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Volumn 12, Issue 2, 2005, Pages 110-112

Reading signals on the nucleosome with a new nomenclature for modified histones

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; GLUTAMIC ACID; HISTONE; LYSINE; SERINE; THREONINE;

EID: 15044358494     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb0205-110     Document Type: Review
Times cited : (200)

References (20)
  • 1
    • 0017755951 scopus 로고
    • Structure of the nucleosome core particle of chromatin
    • Finch, J.T. et al. Structure of the nucleosome core particle of chromatin. Nature 269, 29-36 (1977).
    • (1977) Nature , vol.269 , pp. 29-36
    • Finch, J.T.1
  • 2
    • 0016221697 scopus 로고
    • Chromatin structure: A repeating unit of histones and DNA
    • Kornberg, R.D. Chromatin structure: a repeating unit of histones and DNA. Science 184, 868-871 (1974).
    • (1974) Science , vol.184 , pp. 868-871
    • Kornberg, R.D.1
  • 3
    • 0017622808 scopus 로고
    • Histone nomenclature
    • Bradbury, E.M. Histone nomenclature. Methods Cell Biol. 16, 179-181 (1977).
    • (1977) Methods Cell Biol. , vol.16 , pp. 179-181
    • Bradbury, E.M.1
  • 5
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V.G., Faulkner, R. & Mirsky, A.E. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. USA 51, 786-794 (1964).
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 6
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes, T.R., Thorne, A.W. & Crane-Robinson, C. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J. 7, 1395-1403 (1988).
    • (1988) EMBO J. , vol.7 , pp. 1395-1403
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 7
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner, B.M., Birley, A.J. & Lavender, J. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 69, 375-384 (1992).
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 8
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner, B.M. Decoding the nucleosome. Cell 75, 5-8 (1993)
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 9
    • 85015069067 scopus 로고    scopus 로고
    • Controlling the double helix
    • Felsenfeld, G. & Groudine, M. Controlling the double helix. Nature 421, 448-453 (2003).
    • (2003) Nature , vol.421 , pp. 448-453
    • Felsenfeld, G.1    Groudine, M.2
  • 10
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • Lachner, M., O'Sullivan, R.J. & Jenuwein, T. An epigenetic road map for histone lysine methylation. J. Cell Sci. 116, 2117-2124 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 2117-2124
    • Lachner, M.1    O'Sullivan, R.J.2    Jenuwein, T.3
  • 11
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Métivier, R. et al. Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115, 751-763 (2003).
    • (2003) Cell , vol.115 , pp. 751-763
    • Métivier, R.1
  • 12
    • 0037074010 scopus 로고    scopus 로고
    • Signaling network model of chromatin
    • Schreiber, S.L. & Bernstein, B. Signaling network model of chromatin. Cell 111, 771-778 (2002).
    • (2002) Cell , vol.111 , pp. 771-778
    • Schreiber, S.L.1    Bernstein, B.2
  • 13
    • 0344824404 scopus 로고    scopus 로고
    • Histone sumoylation is associated with transcriptional repression
    • Shiio, Y. & Eisenman, R.N. Histone sumoylation is associated with transcriptional repression. Proc. Natl. Acad. Sci. USA 100, 13225-23230 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13225-23230
    • Shiio, Y.1    Eisenman, R.N.2
  • 14
    • 2642542643 scopus 로고    scopus 로고
    • Silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin
    • Schotta, G. et al. Silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev. 18, 1251-1262 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 1251-1262
    • Schotta, G.1
  • 15
    • 9144268924 scopus 로고    scopus 로고
    • Partitioning and plasticity of repressive histone methylation states in mammalian chromatin
    • Peters, A.H. et al. Partitioning and plasticity of repressive histone methylation states in mammalian chromatin. Mol. Cell 12, 1577-1589 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1577-1589
    • Peters, A.H.1
  • 16
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner, B.M. Histone acetylation and an epigenetic code. BioEssays 22, 836-845 (2000).
    • (2000) BioEssays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 17
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. & Allis, C.D. The language of covalent histone modifications Nature 403, 41-45 (2000).
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.1    Allis, C.D.2
  • 18
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner, B.M. Cellular memory and the histone code. Cell 111, 285-291 (2002).
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 19
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle, W., Wang, Y. & Allis, C.D. Binary switches and modification cassettes in histone biology and beyond. Nature 425, 475-479 (2003).
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 20
    • 2942610993 scopus 로고    scopus 로고
    • Tethering of HP1 proteins to chromatin is relieved by phosphoacetylation of histone H3
    • Mateescu, B. et al. Tethering of HP1 proteins to chromatin is relieved by phosphoacetylation of histone H3. EMBO Rep. 5, 490-496 (2004).
    • (2004) EMBO Rep. , vol.5 , pp. 490-496
    • Mateescu, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.