메뉴 건너뛰기




Volumn 21, Issue 3, 2011, Pages 435-441

Epigenetic inheritance: Uncontested?

Author keywords

Epigenetics; histone; inheritance; modifications

Indexed keywords

HISTONE;

EID: 79952536795     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2011.26     Document Type: Review
Times cited : (82)

References (70)
  • 1
    • 78049402859 scopus 로고    scopus 로고
    • Molecular signals of epigenetic states
    • Bonasio R, Tu S, Reinberg D. Molecular signals of epigenetic states. Science 2010;330:612-616.
    • (2010) Science , vol.330 , pp. 612-616
    • Bonasio, R.1    Tu, S.2    Reinberg, D.3
  • 2
    • 0016211838 scopus 로고
    • Chromatin structure: Oligomers of the histones
    • Kornberg RD, Thomas JO. Chromatin structure: oligomers of the histones. Science 1974;184:865-868.
    • (1974) Science , vol.184 , pp. 865-868
    • Kornberg, R.D.1    Thomas, J.O.2
  • 3
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Feb. 15. doi:10.1038/cr.2011.22
    • Bannister AJ, Kouzarides T. Regulation of chromatin by histone modifications. Cell Res 2011 Feb. 15. doi:10.1038/cr.2011.22
    • (2011) Cell. Res.
    • Bannister, A.J.1    Kouzarides, T.2
  • 4
    • 36248982297 scopus 로고    scopus 로고
    • Overviews and concepts
    • Allis CD, Jenuwein T, Reinberg D, eds, New York: Cold Spring Harbor Laboratory Press
    • Allis CD, Jenuwein T, Reinberg D. Overviews and concepts. In: Allis CD, Jenuwein T, Reinberg D, eds. Epigenetics. New York: Cold Spring Harbor Laboratory Press, 2006:23-56.
    • (2006) Epigenetics , pp. 23-56
    • Allis, C.D.1    Jenuwein, T.2    Reinberg, D.3
  • 6
    • 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. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 2001;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
  • 9
    • 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, Melf R, McCabe D, Seitz V, Imhof A, Pirrotta V. Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 2002;111:185-196. (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
  • 11
    • 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. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev 2002;16:2893-2905. (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
  • 13
    • 0942268864 scopus 로고    scopus 로고
    • Epigenetic Dynamics of Imprinted X Inactivation during Early Mouse Development
    • DOI 10.1126/science.1092727
    • Okamoto I, Otte AP, Allis CD, Reinberg D, Heard E. Epigenetic dynamics of imprinted X inactivation during early mouse development. Science 2004;303:644-649. (Pubitemid 38141624)
    • (2004) Science , vol.303 , Issue.5658 , pp. 644-649
    • Okamoto, I.1    Otte, A.P.2    Allis, C.D.3    Reinberg, D.4    Heard, E.5
  • 14
    • 0016439429 scopus 로고
    • DNA modification mechanisms and gene activity during development
    • Holliday R, Pugh JE. DNA modification mechanisms and gene activity during development. Science 1975;187:226-232.
    • (1975) Science , vol.187 , pp. 226-232
    • Holliday, R.1    Pugh, J.E.2
  • 15
    • 0026697174 scopus 로고
    • Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain
    • Bestor TH. Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain. EMBO J 1992;11:2611-2617.
    • (1992) EMBO J. , vol.11 , pp. 2611-2617
    • Bestor, T.H.1
  • 16
    • 0026439115 scopus 로고
    • A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei
    • Leonhardt H, Page AW, Weier HU, Bestor TH. A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei. Cell 1992;71:865-873.
    • (1992) Cell. , vol.71 , pp. 865-873
    • Leonhardt, H.1    Page, A.W.2    Weier, H.U.3    Bestor, T.H.4
  • 17
    • 0017041240 scopus 로고
    • A model for chromatin based upon two symmetrically paired half nucleosomes
    • Weintraub H, Worcel A, Alberts B. A model for chromatin based upon two symmetrically paired half-nucleosomes. Cell 1976;9:409-417. (Pubitemid 8003667)
    • (1976) Cell , vol.9 , Issue.3 , pp. 409-417
    • Weintraub, H.1    Worcel, A.2    Alberts, B.3
  • 18
    • 0017054798 scopus 로고
    • Studies on the mode of segregation of histone nu bodies during replication in HeLa cells
    • Seale RL. Studies on the mode of segregation of histone nu bodies during replication in HeLa cells. Cell 1976;9:423-429. (Pubitemid 8003669)
    • (1976) Cell , vol.9 , Issue.3 , pp. 423-429
    • Seale, R.L.1
  • 19
    • 0017715478 scopus 로고
    • Conservative assembly and segregation of nucleosomal histones
    • Leffak IM, Grainger R, Weintraub H. Conservative assembly and segregation of nucleosomal histones. Cell 1977;12:837-845. (Pubitemid 8224422)
    • (1977) Cell , vol.12 , Issue.3 , pp. 837-845
    • Leffak, I.M.1    Grainger, R.2    Weintraub, H.3
  • 20
    • 0019888372 scopus 로고
    • Formation of hybrid nucleosomes containing new and old histones
    • Russev G, Hancock R. Formation of hybrid nucleosomes containing new and old histones. Nucleic Acids Res 1981;9:4129-4137.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 4129-4137
    • Russev, G.1    Hancock, R.2
  • 21
    • 0019351449 scopus 로고
    • A new method for the isolation of replicative chromatin: Selective deposition of histone on both new and old DNA
    • Jackson V, Chalkley R. A new method for the isolation of replicative chromatin: selective deposition of histone on both new and old DNA. Cell 1981;23:121-134. (Pubitemid 11173616)
    • (1981) Cell , vol.23 , Issue.1 , pp. 121-134
    • Jackson, V.1    Chalkley, R.2
  • 22
    • 0019888031 scopus 로고
    • A reevaluation of new histone deposition on replicating chromatin
    • Jackson V, Chalkley R. A reevaluation of new histone deposition on replicating chromatin. J Biol Chem 1981;256:5095-5103.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5095-5103
    • Jackson, V.1    Chalkley, R.2
  • 23
    • 0020490906 scopus 로고
    • Association of newly synthesized histones with replicating and nonreplicating regions of chromatin
    • Annunziato AT, Schindler RK, Riggs MG, Seale RL. Association of newly synthesized histones with replicating and nonreplicating regions of chromatin. J Biol Chem 1982;257:8507-8515.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8507-8515
    • Annunziato, A.T.1    Schindler, R.K.2    Riggs, M.G.3    Seale, R.L.4
  • 24
    • 0018891793 scopus 로고
    • Incorporation of exogenous pyrene-labeled histone into Physarum chromatin: A system for studying changes in nucleosomes assembled in vivo
    • Prior CP, Canto CR, Johnson EM, Allfrey VG. Incorporation of exogenous pyrene-labeled histone into Physarum chromatin: a system for studying changes in nucleosomes assembled in vivo. Cell 1980;20:597-608. (Pubitemid 10078539)
    • (1980) Cell , vol.20 , Issue.3 , pp. 597-608
    • Prior, C.P.1    Cantor, C.R.2    Johnson, E.M.3    Allfrey, V.G.4
  • 25
    • 0023945277 scopus 로고
    • Deposition of newly synthesized histones: Hybrid nucleosomes are not tandemly arranged on daughter DNA strands
    • Jackson V. Deposition of newly synthesized histones: hybrid nucleosomes are not tandemly arranged on daughter DNA strands. Biochemistry 1988;27:2109-2120.
    • (1988) Biochemistry , vol.27 , pp. 2109-2120
    • Jackson, V.1
  • 26
    • 0025134076 scopus 로고
    • In vivo studies on the dynamics of histone-DNA interaction: Evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both
    • DOI 10.1021/bi00455a019
    • Jackson V. In vivo studies on the dynamics of histone-DNA interaction: evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both. Biochemistry 1990;29:719-731. (Pubitemid 20041955)
    • (1990) Biochemistry , vol.29 , Issue.3 , pp. 719-731
    • Jackson, V.1
  • 27
    • 0025138502 scopus 로고
    • Conservative segregation of tetrameric units of H3 and H4 histones during nucleosome replication
    • Yamasu K, Senshu T. Conservative segregation of tetrameric units of H3 and H4 histones during nucleosome replication. J Biochem 1990;107:15-20. (Pubitemid 20027261)
    • (1990) Journal of Biochemistry , vol.107 , Issue.1 , pp. 15-20
    • Yamasu, K.1    Senshu, T.2
  • 28
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 Complexes Mediate Nucleosome Assembly Pathways Dependent or Independent of DNA Synthesis
    • DOI 10.1016/S0092-8674(03)01064-X
    • Tagami H, Ray-Gallet D, Almouzni G, Nakatani Y. Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell 2004;116:51-61. (Pubitemid 38156183)
    • (2004) Cell , vol.116 , Issue.1 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 29
    • 27144453690 scopus 로고    scopus 로고
    • ASF1 binds to a heterodimer of histones H3 and H4: A two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA
    • DOI 10.1021/bi051333h
    • English CM, Maluf NK, Tripet B, Churchill ME, Tyler JK. ASF1 binds to a heterodimer of histones H3 and H4: a twostep mechanism for the assembly of H3-H4 heterotetramer on DNA. Biochemistry 2005;44:13673-13682. (Pubitemid 41507448)
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 13673-13682
    • English, C.M.1    Maluf, N.K.2    Tripet, B.3    Churchill, M.E.A.4    Tyler, J.K.5
  • 31
    • 33750477650 scopus 로고    scopus 로고
    • Structural Basis for the Histone Chaperone Activity of Asf1
    • DOI 10.1016/j.cell.2006.08.047, PII S0092867406012736
    • English CM, Adkins MW, Carson JJ, Churchill ME, Tyler JK. Structural basis for the histone chaperone activity of Asf1. Cell 2006;127:495-508. (Pubitemid 44647420)
    • (2006) Cell , vol.127 , Issue.3 , pp. 495-508
    • English, C.M.1    Adkins, M.W.2    Carson, J.J.3    Churchill, M.E.A.4    Tyler, J.K.5
  • 32
    • 33847226680 scopus 로고    scopus 로고
    • Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
    • DOI 10.1038/nature05613, PII NATURE05613
    • Natsume R, Eitoku M, Akai Y, Sano N, Horikoshi M, Senda T. Structure and function of the histone chaperon CIA/ASF1 complexed with histones H3 and H4. Nature 2007;446:338-341. (Pubitemid 46437114)
    • (2007) Nature , vol.446 , Issue.7133 , pp. 338-341
    • Natsume, R.1    Eitoku, M.2    Akai, Y.3    Sano, N.4    Horikoshi, M.5    Senda, T.6
  • 33
    • 16844384065 scopus 로고    scopus 로고
    • Split decision: What happens to nucleosomes during DNA replication?
    • Annunziato AT. Split decision: what happens to nucleosomes during DNA replication? J Biol Chem 2005;280:12065-12068.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12065-12068
    • Annunziato, A.T.1
  • 34
    • 23044488979 scopus 로고    scopus 로고
    • Two distinct nucleosome assembly pathways: Dependent or independent of DNA synthesis promoted by histone H3.1 and H3.3 complexes
    • DOI 10.1101/sqb.2004.69.273
    • Nakatani Y, Ray-Gallet D, Quivy JP, Tagami H, Almouzni G. Two distinct nucleosome assembly pathways: dependent or independent of DNA synthesis promoted by histone H3.1 and H3.3 complexes. Cold Spring Harb Symp Quant Biol 2004;69:273-280. (Pubitemid 41056564)
    • (2004) Cold Spring Harbor Symposia on Quantitative Biology , vol.69 , pp. 273-280
    • Nakatani, Y.1    Ray-Gallet, D.2    Quivy, J.-P.3    Tagami, H.4    Almouzni, G.5
  • 35
    • 2942746179 scopus 로고    scopus 로고
    • Histone variants, nucleosome assembly and epigenetic inheritance
    • DOI 10.1016/j.tig.2004.05.004, PII S0168952504001295
    • Henikoff S, Furuyama T, Ahmad K. Histone variants, nucleosome assembly and epigenetic inheritance. Trends Genet 2004;20:320-326. (Pubitemid 38798541)
    • (2004) Trends in Genetics , vol.20 , Issue.7 , pp. 320-326
    • Henikoff, S.1    Furuyama, T.2    Ahmad, K.3
  • 36
    • 33646239638 scopus 로고    scopus 로고
    • Histone H3 variants and their potential role in indexing mammalian genomes: The "H3 barcode hypothesis"
    • Hake SB, Allis CD. Histone H3 variants and their potential role in indexing mammalian genomes: the "H3 barcode hypothesis". Proc Natl Acad Sci USA 2006;103:6428-6435.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6428-6435
    • Hake, S.B.1    Allis, C.D.2
  • 37
    • 33847076248 scopus 로고    scopus 로고
    • Chromatin Challenges during DNA Replication and Repair
    • DOI 10.1016/j.cell.2007.01.030, PII S0092867407001298
    • Groth A, Rocha W, Verreault A, Almouzni G. Chromatin challenges during DNA replication and repair. Cell 2007;128:721-733. (Pubitemid 46273574)
    • (2007) Cell , vol.128 , Issue.4 , pp. 721-733
    • Groth, A.1    Rocha, W.2    Verreault, A.3    Almouzni, G.4
  • 38
    • 34250192537 scopus 로고    scopus 로고
    • Mechanisms of epigenetic inheritance
    • DOI 10.1016/j.ceb.2007.04.002, PII S0955067407000543, Nucleus and Gene Expression
    • Martin C, Zhang Y. Mechanisms of epigenetic inheritance. Curr Opin Cell Biol 2007;19:266-272. (Pubitemid 46899505)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.3 , pp. 266-272
    • Martin, C.1    Zhang, Y.2
  • 40
    • 77950462427 scopus 로고    scopus 로고
    • Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly
    • Xu M, Long C, Chen X, Huang C, Chen S, Zhu B. Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly. Science 2010;328:94-98.
    • (2010) Science , vol.328 , pp. 94-98
    • Xu, M.1    Long, C.2    Chen, X.3    Huang, C.4    Chen, S.5    Zhu, B.6
  • 41
    • 0026439115 scopus 로고
    • A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei
    • Leonhardt H, Page AW, Weier HU, Bestor TH. A targeting sequence directs DNA methyltransferase to sites of DNA replication in mammalian nuclei. Cell 1992;71:865-873.
    • (1992) Cell. , vol.71 , pp. 865-873
    • Leonhardt, H.1    Page, A.W.2    Weier, H.U.3    Bestor, T.H.4
  • 42
    • 0030770835 scopus 로고    scopus 로고
    • Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21(WAF1)
    • DOI 10.1126/science.277.5334.1996
    • Chuang LS, Ian HI, Koh TW, Ng HH, Xu G, Li BF. Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1. Science 1997;277:1996-2000. (Pubitemid 27449142)
    • (1997) Science , vol.277 , Issue.5334 , pp. 1996-2000
    • Chuang, L.S.-H.1    Ian, H.-I.2    Koh, T.-W.3    Ng, H.-H.4    Xu, G.5    Li, B.F.L.6
  • 43
    • 34648833002 scopus 로고    scopus 로고
    • UHRF1 plays a role in maintaining DNA methylation in mammalian cells
    • DOI 10.1126/science.1147939
    • Bostick M, Kim JK, Estève PO, Clark A, Pradhan S, Jacobsen SE. UHRF1 plays a role in maintaining DNA methylation in mammalian cells. Science 2007;317:1760-1764. (Pubitemid 47461842)
    • (2007) Science , vol.317 , Issue.5845 , pp. 1760-1764
    • Bostick, M.1    Jong, K.K.2    Esteve, P.-O.3    Clark, A.4    Pradhan, S.5    Jacobsen, S.E.6
  • 45
    • 0037036465 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification
    • DOI 10.1074/jbc.M202504200
    • Milutinovic S, Zhuang Q, Szyf M. Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification. J Biol Chem 2002;277:20974-20978. (Pubitemid 34967408)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20974-20978
    • Milutinovic, S.1    Zhuang, Q.2    Szyf, M.3
  • 46
    • 0037405867 scopus 로고    scopus 로고
    • The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1
    • DOI 10.1128/MCB.23.9.3226-3236.2003
    • Reese BE, Bachman KE, Baylin SB, Rountree MR. The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1. Mol Cell Biol 2003;23:3226-3236. (Pubitemid 36459235)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.9 , pp. 3226-3236
    • Reese, B.E.1    Bachman, K.E.2    Baylin, S.B.3    Rountree, M.R.4
  • 47
    • 4344685735 scopus 로고    scopus 로고
    • Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly
    • DOI 10.1016/j.molcel.2004.06.043, PII S1097276504004046
    • Sarraf SA, Stancheva I. Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly. Mol Cell 2004;15:595-605. (Pubitemid 39141786)
    • (2004) Molecular Cell , vol.15 , Issue.4 , pp. 595-605
    • Sarraf, S.A.1    Stancheva, I.2
  • 48
    • 67650096728 scopus 로고    scopus 로고
    • The HP1alpha-CAF1-SetDB1-containing complex provides H3K9me1 for Suv39-mediated K9me3 in pericentric heterochromatin
    • Loyola A, Tagami H, Bonaldi T, et al. The HP1alpha-CAF1-SetDB1-containing complex provides H3K9me1 for Suv39-mediated K9me3 in pericentric heterochromatin. EMBO Rep 2009;10:769-775.
    • (2009) EMBO Rep. , vol.10 , pp. 769-775
    • Loyola, A.1    Tagami, H.2    Bonaldi, T.3
  • 50
    • 55549103314 scopus 로고    scopus 로고
    • A model for transmission of the H3K27me3 epigenetic mark
    • Hansen KH, Bracken AP, Pasini D, et al. A model for transmission of the H3K27me3 epigenetic mark. Nat Cell Biol 2008;10:1291-1300.
    • (2008) Nat. Cell. Biol. , vol.10 , pp. 1291-1300
    • Hansen, K.H.1    Bracken, A.P.2    Pasini, D.3
  • 51
    • 37549014575 scopus 로고    scopus 로고
    • Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle
    • Pesavento JJ, Yang H, Kelleher NL, Mizzen CA. Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle. Mol Cell Biol 2008;28:468-486.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 468-486
    • Pesavento, J.J.1    Yang, H.2    Kelleher, N.L.3    Mizzen, C.A.4
  • 52
    • 69849087056 scopus 로고    scopus 로고
    • Establishment of histone modifications after chromatin assembly
    • Scharf AN, Barth TK, Imhof A. Establishment of histone modifications after chromatin assembly. Nucleic Acids Res 2009;37:5032-5040.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5032-5040
    • Scharf, A.N.1    Barth, T.K.2    Imhof, A.3
  • 53
    • 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, Okamoto I, Murphy N, et al. Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development. Mol Cell Biol 2009;29:2278-2295.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2278-2295
    • Oda, H.1    Okamoto, I.2    Murphy, N.3
  • 54
    • 78149423004 scopus 로고    scopus 로고
    • Regulation of the histone H4 monomethylase PR-Set7 by CRL4 Cdt2-mediated PCNA-dependent degradation during DNA damage
    • Oda H, Hübner MR, Beck DB, et al. Regulation of the histone H4 monomethylase PR-Set7 by CRL4 Cdt2-mediated PCNA-dependent degradation during DNA damage. Mol Cell 2010;40:364-376.
    • (2010) Mol. Cell. , vol.40 , pp. 364-376
    • Oda, H.1    Hübner, M.R.2    Beck, D.B.3
  • 55
    • 78349272437 scopus 로고    scopus 로고
    • Dynamic regulation of the PR-Set7 histone methyltransferase is required for normal cell cycle progression
    • Wu S, Wang W, Kong X, et al. Dynamic regulation of the PR-Set7 histone methyltransferase is required for normal cell cycle progression. Genes Dev 2010;24:2531-2542.
    • (2010) Genes Dev. , vol.24 , pp. 2531-2542
    • Wu, S.1    Wang, W.2    Kong, X.3
  • 56
    • 77957378110 scopus 로고    scopus 로고
    • CRL4 (Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation
    • Abbas T, Shibata E, Park J, Jha S, Karnani N, Dutta A. CRL4 (Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation. Mol Cell 2010;40:9-21.
    • (2010) Mol. Cell. , vol.40 , pp. 9-21
    • Abbas, T.1    Shibata, E.2    Park, J.3    Jha, S.4    Karnani, N.5    Dutta, A.6
  • 57
    • 77957367739 scopus 로고    scopus 로고
    • CRL4 (Cdt2) - Mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase
    • Centore RC, Havens CG, Manning AL, et al. CRL4 (Cdt2) - mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase. Mol Cell 2010;40:22-33.
    • (2010) Mol. Cell. , vol.40 , pp. 22-33
    • Centore, R.C.1    Havens, C.G.2    Manning, A.L.3
  • 58
    • 78149281634 scopus 로고    scopus 로고
    • The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells
    • Tardat M, Brustel J, Kirsh O, et al. The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells. Nat Cell Biol 2010;12:1086-1093.
    • (2010) Nat. Cell. Biol. , vol.12 , pp. 1086-1093
    • Tardat, M.1    Brustel, J.2    Kirsh, O.3
  • 59
    • 77958452889 scopus 로고    scopus 로고
    • Kinetics of re-establishing H3 K79 methylation marks in global human chromatin
    • Sweet SM, Li M, Thomas PM, Durbin KR, Kelleher NL. Kinetics of re-establishing H3 K79 methylation marks in global human chromatin. J Biol Chem 2010;285:32778-32786.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32778-32786
    • Sweet, S.M.1    Li, M.2    Thomas, P.M.3    Durbin, K.R.4    Kelleher, N.L.5
  • 61
    • 78049246250 scopus 로고    scopus 로고
    • Fast signals and slow marks: The dynamics of histone modifications
    • Barth TK, Imhof A. Fast signals and slow marks: the dynamics of histone modifications. Trends Biochem Sci 2010;35:618-626.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 618-626
    • Barth, T.K.1    Imhof, A.2
  • 62
    • 79952283000 scopus 로고    scopus 로고
    • Nucleosome assembly and epigenetic inheritance
    • Xu M, Zhu B. Nucleosome assembly and epigenetic inheritance. Protein Cell 2010;1:820-829.
    • (2010) Protein Cell. , vol.1 , pp. 820-829
    • Xu, M.1    Zhu, B.2
  • 64
    • 0042528729 scopus 로고    scopus 로고
    • Heterochromatin and epigenetic control of gene expression
    • DOI 10.1126/science.1086887
    • Grewal SI, Moazed D. Heterochromatin and epigenetic control of gene expression. Science 2003;301:798-802. (Pubitemid 36962612)
    • (2003) Science , vol.301 , Issue.5634 , pp. 798-802
    • Grewal, S.I.S.1    Moazed, D.2
  • 65
    • 70349952171 scopus 로고    scopus 로고
    • Role of the polycomb protein EED in the propagation of repressive histone marks
    • Margueron R, Justin N, Ohno K, et al. Role of the polycomb protein EED in the propagation of repressive histone marks. Nature 2009;461:762-767.
    • (2009) Nature , vol.461 , pp. 762-767
    • Margueron, R.1    Justin, N.2    Ohno, K.3
  • 66
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • DOI 10.1038/35001622
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 2000;403:795-800. (Pubitemid 30111843)
    • (2000) Nature , vol.403 , Issue.6771 , pp. 795-800
    • Imai, S.-I.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 67
    • 0028919756 scopus 로고
    • Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
    • Hecht A, Laroche T, Strahl-Bolsinger S, Gasser SM, Grunstein M. Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell 1995;80:583-592.
    • (1995) Cell. , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Bolsinger, S.3    Gasser, S.M.4    Grunstein, M.5
  • 68
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • DOI 10.1126/science.1060118
    • Nakayama J, Rice JC, Strahl BD, Allis CD, Grewal SI. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 2001;292:110-113. (Pubitemid 32289138)
    • (2001) Science , vol.292 , Issue.5514 , pp. 110-113
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.S.5
  • 69
    • 37849038263 scopus 로고    scopus 로고
    • ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation
    • Karagianni P, Amazit L, Qin J, Wong J. ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation. Mol Cell Biol. 2008;28:705-717.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 705-717
    • Karagianni, P.1    Amazit, L.2    Qin, J.3    Wong, J.4
  • 70
    • 33847070442 scopus 로고    scopus 로고
    • The Role of Chromatin during Transcription
    • DOI 10.1016/j.cell.2007.01.015, PII S0092867407001092
    • Li B, Carey M, Workman JL. The role of chromatin during transcription. Cell 2007;128:707-719. (Pubitemid 46273570)
    • (2007) Cell , vol.128 , Issue.4 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.