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Volumn 403, Issue 6765, 2000, Pages 41-45

The language of covalent histone modifications

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HISTONE;

EID: 0034610814     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/47412     Document Type: Review
Times cited : (6948)

References (69)
  • 2
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryotic chromosome
    • Kornberg, R. D. & Lorch, Y. Twenty-five years of the nucleosome, fundamental particle of the eukaryotic chromosome. Cell 98, 285-294 (1999).
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 3
    • 0001932547 scopus 로고
    • ed. Rich, A. Springer, New York
    • van Holde, K. E. in Chromatin (ed. Rich, A.) 111-148 (Springer, New York, 1988).
    • (1988) Chromatin , pp. 111-148
    • Van Holde, K.E.1
  • 4
    • 0033080794 scopus 로고    scopus 로고
    • Chromatin disruption and modification
    • Wolffe, A. P. & Hayes, J. J. Chromatin disruption and modification. Nucleic Acids Res. 27, 711-720 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 711-720
    • Wolffe, A.P.1    Hayes, J.J.2
  • 5
    • 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, S. M. & 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 80, 583-592 (1995).
    • (1995) Cell , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Bolsinger, S.3    Gasser, S.M.4    Grunstein, M.5
  • 6
    • 0030003051 scopus 로고    scopus 로고
    • Repression domain of the yeast global repressor Tupl interacts directly with histones H3 and H4
    • Edmondson, D. G., Smith, M. M. & Roth, S. Y. Repression domain of the yeast global repressor Tupl interacts directly with histones H3 and H4. Genes Dev. 10, 1247-1259 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 1247-1259
    • Edmondson, D.G.1    Smith, M.M.2    Roth, S.Y.3
  • 7
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F. & Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389, 251-260 (1997).
    • (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
  • 8
    • 0032558998 scopus 로고    scopus 로고
    • Structure and function of the core histone N-termini: More than meets the eye
    • Hansen, J. C., Tse, C. & Wolffe, A. P. Structure and function of the core histone N-termini: more than meets the eye. Biochemistry 37, 17637-17641 (1998).
    • (1998) Biochemistry , vol.37 , pp. 17637-17641
    • Hansen, J.C.1    Tse, C.2    Wolffe, A.P.3
  • 9
    • 0032467010 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications: How clear is the signal?
    • Mizzen, C. et al. Signaling to chromatin through histone modifications: how clear is the signal? Cold Spring Harb. Symp. Quant. Biol. 63, 469-481 (1998).
    • (1998) Cold Spring Harb. Symp. Quant. Biol. , vol.63 , pp. 469-481
    • Mizzen, C.1
  • 10
    • 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
  • 11
    • 0027916769 scopus 로고
    • Histone deacetylase. A key enzyme for the binding of regulatory proteins to chromatin
    • Lopez-Rodas, G. et al. Histone deacetylase. A key enzyme for the binding of regulatory proteins to chromatin. FEBS Lett. 317, 175-180 (1993).
    • (1993) FEBS Lett. , vol.317 , pp. 175-180
    • Lopez-Rodas, G.1
  • 12
    • 0028608018 scopus 로고
    • Histone acetylation: Facts and questions
    • Loidl, P. Histone acetylation: facts and questions. Chromosoma 103, 441-449 (1944).
    • (1944) Chromosoma , vol.103 , pp. 441-449
    • Loidl, P.1
  • 13
    • 0027366656 scopus 로고
    • The role of histones and their modifications in the informative content of chromatin
    • Tordera, V., Sendra, R. & Perez-Ortin, J. E. The role of histones and their modifications in the informative content of chromatin. Experientia 49, 780-788 (1993).
    • (1993) Experientia , vol.49 , pp. 780-788
    • Tordera, V.1    Sendra, R.2    Perez-Ortin, J.E.3
  • 14
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. Histone acetylation in chromatin structure and transcription. Nature 389, 349-352 (1997).
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 15
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl, K. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 12, 599-606 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 599-606
    • Struhl, K.1
  • 17
    • 0029835806 scopus 로고    scopus 로고
    • Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
    • Kuo, M. H. et al. Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Nature 383, 269-272 (1996).
    • (1996) Nature , vol.383 , pp. 269-272
    • Kuo, M.H.1
  • 18
    • 0033605238 scopus 로고    scopus 로고
    • Expanded lysine acetylation specificity of Gcn5 in native complexes
    • Grant, P. A. et al. Expanded lysine acetylation specificity of Gcn5 in native complexes. J. Biol. Chem. 274, 5895-5900 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 5895-5900
    • Grant, P.A.1
  • 19
    • 0032101179 scopus 로고    scopus 로고
    • Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
    • Zhang, W., Bone, J. R., Edmondson, D. G., Turner, B. M. & Roth, S. Y. Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase. EMBO J. 17, 3155-3167 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3155-3167
    • Zhang, W.1    Bone, J.R.2    Edmondson, D.G.3    Turner, B.M.4    Roth, S.Y.5
  • 20
    • 0033517354 scopus 로고    scopus 로고
    • Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide
    • Rojas, J. R. et al. Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Nature 401, 93-98 (1999).
    • (1999) Nature , vol.401 , pp. 93-98
    • Rojas, J.R.1
  • 21
    • 0033603555 scopus 로고    scopus 로고
    • Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltranferase GCN5 transcriptional coactivator
    • Tanner, K. G. et al. Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltranferase GCN5 transcriptional coactivator. J. Biol. Chem. 274, 18157-18160 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 18157-18160
    • Tanner, K.G.1
  • 22
    • 0033529845 scopus 로고    scopus 로고
    • Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator
    • Trievel, R. C. et al. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl Acad. Sci. USA 96, 8931-8936 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8931-8936
    • Trievel, R.C.1
  • 23
    • 0033168714 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
    • Clements, A. et al. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. EMBO J. 18, 3521-3532 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3521-3532
    • Clements, A.1
  • 24
    • 0033168497 scopus 로고    scopus 로고
    • Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A
    • Lin, Y., Fletcher, C. M., Zhou, I., Allis, C. D. & Wagner, G. Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A. Nature 400, 86-89 (1999).
    • (1999) Nature , vol.400 , pp. 86-89
    • Lin, Y.1    Fletcher, C.M.2    Zhou, I.3    Allis, C.D.4    Wagner, G.5
  • 25
    • 0033529962 scopus 로고    scopus 로고
    • Structure and mechanism of action of the histone acetyltransferase gcn5 and similarity to other N-acetyltransferases
    • Sternglanz, R. & Schindelin, H. Structure and mechanism of action of the histone acetyltransferase gcn5 and similarity to other N-acetyltransferases. Proc. Natl Acad. Sci. USA 96, 8807-8808 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8807-8808
    • Sternglanz, R.1    Schindelin, H.2
  • 26
    • 0032540755 scopus 로고    scopus 로고
    • How do histone acetyltransferases select lysine residues in core histones?
    • Kimura, A. & Horikoshi, M. How do histone acetyltransferases select lysine residues in core histones? FEBS Lett. 431, 131-133 (1998).
    • (1998) FEBS Lett. , vol.431 , pp. 131-133
    • Kimura, A.1    Horikoshi, M.2
  • 27
    • 0029349023 scopus 로고
    • Histone acetylation in chromatin and chromosomes
    • Turner, B. M. & O'Neill, L. P. Histone acetylation in chromatin and chromosomes. Semin. Cell Biol. 6, 229-236 (1995).
    • (1995) Semin. Cell Biol. , vol.6 , pp. 229-236
    • Turner, B.M.1    O'Neill, L.P.2
  • 28
    • 0002216824 scopus 로고
    • ed. Wolffe, A. P. JAI, Greenwich, Connecticut
    • Annunziato, A. T. in The Nucleus (ed. Wolffe, A. P.) 31-56 (JAI, Greenwich, Connecticut, 1995).
    • (1995) The Nucleus , pp. 31-56
    • Annunziato, A.T.1
  • 29
    • 0022365083 scopus 로고
    • Deposition-related histone acetylation in micronuclei of conjugating Tetrahymena
    • Allis, C. D., Chicoine, L. G., Richman, R. & Schulman, I. G. Deposition-related histone acetylation in micronuclei of conjugating Tetrahymena. Proc. Natl Acad. Sci. USA 82, 8048-8052 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 8048-8052
    • Allis, C.D.1    Chicoine, L.G.2    Richman, R.3    Schulman, I.G.4
  • 30
    • 0028847955 scopus 로고
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4
    • Sobel, R. E., Cook, R. G., Perry, C. A., Annunziato, A. T. & Allis, C. D. Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4. Proc. Natl Acad. Sci. USA 92, 1237-1241 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1237-1241
    • Sobel, R.E.1    Cook, R.G.2    Perry, C.A.3    Annunziato, A.T.4    Allis, C.D.5
  • 31
    • 0033518179 scopus 로고    scopus 로고
    • The RCAF complex mediates chromatin assembly during DNA replication and repair
    • Tyler, J. K. et al. The RCAF complex mediates chromatin assembly during DNA replication and repair. Nature 402, 555-560 (1999).
    • (1999) Nature , vol.402 , pp. 555-560
    • Tyler, J.K.1
  • 32
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury, E. M. Reversible histone modifications and the chromosome cell cycle. Bioessays 14, 9-16 (1992).
    • (1992) Bioessays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 34
    • 0025872683 scopus 로고
    • Rapid histone H3 phosphorylation in response to growth factors, phorbol acid and protein synthesis inhibitors
    • Mahadevan, L. C., Willis, A. C. & Barratt, M. J. Rapid histone H3 phosphorylation in response to growth factors, phorbol tors, rJcUic acid, and protein synthesis inhibitors. Cell 65, 775-783 (1991).
    • (1991) Cell , vol.65 , pp. 775-783
    • Mahadevan, L.C.1    Willis, A.C.2    Barratt, M.J.3
  • 35
    • 0033113010 scopus 로고    scopus 로고
    • MAP kinase-mediated signalling to nucleosomes and immediate early gene induction
    • Thomson, S., Mahadevan, L. C. & Clayton, A. L. MAP kinase-mediated signalling to nucleosomes and immediate early gene induction. Semin. Cell Dev. Biol. 10, 205-214 (1999).
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 205-214
    • Thomson, S.1    Mahadevan, L.C.2    Clayton, A.L.3
  • 36
    • 0033609882 scopus 로고    scopus 로고
    • Increased Ser-10 phosphorylation of histone H3 in mitogen-stimulated and oncogene-transformed mouse fibroblast
    • Chadee, D. N. et al. Increased Ser-10 phosphorylation of histone H3 in mitogen-stimulated and oncogene-transformed mouse fibroblast. J. Biol. Chem. 274, 24914-24920 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 24914-24920
    • Chadee, D.N.1
  • 37
    • 0033529706 scopus 로고    scopus 로고
    • Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3
    • Sassone-Corsi, P. et al. Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3. Science 285, 886-891 (1999).
    • (1999) Science , vol.285 , pp. 886-891
    • Sassone-Corsi, P.1
  • 38
    • 0032514734 scopus 로고    scopus 로고
    • Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene
    • De Cesare, D., Jacquot, S., Hanauer, A. & Sassone-Corsi, P. Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene. Proc. Natl Acad. Sci. USA 95, 12202-12207 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12202-12207
    • De Cesare, D.1    Jacquot, S.2    Hanauer, A.3    Sassone-Corsi, P.4
  • 39
    • 0033200205 scopus 로고    scopus 로고
    • The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSKI as a potential histone H3/HMG-14 kinase
    • Thomson, S. et al. The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSKI as a potential histone H3/HMG-14 kinase. EMBO J. 18, 4779-4793 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4779-4793
    • Thomson, S.1
  • 40
    • 0033166349 scopus 로고    scopus 로고
    • JIL-1: A novel chromosomal tandem kinase implicated in transcriptional regulation in Drosophila
    • Jin, Y. et al. JIL-1: a novel chromosomal tandem kinase implicated in transcriptional regulation in Drosophila. Mol. Cell 4, 129-133 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 129-133
    • Jin, Y.1
  • 41
    • 0032055416 scopus 로고    scopus 로고
    • Dosage compensation in flies and worms: The ups and downs of X-chromosome regulation
    • Lucchesi, J. C. Dosage compensation in flies and worms: the ups and downs of X-chromosome regulation. Curr. Opin. Genet. Dev. 8, 179-184 (1998).
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 179-184
    • Lucchesi, J.C.1
  • 42
    • 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
  • 43
    • 0024446935 scopus 로고
    • Isolation and characterization of histone
    • von Holt, C. et al. Isolation and characterization of histone. Methods Enzymol. 170, 431-523 (1989).
    • (1989) Methods Enzymol. , vol.170 , pp. 431-523
    • Von Holt, C.1
  • 44
    • 0033592999 scopus 로고    scopus 로고
    • Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena
    • Strahl, B. D., Ohba, R., Cook, R. G. & Allis, C. D. Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena. Proc. Natl Acad. Sci. USA 96, 14967-14972 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14967-14972
    • Strahl, B.D.1    Ohba, R.2    Cook, R.G.3    Allis, C.D.4
  • 45
    • 0033603396 scopus 로고    scopus 로고
    • Regulation of transcription by a protein methyltransferase
    • Chen, D. et al. Regulation of transcription by a protein methyltransferase. Science 284, 2174-2177 (1999).
    • (1999) Science , vol.284 , pp. 2174-2177
    • Chen, D.1
  • 46
    • 0000631273 scopus 로고    scopus 로고
    • The signal-dependent coactivator CBP is a nuclear target for pp90RSK
    • Nakajima, T. et al. The signal-dependent coactivator CBP is a nuclear target for pp90RSK. Cell 86, 465-474 (1996).
    • (1996) Cell , vol.86 , pp. 465-474
    • Nakajima, T.1
  • 47
    • 0033153358 scopus 로고    scopus 로고
    • Gene activation by histone and factor acetyltransfentses
    • Berger, S. L. Gene activation by histone and factor acetyltransfentses. Curr. Opin. Cell Biol. 11, 336-341 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 336-341
    • Berger, S.L.1
  • 48
    • 0033617334 scopus 로고    scopus 로고
    • Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter
    • Cosma, M. P., Tanaka, T. & Nasmyth, K. Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter. Cell 97, 299-311 (1999).
    • (1999) Cell , vol.97 , pp. 299-311
    • Cosma, M.P.1    Tanaka, T.2    Nasmyth, K.3
  • 49
    • 0033152279 scopus 로고    scopus 로고
    • Cell cycle-regulated histone acetylation required for expression of the yeast HO gene
    • Krebs, J. E., Kuo, M. H., Allis, C. D. & Peterson, C. L. Cell cycle-regulated histone acetylation required for expression of the yeast HO gene. Genes Dev. 13, 1412-1421 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1412-1421
    • Krebs, J.E.1    Kuo, M.H.2    Allis, C.D.3    Peterson, C.L.4
  • 50
    • 0027819350 scopus 로고
    • Chromatin structure of transcriptionally active genes
    • Clark, D. et al. Chromatin structure of transcriptionally active genes. Cold Spring Harb. Symp. Quant. Biol. 58, 1-6 (1993).
    • (1993) Cold Spring Harb. Symp. Quant. Biol. , vol.58 , pp. 1-6
    • Clark, D.1
  • 51
    • 0026545414 scopus 로고
    • Chromatin condensation: Does histone H1 dephosphorylation play a role?
    • Roth, S. Y. & Allis, C. D. Chromatin condensation: does histone H1 dephosphorylation play a role? Trends Biochem. Sci. 17, 93-98 (1992).
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 93-98
    • Roth, S.Y.1    Allis, C.D.2
  • 52
    • 0028291992 scopus 로고
    • Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction
    • Barrait, M. J., Hazzalin, C. A., Cano, E. & Mahadevan, L. C. Mitogen-stimulated phosphorylation of histone H3 is targeted to a small hyperacetylation-sensitive fraction. Proc. Natl Acad. Sci. USA 91, 4781-4785 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4781-4785
    • Barratt, M.J.1    Hazzalin, C.A.2    Cano, E.3    Mahadevan, L.C.4
  • 53
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreeds in an ordered fashion coincident with mitotic chromosome condensation
    • Hendzel, M. J. Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreeds in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 106, 348-360 (1997).
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.J.1
  • 54
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei, Y., Yu, L., Bowen, J., Gorovsky, M. A. & Allis, C. D. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 97, 99-109 (1999).
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 55
    • 0033520367 scopus 로고    scopus 로고
    • Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation
    • Goto, H. et al. Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation. J. Biol. Chem. 274, 25543-25549 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 25543-25549
    • Goto, H.1
  • 56
    • 0028104174 scopus 로고
    • Human CENP-A contains a histone H3 related histone fold domain thai is required for targeting to the centromere
    • Sullivan, K. F., Hechenberger, M. & Masri, K. Human CENP-A contains a histone H3 related histone fold domain thai is required for targeting to the centromere. J. Cell Biol. 127, 581-592 (1994).
    • (1994) J. Cell Biol. , vol.127 , pp. 581-592
    • Sullivan, K.F.1    Hechenberger, M.2    Masri, K.3
  • 57
    • 0032901198 scopus 로고    scopus 로고
    • SMC-mediated chromosome mechanics: A conserved scheme from bacteria to vertebrates?
    • Hirano, T. SMC-mediated chromosome mechanics: a conserved scheme from bacteria to vertebrates? Genes Dev. 13, 11-19 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 11-19
    • Hirano, T.1
  • 58
    • 0029805633 scopus 로고    scopus 로고
    • The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast
    • De Rubertis, F. et al. The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast. Nature 384, 589-591 (1996).
    • (1996) Nature , vol.384 , pp. 589-591
    • De Rubertis, F.1
  • 59
    • 0029953722 scopus 로고    scopus 로고
    • Effecient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern
    • Braunstein, M., Sobel, R. E., Allis, C. D., Turner, B. M. & Broach, J. R. Effecient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern. Mol. Cell. Biol. 16, 4349-4356 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4349-4356
    • Braunstein, M.1    Sobel, R.E.2    Allis, C.D.3    Turner, B.M.4    Broach, J.R.5
  • 60
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin, C. et al. Structure and ligand of a histone acetyltransferase bromodomain. Nature 399, 491-496 (1999).
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1
  • 61
    • 17444386662 scopus 로고    scopus 로고
    • The bromodomain: A chromatin-targeting module?
    • Winston, F. & Allis, C. D. The bromodomain: a chromatin-targeting module? Nature Struct. Biol. 6, 601-604 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 601-604
    • Winston, F.1    Allis, C.D.2
  • 62
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. Protein modules and signalling networks. Nature 373, 573-580 (1995).
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 63
    • 0030876429 scopus 로고    scopus 로고
    • Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf/Swi and Srb/mediator complexes
    • Roberts, S. M. & Winston, F. Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf/Swi and Srb/mediator complexes. Genetics 147, 451-465 (1997).
    • (1997) Genetics , vol.147 , pp. 451-465
    • Roberts, S.M.1    Winston, F.2
  • 64
    • 0033561043 scopus 로고    scopus 로고
    • Continuous and widespread roles for the Swi-Snf complex in transcription
    • Biggar, S. R. & Crabtree, G. R. Continuous and widespread roles for the Swi-Snf complex in transcription. EMBO J. 18, 2254-2264 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2254-2264
    • Biggar, S.R.1    Crabtree, G.R.2
  • 65
    • 0033151812 scopus 로고    scopus 로고
    • The nucleosome remodeling complex, Snf/Swi, is required for the maintenance of transcription in vivo and is partially redundant with the histone acetyltransferase, Gcn5
    • Sudarsanam, P., Cao, Y., Wu, L., Laurent, B. C. & Winston, F. The nucleosome remodeling complex, Snf/Swi, is required for the maintenance of transcription in vivo and is partially redundant with the histone acetyltransferase, Gcn5. EMBO J. 18, 3101-3106 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3101-3106
    • Sudarsanam, P.1    Cao, Y.2    Wu, L.3    Laurent, B.C.4    Winston, F.5
  • 66
    • 0030741529 scopus 로고    scopus 로고
    • Role of histone tails in nucleosome remodeling by Drosophilia NURF
    • Georgel, P. T., Tsukiyama, T. & Wu, C. Role of histone tails in nucleosome remodeling by Drosophilia NURF. EMBO J. 16, 4717-4726 (1997).
    • (1997) EMBO J. , vol.16 , pp. 4717-4726
    • Georgel, P.T.1    Tsukiyama, T.2    Wu, C.3
  • 67
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: Different gene products and covalent modifications
    • Luduena, R. F. Multiple forms of tubulin: different gene products and covalent modifications. Int. Rev. Cytol. 178, 207-275 (1998).
    • (1998) Int. Rev. Cytol. , vol.178 , pp. 207-275
    • Luduena, R.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.