메뉴 건너뛰기




Volumn 188, Issue 3, 1997, Pages 379-385

Nucleosomes: A solution to a crowded intracellular environment?

Author keywords

[No Author keywords available]

Indexed keywords

DNA;

EID: 0031558565     PISSN: 00225193     EISSN: None     Source Type: Journal    
DOI: 10.1006/jtbi.1997.0525     Document Type: Article
Times cited : (37)

References (75)
  • 1
    • 0025098652 scopus 로고
    • In vitro replication through nucleosomes without histone displacement
    • ANDREA, C. B., WONG, M. L. & ALBERTS, B. M. (1990). In vitro replication through nucleosomes without histone displacement. Nature 343, 719-726.
    • (1990) Nature , vol.343 , pp. 719-726
    • Andrea, C.B.1    Wong, M.L.2    Alberts, B.M.3
  • 2
    • 0027431478 scopus 로고
    • Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA
    • ARENTS, G. & MOUDRIANAKIS, E. N. (1993). Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA. Proc. Natl. Acad. Sci. U.S.A. 90, 10489-10493.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10489-10493
    • Arents, G.1    Moudrianakis, E.N.2
  • 3
    • 0026253815 scopus 로고
    • Condensation of DNA by multivalent cations: Considerations on mechanism
    • BLOOMFIELD, V. A. (1991). Condensation of DNA by multivalent cations: considerations on mechanism. Biopolymers 31, 1471-1481.
    • (1991) Biopolymers , vol.31 , pp. 1471-1481
    • Bloomfield, V.A.1
  • 5
    • 0027542926 scopus 로고
    • Concentration evaluation of chromatin in unstained resin-embedded sections by means of low-dose ratio-contrast imaging in STEM
    • BOHRMANN, B., HAIDER, M. & KELLENBERGER, E. (1993). Concentration evaluation of chromatin in unstained resin-embedded sections by means of low-dose ratio-contrast imaging in STEM. Ultramicroscopy 49, 235-251.
    • (1993) Ultramicroscopy , vol.49 , pp. 235-251
    • Bohrmann, B.1    Haider, M.2    Kellenberger, E.3
  • 6
    • 0026073819 scopus 로고
    • Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus
    • BOOY, F. P., NEWCOMB, W. W., TRUS, B. L., BROWN, J. C., BAKER, T. S. & STEVEN, A. C. (1991). Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus. Cell 64, 1007-1015.
    • (1991) Cell , vol.64 , pp. 1007-1015
    • Booy, F.P.1    Newcomb, W.W.2    Trus, B.L.3    Brown, J.C.4    Baker, T.S.5    Steven, A.C.6
  • 7
    • 0025269856 scopus 로고
    • Facilitated nuclear transport of histone H1 and other small nucleophilic proteins
    • BREEUWER, M. & GOLDFARB, D. S. (1990). Facilitated nuclear transport of histone H1 and other small nucleophilic proteins. Cell 60, 999-1008.
    • (1990) Cell , vol.60 , pp. 999-1008
    • Breeuwer, M.1    Goldfarb, D.S.2
  • 8
    • 0028569171 scopus 로고
    • Upsetting the balance of forces in DNA
    • CROTHERS, D. M. (1994). Upsetting the balance of forces in DNA. Science 266, 1819-1820.
    • (1994) Science , vol.266 , pp. 1819-1820
    • Crothers, D.M.1
  • 9
    • 0028327575 scopus 로고
    • Identification and characterization of drosophila relatives of the yeast transcriptional activator SNF2/SWI2
    • ELFRING, L. K., DEURING, R., MCCALLUM, C. M., PETERSON, C. L. & TAMKUN, J. W. (1994). Identification and characterization of Drosophila relatives of the yeast transcriptional activator SNF2/SWI2. Mol. Cell. Biol. 14, 2225-2234.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2225-2234
    • Elfring, L.K.1    Deuring, R.2    McCallum, C.M.3    Peterson, C.L.4    Tamkun, J.W.5
  • 10
    • 0026599021 scopus 로고
    • Chromatin as an essential part of the transcriptional mechanism
    • FELSENFELD, G. (1992). Chromatin as an essential part of the transcriptional mechanism. Nature 355, 219-224.
    • (1992) Nature , vol.355 , pp. 219-224
    • Felsenfeld, G.1
  • 11
    • 0030581149 scopus 로고    scopus 로고
    • Chromatin unfolds
    • FELSENFELD, G. (1996). Chromatin unfolds. Cell 86, 13-19.
    • (1996) Cell , vol.86 , pp. 13-19
    • Felsenfeld, G.1
  • 12
    • 0002429374 scopus 로고
    • Phase equilibria in solutions of rod-like particles
    • FLORY, P. J. (1956). Phase equilibria in solutions of rod-like particles. Proc. R. Soc. Lond. A. 234, 73-89.
    • (1956) Proc. R. Soc. Lond. A. , vol.234 , pp. 73-89
    • Flory, P.J.1
  • 13
    • 0018176160 scopus 로고
    • Description et interpretation des nucleoides structures observes dans des bacteroides de Rhizobium
    • GOURRET, J. P. (1978). Description et interpretation des nucleoides structures observes dans des bacteroides de Rhizobium. Biol. Cell. 32, 299-306.
    • (1978) Biol. Cell. , vol.32 , pp. 299-306
    • Gourret, J.P.1
  • 14
    • 0024284847 scopus 로고
    • UASs and enhancers: Common mechanism of transcriptional activation in yeast and mammals
    • GUARENTE, L. (1988). UASs and enhancers: common mechanism of transcriptional activation in yeast and mammals. Cell 52, 303-305.
    • (1988) Cell , vol.52 , pp. 303-305
    • Guarente, L.1
  • 15
    • 0026543897 scopus 로고
    • Conservation and evolution of transcriptional mechanisms in eukaryotes
    • GUARENTE, L. & MCDONOGH, O. B. (1992). Conservation and evolution of transcriptional mechanisms in eukaryotes. Trends Genet. 8, 27-31.
    • (1992) Trends Genet. , vol.8 , pp. 27-31
    • Guarente, L.1    Mcdonogh, O.B.2
  • 16
    • 0027068143 scopus 로고
    • Evidence that SNF2/SWI2 and SNF5 activate transcription in yeast by altering chromatin structure
    • HIRSCHHORN, J. N., BROWN, S. A., CLARK, C. D. & WINSTON, F. (1992). Evidence that SNF2/SWI2 and SNF5 activate transcription in yeast by altering chromatin structure. Genes Dev. 6, 2288-2298.
    • (1992) Genes Dev. , vol.6 , pp. 2288-2298
    • Hirschhorn, J.N.1    Brown, S.A.2    Clark, C.D.3    Winston, F.4
  • 17
    • 0028286473 scopus 로고
    • Evidence of novel secondary structure in DNA-bound protamine is revealed by Raman spectroscopy
    • HUD, N. V., MILANOVICH, F. P. & BALHORN, R. (1994). Evidence of novel secondary structure in DNA-bound protamine is revealed by Raman spectroscopy. Biochemistry 33, 7528-7535.
    • (1994) Biochemistry , vol.33 , pp. 7528-7535
    • Hud, N.V.1    Milanovich, F.P.2    Balhorn, R.3
  • 18
    • 0023117198 scopus 로고
    • The compactness of cellular plasms; in particular, chromatin compactness in relation to function
    • KELLENBERGER, E. (1987). The compactness of cellular plasms; in particular, chromatin compactness in relation to function. Trends Biochem. Sci. 12, 105-107.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 105-107
    • Kellenberger, E.1
  • 19
    • 0023958011 scopus 로고
    • About the organisation of condensed and decondensed non-eukaryotic DNA and the concept of vegetative DNA
    • KELLENBERGER, E. (1988). About the organisation of condensed and decondensed non-eukaryotic DNA and the concept of vegetative DNA. Biophys. Chem. 29, 51-62.
    • (1988) Biophys. Chem. , vol.29 , pp. 51-62
    • Kellenberger, E.1
  • 20
    • 0026685334 scopus 로고
    • Chromatins of low-protein content: Special features of their compaction and condensation
    • KELLENBERGER, E. & ARNOLD-SCHULZ-GAHMEN, B. (1992). Chromatins of low-protein content: special features of their compaction and condensation. FEMS Microbiol. Lett. 100, 361-370.
    • (1992) FEMS Microbiol. Lett. , vol.100 , pp. 361-370
    • Kellenberger, E.1    Arnold-Schulz-Gahmen, B.2
  • 21
    • 36549098429 scopus 로고
    • Theory of the interaction of light with large inhomogeneous molecular aggregates. II. Psi-type circular dichroism
    • KELLER, D. & BUSTAMANTE, C. (1986). Theory of the interaction of light with large inhomogeneous molecular aggregates. II. Psi-type circular dichroism. J. Chem. Phys. 84, 2972-2980.
    • (1986) J. Chem. Phys. , vol.84 , pp. 2972-2980
    • Keller, D.1    Bustamante, C.2
  • 22
    • 0029063189 scopus 로고
    • Interplay between chromatin structure and transcription
    • KORNBERG, R. D. & LORCH, Y. (1995). Interplay between chromatin structure and transcription. Curr. Opin. Cell. Biol. 7, 371-375.
    • (1995) Curr. Opin. Cell. Biol. , vol.7 , pp. 371-375
    • Kornberg, R.D.1    Lorch, Y.2
  • 23
    • 0028787059 scopus 로고
    • Crowding-induced organization of cytoskeletal elements. III. Spontaneous bundling and sorting of self-assembled filaments with different flexibilities
    • KULP, D. T. & HERZFELD, J. (1995). Crowding-induced organization of cytoskeletal elements. III. Spontaneous bundling and sorting of self-assembled filaments with different flexibilities. Biophys. Chem. 57, 93-102.
    • (1995) Biophys. Chem. , vol.57 , pp. 93-102
    • Kulp, D.T.1    Herzfeld, J.2
  • 24
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nucleosomal DNA
    • LEE, D. Y., HAYES, J. J., PRUSS, D. & WOLFFE, A. P. (1993). A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 72, 73-84.
    • (1993) Cell , vol.72 , pp. 73-84
    • Lee, D.Y.1    Hayes, J.J.2    Pruss, D.3    Wolffe, A.P.4
  • 25
    • 0027226299 scopus 로고
    • Supramolecular ordering of DNA in the cholesteric liquid crystalline phase: An ultrastructural study
    • LEFORESTIER, A. & LIVOLANT, F. (1993). Supramolecular ordering of DNA in the cholesteric liquid crystalline phase: an ultrastructural study. Biophys. J. 65, 56-72.
    • (1993) Biophys. J. , vol.65 , pp. 56-72
    • Leforestier, A.1    Livolant, F.2
  • 26
    • 0011064050 scopus 로고
    • Chromatin remodelling by nucleoplasmin
    • Dorchester, UK: Dorset Press
    • LENO, G. H., PHILPOTT, A. & LASKEY, R. A. (1993). Chromatin remodelling by nucleoplasmin. In: The Chromosome. pp. 135-147. Dorchester, UK: Dorset Press.
    • (1993) The Chromosome , pp. 135-147
    • Leno, G.H.1    Philpott, A.2    Laskey, R.A.3
  • 27
    • 0023341103 scopus 로고
    • Organization of double-stranded DNA in bacteriophages: A study by cryo-electron microscopy of vitrified samples
    • LEPAULT, J., DUBOCHET, J., BASCHONG, W. & KELLENBERGER, E. (1987). Organization of double-stranded DNA in bacteriophages: a study by cryo-electron microscopy of vitrified samples. EMBO J. 6, 1507-1512.
    • (1987) EMBO J. , vol.6 , pp. 1507-1512
    • Lepault, J.1    Dubochet, J.2    Baschong, W.3    Kellenberger, E.4
  • 28
    • 0026659070 scopus 로고
    • DNA-protein interactions. HMG has DNA wrapped up
    • LILLEY, D. M. (1992). DNA-protein interactions. HMG has DNA wrapped up. Nature 357, 282-283.
    • (1992) Nature , vol.357 , pp. 282-283
    • Lilley, D.M.1
  • 29
    • 0021219772 scopus 로고
    • Cholesteric organization of DNA in the stallion sperm head
    • LIVOLANT, F. (1984). Cholesteric organization of DNA in the stallion sperm head. Tissue & Cell. 16, 535-555.
    • (1984) Tissue & Cell. , vol.16 , pp. 535-555
    • Livolant, F.1
  • 30
    • 44949277387 scopus 로고
    • Ordered phases of DNA in vivo and in vitro
    • LIVOLANT, F. (1991a). Ordered phases of DNA in vivo and in vitro. Physica A 176, 117-137.
    • (1991) Physica A , vol.176 , pp. 117-137
    • Livolant, F.1
  • 31
    • 0026084935 scopus 로고
    • Supramolecular organization of double-stranded DNA molecules in the columnar hexagonal liquid crystalline phase. An electron microscopic analysis using freeze-fracture methods
    • LIVOLANT, F. (1991b). Supramolecular organization of double-stranded DNA molecules in the columnar hexagonal liquid crystalline phase. An electron microscopic analysis using freeze-fracture methods. J. Mol. Biol. 218, 165-181.
    • (1991) J. Mol. Biol. , vol.218 , pp. 165-181
    • Livolant, F.1
  • 32
    • 0024335507 scopus 로고
    • The highly concentrated liquid-crystalline phase of DNA is columnar hexagonal
    • LIVOLANT, F., LEVELUT, A. M., DOUCET, J. & BENOIT, J. P. (1989). The highly concentrated liquid-crystalline phase of DNA is columnar hexagonal. Nature 339, 724-726.
    • (1989) Nature , vol.339 , pp. 724-726
    • Livolant, F.1    Levelut, A.M.2    Doucet, J.3    Benoit, J.P.4
  • 33
    • 0024291652 scopus 로고
    • Circular dichroism microscopy of compact forms of DNA and chromatin in vivo and in vitro: Cholesteric liquid-crystalline phases of DNA and single dinoflagellate nuclei
    • LIVOLANT, F. & MAESTRE, M. F. (1988). Circular dichroism microscopy of compact forms of DNA and chromatin in vivo and in vitro: cholesteric liquid-crystalline phases of DNA and single dinoflagellate nuclei. Biochemistry 27, 3056-3068.
    • (1988) Biochemistry , vol.27 , pp. 3056-3068
    • Livolant, F.1    Maestre, M.F.2
  • 34
    • 0028920599 scopus 로고
    • Condensation of plasmids enhanced by Z-DNA conformation of d(CG)n inserts
    • MA, C., SUN, L. & BLOOMFIELD, V. A. (1995). Condensation of plasmids enhanced by Z-DNA conformation of d(CG)n inserts. Biochemistry 34, 3521-3528.
    • (1995) Biochemistry , vol.34 , pp. 3521-3528
    • Ma, C.1    Sun, L.2    Bloomfield, V.A.3
  • 35
    • 0027235856 scopus 로고
    • Crowding-induced organization of cytoskeletal elements: I. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles
    • MADDEN, T. L. & HERZFELD, J. (1993). Crowding-induced organization of cytoskeletal elements: I. Spontaneous demixing of cytosolic proteins and model filaments to form filament bundles. Biophys. J. 65, 1147-1154.
    • (1993) Biophys. J. , vol.65 , pp. 1147-1154
    • Madden, T.L.1    Herzfeld, J.2
  • 36
    • 0028415973 scopus 로고
    • Isotropic to anisotropic phase transition of extremely long DNA in an aqueous saline solution
    • MERCHANT, K. & RILL, R. L. (1994). Isotropic to anisotropic phase transition of extremely long DNA in an aqueous saline solution. Macromolecules 27, 2365-2370.
    • (1994) Macromolecules , vol.27 , pp. 2365-2370
    • Merchant, K.1    Rill, R.L.2
  • 37
    • 84985735713 scopus 로고
    • Excluded volume as a determinant of macromolecular structure and reactivity
    • MINTON, A. P. (1981). Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers 20, 2093-2120.
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 38
    • 0642365065 scopus 로고
    • Macromolecular crowding: A forward
    • MINTON, A. P. (1995). Macromolecular crowding: a forward. Biophys. Chem. 57, 1.
    • (1995) Biophys. Chem. , vol.57 , pp. 1
    • Minton, A.P.1
  • 39
    • 0027434083 scopus 로고
    • A human homologue of saccharomyces cerevisiae SNF2/SWI2 and drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor
    • MUCHARDT, C. & YANIV, M. (1993). A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. EMBO J. 12, 4279-4290.
    • (1993) EMBO J. , vol.12 , pp. 4279-4290
    • Muchardt, C.1    Yaniv, M.2
  • 40
    • 0028839750 scopus 로고
    • Condensation and cohesion of lambda DNA in cell extracts and other media: Implications for the structure and function of DNA in prokaryotes
    • MURPHY, L. D. & ZIMMERMAN, S. B. (1995). Condensation and cohesion of lambda DNA in cell extracts and other media: implications for the structure and function of DNA in prokaryotes. Biophys. Chem. 57, 71-92.
    • (1995) Biophys. Chem. , vol.57 , pp. 71-92
    • Murphy, L.D.1    Zimmerman, S.B.2
  • 41
    • 84971301149 scopus 로고
    • The effects of shape on the interaction of colloidal particles
    • ONSAGER, L. (1949). The effects of shape on the interaction of colloidal particles. Ann. N.Y. Acad. Sci. 51, 627-659.
    • (1949) Ann. N.Y. Acad. Sci. , vol.51 , pp. 627-659
    • Onsager, L.1
  • 42
    • 0028598182 scopus 로고
    • ATP-dependent nucleosome reconfiguration and transcriptional activation from preassembled chromatin templates
    • PAZIN, M. J., KAMAKAKA, R. T. & KADONAGA, J. T. (1994). ATP-dependent nucleosome reconfiguration and transcriptional activation from preassembled chromatin templates. Science 266, 2007-2011.
    • (1994) Science , vol.266 , pp. 2007-2011
    • Pazin, M.J.1    Kamakaka, R.T.2    Kadonaga, J.T.3
  • 43
    • 0029933808 scopus 로고    scopus 로고
    • DNA mesophases induced by spermidine: Structural properties and biological implications
    • PELTA, J., DURAND, D., DOUCET, J. & LIVOLANT, F. (1996). DNA Mesophases induced by spermidine: structural properties and biological implications. Biophys. J. 71, 48-63.
    • (1996) Biophys. J. , vol.71 , pp. 48-63
    • Pelta, J.1    Durand, D.2    Doucet, J.3    Livolant, F.4
  • 44
    • 0026630997 scopus 로고
    • Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts
    • PHILPOTT, A. & LENO, G. H. (1992). Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts. Cell 69, 759-767.
    • (1992) Cell , vol.69 , pp. 759-767
    • Philpott, A.1    Leno, G.H.2
  • 45
    • 0020212742 scopus 로고
    • Theory of DNA condensation: Collapse versus aggregation
    • POST, C. B. & ZIMM, B. H. (1982). Theory of DNA condensation: collapse versus aggregation. Biopolymers 21, 2123-2137.
    • (1982) Biopolymers , vol.21 , pp. 2123-2137
    • Post, C.B.1    Zimm, B.H.2
  • 46
    • 0026558204 scopus 로고
    • Direct measurement of the intermolecular forces between counterion-condensed DNA double helices. Evidence for long range attractive hydration forces
    • RAU, D. C. & PARSEGIAN, V. A. (1992). Direct measurement of the intermolecular forces between counterion-condensed DNA double helices. Evidence for long range attractive hydration forces. Biophys. J. 61, 246-259.
    • (1992) Biophys. J. , vol.61 , pp. 246-259
    • Rau, D.C.1    Parsegian, V.A.2
  • 47
    • 0026070060 scopus 로고
    • Secondary conformational polymorphism of nucleic acids as a possible functional link between cellular parameters and DNA packaging processes
    • REICH, Z., GHIRLANDO, R. & MINSKY, A. (1991). Secondary conformational polymorphism of nucleic acids as a possible functional link between cellular parameters and DNA packaging processes. Biochemistry 30, 7828-7836.
    • (1991) Biochemistry , vol.30 , pp. 7828-7836
    • Reich, Z.1    Ghirlando, R.2    Minsky, A.3
  • 48
    • 0028140753 scopus 로고
    • Protein-independent spontaneous packaging of long DNA molecules into ordered phases
    • REICH, Z., WACHTEL, E., DE-ROOS, R. & MINSKY, A. (1994a). Protein-independent spontaneous packaging of long DNA molecules into ordered phases. J. Am. Chem. Soc. 116, 7905-7906.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 7905-7906
    • Reich, Z.1    Wachtel, E.2    De-Roos, R.3    Minsky, A.4
  • 49
    • 0028088779 scopus 로고
    • Supercoiling-regulated liquid-crystalline packaging of topologically-constrained, nucleosome-free DNA molecules
    • REICH, Z., LEVIN, Z. S., GUTMAN, S. B., ARAD, T. & MINSKY, A. (1994b). Supercoiling-regulated liquid-crystalline packaging of topologically-constrained, nucleosome-free DNA molecules. Biochemistry 33, 14177-14184.
    • (1994) Biochemistry , vol.33 , pp. 14177-14184
    • Reich, Z.1    Levin, Z.S.2    Gutman, S.B.3    Arad, T.4    Minsky, A.5
  • 50
    • 0028363139 scopus 로고
    • Liquid-crystalline mesophases of plasmid DNA in bacteria
    • REICH, Z., WACHTEL, E. J. & MINSKY, A. (1994c). Liquid-crystalline mesophases of plasmid DNA in bacteria. Science 264, 1460-1463.
    • (1994) Science , vol.264 , pp. 1460-1463
    • Reich, Z.1    Wachtel, E.J.2    Minsky, A.3
  • 51
    • 0028926169 scopus 로고
    • In vivo quantitative characterization of intermolecular interactions
    • REICH, Z., WACHTEL, E. J. & MINSKY, A. (1995). In vivo quantitative characterization of intermolecular interactions. J. Biol. Chem. 270, 7045-7046.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7045-7046
    • Reich, Z.1    Wachtel, E.J.2    Minsky, A.3
  • 52
    • 0001389057 scopus 로고
    • Liquid crystalline phases in concentrated aqueous solutions of Na+ DNA
    • RILL, R. L. (1986). Liquid crystalline phases in concentrated aqueous solutions of Na+ DNA. Proc. Natl. Acad. Sci. U.S.A. 83, 342-346.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 342-346
    • Rill, R.L.1
  • 53
    • 0024744558 scopus 로고
    • Electron microscopy of liquid crystalline DNA: Direct evidence for cholesteric-like organization of DNA in dinoflagellate chromosomes
    • RILL, R. L., LIVOLANT, F., ALDRICH, H. C. & DAVIDSON, M. W. (1989). Electron microscopy of liquid crystalline DNA: direct evidence for cholesteric-like organization of DNA in dinoflagellate chromosomes. Chromosoma 98, 280-286.
    • (1989) Chromosoma , vol.98 , pp. 280-286
    • Rill, R.L.1    Livolant, F.2    Aldrich, H.C.3    Davidson, M.W.4
  • 54
    • 0025119580 scopus 로고
    • Nucleosome depletion alters the chromatin structure of saccharomyces cerevisiae centromeres
    • SAUNDERS, M. J., YEH, E., GRUNSTEIN, M. & BLOOM, K. (1990). Nucleosome depletion alters the chromatin structure of Saccharomyces cerevisiae centromeres. Mol. Cell. Biol. 10, 5721-5727.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5721-5727
    • Saunders, M.J.1    Yeh, E.2    Grunstein, M.3    Bloom, K.4
  • 55
    • 0027459196 scopus 로고
    • A nucleosome-dependent static loop potentiates estrogen-regulated transcription from the Xenopus vitellogenin B1 promoter in vitro
    • SCHILD, C., CLARET, F. X., WAHLI, W. & WOLFFE, A. P. (1993). A nucleosome-dependent static loop potentiates estrogen-regulated transcription from the Xenopus vitellogenin B1 promoter in vitro. EMBO J. 12, 423-433.
    • (1993) EMBO J. , vol.12 , pp. 423-433
    • Schild, C.1    Claret, F.X.2    Wahli, W.3    Wolffe, A.P.4
  • 56
    • 0028059323 scopus 로고
    • A liquid crystalline phase in spermidine-condensed DNA
    • SIKORAV, J. L., PELTA, J. & LIVOLANT, F. (1994). A liquid crystalline phase in spermidine-condensed DNA. Biophys. J. 67, 1387-1392.
    • (1994) Biophys. J. , vol.67 , pp. 1387-1392
    • Sikorav, J.L.1    Pelta, J.2    Livolant, F.3
  • 57
    • 0025067370 scopus 로고
    • Nucleosome positioning can affect the function of a cis-acting DNA element in vivo
    • SIMPSON, R. T. (1990). Nucleosome positioning can affect the function of a cis-acting DNA element in vivo. Nature 343, 387-389.
    • (1990) Nature , vol.343 , pp. 387-389
    • Simpson, R.T.1
  • 59
    • 0030297734 scopus 로고    scopus 로고
    • Remodeling chromatin structures for transcription: What happens to the histones?
    • STEGER, D. J. & WORKMAN, J. L. (1996). Remodeling chromatin structures for transcription: what happens to the histones? BioEssays 18, 875-884.
    • (1996) BioEssays , vol.18 , pp. 875-884
    • Steger, D.J.1    Workman, J.L.2
  • 61
    • 0028597967 scopus 로고
    • DNA bending by asymmetric phosphate neutralization
    • STRAUSS, J. K. & MAHER, L. (1994). DNA bending by asymmetric phosphate neutralization. Science 266, 1829-1834.
    • (1994) Science , vol.266 , pp. 1829-1834
    • Strauss, J.K.1    Maher, L.2
  • 62
    • 0023835499 scopus 로고
    • Multiple liquid crystal phases of DNA at high concentrations
    • STRZELECKA, T. E., DAVIDSON, M. W. & RILL, R. L. (1988). Multiple liquid crystal phases of DNA at high concentrations. Nature 331, 457-460.
    • (1988) Nature , vol.331 , pp. 457-460
    • Strzelecka, T.E.1    Davidson, M.W.2    Rill, R.L.3
  • 63
    • 0025148816 scopus 로고
    • Phase transitions of concentrated DNA solutions in low concentrations of 1:1 supporting electrolyte
    • STRZELECKA, T. E. & RILL, R. L. (1990) Phase transitions of concentrated DNA solutions in low concentrations of 1:1 supporting electrolyte. Biopolymers 30, 57-71.
    • (1990) Biopolymers , vol.30 , pp. 57-71
    • Strzelecka, T.E.1    Rill, R.L.2
  • 64
    • 0028125847 scopus 로고
    • A histone octamer can step around a transcribing polymerase without leaving the template
    • STUDITSKY, V. M., CLARK, D. J. & FELSENFELD, G. (1994). A histone octamer can step around a transcribing polymerase without leaving the template. Cell 76, 371-382.
    • (1994) Cell , vol.76 , pp. 371-382
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 65
    • 0025174655 scopus 로고
    • The structure and assembly of active chromatin
    • SVAREN, J. & CHALKLEY, R. (1990). The structure and assembly of active chromatin. Trends Genet. 6, 52-56.
    • (1990) Trends Genet. , vol.6 , pp. 52-56
    • Svaren, J.1    Chalkley, R.2
  • 66
    • 0026582986 scopus 로고
    • Order and disorder in 30 nm chromatin fibers
    • SUBIRANA, J. A. (1992). Order and disorder in 30 nm chromatin fibers. FEBS Lett. 302, 105-107.
    • (1992) FEBS Lett. , vol.302 , pp. 105-107
    • Subirana, J.A.1
  • 67
    • 0028226799 scopus 로고
    • DNA chaperones: A solution to a persistence problem?
    • TRAVERS, A. A., NER, S. S. & CHURCHILL, M. E. (1994). DNA chaperones: a solution to a persistence problem? Cell 77, 167-169.
    • (1994) Cell , vol.77 , pp. 167-169
    • Travers, A.A.1    Ner, S.S.2    Churchill, M.E.3
  • 68
    • 0027914496 scopus 로고
    • The omnipotent nucleosome
    • VAN HOLDE, K. (1993). The omnipotent nucleosome [news]. Nature 362, 111-112.
    • (1993) Nature , vol.362 , pp. 111-112
    • Van Holde, K.1
  • 69
    • 0028388715 scopus 로고
    • Architectural variations of inducible eukaryotic promoters: Preset and remodeling chromatin structures
    • WALLRATH, L. L., LU, Q., GRANOK, H. & ELGIN, S. C. (1994). Architectural variations of inducible eukaryotic promoters: preset and remodeling chromatin structures. BioEssays 16, 165-170.
    • (1994) BioEssays , vol.16 , pp. 165-170
    • Wallrath, L.L.1    Lu, Q.2    Granok, H.3    Elgin, S.C.4
  • 70
    • 0026641776 scopus 로고
    • Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection
    • WINSTON, F. & CARLSON, M. (1992). Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection. Trends Genet. 8, 387-391.
    • (1992) Trends Genet. , vol.8 , pp. 387-391
    • Winston, F.1    Carlson, M.2
  • 71
    • 0029093284 scopus 로고
    • Structure and partitioning of bacterial DNA: Determined by a balance of compaction and expansion forces?
    • WOLDRINGH, C. L., JENSEN, P. R. & WESTERHOFF, H. S. (1995). Structure and partitioning of bacterial DNA: determined by a balance of compaction and expansion forces? FEMS Microbiol. Lett. 131, 235-242.
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 235-242
    • Woldringh, C.L.1    Jensen, P.R.2    Westerhoff, H.S.3
  • 72
    • 0028236523 scopus 로고
    • Transcription: In tune with the histones
    • WOLFFE, A. P. (1994). Transcription: in tune with the histones. Cell 77, 13-16.
    • (1994) Cell , vol.77 , pp. 13-16
    • Wolffe, A.P.1
  • 73
    • 0027496418 scopus 로고
    • Macromolecular crowding effects on macromolecular interactions: Some implications for genome structure and function
    • ZIMMERMAN, S. B. (1993). Macromolecular crowding effects on macromolecular interactions: some implications for genome structure and function. Biochim. Biophys. Acta 1216, 175-185.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 175-185
    • Zimmerman, S.B.1
  • 74
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical and physiological consequences
    • ZIMMERMAN, S. B. & MINTON, A. P. (1993). Macromolecular crowding: biochemical, biophysical and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22, 27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 75
    • 0030605841 scopus 로고    scopus 로고
    • Macromolecular crowding and the mandatory condensation of DNA in bacteria
    • ZIMMERMAN, S. B. & MURPHY, L. D. (1996). Macromolecular crowding and the mandatory condensation of DNA in bacteria. FEBS Lett. 390, 245-248.
    • (1996) FEBS Lett. , vol.390 , pp. 245-248
    • Zimmerman, S.B.1    Murphy, L.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.