메뉴 건너뛰기




Volumn 1839, Issue 12, 2014, Pages 1433-1439

Histone lysine methylation and chromatin replication

Author keywords

Chromatin assembly; Epigenetics; Genomic integrity; Heterochromatin; Histones; Post translational modifications

Indexed keywords

CHROMATIN ASSEMBLY FACTOR 1; HETEROCHROMATIN PROTEIN 1; CHROMATIN; HISTONE; HISTONE LYSINE METHYLTRANSFERASE; LYSINE;

EID: 84913533215     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2014.03.009     Document Type: Review
Times cited : (71)

References (76)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8A resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8A resolution. Nature 1997, 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
  • 3
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007, 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 4
    • 84870375316 scopus 로고    scopus 로고
    • Histone lysine methylation dynamics: establishment, regulation, and biological impact
    • Black J.C., Van Rechem C., Whetstine J.R. Histone lysine methylation dynamics: establishment, regulation, and biological impact. Mol. Cell 2012, 48:491-507.
    • (2012) Mol. Cell , vol.48 , pp. 491-507
    • Black, J.C.1    Van Rechem, C.2    Whetstine, J.R.3
  • 5
    • 84857430552 scopus 로고    scopus 로고
    • Chromatin replication and epigenome maintenance
    • Alabert C., Groth A. Chromatin replication and epigenome maintenance. Nat. Rev. Mol. Cell Biol. 2012, 13:153-167.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 153-167
    • Alabert, C.1    Groth, A.2
  • 7
    • 70549085855 scopus 로고    scopus 로고
    • Eukaryotic DNA replication control: lock and load, then fire
    • Remus D., Diffley J.F. Eukaryotic DNA replication control: lock and load, then fire. Curr. Opin. Cell Biol. 2009, 21:771-777.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 771-777
    • Remus, D.1    Diffley, J.F.2
  • 8
    • 77957168933 scopus 로고    scopus 로고
    • Eukaryotic DNA replication origins: many choices for appropriate answers
    • Mechali M. Eukaryotic DNA replication origins: many choices for appropriate answers. Nat Rev Mol Cell Biol 2010, 11:728-738.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 728-738
    • Mechali, M.1
  • 10
    • 79957564427 scopus 로고    scopus 로고
    • Nucleosomes in the neighborhood: new roles for chromatin modifications in replication origin control
    • Dorn E.S., Cook J.G. Nucleosomes in the neighborhood: new roles for chromatin modifications in replication origin control. Epigenetics 2011, 6:552-559.
    • (2011) Epigenetics , vol.6 , pp. 552-559
    • Dorn, E.S.1    Cook, J.G.2
  • 13
    • 84878443103 scopus 로고    scopus 로고
    • Structure and function of the BAH domain in chromatin biology
    • Yang N., Xu R.M. Structure and function of the BAH domain in chromatin biology. Crit. Rev. Biochem. Mol. Biol. 2013, 48:211-221.
    • (2013) Crit. Rev. Biochem. Mol. Biol. , vol.48 , pp. 211-221
    • Yang, N.1    Xu, R.M.2
  • 17
    • 84857187167 scopus 로고    scopus 로고
    • PR-Set7 and H4K20me1: at the crossroads of genome integrity, cell cycle, chromosome condensation, and transcription
    • Beck D.B., Oda H., Shen S.S., Reinberg D. PR-Set7 and H4K20me1: at the crossroads of genome integrity, cell cycle, chromosome condensation, and transcription. Genes Dev. 2012, 26:325-337.
    • (2012) Genes Dev. , vol.26 , pp. 325-337
    • Beck, D.B.1    Oda, H.2    Shen, S.S.3    Reinberg, D.4
  • 18
    • 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., Lefevbre C., Callanan M., Sardet C., Julien E. 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    Lefevbre, C.4    Callanan, M.5    Sardet, C.6    Julien, E.7
  • 19
    • 84867163924 scopus 로고    scopus 로고
    • DNA replication origin function is promoted by H3K4 di-methylation in Saccharomyces cerevisiae
    • Rizzardi L.F., Dorn E.S., Strahl B.D., Cook J.G. DNA replication origin function is promoted by H3K4 di-methylation in Saccharomyces cerevisiae. Genetics 2012, 192:371-384.
    • (2012) Genetics , vol.192 , pp. 371-384
    • Rizzardi, L.F.1    Dorn, E.S.2    Strahl, B.D.3    Cook, J.G.4
  • 21
    • 67651245131 scopus 로고    scopus 로고
    • H3 k36 methylation helps determine the timing of cdc45 association with replication origins
    • Pryde F., Jain D., Kerr A., Curley R., Mariotti F.R., Vogelauer M. H3 k36 methylation helps determine the timing of cdc45 association with replication origins. PLoS One 2009, 4:e5882.
    • (2009) PLoS One , vol.4 , pp. e5882
    • Pryde, F.1    Jain, D.2    Kerr, A.3    Curley, R.4    Mariotti, F.R.5    Vogelauer, M.6
  • 22
    • 84879610545 scopus 로고    scopus 로고
    • Methylation of histone H3 on lysine 79 associates with a group of replication origins and helps limit DNA replication once per cell cycle
    • Fu H., Maunakea A.K., Martin M.M., Huang L., Zhang Y., Ryan M., Kim R., Lin C.M., Zhao K., Aladjem M.I. Methylation of histone H3 on lysine 79 associates with a group of replication origins and helps limit DNA replication once per cell cycle. PLoS Genet. 2013, 9:e1003542.
    • (2013) PLoS Genet. , vol.9 , pp. e1003542
    • Fu, H.1    Maunakea, A.K.2    Martin, M.M.3    Huang, L.4    Zhang, Y.5    Ryan, M.6    Kim, R.7    Lin, C.M.8    Zhao, K.9    Aladjem, M.I.10
  • 24
    • 33845786515 scopus 로고    scopus 로고
    • The control of histone lysine methylation in epigenetic regulation
    • Volkel P., Angrand P.O. The control of histone lysine methylation in epigenetic regulation. Biochimie 2007, 89:1-20.
    • (2007) Biochimie , vol.89 , pp. 1-20
    • Volkel, P.1    Angrand, P.O.2
  • 25
    • 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
    • Nakatani Y., Ray-Gallet D., Quivy J.P., 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.
    • (2004) Cold Spring Harb. Symp. Quant. Biol. , vol.69 , pp. 273-280
    • Nakatani, Y.1    Ray-Gallet, D.2    Quivy, J.P.3    Tagami, H.4    Almouzni, G.5
  • 26
    • 84856271742 scopus 로고    scopus 로고
    • DNA replication, RNAi and epigenetic inheritance
    • Gonzalez M., Li F. DNA replication, RNAi and epigenetic inheritance. Epigenetics 2012, 7:14-19.
    • (2012) Epigenetics , vol.7 , pp. 14-19
    • Gonzalez, M.1    Li, F.2
  • 27
    • 79952536795 scopus 로고    scopus 로고
    • Epigenetic inheritance: uncontested?
    • Zhu B., Reinberg D. Epigenetic inheritance: uncontested?. Cell Res. 2011, 21:435-441.
    • (2011) Cell Res. , vol.21 , pp. 435-441
    • Zhu, B.1    Reinberg, D.2
  • 28
    • 70449713419 scopus 로고    scopus 로고
    • Mechanisms of epigenetic inheritance: copying of polycomb repressed chromatin
    • Francis N.J. Mechanisms of epigenetic inheritance: copying of polycomb repressed chromatin. Cell Cycle 2009, 8:3513-3518.
    • (2009) Cell Cycle , vol.8 , pp. 3513-3518
    • Francis, N.J.1
  • 29
    • 77949678340 scopus 로고    scopus 로고
    • Chromatin structure and the inheritance of epigenetic information
    • Margueron R., Reinberg D. Chromatin structure and the inheritance of epigenetic information. Nat. Rev. Genet. 2010, 11:285-296.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 285-296
    • Margueron, R.1    Reinberg, D.2
  • 30
    • 16844384065 scopus 로고    scopus 로고
    • Split decision: what happens to nucleosomes during DNA replication?
    • Annunziato A.T. 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
  • 31
    • 84857119394 scopus 로고    scopus 로고
    • Assembling chromatin: the long and winding road
    • Annunziato A.T. Assembling chromatin: the long and winding road. Biochim. Biophys. Acta 2012, 1819:196-210.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 196-210
    • Annunziato, A.T.1
  • 32
    • 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
  • 33
    • 84879656010 scopus 로고    scopus 로고
    • H3.3-H4 tetramer splitting events feature cell-type specific enhancers
    • Huang C., Zhang Z., Xu M., Li Y., Li Z., Ma Y., Cai T., Zhu B. H3.3-H4 tetramer splitting events feature cell-type specific enhancers. PLoS Genet. 2013, 9:e1003558.
    • (2013) PLoS Genet. , vol.9 , pp. e1003558
    • Huang, C.1    Zhang, Z.2    Xu, M.3    Li, Y.4    Li, Z.5    Ma, Y.6    Cai, T.7    Zhu, B.8
  • 37
    • 33749657892 scopus 로고    scopus 로고
    • PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state
    • Loyola A., Bonaldi T., Roche D., Imhof A., Almouzni G. PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state. Mol. Cell 2006, 24:309-316.
    • (2006) Mol. Cell , vol.24 , pp. 309-316
    • Loyola, A.1    Bonaldi, T.2    Roche, D.3    Imhof, A.4    Almouzni, G.5
  • 39
    • 1542298307 scopus 로고    scopus 로고
    • Histone chaperones, a supporting role in the limelight
    • Loyola A., Almouzni G. Histone chaperones, a supporting role in the limelight. Biochim. Biophys. Acta 2004, 1677:3-11.
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 3-11
    • Loyola, A.1    Almouzni, G.2
  • 40
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • 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.
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 41
    • 12344321682 scopus 로고    scopus 로고
    • Human Asf1 regulates the flow of S phase histones during replicational stress
    • Groth A., Ray-Gallet D., Quivy J.P., Lukas J., Bartek J., Almouzni G. Human Asf1 regulates the flow of S phase histones during replicational stress. Mol. Cell 2005, 17:301-311.
    • (2005) Mol. Cell , vol.17 , pp. 301-311
    • Groth, A.1    Ray-Gallet, D.2    Quivy, J.P.3    Lukas, J.4    Bartek, J.5    Almouzni, G.6
  • 42
    • 77049107080 scopus 로고    scopus 로고
    • Restoring chromatin after replication: how new and old histone marks come together
    • Jasencakova Z., Groth A. Restoring chromatin after replication: how new and old histone marks come together. Semin. Cell Dev. Biol. 2010, 21:231-237.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 231-237
    • Jasencakova, Z.1    Groth, A.2
  • 45
    • 0033118322 scopus 로고    scopus 로고
    • Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31
    • Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G., Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T. Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. EMBO J. 1999, 18:1923-1938.
    • (1999) EMBO J. , vol.18 , pp. 1923-1938
    • Aagaard, L.1    Laible, G.2    Selenko, P.3    Schmid, M.4    Dorn, R.5    Schotta, G.6    Kuhfittig, S.7    Wolf, A.8    Lebersorger, A.9    Singh, P.B.10    Reuter, G.11    Jenuwein, T.12
  • 47
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • 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.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 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., Roche D., Quivy J.P., Imhof A., Nakatani Y., Dent S.Y., Almouzni G. 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    Roche, D.4    Quivy, J.P.5    Imhof, A.6    Nakatani, Y.7    Dent, S.Y.8    Almouzni, G.9
  • 50
    • 0018240421 scopus 로고
    • A gene complex controlling segmentation in Drosophila
    • Lewis E.B. A gene complex controlling segmentation in Drosophila. Nature 1978, 276:565-570.
    • (1978) Nature , vol.276 , pp. 565-570
    • Lewis, E.B.1
  • 51
    • 0021880669 scopus 로고
    • A group of genes controlling the spatial expression of the bithorax complex in Drosophila
    • Jürgens G.A. A group of genes controlling the spatial expression of the bithorax complex in Drosophila. Nature 1985, 316:153-155.
    • (1985) Nature , vol.316 , pp. 153-155
    • Jürgens, G.A.1
  • 53
    • 8844265508 scopus 로고    scopus 로고
    • Epigenetic regulation of cellular memory by the Polycomb and Trithorax group proteins
    • Ringrose L., Paro R. Epigenetic regulation of cellular memory by the Polycomb and Trithorax group proteins. Annu. Rev. Genet. 2004, 38:413-443.
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 413-443
    • Ringrose, L.1    Paro, R.2
  • 54
    • 84876871047 scopus 로고    scopus 로고
    • Occupying chromatin: Polycomb mechanisms for getting to genomic targets, stopping transcriptional traffic, and staying put
    • Simon J.A., Kingston R.E. Occupying chromatin: Polycomb mechanisms for getting to genomic targets, stopping transcriptional traffic, and staying put. Mol. Cell 2013, 49:808-824.
    • (2013) Mol. Cell , vol.49 , pp. 808-824
    • Simon, J.A.1    Kingston, R.E.2
  • 55
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains
    • Fischle W., Wang Y., Jacobs S.A., Kim Y., Allis C.D., Khorasanizadeh S. Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev. 2003, 17:1870-1881.
    • (2003) Genes Dev. , vol.17 , pp. 1870-1881
    • Fischle, W.1    Wang, Y.2    Jacobs, S.A.3    Kim, Y.4    Allis, C.D.5    Khorasanizadeh, S.6
  • 56
    • 0041624288 scopus 로고    scopus 로고
    • Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27
    • Min J., Zhang Y., Xu R.M. Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev. 2003, 17:1823-1828.
    • (2003) Genes Dev. , vol.17 , pp. 1823-1828
    • Min, J.1    Zhang, Y.2    Xu, R.M.3
  • 57
    • 49649099991 scopus 로고    scopus 로고
    • Polycomb group protein-associated chromatin is reproduced in post-mitotic G1 phase and is required for S phase progression
    • Aoto T., Saitoh N., Sakamoto Y., Watanabe S., Nakao M. Polycomb group protein-associated chromatin is reproduced in post-mitotic G1 phase and is required for S phase progression. J. Biol. Chem. 2008, 283:18905-18915.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18905-18915
    • Aoto, T.1    Saitoh, N.2    Sakamoto, Y.3    Watanabe, S.4    Nakao, M.5
  • 58
    • 63049138876 scopus 로고    scopus 로고
    • Polycomb proteins remain bound to chromatin and DNA during DNA replication in vitro
    • Francis N.J., Follmer N.E., Simon M.D., Aghia G., Butler J.D. Polycomb proteins remain bound to chromatin and DNA during DNA replication in vitro. Cell 2009, 137:110-122.
    • (2009) Cell , vol.137 , pp. 110-122
    • Francis, N.J.1    Follmer, N.E.2    Simon, M.D.3    Aghia, G.4    Butler, J.D.5
  • 59
    • 84867423907 scopus 로고    scopus 로고
    • Chromatin modification by PSC occurs at one PSC per nucleosome and does not require the acidic patch of histone H2A
    • Lo S.M., McElroy K.A., Francis N.J. Chromatin modification by PSC occurs at one PSC per nucleosome and does not require the acidic patch of histone H2A. PLoS One 2012, 7:e47162.
    • (2012) PLoS One , vol.7 , pp. e47162
    • Lo, S.M.1    McElroy, K.A.2    Francis, N.J.3
  • 60
    • 78049246250 scopus 로고    scopus 로고
    • Fast signals and slow marks: the dynamics of histone modifications
    • Barth T.K., 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
  • 61
    • 78649698079 scopus 로고    scopus 로고
    • Global turnover of histone post-translational modifications and variants in human cells
    • Zee B.M., Levin R.S., Dimaggio P.A., Garcia B.A. Global turnover of histone post-translational modifications and variants in human cells. Epigenetics Chromatin 2010, 3:22.
    • (2010) Epigenetics Chromatin , vol.3 , pp. 22
    • Zee, B.M.1    Levin, R.S.2    Dimaggio, P.A.3    Garcia, B.A.4
  • 64
    • 84906725999 scopus 로고    scopus 로고
    • Stepwise histone modifications are mediated by multiple enzymes that rapidly associate with nascent DNA during replication
    • Petruk S., Black K.L., Kovermann S.K., Brock H.W., Mazo A. Stepwise histone modifications are mediated by multiple enzymes that rapidly associate with nascent DNA during replication. Nat. Commun. 2013, 4:2841.
    • (2013) Nat. Commun. , vol.4 , pp. 2841
    • Petruk, S.1    Black, K.L.2    Kovermann, S.K.3    Brock, H.W.4    Mazo, A.5
  • 65
    • 84655170009 scopus 로고    scopus 로고
    • A model for mitotic inheritance of histone lysine methylation
    • Xu M., Wang W., Chen S., Zhu B. A model for mitotic inheritance of histone lysine methylation. EMBO Rep. 2012, 13:60-67.
    • (2012) EMBO Rep. , vol.13 , pp. 60-67
    • Xu, M.1    Wang, W.2    Chen, S.3    Zhu, B.4
  • 66
    • 84864013839 scopus 로고    scopus 로고
    • Origins and formation of histone methylation across the human cell cycle
    • Zee B.M., Britton L.M., Wolle D., Haberman D.M., Garcia B.A. Origins and formation of histone methylation across the human cell cycle. Mol. Cell. Biol. 2012, 32:2503-2514.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2503-2514
    • Zee, B.M.1    Britton, L.M.2    Wolle, D.3    Haberman, D.M.4    Garcia, B.A.5
  • 67
    • 80054679198 scopus 로고    scopus 로고
    • Heterochromatin maintenance and establishment: lessons from the mouse pericentromere
    • Almouzni G., Probst A.V. Heterochromatin maintenance and establishment: lessons from the mouse pericentromere. Nucleus 2011, 2:332-338.
    • (2011) Nucleus , vol.2 , pp. 332-338
    • Almouzni, G.1    Probst, A.V.2
  • 68
    • 84555204362 scopus 로고    scopus 로고
    • Linking DNA replication to heterochromatin silencing and epigenetic inheritance
    • Li Q., Zhang Z. Linking DNA replication to heterochromatin silencing and epigenetic inheritance. Acta Biochim. Biophys. Sin. 2012, 44:3-13.
    • (2012) Acta Biochim. Biophys. Sin. , vol.44 , pp. 3-13
    • Li, Q.1    Zhang, Z.2
  • 76
    • 84874295117 scopus 로고    scopus 로고
    • H3K56me3 is a novel, conserved heterochromatic mark that largely but not completely overlaps with H3K9me3 in both regulation and localization
    • Jack A.P., Bussemer S., Hahn M., Punzeler S., Snyder M., Wells M., Csankovszki G., Solovei I., Schotta G., Hake S.B. H3K56me3 is a novel, conserved heterochromatic mark that largely but not completely overlaps with H3K9me3 in both regulation and localization. PLoS One 2013, 8:e51765.
    • (2013) PLoS One , vol.8 , pp. e51765
    • Jack, A.P.1    Bussemer, S.2    Hahn, M.3    Punzeler, S.4    Snyder, M.5    Wells, M.6    Csankovszki, G.7    Solovei, I.8    Schotta, G.9    Hake, S.B.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.