510707000279, Chromatin: Repair, Remodeling and Regulation
    • Cheng X, Zhang X (2007) Structural dynamics of protein lysine methylation and demethylation. Mutat Res/Fundam Mol Mech Mutagen 618:102-115 (Pubitemid 46574740)
    • (2007) Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis , vol.618 , Issue.1-2 , pp. 102-115
    • Cheng, X.1    Zhang, X.2
  • 25
    • 33845786515 scopus 로고    scopus 로고
    • The control of histone lysine methylation in epigenetic regulation
    • DOI 10.1016/j.biochi.2006.07.009, PII S0300908406001507
    • Volkel P, Angrand PO (2007) The control of histone lysine methylation in epigenetic regulation. Biochimie 89:1-20 (Pubitemid 44970511)
    • (2007) Biochimie , vol.89 , Issue.1 , pp. 1-20
    • Volkel, P.1    Angrand, P.-O.2
  • 26
    • 0042164227 scopus 로고    scopus 로고
    • Structural basis for the product specificity of histone lysine methyltransferases
    • DOI 10.1016/S1097-2765(03)00224-7
    • Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X (2003) Structural basis for the product specificity of histone lysine methyltransferases. Mol Cell 12:177-185 (Pubitemid 36957834)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 177-185
    • Zhang, X.1    Yang, Z.2    Khan, S.I.3    Horton, J.R.4    Tamaru, H.5    Selker, E.U.6    Cheng, X.7
  • 29
    • 67650091137 scopus 로고    scopus 로고
    • Regulation of H3K4 trimethylation via Cps40 (Spp 1) of COMPASS is monoubiquitination independent: Implication for a Phe/Tyr switch by the catalytic domain of Set1
    • Takahashi YH, Lee JS, Swanson SK, Saraf A, Florens L, Washburn MP, Trievel RC, Shilatifard A (2009) Regulation of H3K4 trimethylation via Cps40 (Spp 1) of COMPASS is monoubiquitination independent: implication for a Phe/Tyr switch by the catalytic domain of Set1. Mol Cell Biol 29:3478-3486
    • (2009) Mol Cell Biol , vol.29 , pp. 3478-3486
    • Takahashi, Y.H.1    Lee, J.S.2    Swanson, S.K.3    Saraf, A.4    Florens, L.5    Washburn, M.P.6    Trievel, R.C.7    Shilatifard, A.8
  • 30
    • 0037020217 scopus 로고    scopus 로고
    • Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase
    • Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X (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    Selker, E.U.6    Cheng, X.7
  • 35
    • 1942534675 scopus 로고    scopus 로고
    • Gene-specific modulation of TAF10 function by SET9-mediated methylation
    • DOI 10.1016/S1097-2765(04)00182-0, PII S1097276504001820
    • Kouskouti A, Scheer E, Staub A, Tora L, Talianidis I (2004) Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol Cell 14:175-182 (Pubitemid 38515645)
    • (2004) Molecular Cell , vol.14 , Issue.2 , pp. 175-182
    • Kouskouti, A.1    Scheer, E.2    Staub, A.3    Tora, L.4    Talianidis, I.5
  • 40
    • 44349108499 scopus 로고    scopus 로고
    • The emerging field of dynamic lysine methylation of non-histone proteins
    • DOI 10.1016/j.gde.2008.01.012, PII S0959437X08000166
    • Huang J, Berger SL (2008) The emerging field of dynamic lysine methylation of non-histone proteins. Curr Opin Genet Dev 18:152-158 (Pubitemid 351749824)
    • (2008) Current Opinion in Genetics and Development , vol.18 , Issue.2 , pp. 152-158
    • Huang, J.1    Berger, S.L.2
  • 41
    • 33745632390 scopus 로고    scopus 로고
    • The epigenetic magic of histone lysine methylation
    • Jenuwein T (2006) The epigenetic magic of histone lysine methylation. Febs J 273:3121-3135
    • (2006) Febs J , vol.273 , pp. 3121-3135
    • Jenuwein, T.1
  • 42
    • 33845755946 scopus 로고    scopus 로고
    • Heterochromatin revisited
    • DOI 10.1038/nrg2008, PII NRG2008
    • Grewal SI, Jia S (2007) Heterochromatin revisited. Nat Rev Genet 8:35-46 (Pubitemid 46006048)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.1 , pp. 35-46
    • Grewal, S.I.S.1    Jia, S.2
  • 43
    • 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
    • DOI 10.1101/gad.989402
    • Tachibana M, Sugimoto K, Nozaki M, Ueda J, Ohta T, Ohki M, Fukuda M, Takeda N, Niida H, Kato H, Shinkai Y (2002) G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev 16:1779-1791 (Pubitemid 34803894)
    • (2002) Genes and Development , vol.16 , Issue.14 , pp. 1779-1791
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3    Ueda, J.4    Ohta, T.5    Ohki, M.6    Fukuda, M.7    Takeda, N.8    Niida, H.9    Kato, H.10    Shinkai, Y.11
  • 45
    • 33645751058 scopus 로고    scopus 로고
    • Silenced tumor suppressor genes reactivated by DNA demethylation do not return to a fully euchromatic chromatin state
    • McGarvey KM, Fahrner JA, Greene E, Martens J, Jenuwein T, Baylin SB (2006) Silenced tumor suppressor genes reactivated by DNA demethylation do not return to a fully euchromatic chromatin state. Cancer Res 66:3541-3549
    • (2006) Cancer Res , vol.66 , pp. 3541-3549
    • McGarvey, K.M.1    Fahrner, J.A.2    Greene, E.3    Martens, J.4    Jenuwein, T.5    Baylin, S.B.6
  • 46
    • 33846038833 scopus 로고    scopus 로고
    • 5-Aza-2′-deoxycytidine-mediated reductions in G9A histone methyltransferase and histone H3 K9 di-methylation levels are linked to tumor suppressor gene reactivation
    • DOI 10.1038/sj.onc.1209763, PII 1209763
    • Wozniak RJ, Klimecki WT, Lau SS, Feinstein Y, Futscher BW (2007) 5-Aza-20-deoxycytidine- mediated reductions in G9A histone methyltransferase and histone H3 K9 dimethylation levels are linked to tumor suppressor gene reactivation. Oncogene 26:77-90 (Pubitemid 46067333)
    • (2007) Oncogene , vol.26 , Issue.1 , pp. 77-90
    • Wozniak, R.J.1    Klimecki, W.T.2    Lau, S.S.3    Feinstein, Y.4    Futscher, B.W.5
  • 50
    • 67649800263 scopus 로고    scopus 로고
    • Dynamic histone H1 isotype 4 methylation and demethylation by histone lysine methyltransferase G9a/KMT1C and the jumonji domain-containing JMJD2/KDM4 proteins
    • Trojer P, Zhang J, Yonezawa M, Schmidt A, Zheng H, Jenuwein T, Reinberg D (2009) Dynamic histone H1 isotype 4 methylation and demethylation by histone lysine methyltransferase G9a/KMT1C and the jumonji domain-containing JMJD2/KDM4 proteins. J Biol Chem 284:8395-8405
    • (2009) J Biol Chem , vol.284 , pp. 8395-8405
    • Trojer, P.1    Zhang, J.2    Yonezawa, M.3    Schmidt, A.4    Zheng, H.5    Jenuwein, T.6    Reinberg, D.7
  • 51
    • 44349103591 scopus 로고    scopus 로고
    • A combined chemical and genetic approach for the generation of induced pluripotent stem cells
    • DOI 10.1016/j.stem.2008.05.011, PII S1934590908002257
    • Shi Y, Do JT, Desponts C, Hahm HS, Scholer HR, Ding S (2008) A combined chemical and genetic approach for the generation of induced pluripotent stem cells. Cell Stem Cell 2:525-528 (Pubitemid 351729222)
    • (2008) Cell Stem Cell , vol.2 , Issue.6 , pp. 525-528
    • Shi, Y.1    Tae Do, J.2    Desponts, C.3    Hahm, H.S.4    Scholer, H.R.5    Ding, S.6
  • 52
    • 43749104249 scopus 로고    scopus 로고
    • A chemical approach to stem-cell biology and regenerative medicine
    • DOI 10.1038/nature07042, PII NATURE07042
    • Xu Y, Shi Y, Ding S (2008) A chemical approach to stem-cell biology and regenerative medicine. Nature 453:338-344 (Pubitemid 351693140)
    • (2008) Nature , vol.453 , Issue.7193 , pp. 338-344
    • Xu, Y.1    Shi, Y.2    Ding, S.3
  • 53
    • 62949220231 scopus 로고    scopus 로고
    • Molecules that promote or enhance reprogramming of somatic cells to induced pluripotent stem cells
    • Feng B, Ng JH, Heng JC, Ng HH (2009) Molecules that promote or enhance reprogramming of somatic cells to induced pluripotent stem cells. Cell Stem Cell 4:301-312
    • (2009) Cell Stem Cell , vol.4 , pp. 301-312
    • Feng, B.1    Ng, J.H.2    Heng, J.C.3    Ng, H.H.4
  • 54
    • 33747195353 scopus 로고    scopus 로고
    • Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors
    • DOI 10.1016/j.cell.2006.07.024, PII S0092867406009767
    • Takahashi K, Yamanaka S (2006) Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors. Cell 126:663-676 (Pubitemid 44233629)
    • (2006) Cell , vol.126 , Issue.4 , pp. 663-676
    • Takahashi, K.1    Yamanaka, S.2
  • 57
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • DOI 10.1016/j.cell.2004.12.012, PII S0092867404011997
    • Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, Casero RA, Shi Y (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119:941-953 (Pubitemid 40037608)
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 58
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor- dependent transcription
    • DOI 10.1038/nature04020, PII N04020
    • Metzger E, Wissmann M, Yin N, Muller JM, Schneider R, Peters AH, Gunther T, Buettner R, Schule R (2005) LSD1 demethylates repressive histone marks to promote androgen-receptor- dependent transcription. Nature 437:436-439 (Pubitemid 41613508)
    • (2005) Nature , vol.437 , Issue.7057 , pp. 436-439
    • Metzger, E.1    Wissmann, M.2    Yin, N.3    Muller, J.M.4    Schneider, R.5    Peters, A.H.F.M.6    Gunther, T.7    Buettner, R.8    Schule, R.9
  • 61
    • 70349272130 scopus 로고    scopus 로고
    • KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
    • Ciccone DN, Su H, Hevi S, Gay F, Lei H, Bajko J, Xu G, Li E, Chen T (2009) KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints. Nature 461 (7262):415-418
    • (2009) Nature , vol.461 , Issue.7262 , pp. 415-418
    • Ciccone, D.N.1    Su, H.2    Hevi, S.3    Gay, F.4    Lei, H.5    Bajko, J.6    Xu, G.7    Li, E.8    Chen, T.9
  • 62
    • 33846025127 scopus 로고    scopus 로고
    • Dynamic regulation of histone lysine methylation by demethylases
    • DOI 10.1016/j.molcel.2006.12.010, PII S1097276506008689
    • Shi Y, Whetstine JR (2007) Dynamic regulation of histone lysine methylation by demethylases. Mol Cell 25:1-14 (Pubitemid 46049067)
    • (2007) Molecular Cell , vol.25 , Issue.1 , pp. 1-14
    • Shi, Y.1    Whetstine, J.R.2
  • 63
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of LSD1 histone demethylase activity by its associated factors
    • DOI 10.1016/j.molcel.2005.08.027, PII S1097276505015698
    • Shi YJ, Matson C, Lan F, Iwase S, Baba T, Shi Y (2005) Regulation of LSD1 histone demethylase activity by its associated factors. Mol Cell 19:857-864 (Pubitemid 41316679)
    • (2005) Molecular Cell , vol.19 , Issue.6 , pp. 857-864
    • Shi, Y.-J.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 64
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • DOI 10.1038/nature04021, PII N04021
    • Lee MG, Wynder C, Cooch N, Shiekhattar R (2005) An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature 437:432-435 (Pubitemid 41613507)
    • (2005) Nature , vol.437 , Issue.7057 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 68
    • 33745862395 scopus 로고    scopus 로고
    • Crystal structure and mechanism of human lysine-specific demethylase-1
    • DOI 10.1038/nsmb1113, PII NSMB1113
    • Stavropoulos P, Blobel G, Hoelz A (2006) Crystal structure and mechanism of human lysinespecific demethylase-1. Nat Struct Mol Biol 13:626-632 (Pubitemid 44036473)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.7 , pp. 626-632
    • Stavropoulos, P.1    Blobel, G.2    Hoelz, A.3
  • 69
    • 33746435258 scopus 로고    scopus 로고
    • Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase
    • DOI 10.1016/j.molcel.2006.07.012, PII S1097276506004928
    • Yang M, Gocke CB, Luo X, Borek D, Tomchick DR, Machius M, Otwinowski Z, Yu H (2006) Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol Cell 23:377-387 (Pubitemid 44128856)
    • (2006) Molecular Cell , vol.23 , Issue.3 , pp. 377-387
    • Yang, M.1    Gocke, C.B.2    Luo, X.3    Borek, D.4    Tomchick, D.R.5    Machius, M.6    Otwinowski, Z.7    Yu, H.8
  • 74
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • DOI 10.1038/nature01048
    • Falnes PO, Johansen RF, Seeberg E (2002) AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature 419:178-182 (Pubitemid 35025447)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 75
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • DOI 10.1038/nature00908
    • Trewick SC, Henshaw TF, Hausinger RP, Lindahl T, Sedgwick B (2002) Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage. Nature 419:174-178 (Pubitemid 35025446)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 76
    • 27544495625 scopus 로고    scopus 로고
    • 2-dependent regulators of the hypoxic response pathway
    • DOI 10.1016/j.bbrc.2005.08.140, PII S0006291X05018590
    • Dann CE 3rd, Bruick RK (2005) Dioxygenases as O2-dependent regulators of the hypoxic response pathway. Biochem Biophys Res Commun 338:639-647 (Pubitemid 41540611)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 639-647
    • Dann III, C.E.1    Bruick, R.K.2
  • 80
    • 33847050240 scopus 로고    scopus 로고
    • Non-heme dioxygenases: Cellular sensors and regulators jelly rolled into one?
    • Ozer A, Bruick RK (2007) Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one? Nat Chem Biol 3:144-153
    • (2007) Nat Chem Biol , vol.3 , pp. 144-153
    • Ozer, A.1    Bruick, R.K.2
  • 87
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM (2006) Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312:748-751
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 88
    • 37849015924 scopus 로고    scopus 로고
    • Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
    • Lee J, Thompson JR, Botuyan MV, Mer G (2008) Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nat Struct Mol Biol 15:109-111
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 109-111
    • Lee, J.1    Thompson, J.R.2    Botuyan, M.V.3    Mer, G.4
  • 89
    • 77949432014 scopus 로고    scopus 로고
    • PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an N {varepsilon}-dimethyl lysine demethylase
    • Loenarz C, Ge W, Coleman ML, Rose NR, Cooper CD, Klose RJ, Ratcliffe PJ, Schofield CJ (2010) PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an N {varepsilon}-dimethyl lysine demethylase. Hum Mol Genet 19:217-222
    • (2010) Hum Mol Genet , vol.19 , pp. 217-222
    • Loenarz, C.1    Ge, W.2    Coleman, M.L.3    Rose, N.R.4    Cooper, C.D.5    Klose, R.J.6    Ratcliffe, P.J.7    Schofield, C.J.8
  • 90
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of Jumonji histone lysine demethylases
    • Horton JR, Upadhyay AK, Qi HH, Zhang X, Shi Y, Cheng X (2010) Enzymatic and structural insights for substrate specificity of a family of Jumonji histone lysine demethylases. Nat Struct Mol Biol 17:38-43
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.6
  • 91
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • Yamane K, Toumazou C, Tsukada Y, Erdjument-Bromage H, Tempst P, Wong J, Zhang Y (2006) JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell 125:483-495
    • (2006) Cell , vol.125 , pp. 483-495
    • Yamane, K.1    Toumazou, C.2    Tsukada, Y.3    Erdjument-Bromage, H.4    Tempst, P.5    Wong, J.6    Zhang, Y.7
  • 93
    • 53549088904 scopus 로고    scopus 로고
    • Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin
    • Li F, Huarte M, Zaratiegui M, Vaughn MW, Shi Y, Martienssen R, Cande WZ (2008) Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Cell 135:272-283
    • (2008) Cell , vol.135 , pp. 272-283
    • Li, F.1    Huarte, M.2    Zaratiegui, M.3    Vaughn, M.W.4    Shi, Y.5    Martienssen, R.6    Cande, W.Z.7
  • 94
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • DOI 10.1038/47412
    • Strahl BD, Allis CD (2000) The language of covalent histone modifications. Nature 403:41-45 (Pubitemid 30038513)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 95
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein T, Allis CD (2001) Translating the histone code. Science 293:1074-1080 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 96
    • 33845877732 scopus 로고    scopus 로고
    • Defining an epigenetic code
    • DOI 10.1038/ncb0107-2, PII NCB0107-2
    • Turner BM (2007) Defining an epigenetic code. Nat Cell Biol 9:2-6 (Pubitemid 46024187)
    • (2007) Nature Cell Biology , vol.9 , Issue.1 , pp. 2-6
    • Turner, B.M.1
  • 97
    • 55449096356 scopus 로고    scopus 로고
    • Crosstalk among histone modifications
    • Suganuma T, Workman JL (2008) Crosstalk among histone modifications. Cell 135:604-607
    • (2008) Cell , vol.135 , pp. 604-607
    • Suganuma, T.1    Workman, J.L.2
  • 98
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • DOI 10.1038/nature05915, PII NATURE05915
    • Berger SL (2007) The complex language of chromatin regulation during transcription. Nature 447:407-412 (Pubitemid 46816746)
    • (2007) Nature , vol.447 , Issue.7143 , pp. 407-412
    • Berger, S.L.1
  • 102
    • 58649110597 scopus 로고    scopus 로고
    • Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks
    • Southall SM, Wong PS, Odho Z, Roe SM, Wilson JR (2009) Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks. Mol Cell 33:181-191
    • (2009) Mol Cell , vol.33 , pp. 181-191
    • Southall, S.M.1    Wong, P.S.2    Odho, Z.3    Roe, S.M.4    Wilson, J.R.5
  • 103
    • 22344454519 scopus 로고    scopus 로고
    • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
    • DOI 10.1101/gad.1318405
    • 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 (Pubitemid 41003012)
    • (2005) Genes and Development , vol.19 , Issue.12 , pp. 1455-1465
    • Couture, J.-F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.