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Volumn 1824, Issue 8, 2012, Pages 974-982

Effects of histone acetylation and CpG methylation on the structure of nucleosomes

Author keywords

DNA methylation; Fluorescence anisotropy; FRET; Histone acetylation; Nucleosome; Single molecule

Indexed keywords

ANISOTROPY; CHROMATIN STRUCTURE; CPG ISLAND; DNA METHYLATION; EUKARYOTE; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENE CONTROL; HISTONE ACETYLATION; HUMAN; NUCLEOSOME; PRIORITY JOURNAL; REVIEW;

EID: 84861941362     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.05.006     Document Type: Review
Times cited : (34)

References (65)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • DOI 10.1038/38444
    • K. Luger, A.W. Mader, R.K. Richmond, D.F. Sargent, T.J. Richmond, Crystal structure of the nucleosome core particle at 2.8 A resolution, Nature 389 (1997) 251-260. (Pubitemid 27406632)
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 0032006717 scopus 로고    scopus 로고
    • DNA binding within the nucleosome core
    • DOI 10.1016/S0959-440X(98)80007-9
    • K. Luger, T.J. Richmond, DNA binding within the nucleosome core, Curr. Opin. Struct. Biol. 8 (1998) 33-40. (Pubitemid 28107913)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.1 , pp. 33-40
    • Luger, K.1    Richmond, T.J.2
  • 3
  • 4
    • 78649838453 scopus 로고    scopus 로고
    • Single-pair FRET experiments on nucleosome conformational dynamics
    • R. Buning, J. Van Noort, Single-pair FRET experiments on nucleosome conformational dynamics, Biochimie 92 (2010) 1729-1740.
    • (2010) Biochimie , vol.92 , pp. 1729-1740
    • Buning, R.1    Van Noort, J.2
  • 5
    • 80052805267 scopus 로고    scopus 로고
    • Histone modification: Cause or cog?
    • S. Henikoff, A. Shilatifard, Histone modification: cause or cog? Trends Genet. 27 (2011) 389-396.
    • (2011) Trends Genet. , vol.27 , pp. 389-396
    • Henikoff, S.1    Shilatifard, A.2
  • 6
    • 79959484677 scopus 로고    scopus 로고
    • Signals and combinatorial functions of histone modifications
    • T. Suganuma, J.L. Workman, Signals and combinatorial functions of histone modifications, Annu. Rev. Biochem. 80 (2011) 473-499.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 473-499
    • Suganuma, T.1    Workman, J.L.2
  • 7
    • 33748314757 scopus 로고    scopus 로고
    • Breaking barriers to transcription elongation
    • DOI 10.1038/nrm1981, PII NRM1981
    • A. Saunders, L.J. Core, J.T. Lis, Breaking barriers to transcription elongation, Nat. Rev. Mol. Cell Biol. 7 (2006) 557-567. (Pubitemid 44325347)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.8 , pp. 557-567
    • Saunders, A.1    Core, L.J.2    Lis, J.T.3
  • 8
    • 35848958821 scopus 로고    scopus 로고
    • Chromatin remodeling: Insights and intrigue from single-molecule studies
    • DOI 10.1038/nsmb1333, PII NSMB1333
    • B.R. Cairns, Chromatin remodeling: insights and intrigue from single-molecule studies, Nat. Struct. Mol. Biol. 14 (2007) 989-996. (Pubitemid 350060341)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.11 , pp. 989-996
    • Cairns, B.R.1
  • 9
    • 67650725820 scopus 로고    scopus 로고
    • The biology of chromatin remodeling complexes
    • C.R. Clapier, B.R. Cairns, The biology of chromatin remodeling complexes, Annu. Rev. Biochem. 78 (2009) 273-304.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 273-304
    • Clapier, C.R.1    Cairns, B.R.2
  • 10
    • 58249118858 scopus 로고    scopus 로고
    • The H4 tail domain participates in intra-and internucleosome interactions with protein and DNA during folding and oligomerization of nucleosome arrays
    • P.Y. Kan, T.L. Caterino, J.J. Hayes, The H4 tail domain participates in intra-and internucleosome interactions with protein and DNA during folding and oligomerization of nucleosome arrays, Mol. Cell. Biol. 29 (2009) 538.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 538
    • Kan, P.Y.1    Caterino, T.L.2    Hayes, J.J.3
  • 12
    • 84862908551 scopus 로고    scopus 로고
    • Effects of DNA methylation on the structure of nucleosomes
    • J.Y. Lee, T.H. Lee, Effects of DNA methylation on the structure of nucleosomes, J. Am. Chem. Soc. 134 (2012) 173-175.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 173-175
    • Lee, J.Y.1    Lee, T.H.2
  • 13
    • 79953175642 scopus 로고    scopus 로고
    • Effects of histone acetylation by Piccolo NuA4 on the structure of a nucleosome and the interactions between two nucleosomes
    • J.Y. Lee, S. Wei, T.H. Lee, Effects of histone acetylation by Piccolo NuA4 on the structure of a nucleosome and the interactions between two nucleosomes, J. Biol. Chem. 286 (2011) 11099.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11099
    • Lee, J.Y.1    Wei, S.2    Lee, T.H.3
  • 14
    • 77249178763 scopus 로고    scopus 로고
    • DNA methylation increases nucleosome compaction and rigidity
    • J.S. Choy, S. Wei, J.Y. Lee, S. Tan, S. Chu, T.H. Lee, DNA methylation increases nucleosome compaction and rigidity, J. Am. Chem. Soc. 132 (2010) 1782-1783.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1782-1783
    • Choy, J.S.1    Wei, S.2    Lee, J.Y.3    Tan, S.4    Chu, S.5    Lee, T.H.6
  • 15
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • G. Arents, E.N. Moudrianakis, The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization, Proc. Natl. Acad. Sci. 92 (1995) 11170.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 11170
    • Arents, G.1    Moudrianakis, E.N.2
  • 17
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin Modifications and Their Function
    • DOI 10.1016/j.cell.2007.02.005, PII S0092867407001845
    • T. Kouzarides, Chromatin modifications and their function, Cell 128 (2007) 693-705. (Pubitemid 46273577)
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 18
    • 34548526743 scopus 로고    scopus 로고
    • Chromatin remodeling and cancer, part I: covalent histone modifications
    • DOI 10.1016/j.molmed.2007.07.003, PII S1471491407001463
    • G.G. Wang, C.D. Allis, P. Chi, Chromatin remodeling and cancer, Part I: Covalent histone modifications, Trends Mol. Med. 13 (2007) 363-372. (Pubitemid 47385381)
    • (2007) Trends in Molecular Medicine , vol.13 , Issue.9 , pp. 363-372
    • Wang, G.G.1    Allis, C.D.2    Chi, P.3
  • 19
    • 65649099698 scopus 로고    scopus 로고
    • A tale of tails: How histone tails mediate chromatin compaction in different salt and linker histone environments??
    • G. Arya, T. Schlick, A tale of tails: how histone tails mediate chromatin compaction in different salt and linker histone environments?? J. Phys. Chem. A 113 (2009) 4045-4059.
    • (2009) J. Phys. Chem. A , vol.113 , pp. 4045-4059
    • Arya, G.1    Schlick, T.2
  • 20
    • 34047232501 scopus 로고    scopus 로고
    • H3 and H4 histone tails play a central role in the interactions of recombinant NCPs
    • DOI 10.1529/biophysj.106.093815
    • A. Bertin, M. Renouard, J.S. Pedersen, F. Livolant, D. Durand, H3 and H4 histone tails play a central role in the interactions of recombinant NCPs, Biophys. J. 92 (2007) 2633-2645. (Pubitemid 46536442)
    • (2007) Biophysical Journal , vol.92 , Issue.7 , pp. 2633-2645
    • Bertin, A.1    Renouard, M.2    Pedersen, J.S.3    Livolant, F.4    Durand, D.5
  • 21
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: Requirement for the histone H4 N-terminal tail
    • DOI 10.1016/S0022-2836(03)00025-1
    • B. Dorigo, T. Schalch, K. Bystricky, T.J. Richmond, Chromatin fiber folding: requirement for the histone H4 N-terminal tail, J. Mol. Biol. 327 (2003) 85-96. (Pubitemid 36293304)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.1 , pp. 85-96
    • Dorigo, B.1    Schalch, T.2    Bystricky, K.3    Richmond, T.J.4
  • 22
    • 0035704707 scopus 로고    scopus 로고
    • Role of DNA sequence in nucleosome stability and dynamics
    • J. Widom, Role of DNA sequence in nucleosome stability and dynamics, Q. Rev. Biophys. 34 (2001) 269-324. (Pubitemid 34121497)
    • (2001) Quarterly Reviews of Biophysics , vol.34 , Issue.3 , pp. 269-324
    • Widom, J.1
  • 23
    • 0032512794 scopus 로고    scopus 로고
    • New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning
    • DOI 10.1006/jmbi.1997.1494
    • P.T. Lowary, J. Widom, New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning1, J. Mol. Biol. 276 (1998) 19-42. (Pubitemid 28085408)
    • (1998) Journal of Molecular Biology , vol.276 , Issue.1 , pp. 19-42
    • Lowary, P.T.1    Widom, J.2
  • 24
    • 77957367439 scopus 로고    scopus 로고
    • Structure of RCC1 chromatin factor bound to the nucleosome core particle
    • R.D. Makde, J.R. England, H.P. Yennawar, S. Tan, Structure of RCC1 chromatin factor bound to the nucleosome core particle, Nature 467 (2010) 562-566.
    • (2010) Nature , vol.467 , pp. 562-566
    • Makde, R.D.1    England, J.R.2    Yennawar, H.P.3    Tan, S.4
  • 25
    • 0037381213 scopus 로고    scopus 로고
    • Structure and dynamic behavior of nucleosomes
    • DOI 10.1016/S0959-437X(03)00026-1
    • K. Luger, Structure and dynamic behavior of nucleosomes, Curr. Opin. Genet. Dev. 13 (2003) 127-135. (Pubitemid 36369736)
    • (2003) Current Opinion in Genetics and Development , vol.13 , Issue.2 , pp. 127-135
    • Luger, K.1
  • 26
    • 0033039285 scopus 로고    scopus 로고
    • Preparation of nucleosome core particle from recombinant histones
    • DOI 10.1016/S0076-6879(99)04003-3
    • K. Luger, T.J. Rechsteiner, T.J. Richmond, Preparation of nucleosome core particle from recombinant histones, Methods Enzymol. 304 (1999) 3-19. (Pubitemid 29268874)
    • (1999) Methods in Enzymology , vol.304 , pp. 3-19
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 27
    • 84981779372 scopus 로고
    • Zwischenmolekulare energiewanderung und fluoreszenz
    • T. Förster, Zwischenmolekulare energiewanderung und fluoreszenz, Ann. Phys. 437 (1948) 55-75.
    • (1948) Ann. Phys. , vol.437 , pp. 55-75
    • Förster, T.1
  • 29
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • M.D. Shahbazian, M. Grunstein, Functions of site-specific histone acetylation and deacetylation, Annu. Rev. Biochem. 76 (2007) 75-100.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 30
    • 77953639338 scopus 로고    scopus 로고
    • Histone chaperones, histone acetylation, and the fluidity of the chromogenome
    • J.C. Hansen, J.K. Nyborg, K. Luger, L.A. Stargell, Histone chaperones, histone acetylation, and the fluidity of the chromogenome, J. Cell. Physiol. 224 (2010) 289-299.
    • (2010) J. Cell. Physiol. , vol.224 , pp. 289-299
    • Hansen, J.C.1    Nyborg, J.K.2    Luger, K.3    Stargell, L.A.4
  • 31
    • 0022551060 scopus 로고
    • Histone hyperacetylation: Its effects on nucleosome conformation and stability
    • J. Ausio, K.E. Van Holde, Histone hyperacetylation: its effects on nucleosome conformation and stability, Biochemistry 25 (1986) 1421-1428. (Pubitemid 16048119)
    • (1986) Biochemistry , vol.25 , Issue.6 , pp. 1421-1428
    • Ausio, J.1    Van Holde, K.E.2
  • 32
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • K. Struhl, Histone acetylation and transcriptional regulatory mechanisms, Genes Dev. 12 (1998) 599-606. (Pubitemid 28134293)
    • (1998) Genes and Development , vol.12 , Issue.5 , pp. 599-606
    • Struhl, K.1
  • 34
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • V.G. Allfrey, R. Faulkner, A.E. Mirsky, Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis, Proc. Natl. Acad. Sci. U. S. A. 51 (1964) 786-794.
    • (1964) Proc. Natl. Acad. Sci. U. S. A. , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 35
    • 0025244999 scopus 로고
    • Nucleosome linking number change controlled by acetylation of histones H3 and H4
    • V.G. Norton, K.W. Marvin, P. Yau, E.M. Bradbury, Nucleosome linking number change controlled by acetylation of histones H3 and H4, J. Biol. Chem. 265 (1990) 19848.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19848
    • Norton, V.G.1    Marvin, K.W.2    Yau, P.3    Bradbury, E.M.4
  • 36
    • 33847655626 scopus 로고    scopus 로고
    • Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex
    • DOI 10.1021/bi602366n
    • C.E. Berndsen, W. Selleck, S.J. McBryant, J.C. Hansen, S. Tan, J.M. Denu, Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex, Biochemistry 46 (2007) 2091-2099. (Pubitemid 46355320)
    • (2007) Biochemistry , vol.46 , Issue.8 , pp. 2091-2099
    • Berndsen, C.E.1    Selleck, W.2    McBryant, S.J.3    Hansen, J.C.4    Tan, S.5    Denu, J.M.6
  • 37
    • 20744445493 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes
    • W. Selleck, I. Fortin, D. Sermwittayawong, J. Cote, S. Tan, The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes, Mol. Cell. Biol. 25 (2005) 5535.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5535
    • Selleck, W.1    Fortin, I.2    Sermwittayawong, D.3    Cote, J.4    Tan, S.5
  • 38
    • 77949548012 scopus 로고    scopus 로고
    • The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions
    • A.J. Andrews, X. Chen, A. Zevin, L.A. Stargell, K. Luger, The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions, Mol. Cell 37 (2010) 834-842.
    • (2010) Mol. Cell , vol.37 , pp. 834-842
    • Andrews, A.J.1    Chen, X.2    Zevin, A.3    Stargell, L.A.4    Luger, K.5
  • 40
    • 12544258222 scopus 로고    scopus 로고
    • Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding
    • Y.J. Park, J.V. Chodaparambil, Y. Bao, S.J. McBryant, K. Luger, Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding, J. Biol. Chem. 280 (2005) 1817.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1817
    • Park, Y.J.1    Chodaparambil, J.V.2    Bao, Y.3    McBryant, S.J.4    Luger, K.5
  • 41
    • 0026656374 scopus 로고
    • Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity
    • T. Fujii-Nakata, Y. Ishimi, A. Okuda, A. Kikuchi, Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity, J. Biol. Chem. 267 (1992) 20980-20986.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20980-20986
    • Fujii-Nakata, T.1    Ishimi, Y.2    Okuda, A.3    Kikuchi, A.4
  • 44
    • 70449442780 scopus 로고    scopus 로고
    • Principles of fluorescence spectroscopy
    • J.R. Lakowicz, B.R. Masters, Principles of fluorescence spectroscopy, J. Biomed. Opt. 13 (2008) 029901.
    • (2008) J. Biomed. Opt. , vol.13 , pp. 029901
    • Lakowicz, J.R.1    Masters, B.R.2
  • 45
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core particle linking number change
    • DOI 10.1016/0092-8674(89)90920-3
    • V.G. Norton, B.S. Imai, P. Yau, E.M. Bradbury, Histone acetylation reduces nucleosome core particle linking number change, Cell 57 (1989) 449-457. (Pubitemid 19126278)
    • (1989) Cell , vol.57 , Issue.3 , pp. 449-457
    • Norton, V.G.1    Imai, B.S.2    Yau, P.3    Bradbury, E.M.4
  • 47
    • 77952773196 scopus 로고    scopus 로고
    • Role of direct interactions between the histone H4 tail and the H2A core in long range nucleosome contacts
    • D. Sinha, M.A. Shogren-Knaak, Role of direct interactions between the histone H4 tail and the H2A core in long range nucleosome contacts, J. Biol. Chem. 285 (2010) 16572.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16572
    • Sinha, D.1    Shogren-Knaak, M.A.2
  • 48
    • 21844436803 scopus 로고    scopus 로고
    • X-ray structure of a tetranucleosome and its implications for the chromatin fibre
    • DOI 10.1038/nature03686
    • T. Schalch, S. Duda, D.F. Sargent, T.J. Richmond, X-ray structure of a tetranucleosome and its implications for the chromatin fibre, Nature 436 (2005) 138-141. (Pubitemid 40966200)
    • (2005) Nature , vol.436 , Issue.7047 , pp. 138-141
    • Schalch, T.1    Duda, S.2    Sargent, D.F.3    Richmond, T.J.4
  • 49
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms, and functions
    • DOI 10.1146/annurev.biophys.31.101101.140858
    • J.C. Hansen, Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions, Annu. Rev. Biophys. Biomol. Struct. 31 (2002) 361-392. (Pubitemid 34666838)
    • (2002) Annual Review of Biophysics and Biomolecular Structure , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 50
    • 48449106172 scopus 로고    scopus 로고
    • 30 nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction
    • P.J.J. Robinson, W. An, A. Routh, F. Martino, L. Chapman, R.G. Roeder, D. Rhodes, 30 nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction, J. Mol. Biol. 381 (2008) 816-825.
    • (2008) J. Mol. Biol. , vol.381 , pp. 816-825
    • Robinson, P.J.J.1    An, W.2    Routh, A.3    Martino, F.4    Chapman, L.5    Roeder, R.G.6    Rhodes, D.7
  • 51
    • 0036144048 scopus 로고    scopus 로고
    • DNA methylation patterns and epigenetic memory
    • A. Bird, DNA methylation patterns and epigenetic memory, Genes Dev. 16 (2002) 6.
    • (2002) Genes Dev. , vol.16 , pp. 6
    • Bird, A.1
  • 52
    • 31344466008 scopus 로고    scopus 로고
    • DNA methylation and gene silencing in cancer
    • DOI 10.1038/ncponc0354, PII N0354
    • S.B. Baylin, DNA methylation and gene silencing in cancer, Nat. Clin. Pract. Oncol. 2 (2005) S4-S11. (Pubitemid 43135229)
    • (2005) Nature Clinical Practice Oncology , vol.2 , Issue.SUPPL. 1
    • Baylin, S.B.1
  • 54
    • 0021770555 scopus 로고
    • CG dinucleotide clusters in MHC genes and in 5?? demethylated genes
    • M.L. Tykocinski, E.E. Max, CG dinucleotide clusters in MHC genes and in 5?? demethylated genes, Nucleic Acids Res. 12 (1984) 4385-4396.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 4385-4396
    • Tykocinski, M.L.1    Max, E.E.2
  • 55
    • 0022000776 scopus 로고
    • A fraction of the mouse genome that is derived from islands of nonmethylated, CpG-rich DNA
    • A. Bird, M. Taggart, M. Frommer, O.J. Miller, D. Macleod, A fraction of the mouse genome that is derived from islands of nonmethylated, CpG-rich DNA, Cell 40 (1985) 91-99. (Pubitemid 15169310)
    • (1985) Cell , vol.40 , Issue.1 , pp. 91-99
    • Bird, A.1    Taggart, M.2    Frommer, M.3
  • 56
    • 0022540321 scopus 로고
    • CpG-rich islands and the function of DNA methylation
    • A.P. Bird, CpG-rich islands and the function of DNA methylation, Nature 321 (1986) 209-213. (Pubitemid 16016411)
    • (1986) Nature , vol.321 , Issue.6067 , pp. 209-213
    • Bird, A.P.1
  • 57
    • 33947315736 scopus 로고    scopus 로고
    • Cancer epigenomics: DNA methylomes and histone-modification maps
    • DOI 10.1038/nrg2005, PII NRG2005
    • M. Esteller, Cancer epigenomics: DNA methylomes and histone-modification maps, Nat. Rev. Genet. 8 (2007) 286-298. (Pubitemid 46439286)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.4 , pp. 286-298
    • Esteller, M.1
  • 58
    • 0345357773 scopus 로고    scopus 로고
    • Gene Silencing in Cancer in Association with Promoter Hypermethylation
    • DOI 10.1056/NEJMra023075
    • J.G. Herman, S.B. Baylin, Gene silencing in cancer in association with promoter hypermethylation, N. Engl. J. Med. 349 (2003) 2042-2054. (Pubitemid 37448928)
    • (2003) New England Journal of Medicine , vol.349 , Issue.21 , pp. 2042-2054
    • Herman, J.G.1    Baylin, S.B.2
  • 59
    • 0034712712 scopus 로고    scopus 로고
    • The dynamic impact of CpG methylation in DNA
    • DOI 10.1021/bi9917636
    • K.B. Geahigan, G.A. Meints, M.E. Hatcher, J. Orban, G.P. Drobny, The dynamic impact of CpG methylation in DNA, Biochemistry 39 (2000) 4939-4946. (Pubitemid 30225361)
    • (2000) Biochemistry , vol.39 , Issue.16 , pp. 4939-4946
    • Geahigan, K.B.1    Meints, G.A.2    Hatcher, M.E.3    Orban, J.4    Drobny, G.P.5
  • 60
    • 0035369057 scopus 로고    scopus 로고
    • Impact of CpG methylation on structure, dynamics and solvation of cAMP DNA responsive element
    • S. Derreumaux, M. Chaoui, G. Tevanian, S. Fermandjian, Impact of CpG methylation on structure, dynamics and solvation of cAMP DNA responsive element, Nucleic Acids Res. 29 (2001) 2314-2326. (Pubitemid 32514934)
    • (2001) Nucleic Acids Research , vol.29 , Issue.11 , pp. 2314-2326
    • Derreumaux, S.1    Chaoui, M.2    Tevanian, G.3    Fermandjian, S.4
  • 61
    • 0036306349 scopus 로고    scopus 로고
    • Bending and flexibility of methylated and unmethylated EcoRI DNA
    • DOI 10.1006/jmbi.2001.5247
    • D. Nathan, D.M. Crothers, Bending and flexibility of methylated and unmethylated EcoRI DNA1, J. Mol. Biol. 316 (2002) 7-17. (Pubitemid 34729262)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.1 , pp. 7-17
    • Nathan, D.1    Crothers, D.M.2
  • 62
    • 0036219597 scopus 로고    scopus 로고
    • New approaches to the treatment of myelodysplasia
    • A.F. List, New approaches to the treatment of myelodysplasia, Oncologist 7 (2002) 39-49. (Pubitemid 34293059)
    • (2002) Oncologist , vol.7 , Issue.SUPPL. 1 , pp. 39-49
    • List, A.F.1
  • 63
    • 0028068714 scopus 로고
    • Facilitated binding of TATA-binding protein to nucleosomal DNA
    • DOI 10.1038/370481a0
    • A.N. Imbalzano, H. Kwon, M.R. Green, R.E. Kingston, Facilitated binding of TATA-binding protein to nucleosomal DNA, Nature 370 (1994) 481-485. (Pubitemid 24263556)
    • (1994) Nature , vol.370 , Issue.6489 , pp. 481-485
    • Imbalzano, A.N.1    Kwon, H.2    Green, M.R.3    Kingston, R.E.4
  • 64
    • 3042801306 scopus 로고    scopus 로고
    • Precise nucleosome positioning and the TATA box dictate requirements for the histone H4 tail and the bromodomain factor Bdf1
    • DOI 10.1016/j.molcel.2004.05.022, PII S1097276504003089
    • C. Martinez-Campa, P. Politis, J.L. Moreau, N. Kent, J. Goodall, J. Mellor, C.R. Goding, Precise nucleosome positioning and the TATA box dictate requirements for the histone H4 tail and the bromodomain factor Bdf1, Mol. Cell 15 (2004) 69-81. (Pubitemid 38850220)
    • (2004) Molecular Cell , vol.15 , Issue.1 , pp. 69-81
    • Martinez-Campa, C.1    Politis, P.2    Moreau, J.-L.3    Kent, N.4    Goodall, J.5    Mellor, J.6    Goding, C.R.7
  • 65
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • DOI 10.1016/S0092-8674(02)01080-2
    • B.M. Turner, Cellular memory and the histone code, Cell 111 (2002) 285-291. (Pubitemid 35341385)
    • (2002) Cell , vol.111 , Issue.3 , pp. 285-291
    • Turner, B.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.