메뉴 건너뛰기




Volumn 15, Issue 2, 2005, Pages 163-176

The key to development: Interpreting the histone code?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BETA GLOBIN; CITRULLINE; DNA; HEAT SHOCK PROTEIN 26; HISTONE; HISTONE H1; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; HISTONE LYSINE METHYLTRANSFERASE; METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE; RECOMBINASE; RNA POLYMERASE; RNA POLYMERASE II; T LYMPHOCYTE RECEPTOR; TRANSCRIPTION FACTOR SAGA; UNTRANSLATED RNA;

EID: 15744396813     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gde.2005.01.005     Document Type: Review
Times cited : (628)

References (103)
  • 1
    • 0037381213 scopus 로고    scopus 로고
    • Structure and dynamic behavior of nucleosomes
    • K. Luger Structure and dynamic behavior of nucleosomes Curr Opin Genet Dev 13 2003 127 135
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 127-135
    • Luger, K.1
  • 2
    • 0032518799 scopus 로고    scopus 로고
    • Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase
    • J. Wong, D. Patterton, A. Imhof, D. Guschin, Y.B. Shi, and A.P. Wolffe Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase EMBO J 17 1998 520 534
    • (1998) EMBO J , vol.17 , pp. 520-534
    • Wong, J.1    Patterton, D.2    Imhof, A.3    Guschin, D.4    Shi, Y.B.5    Wolffe, A.P.6
  • 3
    • 0033022040 scopus 로고    scopus 로고
    • Architectural regulations and Hmg1
    • A.P. Wolffe Architectural regulations and Hmg1 Nat Genet 22 1999 215 217
    • (1999) Nat Genet , vol.22 , pp. 215-217
    • Wolffe, A.P.1
  • 4
    • 1642326716 scopus 로고    scopus 로고
    • Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation
    • S.J. Nowak, and V.G. Corces Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation Trends Genet 20 2004 214 220
    • (2004) Trends Genet , vol.20 , pp. 214-220
    • Nowak, S.J.1    Corces, V.G.2
  • 5
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • M. Grunstein Histone acetylation in chromatin structure and transcription Nature 389 1997 349 352
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 6
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • D.E. Sterner, and S.L. Berger Acetylation of histones and transcription-related factors Microbiol Mol Biol Rev 64 2000 435 459
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 7
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Y. Zhang, and D. Reinberg Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails Genes Dev 15 2001 2343 2360
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 8
    • 0025341218 scopus 로고
    • Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription
    • J.R. Davie, and L.C. Murphy Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription Biochemistry 29 1990 4752 4757
    • (1990) Biochemistry , vol.29 , pp. 4752-4757
    • Davie, J.R.1    Murphy, L.C.2
  • 9
    • 0344392751 scopus 로고    scopus 로고
    • Histone modifications: Now summoning sumoylation
    • D. Nathan, D.E. Sterner, and S.L. Berger Histone modifications: now summoning sumoylation Proc Natl Acad Sci USA 100 2003 13118 13120
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13118-13120
    • Nathan, D.1    Sterner, D.E.2    Berger, S.L.3
  • 10
    • 0021140803 scopus 로고
    • ADP-ribosylation of nuclear proteins in vivo. Identification of histone H2B as a major acceptor for mono- and poly(ADP-ribose) in dimethyl sulfate-treated hepatoma AH 7974 cells
    • P. Adamietz, and A. Rudolph ADP-ribosylation of nuclear proteins in vivo. Identification of histone H2B as a major acceptor for mono- and poly(ADP-ribose) in dimethyl sulfate-treated hepatoma AH 7974 cells J Biol Chem 259 1984 6841 6846
    • (1984) J Biol Chem , vol.259 , pp. 6841-6846
    • Adamietz, P.1    Rudolph, A.2
  • 12
    • 0028858269 scopus 로고
    • Biotinylation of histones by human serum biotinidase: Assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency
    • J. Hymes, K. Fleischhauer, and B. Wolf Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency Biochem Mol Med 56 1995 76 83
    • (1995) Biochem Mol Med , vol.56 , pp. 76-83
    • Hymes, J.1    Fleischhauer, K.2    Wolf, B.3
  • 15
    • 0242348752 scopus 로고    scopus 로고
    • Histone lysine methylation: A signature for chromatin function
    • R.J. Sims III, K. Nishioka, and D. Reinberg Histone lysine methylation: a signature for chromatin function Trends Genet 19 2003 629 639
    • (2003) Trends Genet , vol.19 , pp. 629-639
    • Sims III, R.J.1    Nishioka, K.2    Reinberg, D.3
  • 16
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • M. Lachner, R.J. O'Sullivan, and T. Jenuwein An epigenetic road map for histone lysine methylation J Cell Sci 116 2003 2117 2124
    • (2003) J Cell Sci , vol.116 , pp. 2117-2124
    • Lachner, M.1    O'Sullivan, R.J.2    Jenuwein, T.3
  • 17
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • M. Lachner, and T. Jenuwein The many faces of histone lysine methylation Curr Opin Cell Biol 14 2002 286 298
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 18
    • 0037380209 scopus 로고    scopus 로고
    • Histone acetylation and deacetylation in yeast
    • S.K. Kurdistani, and M. Grunstein Histone acetylation and deacetylation in yeast Nat Rev Mol Cell Biol 4 2003 276 284
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 276-284
    • Kurdistani, S.K.1    Grunstein, M.2
  • 19
    • 0032491583 scopus 로고    scopus 로고
    • δ-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins
    • P. Zobel-Thropp, J.D. Gary, and S. Clarke δ-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins J Biol Chem 273 1998 29283 29286
    • (1998) J Biol Chem , vol.273 , pp. 29283-29286
    • Zobel-Thropp, P.1    Gary, J.D.2    Clarke, S.3
  • 20
    • 5044228483 scopus 로고    scopus 로고
    • Human PAD4 regulates histone arginine methylation levels via demethylimination
    • Y. Wang, J. Wysocka, J. Sayegh, Y.H. Lee, J.R. Perlin, L. Leonelli, L.S. Sonbuchner, C.H. McDonald, R.G. Cook, and Y. Dou Human PAD4 regulates histone arginine methylation levels via demethylimination Science 306 2004 279 283 The authors report enzymatic deiminiation of the arginine residues within the histone H3 and H4 N-terminal tails. Moreover, conversion of methylated histone H4-R3 to citrulline mediated by PAD4 could be observed in vivo at the estrogen-responsive pS2 promoter following estradiol-mediated induction.
    • (2004) Science , vol.306 , pp. 279-283
    • Wang, Y.1    Wysocka, J.2    Sayegh, J.3    Lee, Y.H.4    Perlin, J.R.5    Leonelli, L.6    Sonbuchner, L.S.7    McDonald, C.H.8    Cook, R.G.9    Dou, Y.10
  • 21
    • 4444372638 scopus 로고    scopus 로고
    • Histone deimination antagonizes arginine methylation
    • G.L. Cuthbert, S. Daujat, A.W. Snowden, H. Erdjument-Bromage, T. Hagiwara, M. Yamada, R. Schneider, P.D. Gregory, P. Tempst, and A.J. Bannister Histone deimination antagonizes arginine methylation Cell 118 2004 545 553 This study shows PADI4-mediated deimination of histone H3 and H4 arginine residues, their conversion to citrulline and involvement of this reaction in transcriptional repression. Collectively, the data strongly suggest that arginine methylation (coinciding with activation of transcription) is antagonized by histone arginine deimination.
    • (2004) Cell , vol.118 , pp. 545-553
    • Cuthbert, G.L.1    Daujat, S.2    Snowden, A.W.3    Erdjument-Bromage, H.4    Hagiwara, T.5    Yamada, M.6    Schneider, R.7    Gregory, P.D.8    Tempst, P.9    Bannister, A.J.10
  • 22
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • T. Kouzarides Histone methylation in transcriptional control Curr Opin Genet Dev 12 2002 198 209
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 23
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • T. Jenuwein, and C.D. Allis Translating the histone code Science 293 2001 1074 1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 24
    • 0035890986 scopus 로고    scopus 로고
    • Code of silence
    • J.C. Rice, and C.D. Allis Code of silence Nature 414 2001 258 261
    • (2001) Nature , vol.414 , pp. 258-261
    • Rice, J.C.1    Allis, C.D.2
  • 25
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • W. Fischle, Y. Wang, and C.D. Allis Binary switches and modification cassettes in histone biology and beyond Nature 425 2003 475 479
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 26
    • 2942610993 scopus 로고    scopus 로고
    • Tethering of HP1 proteins to chromatin is relieved by phosphoacetylation of histone H3
    • B. Mateescu, P. England, F. Halgand, M. Yaniv, and C. Muchardt Tethering of HP1 proteins to chromatin is relieved by phosphoacetylation of histone H3 EMBO Rep 5 2004 490 496
    • (2004) EMBO Rep , vol.5 , pp. 490-496
    • Mateescu, B.1    England, P.2    Halgand, F.3    Yaniv, M.4    Muchardt, C.5
  • 27
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • H.H. Ng, R.M. Xu, Y. Zhang, and K. Struhl Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79 J Biol Chem 277 2002 34655 34657
    • (2002) J Biol Chem , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 28
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Z.W. Sun, and C.D. Allis Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast Nature 418 2002 104 108
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 29
    • 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
    • S.D. Briggs, M. Bryk, B.D. Strahl, W.L. Cheung, J.K. Davie, S.Y. Dent, F. Winston, and C.D. Allis Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae Genes Dev 15 2001 3286 3295
    • (2001) Genes Dev , vol.15 , 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.6    Winston, F.7    Allis, C.D.8
  • 31
    • 1242271997 scopus 로고    scopus 로고
    • Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3
    • E. Ezhkova, and W.P. Tansey Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3 Mol Cell 13 2004 435 442 This study shows for the first time that H2B-mono-ubiquitination, which precedes H3-K4 methylation, also involves the presence of components of the proteasome. The study suggests that parts of the proteasome exhibit chromatin remodelling functions and interact with other regulators/modifiers of chromatin.
    • (2004) Mol Cell , vol.13 , pp. 435-442
    • Ezhkova, E.1    Tansey, W.P.2
  • 32
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • M. Muratani, and W.P. Tansey How the ubiquitin-proteasome system controls transcription Nat Rev Mol Cell Biol 4 2003 192 201
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 34
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel histone post-translational modifications by peptide mass fingerprinting
    • L. Zhang, E.E. Eugeni, M.R. Parthun, and M.A. Freitas Identification of novel histone post-translational modifications by peptide mass fingerprinting Chromosoma 112 2003 77 86
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.E.2    Parthun, M.R.3    Freitas, M.A.4
  • 36
    • 1042276981 scopus 로고    scopus 로고
    • Analysis of genome-wide histone acetylation state and enzyme binding using DNA microarrays
    • D. Robyr, S.K. Kurdistani, and M. Grunstein Analysis of genome-wide histone acetylation state and enzyme binding using DNA microarrays Methods Enzymol 376 2004 289 304
    • (2004) Methods Enzymol , vol.376 , pp. 289-304
    • Robyr, D.1    Kurdistani, S.K.2    Grunstein, M.3
  • 39
    • 2342512015 scopus 로고    scopus 로고
    • Developmental stage differences in chromatin subdomains of the beta-globin locus
    • A. Kim, and A. Dean Developmental stage differences in chromatin subdomains of the beta-globin locus Proc Natl Acad Sci USA 101 2004 7028 7033
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7028-7033
    • Kim, A.1    Dean, A.2
  • 41
    • 9144268924 scopus 로고    scopus 로고
    • Partitioning and plasticity of repressive histone methylation states in mammalian chromatin
    • A.H. Peters, S. Kubicek, K. Mechtler, R.J. O'Sullivan, A.A. Derijck, L. Perez-Burgos, A. Kohlmaier, S. Opravil, M. Tachibana, and Y. Shinkai Partitioning and plasticity of repressive histone methylation states in mammalian chromatin Mol Cell 12 2003 1577 1589 The authors examine the possible methylation states for histone H3-K9 and H3-K27 in mammalian chromatin. They show that pericentric heterochromatin is enriched in H3-K9 trimethylation and H3-K27 monomethylation. SUV39H double-null cells, which lack H3-K9 trimethylation completely, show a distinct pattern of methylation imprints. Thereby, the presented data uncover an impressive level of plasticity for histone methylation patterns.
    • (2003) Mol Cell , vol.12 , pp. 1577-1589
    • Peters, A.H.1    Kubicek, S.2    Mechtler, K.3    O'Sullivan, R.J.4    Derijck, A.A.5    Perez-Burgos, L.6    Kohlmaier, A.7    Opravil, S.8    Tachibana, M.9    Shinkai, Y.10
  • 42
    • 2642542643 scopus 로고    scopus 로고
    • A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin
    • G. Schotta, M. Lachner, K. Sarma, A. Ebert, R. Sengupta, G. Reuter, D. Reinberg, and T. Jenuwein A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin Genes Dev 18 2004 1251 1262 The authors present and characterize two novel histone methyltransferases specific for histone H4-K20. They show that these enzymes exclusively trimethylate K20 and that there is a specific requisite of other histone modifications for their activity. The study adds important findings to the histone code hypothesis.
    • (2004) Genes Dev , vol.18 , pp. 1251-1262
    • Schotta, G.1    Lachner, M.2    Sarma, K.3    Ebert, A.4    Sengupta, R.5    Reuter, G.6    Reinberg, D.7    Jenuwein, T.8
  • 43
    • 0036850346 scopus 로고    scopus 로고
    • Deciphering the transcriptional histone acetylation code for a human gene
    • T. Agalioti, G. Chen, and D. Thanos Deciphering the transcriptional histone acetylation code for a human gene Cell 111 2002 381 392
    • (2002) Cell , vol.111 , pp. 381-392
    • Agalioti, T.1    Chen, G.2    Thanos, D.3
  • 44
    • 0037229898 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 during transcriptional activation depends on promoter structure
    • M. Labrador, and V.G. Corces Phosphorylation of histone H3 during transcriptional activation depends on promoter structure Genes Dev 17 2003 43 48
    • (2003) Genes Dev , vol.17 , pp. 43-48
    • Labrador, M.1    Corces, V.G.2
  • 45
    • 0842304522 scopus 로고    scopus 로고
    • Histone modification patterns during gene activation
    • W.S. Lo, K. Henry, M.F. Schwartz, and S.L. Berger Histone modification patterns during gene activation Methods Enzymol 377 2004 130 153
    • (2004) Methods Enzymol , vol.377 , pp. 130-153
    • Lo, W.S.1    Henry, K.2    Schwartz, M.F.3    Berger, S.L.4
  • 46
    • 0344442779 scopus 로고    scopus 로고
    • Transcriptional regulation by histone ubiquitination and deubiquitination
    • Y. Zhang Transcriptional regulation by histone ubiquitination and deubiquitination Genes Dev 17 2003 2733 2740
    • (2003) Genes Dev , vol.17 , pp. 2733-2740
    • Zhang, Y.1
  • 47
    • 4143074854 scopus 로고    scopus 로고
    • SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells
    • R. Hamamoto, Y. Furukawa, M. Morita, Y. Iimura, F.P. Silva, M. Li, R. Yagyu, and Y. Nakamura SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells Nat Cell Biol 6 2004 731 740 This study presents a novel histone methyltransferase specific for histone H3-K4. Interestingly, this protein also possesses a sequence-specific DNA-binding domain and links functions of histone modifier and classical transcription factors. Furthermore, its involvement in carcinogenesis emphasizes the role of histone methyltransferases for regulation of gene expression and cell identity.
    • (2004) Nat Cell Biol , vol.6 , pp. 731-740
    • Hamamoto, R.1    Furukawa, Y.2    Morita, M.3    Iimura, Y.4    Silva, F.P.5    Li, M.6    Yagyu, R.7    Nakamura, Y.8
  • 52
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAFII250 double bromodomain module
    • R.H. Jacobson, A.G. Ladurner, D.S. King, and R. Tjian Structure and function of a human TAFII250 double bromodomain module Science 288 2000 1422 1425
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H.1    Ladurner, A.G.2    King, D.S.3    Tjian, R.4
  • 54
    • 0034730745 scopus 로고    scopus 로고
    • Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila
    • A.D. Pham, and F. Sauer Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila Science 289 2000 2357 2360
    • (2000) Science , vol.289 , pp. 2357-2360
    • Pham, A.D.1    Sauer, F.2
  • 55
    • 2342506598 scopus 로고    scopus 로고
    • TAF1 activates transcription by phosphorylation of serine 33 in histone H2B
    • T. Maile, S. Kwoczynski, R.J. Katzenberger, D.A. Wassarman, and F. Sauer TAF1 activates transcription by phosphorylation of serine 33 in histone H2B Science 304 2004 1010 1014
    • (2004) Science , vol.304 , pp. 1010-1014
    • Maile, T.1    Kwoczynski, S.2    Katzenberger, R.J.3    Wassarman, D.A.4    Sauer, F.5
  • 56
    • 2342481623 scopus 로고    scopus 로고
    • Recent advances in X-chromosome inactivation
    • E. Heard Recent advances in X-chromosome inactivation Curr Opin Cell Biol 16 2004 247 255
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 247-255
    • Heard, E.1
  • 58
    • 0942268864 scopus 로고    scopus 로고
    • Epigenetic dynamics of imprinted X inactivation during early mouse development
    • p chromosome is inactivated at the early cleavage stage. They correlated this inactivation with specific epigenetic marks.
    • (2004) Science , vol.303 , pp. 644-649
    • Okamoto, I.1    Otte, A.P.2    Allis, C.D.3    Reinberg, D.4    Heard, E.5
  • 59
    • 0347357614 scopus 로고    scopus 로고
    • Inheritance of a pre-inactivated paternal X chromosome in early mouse embryos
    • K.D. Huynh, and J.T. Lee Inheritance of a pre-inactivated paternal X chromosome in early mouse embryos Nature 426 2003 857 862
    • (2003) Nature , vol.426 , pp. 857-862
    • Huynh, K.D.1    Lee, J.T.2
  • 60
    • 0034081857 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female preimplantation mouse embryos
    • C. Costanzi, P. Stein, D.M. Worrad, R.M. Schultz, and J.R. Pehrson Histone macroH2A1 is concentrated in the inactive X chromosome of female preimplantation mouse embryos Development 127 2000 2283 2289
    • (2000) Development , vol.127 , pp. 2283-2289
    • Costanzi, C.1    Stein, P.2    Worrad, D.M.3    Schultz, R.M.4    Pehrson, J.R.5
  • 61
    • 0035839126 scopus 로고    scopus 로고
    • Epigenetic reprogramming in mammalian development
    • W. Reik, W. Dean, and J. Walter Epigenetic reprogramming in mammalian development Science 293 2001 1089 1093
    • (2001) Science , vol.293 , pp. 1089-1093
    • Reik, W.1    Dean, W.2    Walter, J.3
  • 62
    • 19344375746 scopus 로고    scopus 로고
    • A chromosomal memory triggered by xist regulates histone methylation in x inactivation
    • A. Kohlmaier, F. Savarese, M. Lachner, J. Martens, T. Jenuwein, and A. Wutz A chromosomal memory triggered by xist regulates histone methylation in x inactivation PLoS Biol 2 2004 E171
    • (2004) PLoS Biol , vol.2 , pp. 171
    • Kohlmaier, A.1    Savarese, F.2    Lachner, M.3    Martens, J.4    Jenuwein, T.5    Wutz, A.6
  • 64
    • 3042756180 scopus 로고    scopus 로고
    • Regulation of histone H3 lysine 9 methylation in oocytes and early pre-implantation embryos
    • H. Liu, J.M. Kim, and F. Aoki Regulation of histone H3 lysine 9 methylation in oocytes and early pre-implantation embryos Development 131 2004 2269 2280
    • (2004) Development , vol.131 , pp. 2269-2280
    • Liu, H.1    Kim, J.M.2    Aoki, F.3
  • 65
    • 0033214928 scopus 로고    scopus 로고
    • Targeted mutagenesis of Tsix leads to nonrandom X inactivation
    • J.T. Lee, and N. Lu Targeted mutagenesis of Tsix leads to nonrandom X inactivation Cell 99 1999 47 57
    • (1999) Cell , vol.99 , pp. 47-57
    • Lee, J.T.1    Lu, N.2
  • 66
    • 0037059554 scopus 로고    scopus 로고
    • CTCF, a candidate trans-acting factor for X-inactivation choice
    • W. Chao, K.D. Huynh, R.J. Spencer, L.S. Davidow, and J.T. Lee CTCF, a candidate trans-acting factor for X-inactivation choice Science 295 2002 345 347
    • (2002) Science , vol.295 , pp. 345-347
    • Chao, W.1    Huynh, K.D.2    Spencer, R.J.3    Davidow, L.S.4    Lee, J.T.5
  • 68
    • 0036830226 scopus 로고    scopus 로고
    • Hox cluster polarity in early transcriptional availability: A high order regulatory level of clustered Hox genes in the mouse
    • B.A. Roelen, W. de Graaff, S. Forlani, and J. Deschamps Hox cluster polarity in early transcriptional availability: a high order regulatory level of clustered Hox genes in the mouse Mech Dev 119 2002 81 90
    • (2002) Mech Dev , vol.119 , pp. 81-90
    • Roelen, B.A.1    De Graaff, W.2    Forlani, S.3    Deschamps, J.4
  • 69
    • 2442695407 scopus 로고    scopus 로고
    • Chromatin decondensation and nuclear reorganization of the HoxB locus upon induction of transcription
    • S. Chambeyron, and W.A. Bickmore Chromatin decondensation and nuclear reorganization of the HoxB locus upon induction of transcription Genes Dev 18 2004 1119 1130 This study shows the interplay between histone modifications, high order chromatin and gene expression. Analyzing two genes of the Hoxb locus, they showed that whereas two genes exhibit the same pattern of histone modification only one of them is expressed. This apparent discrepancy would be associated to the position of the gene regarding the chromosomes territories.
    • (2004) Genes Dev , vol.18 , pp. 1119-1130
    • Chambeyron, S.1    Bickmore, W.A.2
  • 70
    • 0042378999 scopus 로고    scopus 로고
    • A genetic analysis of chromosome territory looping: Diverse roles for distal regulatory elements
    • T. Ragoczy, A. Telling, T. Sawado, M. Groudine, and S.T. Kosak A genetic analysis of chromosome territory looping: diverse roles for distal regulatory elements Chromosome Res 11 2003 513 525
    • (2003) Chromosome Res , vol.11 , pp. 513-525
    • Ragoczy, T.1    Telling, A.2    Sawado, T.3    Groudine, M.4    Kosak, S.T.5
  • 71
    • 0037423933 scopus 로고    scopus 로고
    • Polycomb, epigenomes, and control of cell identity
    • V. Orlando Polycomb, epigenomes, and control of cell identity Cell 112 2003 599 606
    • (2003) Cell , vol.112 , pp. 599-606
    • Orlando, V.1
  • 72
    • 2342475666 scopus 로고    scopus 로고
    • Polycomb complexes and silencing mechanisms
    • A.H. Lund, and M. Van Lohuizen Polycomb complexes and silencing mechanisms Curr Opin Cell Biol 16 2004 239 246
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 239-246
    • Lund, A.H.1    Van Lohuizen, M.2
  • 73
    • 3042750473 scopus 로고    scopus 로고
    • Histone 3 lysine 4 methylation during the pre-B to immature B-cell transition
    • E.J. Perkins, B.L. Kee, and D.A. Ramsden Histone 3 lysine 4 methylation during the pre-B to immature B-cell transition Nucleic Acids Res 32 2004 1942 1947
    • (2004) Nucleic Acids Res , vol.32 , pp. 1942-1947
    • Perkins, E.J.1    Kee, B.L.2    Ramsden, D.A.3
  • 74
    • 0141705373 scopus 로고    scopus 로고
    • Antigen receptor loci poised for V(D)J rearrangement are broadly associated with BRG1 and flanked by peaks of histone H3 dimethylated at lysine 4
    • K.B. Morshead, D.N. Ciccone, S.D. Taverna, C.D. Allis, and M.A. Oettinger Antigen receptor loci poised for V(D)J rearrangement are broadly associated with BRG1 and flanked by peaks of histone H3 dimethylated at lysine 4 Proc Natl Acad Sci USA 100 2003 11577 11582
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11577-11582
    • Morshead, K.B.1    Ciccone, D.N.2    Taverna, S.D.3    Allis, C.D.4    Oettinger, M.A.5
  • 77
    • 1542347557 scopus 로고    scopus 로고
    • PRDI-BF1 recruits the histone H3 methyltransferase G9a in transcriptional silencing
    • I. Gyory, J. Wu, G. Fejer, E. Seto, and K.L. Wright PRDI-BF1 recruits the histone H3 methyltransferase G9a in transcriptional silencing Nat Immunol 5 2004 299 308
    • (2004) Nat Immunol , vol.5 , pp. 299-308
    • Gyory, I.1    Wu, J.2    Fejer, G.3    Seto, E.4    Wright, K.L.5
  • 78
    • 0037452770 scopus 로고    scopus 로고
    • Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: A potential mechanism for position-effect variegation
    • H.H. Ng, D.N. Ciccone, K.B. Morshead, M.A. Oettinger, and K. Struhl Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation Proc Natl Acad Sci USA 100 2003 1820 1825
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1820-1825
    • Ng, H.H.1    Ciccone, D.N.2    Morshead, K.B.3    Oettinger, M.A.4    Struhl, K.5
  • 79
    • 0037320925 scopus 로고    scopus 로고
    • Ezh2 controls B cell development through histone H3 methylation and Igh rearrangement
    • I.H. Su, A. Basavaraj, A.N. Krutchinsky, O. Hobert, A. Ullrich, B.T. Chait, and A. Tarakhovsky Ezh2 controls B cell development through histone H3 methylation and Igh rearrangement Nat Immunol 4 2003 124 131 This study demonstrated, using conditional knockout, the requirement for the histone methyl transferase Ezh2 in early B-cell development and rearrangement of the immunoglobulin heavy chain gene.
    • (2003) Nat Immunol , vol.4 , pp. 124-131
    • Su, I.H.1    Basavaraj, A.2    Krutchinsky, A.N.3    Hobert, O.4    Ullrich, A.5    Chait, B.T.6    Tarakhovsky, A.7
  • 80
    • 0038148400 scopus 로고    scopus 로고
    • Chromatin dynamics and locus accessibility in the immune system
    • R. Mostoslavsky, F.W. Alt, and C.H. Bassing Chromatin dynamics and locus accessibility in the immune system Nat Immunol 4 2003 603 606
    • (2003) Nat Immunol , vol.4 , pp. 603-606
    • Mostoslavsky, R.1    Alt, F.W.2    Bassing, C.H.3
  • 81
    • 0038610946 scopus 로고    scopus 로고
    • A multistep mechanism for the activation of rearrangement in the immune system
    • Y. Ji, J. Zhang, A.I. Lee, H. Cedar, and Y. Bergman A multistep mechanism for the activation of rearrangement in the immune system Proc Natl Acad Sci USA 100 2003 7557 7562
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7557-7562
    • Ji, Y.1    Zhang, J.2    Lee, A.I.3    Cedar, H.4    Bergman, Y.5
  • 82
    • 2442464995 scopus 로고    scopus 로고
    • Dynamic assembly of silent chromatin during thymocyte maturation
    • R.C. Su, K.E. Brown, S. Saaber, A.G. Fisher, M. Merkenschlager, and S.T. Smale Dynamic assembly of silent chromatin during thymocyte maturation Nat Genet 36 2004 502 506 The authors have analyzed the temporal assembly of silent chromatin at dntt promoter during thymocyte differentiation using primary thymocytes and transformed cell lines.
    • (2004) Nat Genet , vol.36 , pp. 502-506
    • Su, R.C.1    Brown, K.E.2    Saaber, S.3    Fisher, A.G.4    Merkenschlager, M.5    Smale, S.T.6
  • 83
    • 0037115392 scopus 로고    scopus 로고
    • Dependence of histone modifications and gene expression on DNA hypermethylation in cancer
    • J.A. Fahrner, S. Eguchi, J.G. Herman, and S.B. Baylin Dependence of histone modifications and gene expression on DNA hypermethylation in cancer Cancer Res 62 2002 7213 7218
    • (2002) Cancer Res , vol.62 , pp. 7213-7218
    • Fahrner, J.A.1    Eguchi, S.2    Herman, J.G.3    Baylin, S.B.4
  • 84
    • 0242539836 scopus 로고    scopus 로고
    • Cancer epigenetics
    • R.L. Momparler Cancer epigenetics Oncogene 22 2003 6479 6483
    • (2003) Oncogene , vol.22 , pp. 6479-6483
    • Momparler, R.L.1
  • 89
    • 1942502862 scopus 로고    scopus 로고
    • Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3
    • A. Kuzmichev, T. Jenuwein, P. Tempst, and D. Reinberg Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3 Mol Cell 14 2004 183 193
    • (2004) Mol Cell , vol.14 , pp. 183-193
    • Kuzmichev, A.1    Jenuwein, T.2    Tempst, P.3    Reinberg, D.4
  • 92
    • 0015912073 scopus 로고
    • Enzymatic demethylation of calf thymus histones
    • W.K. Paik, and S. Kim Enzymatic demethylation of calf thymus histones Biochem Biophys Res Commun 51 1973 781 788
    • (1973) Biochem Biophys Res Commun , vol.51 , pp. 781-788
    • Paik, W.K.1    Kim, S.2
  • 95
    • 11144237618 scopus 로고    scopus 로고
    • Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation
    • J. Fang, T. Chen, B. Chadwick, E. Li, and Y. Zhang Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation J Biol Chem 279 2004 52812 52815
    • (2004) J Biol Chem , vol.279 , pp. 52812-52815
    • Fang, J.1    Chen, T.2    Chadwick, B.3    Li, E.4    Zhang, Y.5
  • 96
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • H. Wang, R. Cao, L. Xia, H. Erdjument-Bromage, C. Borchers, P. Tempst, and Y. Zhang Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase Mol Cell 8 2001 1207 1217
    • (2001) Mol Cell , vol.8 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6    Zhang, Y.7
  • 99
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • S.A. Jacobs, and S. Khorasanizadeh Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail Science 295 2002 2080 2083
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 100
    • 2942574510 scopus 로고    scopus 로고
    • Hierarchical recruitment of polycomb group silencing complexes
    • L. Wang, J.L. Brown, R. Cao, Y. Zhang, J.A. Kassis, and R.S. Jones Hierarchical recruitment of polycomb group silencing complexes Mol Cell 14 2004 637 646
    • (2004) Mol Cell , vol.14 , pp. 637-646
    • Wang, L.1    Brown, J.L.2    Cao, R.3    Zhang, Y.4    Kassis, J.A.5    Jones, R.S.6
  • 102
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • K. Nishioka, S. Chuikov, K. Sarma, H. Erdjument-Bromage, C.D. Allis, P. Tempst, and D. Reinberg Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation Genes Dev 16 2002 479 489
    • (2002) Genes Dev , vol.16 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3    Erdjument-Bromage, H.4    Allis, C.D.5    Tempst, P.6    Reinberg, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.