메뉴 건너뛰기




Volumn 70, Issue 9, 2013, Pages 1495-1508

Epigenetic methylations and their connections with metabolism

Author keywords

Chromatin modification; Demethylase; DNMT; Epigenetics; Jumonji; Metabolism; Methylation; Methyltransferases; Polycomb; S adenosylmethionine; Trithorax

Indexed keywords

DNA METHYLTRANSFERASE; HISTONE; HISTONE DEMETHYLASE; HISTONE H3; HISTONE METHYLTRANSFERASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; METHYL GROUP; OXYGENASE; POLYCOMB GROUP PROTEIN; S ADENOSYLMETHIONINE; TRANSCRIPTION FACTOR; TRITHORAX GROUP PROTEIN; UNCLASSIFIED DRUG;

EID: 84876685184     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1293-5     Document Type: Review
Times cited : (24)

References (149)
  • 1
    • 4143147468 scopus 로고    scopus 로고
    • Metabolic enzymes and coenzymes in transcription - A direct link between metabolism and transcription?
    • DOI 10.1016/j.tig.2004.07.004, PII S0168952504001842
    • Shi Y, Shi Y (2004) Metabolic enzymes and coenzymes in transcription-a direct link between metabolism and transcription? Trends Genet 20(9):445-452 (Pubitemid 39094574)
    • (2004) Trends in Genetics , vol.20 , Issue.9 , pp. 445-452
    • Shi, Y.1    Shi, Y.2
  • 2
    • 77953194775 scopus 로고    scopus 로고
    • Common patterns - Unique features: Nitrogen metabolism and regulation in Gram-positive bacteria
    • 20337720 1:CAS:528:DC%2BC3cXosFChsbk%3D
    • Amon J, Titgemeyer F, Burkovski A (2010) Common patterns - unique features: nitrogen metabolism and regulation in Gram-positive bacteria. FEMS Microbiol Rev 34(4):588-605
    • (2010) FEMS Microbiol Rev , vol.34 , Issue.4 , pp. 588-605
    • Amon, J.1    Titgemeyer, F.2    Burkovski, A.3
  • 3
    • 33846516797 scopus 로고    scopus 로고
    • The lactose repressor system: Paradigms for regulation, allosteric behavior and protein folding
    • DOI 10.1007/s00018-006-6296-z
    • Wilson CJ, Zhan H, Swint-Kruse L, Matthews KS (2007) The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding. Cell Mol Life Sci 64(1):3-16 (Pubitemid 46164491)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.1 , pp. 3-16
    • Wilson, C.J.1    Zhan, H.2    Swint-Kruse, L.3    Matthews, K.S.4
  • 4
    • 79551534130 scopus 로고    scopus 로고
    • Crosstalk between components of circadian and metabolic cycles in mammals
    • 21284980 1:CAS:528:DC%2BC3MXhtlaju7k%3D 10.1016/j.cmet.2011.01.006
    • Asher G, Schibler U (2011) Crosstalk between components of circadian and metabolic cycles in mammals. Cell Metab 13(2):125-137
    • (2011) Cell Metab , vol.13 , Issue.2 , pp. 125-137
    • Asher, G.1    Schibler, U.2
  • 5
    • 34249727164 scopus 로고    scopus 로고
    • Transcriptional coregulators in the control of energy homeostasis
    • DOI 10.1016/j.tcb.2007.04.001, PII S0962892407000840
    • Feige JN, Auwerx J (2007) Transcriptional coregulators in the control of energy homeostasis. Trends Cell Biol 17(6):292-301 (Pubitemid 46829846)
    • (2007) Trends in Cell Biology , vol.17 , Issue.6 , pp. 292-301
    • Feige, J.N.1    Auwerx, J.2
  • 6
    • 80455143728 scopus 로고    scopus 로고
    • The complex transcription regulatory landscape of our genome: Control in three dimensions
    • 21952046 1:CAS:528:DC%2BC3MXht1anu7fL 10.1038/emboj.2011.344
    • Splinter E, de Laat W (2011) The complex transcription regulatory landscape of our genome: control in three dimensions. EMBO J 30(21):4345-4355
    • (2011) EMBO J , vol.30 , Issue.21 , pp. 4345-4355
    • Splinter, E.1    De Laat, W.2
  • 7
    • 77949678340 scopus 로고    scopus 로고
    • Chromatin structure and the inheritance of epigenetic information
    • 1:CAS:528:DC%2BC3cXjsFSrtb8%3D 10.1038/nrg2752
    • Margueron R, Reinberg D (2010) Chromatin structure and the inheritance of epigenetic information. Nat Rev 11(4):285-296
    • (2010) Nat Rev , vol.11 , Issue.4 , pp. 285-296
    • Margueron, R.1    Reinberg, D.2
  • 8
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein T, Allis CD (2001) Translating the histone code. Science (New York, NY) 293(5532):1074-1080. doi: 10.1126/science.1063127 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 9
    • 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(7143):407-412 (Pubitemid 46816746)
    • (2007) Nature , vol.447 , Issue.7143 , pp. 407-412
    • Berger, S.L.1
  • 10
    • 84859893371 scopus 로고    scopus 로고
    • Histone methylation: A dynamic mark in health, disease and inheritance
    • 10.1038/nrg3173 22473383 1:CAS:528:DC%2BC38XkvVGgsbo%3D 10.1038/nrg3173
    • Greer EL, Shi Y (2012) Histone methylation: a dynamic mark in health, disease and inheritance. Nat Rev Genet 13(5):343-357. doi: 10.1038/nrg3173
    • (2012) Nat Rev Genet , vol.13 , Issue.5 , pp. 343-357
    • Greer, E.L.1    Shi, Y.2
  • 11
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • 10.1016/j.molcel.2008.12.013 19150423 1:CAS:528:DC%2BD1MXhtFOitrg%3D 10.1016/j.molcel.2008.12.013
    • Bedford MT, Clarke SG (2009) Protein arginine methylation in mammals: who, what, and why. Mol Cell 33(1):1-13. doi: 10.1016/j.molcel.2008.12.013
    • (2009) Mol Cell , vol.33 , Issue.1 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 12
    • 78649664485 scopus 로고    scopus 로고
    • Structural insights into histone lysine demethylation
    • 10.1016/j.sbi.2010.09.006 20970991 1:CAS:528:DC%2BC3cXhsV2js77P 10.1016/j.sbi.2010.09.006
    • Hou H, Yu H (2010) Structural insights into histone lysine demethylation. Curr Opin Struct Biol 20(6):739-748. doi: 10.1016/j.sbi.2010.09.006
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.6 , pp. 739-748
    • Hou, H.1    Yu, H.2
  • 13
    • 84863986133 scopus 로고    scopus 로고
    • Functions of DNA methylation: Islands, start sites, gene bodies and beyond
    • 10.1038/nrg3230 22641018 1:CAS:528:DC%2BC38Xns1SqtLw%3D 10.1038/nrg3230
    • Jones PA (2012) Functions of DNA methylation: islands, start sites, gene bodies and beyond. Nat Rev Genet 13(7):484-492. doi: 10.1038/nrg3230
    • (2012) Nat Rev Genet , vol.13 , Issue.7 , pp. 484-492
    • Jones, P.A.1
  • 14
    • 82955207588 scopus 로고    scopus 로고
    • Mechanisms and functions of Tet protein-mediated 5-methylcytosine oxidation
    • 22156206 1:CAS:528:DC%2BC3MXhs1GqtLfN 10.1101/gad.179184.111
    • Wu H, Zhang Y (2011) Mechanisms and functions of Tet protein-mediated 5-methylcytosine oxidation. Genes Dev 25(23):2436-2452
    • (2011) Genes Dev , vol.25 , Issue.23 , pp. 2436-2452
    • Wu, H.1    Zhang, Y.2
  • 15
    • 84860749868 scopus 로고    scopus 로고
    • Tet family proteins and 5-hydroxymethylcytosine in development and disease
    • 10.1242/dev.070771 1:CAS:528:DC%2BC38XhtVGlsLrL 10.1242/dev.070771
    • Tan L, Shi YG (2012) Tet family proteins and 5-hydroxymethylcytosine in development and disease. Development(Cambridge, England) 139(11):1895-1902. doi: 10.1242/dev.070771
    • (2012) Development(Cambridge, England) , vol.139 , Issue.11 , pp. 1895-1902
    • Tan, L.1    Shi, Y.G.2
  • 16
    • 79960820132 scopus 로고    scopus 로고
    • The growing challenge of obesity and cancer: An inflammatory issue
    • 21793838 1:CAS:528:DC%2BC3MXhtFOqtbfN 10.1111/j.1749-6632.2011.06096.x
    • Harvey AE, Lashinger LM, Hursting SD (2011) The growing challenge of obesity and cancer: an inflammatory issue. Ann N Y Acad Sci 1229:45-52
    • (2011) Ann N y Acad Sci , vol.1229 , pp. 45-52
    • Harvey, A.E.1    Lashinger, L.M.2    Hursting, S.D.3
  • 17
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of Polycomb gene silencing: Knowns and unknowns
    • 19738629 1:CAS:528:DC%2BD1MXhtV2qtL%2FO
    • Simon JA, Kingston RE (2009) Mechanisms of Polycomb gene silencing: knowns and unknowns. Nat Rev Mol Cell Biol 10(10):697-708
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 18
    • 0033538578 scopus 로고    scopus 로고
    • Stabilization of chromatin structure by PRC1, a polycomb complex
    • DOI 10.1016/S0092-8674(00)80604-2
    • Shao Z, Raible F, Mollaaghababa R, Guyon JR, Wu CT, Bender W, Kingston RE (1999) Stabilization of chromatin structure by PRC1, a Polycomb complex. Cell 98(1):37-46 (Pubitemid 29331194)
    • (1999) Cell , vol.98 , Issue.1 , pp. 37-46
    • Shao, Z.1    Raible, F.2    Mollaaghababa, R.3    Guyon, J.R.4    Wu, C.-T.5    Bender, W.6    Kingston, R.E.7
  • 19
    • 0023644202 scopus 로고
    • A complex genetic locus, polyhomeotic, is required for segmental specification and epidermal development in D. melanogaster
    • 2890438 1:CAS:528:DyaL1cXltVGisg%3D%3D 10.1016/0092-8674(87)90106-1
    • Dura JM, Randsholt NB, Deatrick J, Erk I, Santamaria P, Freeman JD, Freeman SJ, Weddell D, Brock HW (1987) A complex genetic locus, polyhomeotic, is required for segmental specification and epidermal development in D. melanogaster. Cell 51(5):829-839
    • (1987) Cell , vol.51 , Issue.5 , pp. 829-839
    • Dura, J.M.1    Randsholt, N.B.2    Deatrick, J.3    Erk, I.4    Santamaria, P.5    Freeman, J.D.6    Freeman, S.J.7    Weddell, D.8    Brock, H.W.9
  • 20
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • DOI 10.1038/nature02985
    • Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y (2004) Role of histone H2A ubiquitination in Polycomb silencing. Nature 431(7010):873-878 (Pubitemid 39434086)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 873-878
    • Wang, H.1    Wang, L.2    Erdjument-Bromage, H.3    Vidal, M.4    Tempst, P.5    Jones, R.S.6    Zhang, Y.7
  • 22
    • 29144487990 scopus 로고    scopus 로고
    • Role of Bmi-1 and Ring1A in H2A ubiquitylation and hox gene silencing
    • DOI 10.1016/j.molcel.2005.12.002, PII S1097276505018174
    • Cao R, Tsukada Y, Zhang Y (2005) Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol Cell 20(6):845-854 (Pubitemid 41814874)
    • (2005) Molecular Cell , vol.20 , Issue.6 , pp. 845-854
    • Cao, R.1    Tsukada, Y.-I.2    Zhang, Y.3
  • 23
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • DOI 10.1016/S0092-8674(03)00159-4
    • Kagey MH, Melhuish TA, Wotton D (2003) The Polycomb protein Pc2 is a SUMO E3. Cell 113(1):127-137 (Pubitemid 36411965)
    • (2003) Cell , vol.113 , Issue.1 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 24
    • 13244271351 scopus 로고    scopus 로고
    • Multiple activities contribute to Pc2 E3 function
    • DOI 10.1038/sj.emboj.7600506
    • Kagey MH, Melhuish TA, Powers SE, Wotton D (2005) Multiple activities contribute to Pc2 E3 function. EMBO J 24(1):108-119 (Pubitemid 40188468)
    • (2005) EMBO Journal , vol.24 , Issue.1 , pp. 108-119
    • Kagey, M.H.1    Melhuish, T.A.2    Powers, S.E.3    Wotton, D.4
  • 25
    • 34447127473 scopus 로고    scopus 로고
    • Polycomb protein Cbx4 promotes SUMO modification of de novo DNA methyltransferase Dnmt3a
    • DOI 10.1042/BJ20061873
    • Li B, Zhou J, Liu P, Hu J, Jin H, Shimono Y, Takahashi M, Xu G (2007) Polycomb protein Cbx4 promotes SUMO modification of de novo DNA methyltransferase Dnmt3a. Biochem J 405(2):369-378 (Pubitemid 47075172)
    • (2007) Biochemical Journal , vol.405 , Issue.2 , pp. 369-378
    • Li, B.1    Zhou, J.2    Liu, P.3    Hu, J.4    Jin, H.5    Shimono, Y.6    Takahashi, M.7    Xu, G.8
  • 27
    • 54349083294 scopus 로고    scopus 로고
    • DKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing
    • 18923078 1:CAS:528:DC%2BD1cXht12ht73O 10.1101/gad.484208
    • Lagarou A, Mohd-Sarip A, Moshkin YM, Chalkley GE, Bezstarosti K, Demmers JA, Verrijzer CP (2008) dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing. Genes Dev 22(20):2799-2810
    • (2008) Genes Dev , vol.22 , Issue.20 , pp. 2799-2810
    • Lagarou, A.1    Mohd-Sarip, A.2    Moshkin, Y.M.3    Chalkley, G.E.4    Bezstarosti, K.5    Demmers, J.A.6    Verrijzer, C.P.7
  • 28
    • 33748641974 scopus 로고    scopus 로고
    • Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets
    • DOI 10.1128/MCB.00630-06
    • Gearhart MD, Corcoran CM, Wamstad JA, Bardwell VJ (2006) Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets. Mol Cell Biol 26(18):6880-6889 (Pubitemid 44387637)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.18 , pp. 6880-6889
    • Gearhart, M.D.1    Corcoran, C.M.2    Wamstad, J.A.3    Bardwell, V.J.4
  • 29
    • 34249715325 scopus 로고    scopus 로고
    • Proteomics analysis of Ring1B/Rnf2 interactions identifies a novel complex with the Fbxl10/Jhdm1B histone demethylase and the Bcl6 interacting corepressor
    • DOI 10.1074/mcp.M600275-MCP200
    • Sanchez C, Sanchez I, Demmers JA, Rodriguez P, Strouboulis J, Vidal M (2007) Proteomics analysis of Ring1B/Rnf2 interactors identifies a novel complex with the Fbxl10/Jhdm1B histone demethylase and the Bcl6 interacting corepressor. Mol Cell Prot 6(5):820-834 (Pubitemid 46831934)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.5 , pp. 820-834
    • Sanchez, C.1    Sanches, I.2    Demmers, J.A.A.3    Rodriguez, P.4    Strouboulis, J.5    Vidal, M.6
  • 30
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • DOI 10.1016/S0092-8674(02)00975-3
    • Czermin B, Melfi R, McCabe D, Seitz V, Imhof A, Pirrotta V (2002) Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 111(2):185-196 (Pubitemid 35292439)
    • (2002) Cell , vol.111 , Issue.2 , pp. 185-196
    • Czermin, B.1    Melfi, R.2    McCabe, D.3    Seitz, V.4    Imhof, A.5    Pirrotta, V.6
  • 32
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in polycomb-group silencing
    • DOI 10.1126/science.1076997
    • Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, Jones RS, Zhang Y (2002) Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science (New York, NY) 298(5595):1039-1043 (Pubitemid 35247314)
    • (2002) Science , vol.298 , Issue.5595 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5    Tempst, P.6    Jones, R.S.7    Zhang, Y.8
  • 33
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the enhancer of zeste protein
    • DOI 10.1101/gad.1035902
    • Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D (2002) Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev 16(22):2893-2905 (Pubitemid 35334738)
    • (2002) Genes and Development , vol.16 , Issue.22 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 34
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by polycomb and HP1 chromodomains
    • DOI 10.1101/gad.1110503
    • Fischle W, Wang Y, Jacobs SA, Kim Y, Allis CD, Khorasanizadeh S (2003) Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev 17(15):1870-1881 (Pubitemid 36944564)
    • (2003) Genes and Development , vol.17 , Issue.15 , pp. 1870-1881
    • Fischle, W.1    Wang, Y.2    Jacobs, S.A.3    Kim, Y.4    Allis, C.D.5    Khorasanizadeh, S.6
  • 35
    • 0041624288 scopus 로고    scopus 로고
    • Structural basis for specific binding of polycomb chromodomain to histone H3 methylated at Lys 27
    • DOI 10.1101/gad.269603
    • Min J, Zhang Y, Xu RM (2003) Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev 17(15):1823-1828 (Pubitemid 36944559)
    • (2003) Genes and Development , vol.17 , Issue.15 , pp. 1823-1828
    • Min, J.1    Zhang, Y.2    Xu, R.-M.3
  • 36
    • 33645231102 scopus 로고    scopus 로고
    • Mouse Polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin
    • 10.1128/MCB.26.7.2560-2569.2006 16537902 1:CAS:528:DC%2BD28XivFSrsbo%3D 10.1128/MCB.26.7.2560-2569.2006
    • Bernstein E, Duncan EM, Masui O, Gil J, Heard E, Allis CD (2006) Mouse Polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin. Mol Cell Biol 26(7):2560-2569. doi: 10.1128/MCB.26.7.2560-2569.2006
    • (2006) Mol Cell Biol , vol.26 , Issue.7 , pp. 2560-2569
    • Bernstein, E.1    Duncan, E.M.2    Masui, O.3    Gil, J.4    Heard, E.5    Allis, C.D.6
  • 37
    • 35348993743 scopus 로고    scopus 로고
    • Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination
    • DOI 10.1126/science.1149042
    • Lee MG, Villa R, Trojer P, Norman J, Yan KP, Reinberg D, Di Croce L, Shiekhattar R (2007) Demethylation of H3K27 regulates Polycomb recruitment and H2A ubiquitination. Science (New York, NY) 318(5849):447-450 (Pubitemid 47614529)
    • (2007) Science , vol.318 , Issue.5849 , pp. 447-450
    • Min, G.L.1    Villa, R.2    Trojer, P.3    Norman, J.4    Yan, K.-P.5    Reinberg, D.6    Di Croce, L.7    Shiekhattar, R.8
  • 38
    • 51049114011 scopus 로고    scopus 로고
    • Epigenetic transcriptional repression of cellular genes by a viral SET protein
    • 19160493 1:CAS:528:DC%2BD1cXhtVGgtLnN 10.1038/ncb1772
    • Mujtaba S, Manzur KL, Gurnon JR, Kang M, Van Etten JL, Zhou MM (2008) Epigenetic transcriptional repression of cellular genes by a viral SET protein. Nat Cell Biol 10(9):1114-1122
    • (2008) Nat Cell Biol , vol.10 , Issue.9 , pp. 1114-1122
    • Mujtaba, S.1    Manzur, K.L.2    Gurnon, J.R.3    Kang, M.4    Van Etten, J.L.5    Zhou, M.M.6
  • 39
    • 33748419671 scopus 로고    scopus 로고
    • Polycomb response elements and targeting of Polycomb group proteins in Drosophila
    • DOI 10.1016/j.gde.2006.08.005, PII S0959437X06001560, Differentation and Gene Regulation
    • Muller J, Kassis JA (2006) Polycomb response elements and targeting of Polycomb group proteins in Drosophila. Curr Opin Genet Dev 16(5):476-484 (Pubitemid 44345202)
    • (2006) Current Opinion in Genetics and Development , vol.16 , Issue.5 , pp. 476-484
    • Muller, J.1    Kassis, J.A.2
  • 40
    • 0032861324 scopus 로고    scopus 로고
    • The DNA-binding polycomb group protein Pleiohomeotic mediates silencing of a Drosophila homeotic gene
    • Fritsch C, Brown JL, Kassis JA, Muller J (1999) The DNA-binding Polycomb group protein pleiohomeotic mediates silencing of a Drosophila homeotic gene. Development 126(17):3905-3913 (Pubitemid 29440487)
    • (1999) Development , vol.126 , Issue.17 , pp. 3905-3913
    • Fritsch, C.1    Brown, J.L.2    Kassis, J.A.3    Muller, J.4
  • 41
    • 2942574510 scopus 로고    scopus 로고
    • Hierarchical recruitment of polycomb group silencing complexes
    • DOI 10.1016/j.molcel.2004.05.009, PII S1097276504002928
    • Wang L, Brown JL, Cao R, Zhang Y, Kassis JA, Jones RS (2004) Hierarchical recruitment of Polycomb group silencing complexes. Mol Cell 14(5):637-646 (Pubitemid 38739085)
    • (2004) Molecular Cell , vol.14 , Issue.5 , pp. 637-646
    • Wang, L.1    Brown, J.L.2    Cao, R.3    Zhang, Y.4    Kassis, J.A.5    Jones, R.S.6
  • 42
    • 23744459419 scopus 로고    scopus 로고
    • Synergistic recognition of an epigenetic DNA element by Pleiohomeotic and a Polycomb core complex
    • DOI 10.1101/gad.347005
    • Mohd-Sarip A, Cleard F, Mishra RK, Karch F, Verrijzer CP (2005) Synergistic recognition of an epigenetic DNA element by Pleiohomeotic and a Polycomb core complex. Genes Dev 19(15):1755-1760 (Pubitemid 41126913)
    • (2005) Genes and Development , vol.19 , Issue.15 , pp. 1755-1760
    • Mohd-Sarip, A.1    Cleard, F.2    Mishra, R.K.3    Karch, F.4    Verrijzer, C.P.5
  • 43
    • 73149111929 scopus 로고    scopus 로고
    • A region of the human HOXD cluster that confers Polycomb-group responsiveness
    • Woo CJ, Kharchenko PV, Daheron L, Park PJ, Kingston RE (2010) A region of the human HOXD cluster that confers Polycomb-group responsiveness. Cell 140 (1):99-110
    • (2010) Cell , vol.140 , Issue.1 , pp. 99-110
    • Woo, C.J.1    Kharchenko, P.V.2    Daheron, L.3    Park, P.J.4    Kingston, R.E.5
  • 44
    • 69449086947 scopus 로고    scopus 로고
    • A vertebrate Polycomb response element governs segmentation of the posterior hindbrain
    • 19737517 1:CAS:528:DC%2BD1MXhsVCjs7%2FK 10.1016/j.cell.2009.08.020
    • Sing A, Pannell D, Karaiskakis A, Sturgeon K, Djabali M, Ellis J, Lipshitz HD, Cordes SP (2009) A vertebrate Polycomb response element governs segmentation of the posterior hindbrain. Cell 138(5):885-897
    • (2009) Cell , vol.138 , Issue.5 , pp. 885-897
    • Sing, A.1    Pannell, D.2    Karaiskakis, A.3    Sturgeon, K.4    Djabali, M.5    Ellis, J.6    Lipshitz, H.D.7    Cordes, S.P.8
  • 46
    • 84860370054 scopus 로고    scopus 로고
    • Yin Yang 1 extends the Myc-related transcription factors network in embryonic stem cells
    • Vella P, Barozzi I, Cuomo A, Bonaldi T, Pasini D (2011) Yin Yang 1 extends the Myc-related transcription factors network in embryonic stem cells. Nucleic acids research 40:3403-3418
    • (2011) Nucleic Acids Research , vol.40 , pp. 3403-3418
    • Vella, P.1    Barozzi, I.2    Cuomo, A.3    Bonaldi, T.4    Pasini, D.5
  • 47
    • 76749083433 scopus 로고    scopus 로고
    • Jarid2 and PRC2, partners in regulating gene expression
    • 20123894 10.1101/gad.1886410 1:CAS:528:DC%2BC3cXisVeltLk%3D
    • Li G, Margueron R, Ku M, Chambon P, Bernstein BE, Reinberg D (2010) Jarid2 and PRC2, partners in regulating gene expression. Genes Dev 24(4):368-380
    • (2010) Genes Dev , vol.24 , Issue.4 , pp. 368-380
    • Li, G.1    Margueron, R.2    Ku, M.3    Chambon, P.4    Bernstein, B.E.5    Reinberg, D.6
  • 49
    • 72249119297 scopus 로고    scopus 로고
    • Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells
    • 20064375 10.1016/j.cell.2009.12.002
    • Peng JC, Valouev A, Swigut T, Zhang J, Zhao Y, Sidow A, Wysocka J (2009) Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells. Cell 139(7):1290-1302
    • (2009) Cell , vol.139 , Issue.7 , pp. 1290-1302
    • Peng, J.C.1    Valouev, A.2    Swigut, T.3    Zhang, J.4    Zhao, Y.5    Sidow, A.6    Wysocka, J.7
  • 50
    • 72249104107 scopus 로고    scopus 로고
    • Jumonji modulates Polycomb activity and self-renewal versus differentiation of stem cells
    • 20064376 10.1016/j.cell.2009.12.003
    • Shen X, Kim W, Fujiwara Y, Simon MD, Liu Y, Mysliwiec MR, Yuan GC, Lee Y, Orkin SH (2009) Jumonji modulates Polycomb activity and self-renewal versus differentiation of stem cells. Cell 139(7):1303-1314
    • (2009) Cell , vol.139 , Issue.7 , pp. 1303-1314
    • Shen, X.1    Kim, W.2    Fujiwara, Y.3    Simon, M.D.4    Liu, Y.5    Mysliwiec, M.R.6    Yuan, G.C.7    Lee, Y.8    Orkin, S.H.9
  • 52
    • 26844520965 scopus 로고    scopus 로고
    • Molecular biology: Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3
    • DOI 10.1126/science.1118947
    • Cha TL, Zhou BP, Xia W, Wu Y, Yang CC, Chen CT, Ping B, Otte AP, Hung MC (2005) Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3. Science (New York, NY) 310(5746):306-310 (Pubitemid 41457195)
    • (2005) Science , vol.310 , Issue.5746 , pp. 306-310
    • Cha, T.-L.1    Zhou, B.P.2    Xia, W.3    Wu, Y.4    Yang, C.-C.5    Chen, C.-T.6    Ping, B.7    Otte, A.P.8    Hung, M.-C.9
  • 53
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • DOI 10.1038/nrg1879, PII NRG1879
    • Engelman JA, Luo J, Cantley LC (2006) The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat Rev 7(8):606-619 (Pubitemid 44100518)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.8 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 54
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB Signaling: Navigating Downstream
    • DOI 10.1016/j.cell.2007.06.009, PII S0092867407007751
    • Manning BD, Cantley LC (2007) AKT/PKB signaling: navigating downstream. Cell 129(7):1261-1274 (Pubitemid 46962095)
    • (2007) Cell , vol.129 , Issue.7 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 56
    • 79551534130 scopus 로고    scopus 로고
    • Crosstalk between components of circadian and metabolic cycles in mammals
    • Asher G, Schibler U (2011) Crosstalk between components of circadian and metabolic cycles in mammals. Cell Metabolism 13 (2):125-137
    • (2011) Cell Metabolism , vol.13 , Issue.2 , pp. 125-137
    • Asher, G.1    Schibler, U.2
  • 57
    • 77952208495 scopus 로고    scopus 로고
    • Histone H3K27 methyltransferase Ezh2 represses Wnt genes to facilitate adipogenesis
    • 20368440 1:CAS:528:DC%2BC3cXlsVynsbo%3D 10.1073/pnas.1000031107
    • Wang L, Jin Q, Lee JE, Su IH, Ge K (2010) Histone H3K27 methyltransferase Ezh2 represses Wnt genes to facilitate adipogenesis. Proc Natl Acad Sci USA 107(16):7317-7322
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.16 , pp. 7317-7322
    • Wang, L.1    Jin, Q.2    Lee, J.E.3    Su, I.H.4    Ge, K.5
  • 59
    • 65249093055 scopus 로고    scopus 로고
    • Polycomb protein Ezh2 regulates pancreatic beta-cell Ink4a/Arf expression and regeneration in diabetes mellitus
    • 19390090 1:CAS:528:DC%2BD1MXlslSgtbc%3D 10.1101/gad.1742509
    • Chen H, Gu X, Su IH, Bottino R, Contreras JL, Tarakhovsky A, Kim SK (2009) Polycomb protein Ezh2 regulates pancreatic beta-cell Ink4a/Arf expression and regeneration in diabetes mellitus. Genes Dev 23(8):975-985
    • (2009) Genes Dev , vol.23 , Issue.8 , pp. 975-985
    • Chen, H.1    Gu, X.2    Su, I.H.3    Bottino, R.4    Contreras, J.L.5    Tarakhovsky, A.6    Kim, S.K.7
  • 60
    • 65249121864 scopus 로고    scopus 로고
    • Bmi-1 regulates the Ink4a/Arf locus to control pancreatic beta-cell proliferation
    • 19390085 1:CAS:528:DC%2BD1MXlslSgtb0%3D 10.1101/gad.1742609
    • Dhawan S, Tschen SI, Bhushan A (2009) Bmi-1 regulates the Ink4a/Arf locus to control pancreatic beta-cell proliferation. Genes Dev 23(8):906-911
    • (2009) Genes Dev , vol.23 , Issue.8 , pp. 906-911
    • Dhawan, S.1    Tschen, S.I.2    Bhushan, A.3
  • 61
    • 0345046221 scopus 로고
    • Dosage-dependent modifiers of Polycomb and antennapedia mutations in Drosophila
    • 3141923 1:STN:280:DyaL1M%2Fkt1Wnsg%3D%3D 10.1073/pnas.85.21.8136
    • Kennison JA, Tamkun JW (1988) Dosage-dependent modifiers of Polycomb and antennapedia mutations in Drosophila. Proc Natl Acad Sci USA 85(21):8136-8140
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.21 , pp. 8136-8140
    • Kennison, J.A.1    Tamkun, J.W.2
  • 62
    • 76949107741 scopus 로고    scopus 로고
    • Histone H3 lysine 4 (H3K4) methylation in development and differentiation
    • 19703438 10.1016/j.ydbio.2009.08.017 1:CAS:528:DC%2BC3cXis1ajtLc%3D
    • Eissenberg JC, Shilatifard A (2009) Histone H3 lysine 4 (H3K4) methylation in development and differentiation. Dev biol 339(2):240-249
    • (2009) Dev Biol , vol.339 , Issue.2 , pp. 240-249
    • Eissenberg, J.C.1    Shilatifard, A.2
  • 63
    • 18744373853 scopus 로고    scopus 로고
    • MLL targets SET domain methyltransferase activity to Hox gene promoters
    • DOI 10.1016/S1097-2765(02)00741-4
    • Milne TA, Briggs SD, Brock HW, Martin ME, Gibbs D, Allis CD, Hess JL (2002) MLL targets SET domain methyltransferase activity to Hox gene promoters. Mol Cell 10(5):1107-1117 (Pubitemid 35453828)
    • (2002) Molecular Cell , vol.10 , Issue.5 , pp. 1107-1117
    • Milne, T.A.1    Briggs, S.D.2    Brock, H.W.3    Martin, M.E.4    Gibbs, D.5    Allis, C.D.6    Hess, J.L.7
  • 65
    • 0030668324 scopus 로고    scopus 로고
    • SET1, a yeast member of the Trithorax family, functions in transcriptional silencing and diverse cellular processes
    • Nislow C, Ray E, Pillus L (1997) SET1, a yeast member of the trithorax family, functions in transcriptional silencing and diverse cellular processes. Mol Biol Cell 8(12):2421-2436 (Pubitemid 27528211)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.12 , pp. 2421-2436
    • Nislow, C.1    Ray, E.2    Pillus, L.3
  • 67
    • 0035893240 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae
    • DOI 10.1101/gad.940201
    • Briggs SD, Bryk M, Strahl BD, Cheung WL, Davie JK, Dent SY, Winston F, Allis CD (2001) Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev 15(24):3286-3295 (Pubitemid 34008193)
    • (2001) Genes and Development , vol.15 , Issue.24 , pp. 3286-3295
    • Briggs, S.D.1    Bryk, M.2    Strahl, B.D.3    Cheung, W.L.4    Davie, J.K.5    Dent, S.Y.R.6    Winston, F.7    David Allis, C.8
  • 68
    • 0037126594 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4
    • DOI 10.1093/emboj/20.24.7137
    • Roguev A, Schaft D, Shevchenko A, Pijnappel WW, Wilm M, Aasland R, Stewart AF (2001) The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J 20(24):7137-7148 (Pubitemid 34062305)
    • (2001) EMBO Journal , vol.20 , Issue.24 , pp. 7137-7148
    • Roguev, A.1    Schaft, D.2    Shevchenko, A.3    Pijnappel, W.W.M.P.4    Wilm, M.5    Aasland, R.6    Stewart, A.F.7
  • 69
    • 77954660029 scopus 로고    scopus 로고
    • Members of the H3K4 trimethylation complex regulate lifespan in a germline-dependent manner in C. elegans
    • 20555324 1:CAS:528:DC%2BC3cXnsVylsLo%3D 10.1038/nature09195
    • Greer EL, Maures TJ, Hauswirth AG, Green EM, Leeman DS, Maro GS, Han S, Banko MR, Gozani O, Brunet A (2010) Members of the H3K4 trimethylation complex regulate lifespan in a germline-dependent manner in C. elegans. Nature 466(7304):383-387
    • (2010) Nature , vol.466 , Issue.7304 , pp. 383-387
    • Greer, E.L.1    Maures, T.J.2    Hauswirth, A.G.3    Green, E.M.4    Leeman, D.S.5    Maro, G.S.6    Han, S.7    Banko, M.R.8    Gozani, O.9    Brunet, A.10
  • 70
  • 71
    • 58049206724 scopus 로고    scopus 로고
    • Targeted inactivation of MLL3 histone H3-Lys-4 methyltransferase activity in the mouse reveals vital roles for MLL3 in adipogenesis
    • 19047629 1:CAS:528:DC%2BD1cXhsFamu7zP 10.1073/pnas.0810100105
    • Lee J, Saha PK, Yang QH, Lee S, Park JY, Suh Y, Lee SK, Chan L, Roeder RG, Lee JW (2008) Targeted inactivation of MLL3 histone H3-Lys-4 methyltransferase activity in the mouse reveals vital roles for MLL3 in adipogenesis. Proc Natl Acad Sci USA 105(49):19229-19234
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.49 , pp. 19229-19234
    • Lee, J.1    Saha, P.K.2    Yang, Q.H.3    Lee, S.4    Park, J.Y.5    Suh, Y.6    Lee, S.K.7    Chan, L.8    Roeder, R.G.9    Lee, J.W.10
  • 72
    • 44649177124 scopus 로고    scopus 로고
    • Activating signal cointegrator-2 is an essential adaptor to recruit histone H3 lysine 4 methyltransferases MLL3 and MLL4 to the liver X receptors
    • DOI 10.1210/me.2008-0012
    • Lee S, Lee J, Lee SK, Lee JW (2008) Activating signal cointegrator-2 is an essential adaptor to recruit histone H3 lysine 4 methyltransferases MLL3 and MLL4 to the liver X receptors. Mol Endocrinol (Baltimore, Md) 6(22):1312-1319 (Pubitemid 351786992)
    • (2008) Molecular Endocrinology , vol.22 , Issue.6 , pp. 1312-1319
    • Lee, S.1    Lee, J.2    Lee, S.-K.3    Lee, J.W.4
  • 73
    • 70349766918 scopus 로고    scopus 로고
    • ASCOM controls farnesoid X receptor transactivation through its associated histone H3 lysine 4 methyltransferase activity
    • 1:CAS:528:DC%2BD1MXhtlSitb%2FJ 10.1210/me.2009-0099
    • Kim DH, Lee J, Lee B, Lee JW (2009) ASCOM controls farnesoid X receptor transactivation through its associated histone H3 lysine 4 methyltransferase activity. Mol Endocrinol (Baltimore, Md) 23(10):1556-1562
    • (2009) Mol Endocrinol (Baltimore, Md) , vol.23 , Issue.10 , pp. 1556-1562
    • Kim, D.H.1    Lee, J.2    Lee, B.3    Lee, J.W.4
  • 74
    • 39849106299 scopus 로고    scopus 로고
    • A translational view on the biliary lipid secretory network
    • 18194677 1:CAS:528:DC%2BD1cXivVyjtbw%3D 10.1016/j.bbalip.2007.12.002
    • Lo Sasso G, Petruzzelli M, Moschetta A (2008) A translational view on the biliary lipid secretory network. Biochim Biophys Acta 1781(3):79-96
    • (2008) Biochim Biophys Acta , vol.1781 , Issue.3 , pp. 79-96
    • Lo Sasso, G.1    Petruzzelli, M.2    Moschetta, A.3
  • 75
    • 80054911514 scopus 로고    scopus 로고
    • Forming functional fat: A growing understanding of adipocyte differentiation
    • 21952300 1:CAS:528:DC%2BC3MXht1anu7%2FN 10.1038/nrm3198
    • Cristancho AG, Lazar MA (2011) Forming functional fat: a growing understanding of adipocyte differentiation. Nat Rev Mol Cell Biol 12(11):722-734
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.11 , pp. 722-734
    • Cristancho, A.G.1    Lazar, M.A.2
  • 76
    • 18244365850 scopus 로고    scopus 로고
    • Cell biology: PERIOD1-associated proteins modulate the negative limb of the mammalian circadian oscillator
    • DOI 10.1126/science.1107373
    • Brown SA, Ripperger J, Kadener S, Fleury-Olela F, Vilbois F, Rosbash M, Schibler U (2005) PERIOD1-associated proteins modulate the negative limb of the mammalian circadian oscillator. Science (New York, NY) 308(5722):693-696 (Pubitemid 40594390)
    • (2005) Science , vol.308 , Issue.5722 , pp. 693-696
    • Brown, S.A.1    Ripperger, J.2    Kadener, S.3    Fleury-Olela, F.4    Vilbois, F.5    Rosbash, M.6    Schibler, U.7
  • 78
    • 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(6824):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
  • 79
    • 0347955358 scopus 로고    scopus 로고
    • Histone Methyltransferases Direct Different Degrees of Methylation to Define Distinct Chromatin Domains
    • DOI 10.1016/S1097-2765(03)00479-9
    • Rice JC, Briggs SD, Ueberheide B, Barber CM, Shabanowitz J, Hunt DF, Shinkai Y, Allis CD (2003) Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains. Mol Cell 12(6):1591-1598 (Pubitemid 38037025)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1591-1598
    • Rice, J.C.1    Briggs, S.D.2    Ueberheide, B.3    Barber, C.M.4    Shabanowitz, J.5    Hunt, D.F.6    Shinkai, Y.7    Allis, C.D.8
  • 80
    • 43149086590 scopus 로고    scopus 로고
    • A Metabolic Throttle Regulates the Epigenetic State of rDNA
    • DOI 10.1016/j.cell.2008.04.026, PII S0092867408005564
    • Grummt I, Ladurner AG (2008) A metabolic throttle regulates the epigenetic state of rDNA. Cell 133(4):577-580 (Pubitemid 351637625)
    • (2008) Cell , vol.133 , Issue.4 , pp. 577-580
    • Grummt, I.1    Ladurner, A.G.2
  • 83
    • 34249302408 scopus 로고    scopus 로고
    • Hypothesis: The 'metabolic memory', the new challenge of diabetes
    • DOI 10.1111/j.1464-5491.2007.02138.x
    • Ihnat MA, Thorpe JE, Ceriello A (2007) Hypothesis: the 'metabolic memory', the new challenge of diabetes. Diabet Med 24(6):582-586 (Pubitemid 46808866)
    • (2007) Diabetic Medicine , vol.24 , Issue.6 , pp. 582-586
    • Ihnat, M.A.1    Thorpe, J.E.2    Ceriello, A.3
  • 84
    • 48249127225 scopus 로고    scopus 로고
    • Epigenetic histone H3 lysine 9 methylation in metabolic memory and inflammatory phenotype of vascular smooth muscle cells in diabetes
    • 18579779 1:CAS:528:DC%2BD1cXosVCitbc%3D 10.1073/pnas.0803623105
    • Villeneuve LM, Reddy MA, Lanting LL, Wang M, Meng L, Natarajan R (2008) Epigenetic histone H3 lysine 9 methylation in metabolic memory and inflammatory phenotype of vascular smooth muscle cells in diabetes. Proc Natl Acad Sci USA 105(26):9047-9052
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.26 , pp. 9047-9052
    • Villeneuve, L.M.1    Reddy, M.A.2    Lanting, L.L.3    Wang, M.4    Meng, L.5    Natarajan, R.6
  • 85
    • 79960563344 scopus 로고    scopus 로고
    • Determinants and dynamics of genome accessibility
    • 10.1038/nrg3017 21747402 1:CAS:528:DC%2BC3MXovFyjtbo%3D 10.1038/nrg3017
    • Bell O, Tiwari VK, Thoma NH, Schubeler D (2011) Determinants and dynamics of genome accessibility. Nat Rev Genet 12(8):554-564. doi: 10.1038/nrg3017
    • (2011) Nat Rev Genet , vol.12 , Issue.8 , pp. 554-564
    • Bell, O.1    Tiwari, V.K.2    Thoma, N.H.3    Schubeler, D.4
  • 86
    • 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 (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119(7):941-953. doi: 10.1016/j.cell.2004.12.012 (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
  • 87
    • 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(7057):436-439. doi: 10.1038/nature04020 (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
  • 88
    • 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(9):715-727. doi: 10.1038/nrg1945 (Pubitemid 44260007)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.9 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 89
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • DOI 10.1038/nature04433, PII NATURE04433
    • Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y (2006) Histone demethylation by a family of JmjC domain-containing proteins. Nature 439(7078):811-816. doi: 10.1038/nature04433 (Pubitemid 43255695)
    • (2006) Nature , vol.439 , Issue.7078 , pp. 811-816
    • Tsukada, Y.-I.1    Fang, J.2    Erdjument-Bromage, H.3    Warren, M.E.4    Borchers, C.H.5    Tempst, P.6    Zhang, Y.7
  • 90
    • 78049286684 scopus 로고    scopus 로고
    • Histone demethylases in development and disease
    • 10.1016/j.tcb.2010.08.011 20863703 1:CAS:528:DC%2BC3cXhtlKhs7rF 10.1016/j.tcb.2010.08.011
    • Pedersen MT, Helin K (2010) Histone demethylases in development and disease. Trends Cell Biol 20(11):662-671. doi: 10.1016/j.tcb.2010.08.011
    • (2010) Trends Cell Biol , vol.20 , Issue.11 , pp. 662-671
    • Pedersen, M.T.1    Helin, K.2
  • 91
    • 64749111074 scopus 로고    scopus 로고
    • Role of Jhdm2a in regulating metabolic gene expression and obesity resistance
    • 19194461 1:CAS:528:DC%2BD1MXhsVCru7o%3D 10.1038/nature07777
    • Tateishi K, Okada Y, Kallin EM, Zhang Y (2009) Role of Jhdm2a in regulating metabolic gene expression and obesity resistance. Nature 458(7239):757-761
    • (2009) Nature , vol.458 , Issue.7239 , pp. 757-761
    • Tateishi, K.1    Okada, Y.2    Kallin, E.M.3    Zhang, Y.4
  • 92
    • 77956913456 scopus 로고    scopus 로고
    • Histone demethylase LSD1 regulates adipogenesis
    • 20656681 1:CAS:528:DC%2BC3cXhtFKksL%2FJ 10.1074/jbc.M110.151209
    • Musri MM, Carmona MC, Hanzu FA, Kaliman P, Gomis R, Parrizas M (2010) Histone demethylase LSD1 regulates adipogenesis. J Biol Chem 285(39):30034-30041
    • (2010) J Biol Chem , vol.285 , Issue.39 , pp. 30034-30041
    • Musri, M.M.1    Carmona, M.C.2    Hanzu, F.A.3    Kaliman, P.4    Gomis, R.5    Parrizas, M.6
  • 93
    • 53249108053 scopus 로고    scopus 로고
    • Role of the lysine-specific demethylase 1 in the proinflammatory phenotype of vascular smooth muscle cells of diabetic mice
    • 18688044 1:CAS:528:DC%2BD1cXhtFajsb%2FN 10.1161/CIRCRESAHA.108.175190
    • Reddy MA, Villeneuve LM, Wang M, Lanting L, Natarajan R (2008) Role of the lysine-specific demethylase 1 in the proinflammatory phenotype of vascular smooth muscle cells of diabetic mice. Circ Res 103(6):615-623
    • (2008) Circ Res , vol.103 , Issue.6 , pp. 615-623
    • Reddy, M.A.1    Villeneuve, L.M.2    Wang, M.3    Lanting, L.4    Natarajan, R.5
  • 94
    • 81155139577 scopus 로고    scopus 로고
    • The H3K27 demethylase UTX-1 regulates C. elegans lifespan in a germline-independent, insulin-dependent manner
    • 21834846 1:CAS:528:DC%2BC3MXhs1Sqt73F 10.1111/j.1474-9726.2011.00738.x
    • Maures TJ, Greer EL, Hauswirth AG, Brunet A (2011) The H3K27 demethylase UTX-1 regulates C. elegans lifespan in a germline-independent, insulin-dependent manner. Aging Cell 10(6):980-990
    • (2011) Aging Cell , vol.10 , Issue.6 , pp. 980-990
    • Maures, T.J.1    Greer, E.L.2    Hauswirth, A.G.3    Brunet, A.4
  • 95
    • 57149142495 scopus 로고    scopus 로고
    • The impact of O2 availability on human cancer
    • 10.1038/nrc2540 18987634 1:CAS:528:DC%2BD1cXhsVWhu7fO 10.1038/nrc2540
    • Bertout JA, Patel SA, Simon MC (2008) The impact of O2 availability on human cancer. Nat Rev Cancer 8(12):967-975. doi: 10.1038/nrc2540
    • (2008) Nat Rev Cancer , vol.8 , Issue.12 , pp. 967-975
    • Bertout, J.A.1    Patel, S.A.2    Simon, M.C.3
  • 97
    • 79955014357 scopus 로고    scopus 로고
    • Pathophysiological response to hypoxia - From the molecular mechanisms of malady to drug discovery: Epigenetic regulation of the hypoxic response via hypoxia-inducible factor and histone modifying enzymes
    • 21422728 1:CAS:528:DC%2BC3MXls1Gnt7k%3D 10.1254/jphs.10R19FM
    • Mimura I, Tanaka T, Wada Y, Kodama T, Nangaku M (2011) Pathophysiological response to hypoxia - from the molecular mechanisms of malady to drug discovery: epigenetic regulation of the hypoxic response via hypoxia-inducible factor and histone modifying enzymes. J Pharmacol Sci 115(4):453-458
    • (2011) J Pharmacol Sci , vol.115 , Issue.4 , pp. 453-458
    • Mimura, I.1    Tanaka, T.2    Wada, Y.3    Kodama, T.4    Nangaku, M.5
  • 98
    • 77954661616 scopus 로고    scopus 로고
    • Epigenetics, the epicenter of the hypoxic response
    • 20418669 1:CAS:528:DC%2BC3cXpslKlsbg%3D 10.4161/epi.5.4.11684
    • Watson JA, Watson CJ, McCann A, Baugh J (2010) Epigenetics, the epicenter of the hypoxic response. Epigenetics 5(4):293-296
    • (2010) Epigenetics , vol.5 , Issue.4 , pp. 293-296
    • Watson, J.A.1    Watson, C.J.2    McCann, A.3    Baugh, J.4
  • 99
    • 0012264770 scopus 로고    scopus 로고
    • Regulation of gene expression by the hypoxia-inducible factors
    • 10.1124/mi.2.4.229 1:CAS:528:DC%2BD3sXpsVWq 10.1124/mi.2.4.229
    • Fedele AO, Whitelaw ML, Peet DJ (2002) Regulation of gene expression by the hypoxia-inducible factors. Mol Interven 2(4):229-243. doi: 10.1124/mi.2.4.229
    • (2002) Mol Interven , vol.2 , Issue.4 , pp. 229-243
    • Fedele, A.O.1    Whitelaw, M.L.2    Peet, D.J.3
  • 100
    • 33749494456 scopus 로고    scopus 로고
    • Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells
    • DOI 10.1158/0008-5472.CAN-06-0101
    • Chen H, Yan Y, Davidson TL, Shinkai Y, Costa M (2006) Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells. Cancer Res 66(18):9009-9016. doi: 10.1158/0008-5472.CAN-06- 0101 (Pubitemid 44521119)
    • (2006) Cancer Research , vol.66 , Issue.18 , pp. 9009-9016
    • Chen, H.1    Yan, Y.2    Davidson, T.L.3    Shinkai, Y.4    Costa, M.5
  • 101
    • 40649114443 scopus 로고    scopus 로고
    • Hypoxia induces a novel signature of chromatin modifications and global repression of transcription
    • 10.1016/j.mrfmmm.2008.01.001 18294659 1:CAS:528:DC%2BD1cXjsVSgur4%3D
    • Johnson AB, Denko N, Barton MC (2008) Hypoxia induces a novel signature of chromatin modifications and global repression of transcription. Mutat Res 640(1-2):174-179. doi: 10.1016/j.mrfmmm.2008.01.001
    • (2008) Mutat Res , vol.640 , Issue.1-2 , pp. 174-179
    • Johnson, A.B.1    Denko, N.2    Barton, M.C.3
  • 102
    • 77952160818 scopus 로고    scopus 로고
    • MicroRNA-101 negatively regulates Ezh2 and its expression is modulated by androgen receptor and HIF-1alpha/HIF-1beta
    • 10.1186/1476-4598-9-108 20478051 10.1186/1476-4598-9-108 1:CAS:528:DC%2BC3cXms1GgsL0%3D
    • Cao P, Deng Z, Wan M, Huang W, Cramer SD, Xu J, Lei M, Sui G (2010) MicroRNA-101 negatively regulates Ezh2 and its expression is modulated by androgen receptor and HIF-1alpha/HIF-1beta. Molecular cancer 9:108. doi: 10.1186/1476-4598-9-108
    • (2010) Molecular Cancer , vol.9 , pp. 108
    • Cao, P.1    Deng, Z.2    Wan, M.3    Huang, W.4    Cramer, S.D.5    Xu, J.6    Lei, M.7    Sui, G.8
  • 103
    • 78651454089 scopus 로고    scopus 로고
    • EZH2 promotes expansion of breast tumor initiating cells through activation of RAF1-beta-catenin signaling
    • 10.1016/j.ccr.2010.10.035 21215703 1:CAS:528:DC%2BC3MXpvVaksw%3D%3D 10.1016/j.ccr.2010.10.035
    • Chang CJ, Yang JY, Xia W, Chen CT, Xie X, Chao CH, Woodward WA, Hsu JM, Hortobagyi GN, Hung MC (2011) EZH2 promotes expansion of breast tumor initiating cells through activation of RAF1-beta-catenin signaling. Cancer Cell 19(1):86-100. doi: 10.1016/j.ccr.2010.10.035
    • (2011) Cancer Cell , vol.19 , Issue.1 , pp. 86-100
    • Chang, C.J.1    Yang, J.Y.2    Xia, W.3    Chen, C.T.4    Xie, X.5    Chao, C.H.6    Woodward, W.A.7    Hsu, J.M.8    Hortobagyi, G.N.9    Hung, M.C.10
  • 105
    • 80052221592 scopus 로고    scopus 로고
    • Interplay between HDAC3 and WDR5 is essential for hypoxia-induced epithelial-mesenchymal transition
    • 10.1016/j.molcel.2011.07.012 21884981 1:CAS:528:DC%2BC3MXhtFeku7jJ 10.1016/j.molcel.2011.07.012
    • Wu MZ, Tsai YP, Yang MH, Huang CH, Chang SY, Chang CC, Teng SC, Wu KJ (2011) Interplay between HDAC3 and WDR5 is essential for hypoxia-induced epithelial-mesenchymal transition. Mol Cell 43(5):811-822. doi: 10.1016/j.molcel.2011.07.012
    • (2011) Mol Cell , vol.43 , Issue.5 , pp. 811-822
    • Wu, M.Z.1    Tsai, Y.P.2    Yang, M.H.3    Huang, C.H.4    Chang, S.Y.5    Chang, C.C.6    Teng, S.C.7    Wu, K.J.8
  • 106
    • 63449103705 scopus 로고    scopus 로고
    • Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis
    • 10.1073/pnas.0810067106 19255431 1:CAS:528:DC%2BD1MXjslChu7w%3D 10.1073/pnas.0810067106
    • Xia X, Lemieux ME, Li W, Carroll JS, Brown M, Liu XS, Kung AL (2009) Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis. Proc Natl Acad Sci USA 106(11):4260-4265. doi: 10.1073/pnas.0810067106
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.11 , pp. 4260-4265
    • Xia, X.1    Lemieux, M.E.2    Li, W.3    Carroll, J.S.4    Brown, M.5    Liu, X.S.6    Kung, A.L.7
  • 107
    • 45449110185 scopus 로고    scopus 로고
    • Hypoxia upregulates the histone demethylase JMJD1A via HIF-1
    • 10.1016/j.bbrc.2008.05.150 18538129 1:CAS:528:DC%2BD1cXns1SgtLw%3D 10.1016/j.bbrc.2008.05.150
    • Wellmann S, Bettkober M, Zelmer A, Seeger K, Faigle M, Eltzschig HK, Buhrer C (2008) Hypoxia upregulates the histone demethylase JMJD1A via HIF-1. Biochem Biophys Res Commun 372(4):892-897. doi: 10.1016/j.bbrc.2008.05.150
    • (2008) Biochem Biophys Res Commun , vol.372 , Issue.4 , pp. 892-897
    • Wellmann, S.1    Bettkober, M.2    Zelmer, A.3    Seeger, K.4    Faigle, M.5    Eltzschig, H.K.6    Buhrer, C.7
  • 108
    • 58949097017 scopus 로고    scopus 로고
    • Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha
    • 10.1042/BJ20081238 18713068 1:CAS:528:DC%2BD1cXhsVentrjJ 10.1042/BJ20081238
    • Pollard PJ, Loenarz C, Mole DR, McDonough MA, Gleadle JM, Schofield CJ, Ratcliffe PJ (2008) Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha. Biochem J 416(3):387-394. doi: 10.1042/BJ20081238
    • (2008) Biochem J , vol.416 , Issue.3 , pp. 387-394
    • Pollard, P.J.1    Loenarz, C.2    Mole, D.R.3    McDonough, M.A.4    Gleadle, J.M.5    Schofield, C.J.6    Ratcliffe, P.J.7
  • 109
    • 61349088682 scopus 로고    scopus 로고
    • The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF
    • 10.1074/jbc.M804578200 18984585 1:CAS:528:DC%2BD1cXhsFWnsrfO 10.1074/jbc.M804578200
    • Beyer S, Kristensen MM, Jensen KS, Johansen JV, Staller P (2008) The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. J Biol Chem 283(52):36542-36552. doi: 10.1074/jbc.M804578200
    • (2008) J Biol Chem , vol.283 , Issue.52 , pp. 36542-36552
    • Beyer, S.1    Kristensen, M.M.2    Jensen, K.S.3    Johansen, J.V.4    Staller, P.5
  • 110
    • 76049100577 scopus 로고    scopus 로고
    • HIF-1: Upstream and downstream of cancer metabolism
    • 10.1016/j.gde.2009.10.009 19942427 1:CAS:528:DC%2BC3cXhslWktr0%3D 10.1016/j.gde.2009.10.009
    • Semenza GL (2010) HIF-1: upstream and downstream of cancer metabolism. Curr Opin Genet Dev 20(1):51-56. doi: 10.1016/j.gde.2009.10.009
    • (2010) Curr Opin Genet Dev , vol.20 , Issue.1 , pp. 51-56
    • Semenza, G.L.1
  • 111
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth
    • 10.1128/MCB.00444-09 19858293 1:CAS:528:DC%2BC3cXisVKhtLw%3D 10.1128/MCB.00444-09
    • Krieg AJ, Rankin EB, Chan D, Razorenova O, Fernandez S, Giaccia AJ (2010) Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth. Mol Cell Biol 30(1):344-353. doi: 10.1128/MCB.00444-09
    • (2010) Mol Cell Biol , vol.30 , Issue.1 , pp. 344-353
    • Krieg, A.J.1    Rankin, E.B.2    Chan, D.3    Razorenova, O.4    Fernandez, S.5    Giaccia, A.J.6
  • 112
    • 2342597973 scopus 로고    scopus 로고
    • Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth
    • DOI 10.1371/journal.pbio.0000083
    • Kondo K, Kim WY, Lechpammer M, Kaelin WG Jr (2003) Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth. PLoS Biol 1(3):E83. doi: 10.1371/journal.pbio.0000083 (Pubitemid 39112142)
    • (2003) PLoS Biology , vol.1 , Issue.3
    • Kondo, K.1    Kim, W.Y.2    Lechpammer, M.3    Kaelin Jr., W.G.4
  • 113
    • 84856955226 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein regulates gene expression and tumor growth through histone demethylase JARID1C
    • 10.1038/onc.2011.266
    • Niu X, Zhang T, Liao L, Zhou L, Lindner DJ, Zhou M, Rini B, Yan Q, Yang H (2011) The von Hippel-Lindau tumor suppressor protein regulates gene expression and tumor growth through histone demethylase JARID1C. Oncogene. doi: 10.1038/onc.2011.266
    • (2011) Oncogene
    • Niu, X.1    Zhang, T.2    Liao, L.3    Zhou, L.4    Lindner, D.J.5    Zhou, M.6    Rini, B.7    Yan, Q.8    Yang, H.9
  • 115
    • 64849098267 scopus 로고    scopus 로고
    • Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha
    • 10.1126/science.1170944 19359588 1:CAS:528:DC%2BD1MXktFals7g%3D 10.1126/science.1170944
    • Zhao S, Lin Y, Xu W, Jiang W, Zha Z, Wang P, Yu W, Li Z, Gong L, Peng Y, Ding J, Lei Q, Guan KL, Xiong Y (2009) Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha. Science 324(5924):261-265. doi: 10.1126/science.1170944
    • (2009) Science , vol.324 , Issue.5924 , pp. 261-265
    • Zhao, S.1    Lin, Y.2    Xu, W.3    Jiang, W.4    Zha, Z.5    Wang, P.6    Yu, W.7    Li, Z.8    Gong, L.9    Peng, Y.10    Ding, J.11    Lei, Q.12    Guan, K.L.13    Xiong, Y.14
  • 119
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • Cheng X, Roberts RJ (2001) AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Res 29(18):3784-3795 (Pubitemid 32910519)
    • (2001) Nucleic Acids Research , vol.29 , Issue.18 , pp. 3784-3795
    • Cheng, X.1    Roberts, R.J.2
  • 120
    • 0026740497 scopus 로고
    • Developmental pattern of gene-specific DNA methylation in the mouse embryo and germ line
    • 1577268 1:CAS:528:DyaK38XktVCrt7s%3D 10.1101/gad.6.5.705
    • Kafri T, Ariel M, Brandeis M, Shemer R, Urven L, McCarrey J, Cedar H, Razin A (1992) Developmental pattern of gene-specific DNA methylation in the mouse embryo and germ line. Genes Dev 6(5):705-714
    • (1992) Genes Dev , vol.6 , Issue.5 , pp. 705-714
    • Kafri, T.1    Ariel, M.2    Brandeis, M.3    Shemer, R.4    Urven, L.5    McCarrey, J.6    Cedar, H.7    Razin, A.8
  • 121
    • 0023119242 scopus 로고
    • Temporal and regional changes in DNA methylation in the embryonic, extraembryonic and germ cell lineages during mouse embryo development
    • Monk M, Boubelik M, Lehnert S (1987) Temporal and regional changes in DNA methylation in the embryonic, extraembryonic and germ cell lineages during mouse embryo development. Development (Cambridge, England) 99(3):371-382 (Pubitemid 17048855)
    • (1987) Development , vol.99 , Issue.3 , pp. 371-382
    • Monk, M.1    Boubelik, M.2    Lehnert, S.3
  • 122
    • 0033615717 scopus 로고    scopus 로고
    • DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development
    • DOI 10.1016/S0092-8674(00)81656-6
    • Okano M, Bell DW, Haber DA, Li E (1999) DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development. Cell 99(3):247-257 (Pubitemid 29519904)
    • (1999) Cell , vol.99 , Issue.3 , pp. 247-257
    • Okano, M.1    Bell, D.W.2    Haber, D.A.3    Li, E.4
  • 124
    • 34548603504 scopus 로고    scopus 로고
    • Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation
    • DOI 10.1038/nature06146, PII NATURE06146
    • Jia D, Jurkowska RZ, Zhang X, Jeltsch A, Cheng X (2007) Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation. Nature 449(7159):248-251 (Pubitemid 47402375)
    • (2007) Nature , vol.449 , Issue.7159 , pp. 248-251
    • Jia, D.1    Jurkowska, R.Z.2    Zhang, X.3    Jeltsch, A.4    Cheng, X.5
  • 125
    • 29644440388 scopus 로고    scopus 로고
    • Establishment and maintenance of DNA methylation patterns in mammals
    • Chen T, Li E (2006) Establishment and maintenance of DNA methylation patterns in mammals. Curr Top Microbiol Immunol 301:179-201 (Pubitemid 43022672)
    • (2006) Current Topics in Microbiology and Immunology , vol.301 , pp. 179-201
    • Chen, T.1    Li, E.2
  • 127
    • 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(1):2-6 (Pubitemid 46024187)
    • (2007) Nature Cell Biology , vol.9 , Issue.1 , pp. 2-6
    • Turner, B.M.1
  • 128
    • 39049157446 scopus 로고    scopus 로고
    • Complete nucleotide sequence and experimental host range of Okra mosaic virus
    • 18049886 1:CAS:528:DC%2BD1cXhtlGgsro%3D 10.1007/s11262-007-0181-1
    • Stephan D, Siddiqua M, Ta Hoang A, Engelmann J, Winter S, Maiss E (2008) Complete nucleotide sequence and experimental host range of Okra mosaic virus. Virus Genes 36(1):231-240
    • (2008) Virus Genes , vol.36 , Issue.1 , pp. 231-240
    • Stephan, D.1    Siddiqua, M.2    Ta Hoang, A.3    Engelmann, J.4    Winter, S.5    Maiss, E.6
  • 130
    • 33645132331 scopus 로고    scopus 로고
    • G9a-mediated irreversible epigenetic inactivation of Oct-3/4 during early embryogenesis
    • 16415856 1:CAS:528:DC%2BD28XptFOlsQ%3D%3D 10.1038/ncb1353
    • Feldman N, Gerson A, Fang J, Li E, Zhang Y, Shinkai Y, Cedar H, Bergman Y (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    Gerson, A.2    Fang, J.3    Li, E.4    Zhang, Y.5    Shinkai, Y.6    Cedar, H.7    Bergman, Y.8
  • 131
    • 79961090805 scopus 로고    scopus 로고
    • Evolutionary diversity and developmental regulation of X-chromosome inactivation
    • 21687993 1:CAS:528:DC%2BC3MXoslWksbc%3D 10.1007/s00439-011-1029-2
    • Escamilla-Del-Arenal M, da Rocha ST, Heard E (2011) Evolutionary diversity and developmental regulation of X-chromosome inactivation. Hum Genet 130(2):307-327
    • (2011) Hum Genet , vol.130 , Issue.2 , pp. 307-327
    • Escamilla-Del-Arenal, M.1    Da Rocha, S.T.2    Heard, E.3
  • 133
    • 80051997952 scopus 로고    scopus 로고
    • Dynamic interactions between transposable elements and their hosts
    • 1:CAS:528:DC%2BC3MXhtVeiurrE 10.1038/nrg3030
    • Levin HL, Moran JV (2011) Dynamic interactions between transposable elements and their hosts. Nat Rev 12(9):615-627
    • (2011) Nat Rev , vol.12 , Issue.9 , pp. 615-627
    • Levin, H.L.1    Moran, J.V.2
  • 134
  • 135
    • 0036322831 scopus 로고    scopus 로고
    • Maternal methyl supplements in mice affect epigenetic variation and DNA methylation of offspring
    • Cooney CA, Dave AA, Wolff GL (2002) Maternal methyl supplements in mice affect epigenetic variation and DNA methylation of offspring. J Nutr 132(8 Suppl):2393S-2400S (Pubitemid 34848114)
    • (2002) Journal of Nutrition , vol.132 , Issue.SUPPL. 8
    • Cooney, C.A.1    Dave, A.A.2    Wolff, G.L.3
  • 136
    • 0031873353 scopus 로고    scopus 로고
    • Maternal epigenetics and methyl supplements affect agouti gene expression in A(vy)/a mice
    • Wolff GL, Kodell RL, Moore SR, Cooney CA (1998) Maternal epigenetics and methyl supplements affect agouti gene expression in Avy/a mice. FASEB J 12(11):949-957 (Pubitemid 28359576)
    • (1998) FASEB Journal , vol.12 , Issue.11 , pp. 949-957
    • Wolff, G.L.1    Kodell, R.L.2    Moore, S.R.3    Cooney, C.A.4
  • 138
    • 0043093697 scopus 로고    scopus 로고
    • Transposable elements: Targets for early nutritional effects on epigenetic gene regulation
    • DOI 10.1128/MCB.23.15.5293-5300.2003
    • Waterland RA, Jirtle RL (2003) Transposable elements: targets for early nutritional effects on epigenetic gene regulation. Mol Cell Biol 23(15):5293-5300 (Pubitemid 36950884)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.15 , pp. 5293-5300
    • Waterland, R.A.1    Jirtle, R.L.2
  • 139
    • 79955627138 scopus 로고    scopus 로고
    • A sustained dietary change increases epigenetic variation in isogenic mice
    • 21541011 1:CAS:528:DC%2BC3MXlsVagtLw%3D 10.1371/journal.pgen.1001380
    • Li CC, Cropley JE, Cowley MJ, Preiss T, Martin DI, Suter CM (2011) A sustained dietary change increases epigenetic variation in isogenic mice. PLoS Genet 7(4):e1001380
    • (2011) PLoS Genet , vol.7 , Issue.4 , pp. 1001380
    • Li, C.C.1    Cropley, J.E.2    Cowley, M.J.3    Preiss, T.4    Martin, D.I.5    Suter, C.M.6
  • 140
    • 79954611176 scopus 로고    scopus 로고
    • A dual epigenomic approach for the search of obesity biomarkers: DNA methylation in relation to diet-induced weight loss
    • 21209057 1:CAS:528:DC%2BC3MXkslSks7k%3D 10.1096/fj.10-170365
    • Milagro FI, Campion J, Cordero P, Goyenechea E, Gomez-Uriz AM, Abete I, Zulet MA, Martinez JA (2011) A dual epigenomic approach for the search of obesity biomarkers: DNA methylation in relation to diet-induced weight loss. FASEB J 25(4):1378-1389
    • (2011) FASEB J , vol.25 , Issue.4 , pp. 1378-1389
    • Milagro, F.I.1    Campion, J.2    Cordero, P.3    Goyenechea, E.4    Gomez-Uriz, A.M.5    Abete, I.6    Zulet, M.A.7    Martinez, J.A.8
  • 141
    • 41349085806 scopus 로고    scopus 로고
    • Nutritional control of reproductive status in honeybees via DNA methylation
    • DOI 10.1126/science.1153069
    • Kucharski R, Maleszka J, Foret S, Maleszka R (2008) Nutritional control of reproductive status in honeybees via DNA methylation. Science (New York, NY) 319(5871):1827-1830 (Pubitemid 351451590)
    • (2008) Science , vol.319 , Issue.5871 , pp. 1827-1830
    • Kucharski, R.1    Maleszka, J.2    Foret, S.3    Maleszka, R.4
  • 142
    • 54949122508 scopus 로고    scopus 로고
    • Epigenetic integration of environmental and genomic signals in honey bees: The critical interplay of nutritional, brain and reproductive networks
    • 18719401 10.4161/epi.3.4.6697
    • Maleszka R (2008) Epigenetic integration of environmental and genomic signals in honey bees: the critical interplay of nutritional, brain and reproductive networks. Epigenetics 3(4):188-192
    • (2008) Epigenetics , vol.3 , Issue.4 , pp. 188-192
    • Maleszka, R.1
  • 143
    • 77956095231 scopus 로고    scopus 로고
    • Active DNA demethylation: Many roads lead to Rome
    • 20683471 1:CAS:528:DC%2BC3cXps1egtbY%3D 10.1038/nrm2950
    • Wu SC, Zhang Y (2010) Active DNA demethylation: many roads lead to Rome. Nat Rev Mol Cell Biol 11(9):607-620
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.9 , pp. 607-620
    • Wu, S.C.1    Zhang, Y.2
  • 144
    • 80052303426 scopus 로고    scopus 로고
    • TET family proteins and their role in stem cell differentiation and transformation
    • 21885017 1:CAS:528:DC%2BC3MXhtFeks7nE 10.1016/j.stem.2011.08.007
    • Cimmino L, Abdel-Wahab O, Levine RL, Aifantis I (2011) TET family proteins and their role in stem cell differentiation and transformation. Cell Stem Cell 9(3):193-204
    • (2011) Cell Stem Cell , vol.9 , Issue.3 , pp. 193-204
    • Cimmino, L.1    Abdel-Wahab, O.2    Levine, R.L.3    Aifantis, I.4
  • 146
    • 79960117245 scopus 로고    scopus 로고
    • Hypothesis: Environmental regulation of 5-hydroxymethylcytosine by oxidative stress
    • 21617369 10.4161/epi.6.7.16461 1:CAS:528:DC%2BC38Xht1Orsrc%3D
    • Chia N, Wang L, Lu X, Senut MC, Brenner C, Ruden DM (2011) Hypothesis: environmental regulation of 5-hydroxymethylcytosine by oxidative stress. Epigenetics 6(7):853-856
    • (2011) Epigenetics , vol.6 , Issue.7 , pp. 853-856
    • Chia, N.1    Wang, L.2    Lu, X.3    Senut, M.C.4    Brenner, C.5    Ruden, D.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.