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Volumn 41, Issue , 2007, Pages 3-28

Structural organization of dynamic chromatin

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EUKARYOTA;

EID: 34249788441     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/1-4020-5466-1_1     Document Type: Article
Times cited : (3)

References (147)
  • 1
    • 0033118322 scopus 로고    scopus 로고
    • Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31
    • Aagaard L, Laible G, Selenko P, Schmid M, Dorn R, Schotta G, Kuhfittig S, Wolf A, Lebersorger A, Singh PB et al (1999) Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. Embo J 18: 1923-1938.
    • (1999) Embo J , vol.18 , pp. 1923-1938
    • Aagaard, L.1    Laible, G.2    Selenko, P.3    Schmid, M.4    Dorn, R.5    Schotta, G.6    Kuhfittig, S.7    Wolf, A.8    Lebersorger, A.9    Singh, P.B.10
  • 2
    • 0024826968 scopus 로고
    • Preferential, cooperative binding of DNA topoisomerase II to scaffold-associated regions
    • Adachi Y, Kas E, Laemmli UK (1989) Preferential, cooperative binding of DNA topoisomerase II to scaffold-associated regions. Embo J 8: 3997-4006.
    • (1989) Embo J , vol.8 , pp. 3997-4006
    • Adachi, Y.1    Kas, E.2    Laemmli, U.K.3
  • 3
    • 0025966711 scopus 로고
    • Chromosome assembly in vitro: Topoisomerase II is required for condensation
    • Adachi Y, Luke M, Laemmli UK (1991) Chromosome assembly in vitro: topoisomerase II is required for condensation. Cell 64: 137-148.
    • (1991) Cell , vol.64 , pp. 137-148
    • Adachi, Y.1    Luke, M.2    Laemmli, U.K.3
  • 4
    • 0022622499 scopus 로고
    • Assembly of chromatin fibers into metaphase chromosomes analyzed by transmission electron microscopy and scanning electron microscopy
    • Adolph KW, Kreisman LR, Kuehn RL (1986) Assembly of chromatin fibers into metaphase chromosomes analyzed by transmission electron microscopy and scanning electron microscopy. Biophys J 49: 221-231.
    • (1986) Biophys J , vol.49 , pp. 221-231
    • Adolph, K.W.1    Kreisman, L.R.2    Kuehn, R.L.3
  • 6
    • 0037017393 scopus 로고    scopus 로고
    • Condensin and cohesin display different arm conformations with characteristic hinge angles
    • Anderson DE, Losada A, Erickson HP, Hirano T (2002) Condensin and cohesin display different arm conformations with characteristic hinge angles. J Cell Biol 156: 419-424.
    • (2002) J Cell Biol , vol.156 , pp. 419-424
    • Anderson, D.E.1    Losada, A.2    Erickson, H.P.3    Hirano, T.4
  • 7
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3. 1 A resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents G, Burlingame RW, Wang BC, Love WE, Moudrianakis EN (1991) The nucleosomal core histone octamer at 3. 1 A resolution: a tripartite protein assembly and a left-handed superhelix. Proc Natl Acad Sci U S A 88: 10148-10152.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 10
    • 0026754072 scopus 로고
    • Cell-free system for assembly of transcriptionally repressed chromatin from Drosophila embryos
    • Becker PB, Wu C (1992) Cell-free system for assembly of transcriptionally repressed chromatin from Drosophila embryos. Mol Cell Biol 12: 2241-2249.
    • (1992) Mol Cell Biol , vol.12 , pp. 2241-2249
    • Becker, P.B.1    Wu, C.2
  • 11
    • 0033118880 scopus 로고    scopus 로고
    • Stopped at the border: Boundaries and insulators
    • Bell AC, Felsenfeld G (1999) Stopped at the border: boundaries and insulators. Curr Opin Genet Dev 9: 191-198.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 191-198
    • Bell, A.C.1    Felsenfeld, G.2
  • 12
    • 0028019457 scopus 로고
    • Visualization of G1 chromosomes: A folded, twisted, supercoiled chromonema model of interphase chromatid structure
    • Belmont AS, Bruce K (1994) Visualization of G1 chromosomes: a folded, twisted, supercoiled chromonema model of interphase chromatid structure. J Cell Biol 127: 287-302.
    • (1994) J Cell Biol , vol.127 , pp. 287-302
    • Belmont, A.S.1    Bruce, K.2
  • 15
    • 0040860278 scopus 로고
    • In situ localization of DNA topoisomerase II, a major polypeptide component of the Drosophila nuclear matrix fraction
    • Berrios M, Osheroff N, Fisher PA (1985) In situ localization of DNA topoisomerase II, a major polypeptide component of the Drosophila nuclear matrix fraction. Proc Natl Acad Sci U S A 82: 4142-4146.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 4142-4146
    • Berrios, M.1    Osheroff, N.2    Fisher, P.A.3
  • 16
    • 24344498241 scopus 로고    scopus 로고
    • HMG proteins: Dynamic players in gene regulation and differentiation
    • Bianchi ME, Agresti A (2005) HMG proteins: dynamic players in gene regulation and differentiation. Curr Opin Genet Dev 15: 496-506.
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 496-506
    • Bianchi, M.E.1    Agresti, A.2
  • 17
    • 4243824006 scopus 로고    scopus 로고
    • The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding
    • Bonaldi T, Langst G, Strohner R, Becker PB, Bianchi ME (2002) The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding. Embo J 21: 6865-6873.
    • (2002) Embo J , vol.21 , pp. 6865-6873
    • Bonaldi, T.1    Langst, G.2    Strohner, R.3    Becker, P.B.4    Bianchi, M.E.5
  • 18
    • 0344630574 scopus 로고
    • Chromatin structure is required to block transcription of the methylated herpes simplex virus thymidine kinase gene
    • Buschhausen G, Wittig B, Graessmann M, Graessmann A (1987) Chromatin structure is required to block transcription of the methylated herpes simplex virus thymidine kinase gene. Proc Natl Acad Sci U S A 84: 1177-1181.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 1177-1181
    • Buschhausen, G.1    Wittig, B.2    Graessmann, M.3    Graessmann, A.4
  • 19
    • 0035399963 scopus 로고    scopus 로고
    • Chromatin unfolding and activation by HMGN(*) chromosomal proteins
    • Bustin M (2001) Chromatin unfolding and activation by HMGN(*) chromosomal proteins. Trends Biochem Sci 26: 431-437.
    • (2001) Trends Biochem Sci , vol.26 , pp. 431-437
    • Bustin, M.1
  • 20
    • 9344239339 scopus 로고    scopus 로고
    • Long-range compaction and flexibility of interphase chromatin in budding yeast analyzed by high-resolution imaging techniques
    • Bystricky K, Heun P, Gehlen L, Langowski J, Gasser SM (2004) Long-range compaction and flexibility of interphase chromatin in budding yeast analyzed by high-resolution imaging techniques. Proc Natl Acad Sci U S A 101: 16495-16500.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16495-16500
    • Bystricky, K.1    Heun, P.2    Gehlen, L.3    Langowski, J.4    Gasser, S.M.5
  • 21
    • 0036668636 scopus 로고    scopus 로고
    • Competition between histone H1 and HMGN proteins for chromatin binding sites
    • Catez F, Brown DT, Misteli T, Bustin M (2002) Competition between histone H1 and HMGN proteins for chromatin binding sites. EMBO Rep 3: 760-766.
    • (2002) EMBO Rep , vol.3 , pp. 760-766
    • Catez, F.1    Brown, D.T.2    Misteli, T.3    Bustin, M.4
  • 23
    • 0036006293 scopus 로고    scopus 로고
    • Chromatin motion is constrained by association with nuclear compartments in human cells
    • Chubb JR, Boyle S, Perry P, Bickmore WA (2002) Chromatin motion is constrained by association with nuclear compartments in human cells. Curr Biol 12: 439-445.
    • (2002) Curr Biol , vol.12 , pp. 439-445
    • Chubb, J.R.1    Boyle, S.2    Perry, P.3    Bickmore, W.A.4
  • 24
    • 0027619276 scopus 로고
    • Role of chromatin structure in the regulation of transcription by RNA polymerase II
    • Croston GE, Kadonaga JT (1993) Role of chromatin structure in the regulation of transcription by RNA polymerase II. Curr Opin Cell Biol 5: 417-423.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 417-423
    • Croston, G.E.1    Kadonaga, J.T.2
  • 26
    • 0034142381 scopus 로고    scopus 로고
    • Core histone N-termini play an essential role in mitotic chromosome condensation
    • de la Barre AE, Gerson V, Gout S, Creaven M, Allis CD, Dimitrov S (2000) Core histone N-termini play an essential role in mitotic chromosome condensation. Embo J 19: 379-391.
    • (2000) Embo J , vol.19 , pp. 379-391
    • de la Barre, A.E.1    Gerson, V.2    Gout, S.3    Creaven, M.4    Allis, C.D.5    Dimitrov, S.6
  • 28
    • 0030610561 scopus 로고    scopus 로고
    • Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14
    • Ding HF, Bustin M, Hansen U (1997) Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14. Mol Cell Biol 17: 5843-5855.
    • (1997) Mol Cell Biol , vol.17 , pp. 5843-5855
    • Ding, H.F.1    Bustin, M.2    Hansen, U.3
  • 29
    • 0034081137 scopus 로고    scopus 로고
    • Mechanism for specificity by HMG-1 in enhanceosome assembly
    • Ellwood KB, Yen YM, Johnson RC, Carey M (2000) Mechanism for specificity by HMG-1 in enhanceosome assembly. Mol Cell Biol 20: 4359-4370.
    • (2000) Mol Cell Biol , vol.20 , pp. 4359-4370
    • Ellwood, K.B.1    Yen, Y.M.2    Johnson, R.C.3    Carey, M.4
  • 30
    • 0022548649 scopus 로고
    • Structure of the 30 nm chromatin fiber
    • Felsenfeld G, McGhee JD (1986) Structure of the 30 nm chromatin fiber. Cell 44: 375-377.
    • (1986) Cell , vol.44 , pp. 375-377
    • Felsenfeld, G.1    McGhee, J.D.2
  • 31
    • 0025318655 scopus 로고
    • Transcription factor requirements for in vitro formation of transcriptionally competent 5S rRNA gene chromatin
    • Felts SJ, Weil PA, Chalkley R (1990) Transcription factor requirements for in vitro formation of transcriptionally competent 5S rRNA gene chromatin. Mol Cell Biol 10: 2390-2401.
    • (1990) Mol Cell Biol , vol.10 , pp. 2390-2401
    • Felts, S.J.1    Weil, P.A.2    Chalkley, R.3
  • 32
    • 0022521416 scopus 로고
    • The nonchromatin substructures of the nucleus: The ribonucleoprotein (RNP)-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy
    • Fey EG, Krochmalnic G, Penman S (1986) The nonchromatin substructures of the nucleus: the ribonucleoprotein (RNP)-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy. J Cell Biol 102: 1654-1665.
    • (1986) J Cell Biol , vol.102 , pp. 1654-1665
    • Fey, E.G.1    Krochmalnic, G.2    Penman, S.3
  • 33
    • 0020064097 scopus 로고
    • Isolation and characterization of a proteinaceous subnuclear fraction composed of nuclear matrix, peripheral lamina, and nuclear pore complexes from embryos of Drosophila melanogaster
    • Fisher PA, Berrios M, Blobel G (1982) Isolation and characterization of a proteinaceous subnuclear fraction composed of nuclear matrix, peripheral lamina, and nuclear pore complexes from embryos of Drosophila melanogaster. J Cell Biol 92: 674-686.
    • (1982) J Cell Biol , vol.92 , pp. 674-686
    • Fisher, P.A.1    Berrios, M.2    Blobel, G.3
  • 34
    • 0000506532 scopus 로고
    • The organisation of chromatin loops: Characterization of a scaffold attachment site
    • Gasser SM, Laemmli UK (1986) The organisation of chromatin loops: characterization of a scaffold attachment site. Embo J 5: 511-518.
    • (1986) Embo J , vol.5 , pp. 511-518
    • Gasser, S.M.1    Laemmli, U.K.2
  • 36
    • 0026455115 scopus 로고
    • Chromatin structure of Schizosaccharomyces pombe. A nucleosome repeat length that is shorter than the chromatosomal DNA length
    • Godde JS, Widom J (1992) Chromatin structure of Schizosaccharomyces pombe. A nucleosome repeat length that is shorter than the chromatosomal DNA length. J Mol Biol 226: 1009-1025.
    • (1992) J Mol Biol , vol.226 , pp. 1009-1025
    • Godde, J.S.1    Widom, J.2
  • 37
    • 0032957520 scopus 로고    scopus 로고
    • Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody
    • Gonsior SM, Platz S, Buchmeier S, Scheer U, Jockusch BM, Hinssen H (1999) Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody. J Cell Sci 112(Pt 6): 797-809.
    • (1999) J Cell Sci , vol.112 , pp. 797-809
    • Gonsior, S.M.1    Platz, S.2    Buchmeier, S.3    Scheer, U.4    Jockusch, B.M.5    Hinssen, H.6
  • 38
    • 0015857760 scopus 로고
    • A new group of chromatin-associated proteins with a high content of acidic and basic amino acids
    • Goodwin GH, Sanders C, Johns EW (1973) A new group of chromatin-associated proteins with a high content of acidic and basic amino acids. Eur J Biochem 38: 14-19.
    • (1973) Eur J Biochem , vol.38 , pp. 14-19
    • Goodwin, G.H.1    Sanders, C.2    Johns, E.W.3
  • 40
    • 0017853206 scopus 로고
    • Histone phosphorylation and chromatin structure during mitosis in Chinese hamster cells
    • Gurley LR, D'Anna, JA, Barham SS, Deaven LL, Tobey RA (1978) Histone phosphorylation and chromatin structure during mitosis in Chinese hamster cells. Eur J Biochem 84: 1-15.
    • (1978) Eur J Biochem , vol.84 , pp. 1-15
    • Gurley, L.R.1    D'Anna, J.A.2    Barham, S.S.3    Deaven, L.L.4    Tobey, R.A.5
  • 41
    • 0032784327 scopus 로고    scopus 로고
    • The nuclear actinrelated protein of Saccharomyces cerevisiae, Act3p/Arp4, interacts with core histones
    • Harata M, Oma Y, Mizuno S, Jiang YW, Stillman DJ, Wintersberger U (1999) The nuclear actinrelated protein of Saccharomyces cerevisiae, Act3p/Arp4, interacts with core histones. Mol Biol Cell 10: 2595-2605.
    • (1999) Mol Biol Cell , vol.10 , pp. 2595-2605
    • Harata, M.1    Oma, Y.2    Mizuno, S.3    Jiang, Y.W.4    Stillman, D.J.5    Wintersberger, U.6
  • 42
    • 0031148959 scopus 로고    scopus 로고
    • In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins
    • Hayes JJ, Lee KM (1997) In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins. Methods 12: 2-9.
    • (1997) Methods , vol.12 , pp. 2-9
    • Hayes, J.J.1    Lee, K.M.2
  • 43
    • 0028384699 scopus 로고
    • The chromosome periphery during mitosis
    • Hernandez-Verdun D, Gautier T (1994) The chromosome periphery during mitosis. Bioessays 16: 179-185.
    • (1994) Bioessays , vol.16 , pp. 179-185
    • Hernandez-Verdun, D.1    Gautier, T.2
  • 44
    • 0030830639 scopus 로고    scopus 로고
    • Condensins, chromosome condensation protein complexes containing XCAP-C, XCAP-E and a Xenopus homolog of the Drosophila Barren protein
    • Hirano T, Kobayashi R, Hirano M (1997) Condensins, chromosome condensation protein complexes containing XCAP-C, XCAP-E and a Xenopus homolog of the Drosophila Barren protein. Cell 89: 511-521.
    • (1997) Cell , vol.89 , pp. 511-521
    • Hirano, T.1    Kobayashi, R.2    Hirano, M.3
  • 45
    • 0036947729 scopus 로고    scopus 로고
    • Chromatin reconstitution: Development of a salt-dialysis method monitored by nano-technology
    • Hizume K, Yoshimura SH, Maruyama H, Kim J, Wada H, Takeyasu K (2002) Chromatin reconstitution: development of a salt-dialysis method monitored by nano-technology. Arch Histol Cytol 65: 405-413.
    • (2002) Arch Histol Cytol , vol.65 , pp. 405-413
    • Hizume, K.1    Yoshimura, S.H.2    Maruyama, H.3    Kim, J.4    Wada, H.5    Takeyasu, K.6
  • 46
    • 15944408542 scopus 로고    scopus 로고
    • Atomic force microscopy demonstrates a critical role of DNA superhelicity in nucleosome dynamics
    • Hizume K, Yoshimura SH, Takeyasu K (2004) Atomic force microscopy demonstrates a critical role of DNA superhelicity in nucleosome dynamics. Cell Biochem Biophys 40: 249-262.
    • (2004) Cell Biochem Biophys , vol.40 , pp. 249-262
    • Hizume, K.1    Yoshimura, S.H.2    Takeyasu, K.3
  • 47
    • 25444436189 scopus 로고    scopus 로고
    • Linker histone H1 per se can induce three-dimensional folding of chromatin fiber
    • Hizume K, Yoshimura SH, Takeyasu K (2005) Linker histone H1 per se can induce three-dimensional folding of chromatin fiber. Biochemistry 44: 12978-12989.
    • (2005) Biochemistry , vol.44 , pp. 12978-12989
    • Hizume, K.1    Yoshimura, S.H.2    Takeyasu, K.3
  • 48
    • 32644449429 scopus 로고    scopus 로고
    • Nuclear actin: To polymerize or not to polymerize
    • Hofmann WA, de Lanerolle P (2006) Nuclear actin: to polymerize or not to polymerize. J Cell Biol 172: 495-496.
    • (2006) J Cell Biol , vol.172 , pp. 495-496
    • Hofmann, W.A.1    de Lanerolle, P.2
  • 49
    • 0037072601 scopus 로고    scopus 로고
    • Molecular biology: Chromatin higher order folding-Wrapping up transcription
    • Horn PJ, Peterson CL (2002) Molecular biology: Chromatin higher order folding-Wrapping up transcription. Science 297: 1824-1827.
    • (2002) Science , vol.297 , pp. 1824-1827
    • Horn, P.J.1    Peterson, C.L.2
  • 50
    • 0035709188 scopus 로고    scopus 로고
    • Three-dimensional structure of G-banded human metaphase chromosomes observed by atomic force microscopy
    • Hoshi O, Ushiki T (2001) Three-dimensional structure of G-banded human metaphase chromosomes observed by atomic force microscopy. Arch Histol Cytol 64: 475-482.
    • (2001) Arch Histol Cytol , vol.64 , pp. 475-482
    • Hoshi, O.1    Ushiki, T.2
  • 51
    • 11844299709 scopus 로고    scopus 로고
    • A method for the in vitro reconstitution of a defined "30 nm" chromatin fibre containing stoichiometric amounts of the linker histone
    • Huynh VA, Robinson PJ, Rhodes D (2005) A method for the in vitro reconstitution of a defined "30 nm" chromatin fibre containing stoichiometric amounts of the linker histone. J Mol Biol 345: 957-968.
    • (2005) J Mol Biol , vol.345 , pp. 957-968
    • Huynh, V.A.1    Robinson, P.J.2    Rhodes, D.3
  • 52
    • 0031444148 scopus 로고    scopus 로고
    • ACF, an ISWI-containing and ATPutilizing chromatin assembly and remodeling factor
    • Ito T, Bulger M, Pazin MJ, Kobayashi R, Kadonaga JT (1997) ACF, an ISWI-containing and ATPutilizing chromatin assembly and remodeling factor. Cell 90: 145-155.
    • (1997) Cell , vol.90 , pp. 145-155
    • Ito, T.1    Bulger, M.2    Pazin, M.J.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 53
    • 0029618309 scopus 로고
    • The structural basis of nuclear function
    • Jackson DA, Cook PR (1995) The structural basis of nuclear function. Int Rev Cytol 162A: 125-149.
    • (1995) Int Rev Cytol , vol.162 A , pp. 125-149
    • Jackson, D.A.1    Cook, P.R.2
  • 54
    • 0022818549 scopus 로고
    • Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene
    • James TC, Elgin SC (1986) Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene. Mol Cell Biol 6: 3862-3872.
    • (1986) Mol Cell Biol , vol.6 , pp. 3862-3872
    • James, T.C.1    Elgin, S.C.2
  • 55
    • 0024114856 scopus 로고
    • Nuclear scaffold attachment sites in the human globin gene complexes
    • Jarman AP, Higgs DR (1988) Nuclear scaffold attachment sites in the human globin gene complexes. Embo J 7: 3337-3344.
    • (1988) Embo J , vol.7 , pp. 3337-3344
    • Jarman, A.P.1    Higgs, D.R.2
  • 56
    • 0035204816 scopus 로고    scopus 로고
    • DNA methylation-dependent chromatin fiber compaction in vivo and in vitro: Requirement for linker histone
    • Karymov MA, Tomschik M, Leuba SH, Caiafa P, Zlatanova J (2001) DNA methylation-dependent chromatin fiber compaction in vivo and in vitro: requirement for linker histone. Faseb J 15: 2631-2641.
    • (2001) Faseb J , vol.15 , pp. 2631-2641
    • Karymov, M.A.1    Tomschik, M.2    Leuba, S.H.3    Caiafa, P.4    Zlatanova, J.5
  • 57
    • 0033786116 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is correlated with changes in the maintenance of sister chromatid cohesion during meiosis in maize, rather than the condensation of the chromatin
    • Kaszas E, Cande WZ (2000) Phosphorylation of histone H3 is correlated with changes in the maintenance of sister chromatid cohesion during meiosis in maize, rather than the condensation of the chromatin. J Cell Sci 113(Pt 18): 3217-3226.
    • (2000) J Cell Sci , vol.113 , pp. 3217-3226
    • Kaszas, E.1    Cande, W.Z.2
  • 58
    • 0001074488 scopus 로고
    • Determination of the number of superhelical turns in simian virus 40 DNA by gel electrophoresis
    • Keller W (1975) Determination of the number of superhelical turns in simian virus 40 DNA by gel electrophoresis. Proc Natl Acad Sci U S A 72: 4876-4880.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 4876-4880
    • Keller, W.1
  • 59
    • 0033826256 scopus 로고    scopus 로고
    • Type B histone acetyltransferase Hat1p participates in telomeric silencing
    • Kelly TJ, Qin S, Gottschling DE, Parthun MR (2000) Type B histone acetyltransferase Hat1p participates in telomeric silencing. Mol Cell Biol 20: 7051-7058.
    • (2000) Mol Cell Biol , vol.20 , pp. 7051-7058
    • Kelly, T.J.1    Qin, S.2    Gottschling, D.E.3    Parthun, M.R.4
  • 60
    • 32944469082 scopus 로고    scopus 로고
    • A decade of histone acetylation: Marking eukaryotic chromosomes with specific codes
    • Kimura A, Matsubara K, Horikoshi M (2005) A decade of histone acetylation: marking eukaryotic chromosomes with specific codes. J Biochem (Tokyo) 138: 647-662.
    • (2005) J Biochem (Tokyo) , vol.138 , pp. 647-662
    • Kimura, A.1    Matsubara, K.2    Horikoshi, M.3
  • 61
    • 0030874421 scopus 로고    scopus 로고
    • ATP-dependent positive supercoiling of DNA by 13S condensin: A biochemical implication for chromosome condensation
    • Kimura K, Hirano T (1997) ATP-dependent positive supercoiling of DNA by 13S condensin: a biochemical implication for chromosome condensation. Cell 90: 625-634.
    • (1997) Cell , vol.90 , pp. 625-634
    • Kimura, K.1    Hirano, T.2
  • 62
    • 33646735917 scopus 로고    scopus 로고
    • Comparative structural biology of the genome: Nano-scale imaging of single nucleus from different kingdoms reveals the common physicochemical property of chromatin with a 40 nm structural unit
    • Kobori T, Kodama M, Hizume K, Yoshimura SH, Ohtani T, Takeyasu K (2006) Comparative structural biology of the genome: nano-scale imaging of single nucleus from different kingdoms reveals the common physicochemical property of chromatin with a 40 nm structural unit. J Electron Microsc (Tokyo) 55: 31-40.
    • (2006) J Electron Microsc (Tokyo) , vol.55 , pp. 31-40
    • Kobori, T.1    Kodama, M.2    Hizume, K.3    Yoshimura, S.H.4    Ohtani, T.5    Takeyasu, K.6
  • 63
    • 0016221697 scopus 로고
    • Chromatin structure: A repeating unit of histones and DNA
    • Kornberg RD (1974) Chromatin structure: a repeating unit of histones and DNA. Science 184: 868-871.
    • (1974) Science , vol.184 , pp. 868-871
    • Kornberg, R.D.1
  • 64
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T (2001) Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410: 116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 65
    • 0014443113 scopus 로고
    • Intranuclear fibrillar bodies in actinomycin D-treated oocytes
    • Lane NJ (1969) Intranuclear fibrillar bodies in actinomycin D-treated oocytes. J Cell Biol 40: 286-291.
    • (1969) J Cell Biol , vol.40 , pp. 286-291
    • Lane, N.J.1
  • 67
    • 0031835671 scopus 로고    scopus 로고
    • Linker histone tails and N-tails of histone H3 are redundant: Scanning force microscopy studies of reconstituted fibers
    • Leuba SH, Bustamante C, van Holde K, Zlatanova J (1998) Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers. Biophys J 74: 2830-2839.
    • (1998) Biophys J , vol.74 , pp. 2830-2839
    • Leuba, S.H.1    Bustamante, C.2    van Holde, K.3    Zlatanova, J.4
  • 68
    • 0032498902 scopus 로고    scopus 로고
    • Interphase cell cycle dynamics of a late-replicating, heterochromatic homogeneously staining region: Precise choreography of condensation/decondensation and nuclear positioning
    • Li G, Sudlow G, Belmont AS (1998) Interphase cell cycle dynamics of a late-replicating, heterochromatic homogeneously staining region: precise choreography of condensation/decondensation and nuclear positioning. J Cell Biol 140: 975-989.
    • (1998) J Cell Biol , vol.140 , pp. 975-989
    • Li, G.1    Sudlow, G.2    Belmont, A.S.3
  • 69
    • 0034634545 scopus 로고    scopus 로고
    • Influence of HMG-1 and adenovirus oncoprotein E1A on early stages of transcriptional preinitiation complex assembly
    • Lu W, Peterson R, Dasgupta A, Scovell WM (2000) Influence of HMG-1 and adenovirus oncoprotein E1A on early stages of transcriptional preinitiation complex assembly. J Biol Chem 275: 35006-35012.
    • (2000) J Biol Chem , vol.275 , pp. 35006-35012
    • Lu, W.1    Peterson, R.2    Dasgupta, A.3    Scovell, W.M.4
  • 70
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2. 8 A resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ (1997) Crystal structure of the nucleosome core particle at 2. 8 A resolution. Nature 389: 251-260.
    • (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
  • 71
    • 18744373022 scopus 로고    scopus 로고
    • Strategies for the reconstitution of chromatin
    • Lusser A, Kadonaga JT (2004) Strategies for the reconstitution of chromatin. Nat Methods 1: 19-26.
    • (2004) Nat Methods , vol.1 , pp. 19-26
    • Lusser, A.1    Kadonaga, J.T.2
  • 72
    • 0037387829 scopus 로고    scopus 로고
    • A two-step scaffolding model for mitotic chromosome assembly
    • Maeshima K, Laemmli UK (2003) A two-step scaffolding model for mitotic chromosome assembly. Dev Cell 4: 467-480.
    • (2003) Dev Cell , vol.4 , pp. 467-480
    • Maeshima, K.1    Laemmli, U.K.2
  • 73
    • 0037071535 scopus 로고    scopus 로고
    • Spatial organization of active and inactive genes and noncoding DNA within chromosome territories
    • Mahy NL, Perry PE, Gilchrist S, Baldock RA, Bickmore WA (2002) Spatial organization of active and inactive genes and noncoding DNA within chromosome territories. J Cell Biol 157: 579-589.
    • (2002) J Cell Biol , vol.157 , pp. 579-589
    • Mahy, N.L.1    Perry, P.E.2    Gilchrist, S.3    Baldock, R.A.4    Bickmore, W.A.5
  • 74
    • 0036221883 scopus 로고    scopus 로고
    • Salt-induced conformation and interaction changes of nucleosome core particles
    • Mangenot S, Leforestier A, Vachette P, Durand D, Livolant F (2002) Salt-induced conformation and interaction changes of nucleosome core particles. Biophys J 82: 345-356.
    • (2002) Biophys J , vol.82 , pp. 345-356
    • Mangenot, S.1    Leforestier, A.2    Vachette, P.3    Durand, D.4    Livolant, F.5
  • 75
    • 0018581746 scopus 로고
    • Metaphase chromosome structure: Evidence for a radial loop model
    • Marsden MP, Laemmli UK (1979) Metaphase chromosome structure: evidence for a radial loop model. Cell 17: 849-858.
    • (1979) Cell , vol.17 , pp. 849-858
    • Marsden, M.P.1    Laemmli, U.K.2
  • 78
    • 0032555919 scopus 로고    scopus 로고
    • The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: Long, antiparallel coiled coils, folded at a flexible hinge
    • Melby TE, Ciampaglio CN, Briscoe G, Erickson HP (1998) The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge. J Cell Biol 142: 1595-1604.
    • (1998) J Cell Biol , vol.142 , pp. 1595-1604
    • Melby, T.E.1    Ciampaglio, C.N.2    Briscoe, G.3    Erickson, H.P.4
  • 79
    • 0020467073 scopus 로고
    • The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors and cultured cells
    • Moll R, Franke WW, Schiller DL, Geiger B, Krepler R (1982) The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells. Cell 31: 11-24.
    • (1982) Cell , vol.31 , pp. 11-24
    • Moll, R.1    Franke, W.W.2    Schiller, D.L.3    Geiger, B.4    Krepler, R.5
  • 80
    • 0031915974 scopus 로고    scopus 로고
    • A nuclear matrix/scaffold attachment region colocalizes with the gypsy retrotransposon insulator sequence
    • Nabirochkin S, Ossokina M, Heidmann T (1998) A nuclear matrix/scaffold attachment region colocalizes with the gypsy retrotransposon insulator sequence. J Biol Chem 273: 2473-2479.
    • (1998) J Biol Chem , vol.273 , pp. 2473-2479
    • Nabirochkin, S.1    Ossokina, M.2    Heidmann, T.3
  • 82
    • 0031899366 scopus 로고    scopus 로고
    • Human matrix attachment regions insulate transgene expression from chromosomal position effects in Drosophila melanogaster
    • Namciu SJ, Blochlinger KB, Fournier RE (1998) Human matrix attachment regions insulate transgene expression from chromosomal position effects in Drosophila melanogaster. Mol Cell Biol 18: 2382-2391.
    • (1998) Mol Cell Biol , vol.18 , pp. 2382-2391
    • Namciu, S.J.1    Blochlinger, K.B.2    Fournier, R.E.3
  • 83
    • 0037154963 scopus 로고    scopus 로고
    • Cooperation between complexes that regulate chromatin structure and transcription
    • Narlikar GJ, Fan HY, Kingston RE (2002) Cooperation between complexes that regulate chromatin structure and transcription. Cell 108: 475-487.
    • (2002) Cell , vol.108 , pp. 475-487
    • Narlikar, G.J.1    Fan, H.Y.2    Kingston, R.E.3
  • 84
    • 0032408680 scopus 로고    scopus 로고
    • Molecular structure of human topoisomerase II alpha revealed by atomic force microscopy
    • Nettikadan SR, Furbee CS, Muller MT, Takeyasu K (1998) Molecular structure of human topoisomerase II alpha revealed by atomic force microscopy. J Electron Microsc (Tokyo) 47: 671-674.
    • (1998) J Electron Microsc (Tokyo) , vol.47 , pp. 671-674
    • Nettikadan, S.R.1    Furbee, C.S.2    Muller, M.T.3    Takeyasu, K.4
  • 85
    • 0035110880 scopus 로고    scopus 로고
    • Experimental observations of a nuclear matrix
    • Nickerson J (2001) Experimental observations of a nuclear matrix. J Cell Sci 114: 463-474.
    • (2001) J Cell Sci , vol.114 , pp. 463-474
    • Nickerson, J.1
  • 86
    • 1642326716 scopus 로고    scopus 로고
    • Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation
    • Nowak SJ, Corces VG (2004) Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet 20: 214-220.
    • (2004) Trends Genet , vol.20 , pp. 214-220
    • Nowak, S.J.1    Corces, V.G.2
  • 87
    • 0026512523 scopus 로고
    • Nucleosome arrays inhibit both initiation and elongation of transcripts by bacteriophage T7 RNA polymerase
    • O'Neill TE, Roberge M, Bradbury EM (1992) Nucleosome arrays inhibit both initiation and elongation of transcripts by bacteriophage T7 RNA polymerase. J Mol Biol 223: 67-78.
    • (1992) J Mol Biol , vol.223 , pp. 67-78
    • O'Neill, T.E.1    Roberge, M.2    Bradbury, E.M.3
  • 88
    • 33646487161 scopus 로고    scopus 로고
    • Vertebrate Arp6, a novel nuclear actin-related protein, interacts with heterochromatin protein 1
    • Ohfuchi E, Kato M, Sasaki M, Sugimoto K, Oma Y, Harata M (2006) Vertebrate Arp6, a novel nuclear actin-related protein, interacts with heterochromatin protein 1. Eur J Cell Biol 85: 411-421.
    • (2006) Eur J Cell Biol , vol.85 , pp. 411-421
    • Ohfuchi, E.1    Kato, M.2    Sasaki, M.3    Sugimoto, K.4    Oma, Y.5    Harata, M.6
  • 90
    • 23444445850 scopus 로고
    • Chromosome condensation in Xenopus mitotic extracts without histone H1
    • Ohsumi K, Katagiri C, Kishimoto T (1993) Chromosome condensation in Xenopus mitotic extracts without histone H1. Science 262: 2033-2035.
    • (1993) Science , vol.262 , pp. 2033-2035
    • Ohsumi, K.1    Katagiri, C.2    Kishimoto, T.3
  • 91
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin remodeling
    • Olave IA, Reck-Peterson SL, Crabtree GR (2002) Nuclear actin and actin-related proteins in chromatin remodeling. Annu Rev Biochem 71: 755-781.
    • (2002) Annu Rev Biochem , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 92
    • 0015348336 scopus 로고
    • Physical studies of isolated eucaryotic nuclei
    • Olins DE, Olins AL (1972) Physical studies of isolated eucaryotic nuclei. J Cell Biol 53: 715-736.
    • (1972) J Cell Biol , vol.53 , pp. 715-736
    • Olins, D.E.1    Olins, A.L.2
  • 93
    • 0141987890 scopus 로고    scopus 로고
    • Differential contributions of condensin I and condensin II to mitotic chromosome architecture in vertebrate cells
    • Ono T, Losada A, Hirano M, Myers MP, Neuwald AF, Hirano T (2003) Differential contributions of condensin I and condensin II to mitotic chromosome architecture in vertebrate cells. Cell 115: 109-121.
    • (2003) Cell , vol.115 , pp. 109-121
    • Ono, T.1    Losada, A.2    Hirano, M.3    Myers, M.P.4    Neuwald, A.F.5    Hirano, T.6
  • 94
    • 0035109120 scopus 로고    scopus 로고
    • The effects of DNA supercoiling on the expression of operons of the ilv regulon of Escherichia coli suggest a physiological rationale for divergently transcribed operons
    • Opel ML, Arfin SM, Hatfield GW (2001) The effects of DNA supercoiling on the expression of operons of the ilv regulon of Escherichia coli suggest a physiological rationale for divergently transcribed operons. Mol Microbiol 39: 1109-1115.
    • (2001) Mol Microbiol , vol.39 , pp. 1109-1115
    • Opel, M.L.1    Arfin, S.M.2    Hatfield, G.W.3
  • 95
    • 0028966257 scopus 로고
    • Experimental analysis of chromatin function in transcription control
    • Owen-Hughes T, Workman JL (1994) Experimental analysis of chromatin function in transcription control. Crit Rev Eukaryot Gene Expr 4: 403-441.
    • (1994) Crit Rev Eukaryot Gene Expr , vol.4 , pp. 403-441
    • Owen-Hughes, T.1    Workman, J.L.2
  • 96
    • 0017652886 scopus 로고
    • The structure of histone-depleted metaphase chromosomes
    • Paulson JR, Laemmli UK (1977) The structure of histone-depleted metaphase chromosomes. Cell 12: 817-828.
    • (1977) Cell , vol.12 , pp. 817-828
    • Paulson, J.R.1    Laemmli, U.K.2
  • 97
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson CL, Laniel MA (2004) Histones and histone modifications. Curr Biol 14, R546-551.
    • (2004) Curr Biol , vol.14 , pp. 546-551
    • Peterson, C.L.1    Laniel, M.A.2
  • 98
    • 0025091721 scopus 로고
    • In vitro evidence that transcription-induced stress causes nucleosome dissolution and regeneration
    • Pfaffle P, Gerlach V, Bunzel L, Jackson V (1990) In vitro evidence that transcription-induced stress causes nucleosome dissolution and regeneration. J Biol Chem 265: 16830-16840.
    • (1990) J Biol Chem , vol.265 , pp. 16830-16840
    • Pfaffle, P.1    Gerlach, V.2    Bunzel, L.3    Jackson, V.4
  • 99
    • 0030754347 scopus 로고    scopus 로고
    • Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family
    • Poch O, Winsor B (1997) Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family. Yeast 13: 1053-1058.
    • (1997) Yeast , vol.13 , pp. 1053-1058
    • Poch, O.1    Winsor, B.2
  • 100
    • 0037324194 scopus 로고    scopus 로고
    • Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase
    • Preuss U, Landsberg G, Scheidtmann KH (2003) Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase. Nucleic Acids Res 31: 878-885.
    • (2003) Nucleic Acids Res , vol.31 , pp. 878-885
    • Preuss, U.1    Landsberg, G.2    Scheidtmann, K.H.3
  • 102
    • 0018416116 scopus 로고
    • Nucleosome packing in interphase chromatin
    • Rattner JB, Hamkalo BA (1979) Nucleosome packing in interphase chromatin. J Cell Biol 81: 453-457.
    • (1979) J Cell Biol , vol.81 , pp. 453-457
    • Rattner, J.B.1    Hamkalo, B.A.2
  • 103
    • 0022386283 scopus 로고
    • Radial loops and helical coils coexist in metaphase chromosomes
    • Rattner JB, Lin CC (1985) Radial loops and helical coils coexist in metaphase chromosomes. Cell 42: 291-296.
    • (1985) Cell , vol.42 , pp. 291-296
    • Rattner, J.B.1    Lin, C.C.2
  • 106
    • 0019488496 scopus 로고
    • Sequence-dependent helical periodicity of DNA
    • Rhodes D, Klug A (1981) Sequence-dependent helical periodicity of DNA. Nature 292: 378-380.
    • (1981) Nature , vol.292 , pp. 378-380
    • Rhodes, D.1    Klug, A.2
  • 107
    • 0030006048 scopus 로고    scopus 로고
    • The rDNA transcription machinery is assembled during mitosis in active NORs and absent in inactive NORs
    • Roussel P, Andre C, Comai L, Hernandez-Verdun D (1996) The rDNA transcription machinery is assembled during mitosis in active NORs and absent in inactive NORs. J Cell Biol 133: 235-246.
    • (1996) J Cell Biol , vol.133 , pp. 235-246
    • Roussel, P.1    Andre, C.2    Comai, L.3    Hernandez-Verdun, D.4
  • 108
    • 0023001414 scopus 로고
    • Sequence periodicities in chicken nucleosome core DNA
    • Satchwell SC, Drew HR, Travers AA (1986) Sequence periodicities in chicken nucleosome core DNA. J Mol Biol 191: 659-675.
    • (1986) J Mol Biol , vol.191 , pp. 659-675
    • Satchwell, S.C.1    Drew, H.R.2    Travers, A.A.3
  • 109
    • 0033004573 scopus 로고    scopus 로고
    • Atomic force microscopy sees nucleosome positioning and histone H1-induced compaction in reconstituted chromatin
    • Sato MH, Ura K, Hohmura KI, Tokumasu F, Yoshimura SH, Hanaoka F, Takeyasu K (1999) Atomic force microscopy sees nucleosome positioning and histone H1-induced compaction in reconstituted chromatin. FEBS Lett 452: 267-271.
    • (1999) FEBS Lett , vol.452 , pp. 267-271
    • Sato, M.H.1    Ura, K.2    Hohmura, K.I.3    Tokumasu, F.4    Yoshimura, S.H.5    Hanaoka, F.6    Takeyasu, K.7
  • 112
    • 0029013311 scopus 로고
    • Linker histones are not essential and affect chromatin condensation in vivo
    • Shen X, Yu L, Weir JW, Gorovsky MA (1995) Linker histones are not essential and affect chromatin condensation in vivo. Cell 82: 47-56.
    • (1995) Cell , vol.82 , pp. 47-56
    • Shen, X.1    Yu, L.2    Weir, J.W.3    Gorovsky, M.A.4
  • 113
    • 0018435056 scopus 로고
    • A new procedure for purifying histone pairs H2A + H2B and H3 + H4 from chromatin using hydroxylapatite
    • Simon RH, Felsenfeld G (1979) A new procedure for purifying histone pairs H2A + H2B and H3 + H4 from chromatin using hydroxylapatite. Nucleic Acids Res 6: 689-696.
    • (1979) Nucleic Acids Res , vol.6 , pp. 689-696
    • Simon, R.H.1    Felsenfeld, G.2
  • 114
    • 0018266771 scopus 로고
    • Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones
    • Simpson RT (1978) Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histones. Biochemistry 17: 5524-5531.
    • (1978) Biochemistry , vol.17 , pp. 5524-5531
    • Simpson, R.T.1
  • 115
    • 0020695571 scopus 로고
    • Structural features of a phased nucleosome core particle
    • Simpson RT, Stafford DW (1983) Structural features of a phased nucleosome core particle. Proc Natl Acad Sci U S A 80: 51-55.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 51-55
    • Simpson, R.T.1    Stafford, D.W.2
  • 116
    • 0022234831 scopus 로고
    • Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: A model system for study of higher order structure
    • Simpson RT, Thoma F, Brubaker JM (1985) Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: a model system for study of higher order structure. Cell 42: 799-808.
    • (1985) Cell , vol.42 , pp. 799-808
    • Simpson, R.T.1    Thoma, F.2    Brubaker, J.M.3
  • 117
    • 0038691676 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of 30 nm chromatin fiber from partially relaxed plant chromosomes
    • Sugiyama S, Yoshino T, Kanahara H, Kobori T, Ohtani T (2003) Atomic force microscopic imaging of 30 nm chromatin fiber from partially relaxed plant chromosomes. Scanning 25: 132-136.
    • (2003) Scanning , vol.25 , pp. 132-136
    • Sugiyama, S.1    Yoshino, T.2    Kanahara, H.3    Kobori, T.4    Ohtani, T.5
  • 118
    • 0344062905 scopus 로고    scopus 로고
    • Effects of acetic acid treatment on plant chromosome structures analyzed by atomic force microscopy
    • Sugiyama S, Yoshino T, Kanahara H, Shichiri M, Fukushi D, Ohtani T (2004) Effects of acetic acid treatment on plant chromosome structures analyzed by atomic force microscopy. Anal Biochem 324: 39-44.
    • (2004) Anal Biochem , vol.324 , pp. 39-44
    • Sugiyama, S.1    Yoshino, T.2    Kanahara, H.3    Shichiri, M.4    Fukushi, D.5    Ohtani, T.6
  • 119
    • 0033555550 scopus 로고    scopus 로고
    • High mobility group protein 1 interacts specifically with the core domain of human TATA box-binding protein and interferes with transcription factor IIB within the pre-initiation complex
    • Sutrias-Grau M, Bianchi ME, Bernues J (1999) High mobility group protein 1 interacts specifically with the core domain of human TATA box-binding protein and interferes with transcription factor IIB within the pre-initiation complex. J Biol Chem 274: 1628-1634.
    • (1999) J Biol Chem , vol.274 , pp. 1628-1634
    • Sutrias-Grau, M.1    Bianchi, M.E.2    Bernues, J.3
  • 120
    • 0033964905 scopus 로고    scopus 로고
    • Human chromosome structure studied by scanning force microscopy after an enzymatic digestion of the covering cell material
    • Tamayo J, Miles M (2000) Human chromosome structure studied by scanning force microscopy after an enzymatic digestion of the covering cell material. Ultramicroscopy 82: 245-251.
    • (2000) Ultramicroscopy , vol.82 , pp. 245-251
    • Tamayo, J.1    Miles, M.2
  • 121
    • 0022519692 scopus 로고
    • High-order structure of metaphase chromosomes: Evidence for a multiple coiling model
    • Taniguchi T, Takayama S (1986) High-order structure of metaphase chromosomes: evidence for a multiple coiling model. Chromosoma 93: 511-514.
    • (1986) Chromosoma , vol.93 , pp. 511-514
    • Taniguchi, T.1    Takayama, S.2
  • 122
    • 0017762802 scopus 로고
    • Reconstitution of chromatin core particles
    • Tatchell K, Van Holde KE (1977) Reconstitution of chromatin core particles. Biochemistry 16: 5295-5303.
    • (1977) Biochemistry , vol.16 , pp. 5295-5303
    • Tatchell, K.1    Van Holde, K.E.2
  • 123
    • 0017758036 scopus 로고
    • Influence of histone H1 on chromatin structure
    • Thoma F, Koller T (1977) Influence of histone H1 on chromatin structure. Cell 12: 101-107.
    • (1977) Cell , vol.12 , pp. 101-107
    • Thoma, F.1    Koller, T.2
  • 124
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • Thoma F, Koller T, Klug A (1979) Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J Cell Biol 83: 403-427.
    • (1979) J Cell Biol , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 125
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner BM, Birley AJ, Lavender J (1992) Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 69: 375-384.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 127
    • 0022178109 scopus 로고
    • The 87A7 chromomere. Identification of novel chromatin structures flanking the heat shock locus that may define the boundaries of higher order domains
    • Udvardy A, Maine E, Schedl P (1985) The 87A7 chromomere. Identification of novel chromatin structures flanking the heat shock locus that may define the boundaries of higher order domains. J Mol Biol 185: 341-358.
    • (1985) J Mol Biol , vol.185 , pp. 341-358
    • Udvardy, A.1    Maine, E.2    Schedl, P.3
  • 128
    • 0023651332 scopus 로고
    • DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe
    • Uemura T, Ohkura H, Adachi Y, Morino K, Shiozaki K, Yanagida M (1987) DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe. Cell 50: 917-925.
    • (1987) Cell , vol.50 , pp. 917-925
    • Uemura, T.1    Ohkura, H.2    Adachi, Y.3    Morino, K.4    Shiozaki, K.5    Yanagida, M.6
  • 129
    • 0036948503 scopus 로고    scopus 로고
    • The structure of human metaphase chromosomes: Its histological perspective and new horizons by atomic force microscopy
    • Ushiki T, Hoshi O, Iwai K, Kimura E, Shigeno M (2002) The structure of human metaphase chromosomes: its histological perspective and new horizons by atomic force microscopy. Arch Histol Cytol 65: 377-390.
    • (2002) Arch Histol Cytol , vol.65 , pp. 377-390
    • Ushiki, T.1    Hoshi, O.2    Iwai, K.3    Kimura, E.4    Shigeno, M.5
  • 130
    • 0032442522 scopus 로고    scopus 로고
    • Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation
    • Van Hooser A, Goodrich DW, Allis CD, Brinkley BR, Mancini MA (1998) Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation. J Cell Sci 111(Pt 23): 3497-3506.
    • (1998) J Cell Sci , vol.111 , pp. 3497-3506
    • Van Hooser, A.1    Goodrich, D.W.2    Allis, C.D.3    Brinkley, B.R.4    Mancini, M.A.5
  • 131
    • 0035928736 scopus 로고    scopus 로고
    • Multiple regimes of constrained chromosome motion are regulated in the interphase Drosophila nucleus
    • Vazquez J, Belmont AS, Sedat JW (2001) Multiple regimes of constrained chromosome motion are regulated in the interphase Drosophila nucleus. Curr Biol 11: 1227-1239.
    • (2001) Curr Biol , vol.11 , pp. 1227-1239
    • Vazquez, J.1    Belmont, A.S.2    Sedat, J.W.3
  • 134
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • Wang JC (2002) Cellular roles of DNA topoisomerases: a molecular perspective. Nat Rev Mol Cell Biol 3: 430-440.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 135
    • 0032560517 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena
    • Wei Y, Mizzen CA, Cook RG, Gorovsky MA, Allis CD (1998) Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena. Proc Natl Acad Sci U S A 95: 7480-7484.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7480-7484
    • Wei, Y.1    Mizzen, C.A.2    Cook, R.G.3    Gorovsky, M.A.4    Allis, C.D.5
  • 136
    • 0022273023 scopus 로고
    • Structure of the 300A chromatin filament: X-ray diffraction from oriented samples
    • Widom J, Klug A (1985) Structure of the 300A chromatin filament: X-ray diffraction from oriented samples. Cell 43: 207-213.
    • (1985) Cell , vol.43 , pp. 207-213
    • Widom, J.1    Klug, A.2
  • 137
    • 0037529048 scopus 로고    scopus 로고
    • Transcription and the territory: The ins and outs of gene positioning
    • Williams RR (2003) Transcription and the territory: the ins and outs of gene positioning. Trends Genet 19: 298-302.
    • (2003) Trends Genet , vol.19 , pp. 298-302
    • Williams, R.R.1
  • 139
    • 0021250785 scopus 로고
    • The higher-order structure of chromatin: Evidence for a helical ribbon arrangement
    • Woodcock CL, Frado LL, Rattner JB (1984) The higher-order structure of chromatin: evidence for a helical ribbon arrangement. J Cell Biol 99: 42-52.
    • (1984) J Cell Biol , vol.99 , pp. 42-52
    • Woodcock, C.L.1    Frado, L.L.2    Rattner, J.B.3
  • 140
    • 0015506478 scopus 로고
    • On the structure of the folded chromosome of Escherichia coli
    • Worcel A, Burgi E (1972) On the structure of the folded chromosome of Escherichia coli. J Mol Biol 71: 127-147.
    • (1972) J Mol Biol , vol.71 , pp. 127-147
    • Worcel, A.1    Burgi, E.2
  • 142
    • 0036006301 scopus 로고    scopus 로고
    • Condensin architecture and interaction with DNA. Regulatory non-SMC subunits bind to the head of SMC heterodimer
    • Yoshimura SH, Hizume K, Murakami A, Sutani T, Takeyasu K, Yanagida M (2002) Condensin architecture and interaction with DNA. Regulatory non-SMC subunits bind to the head of SMC heterodimer. Curr Biol 12: 508-513.
    • (2002) Curr Biol , vol.12 , pp. 508-513
    • Yoshimura, S.H.1    Hizume, K.2    Murakami, A.3    Sutani, T.4    Takeyasu, K.5    Yanagida, M.6
  • 143
    • 0142123387 scopus 로고    scopus 로고
    • On-substrate lysis treatment combined with scanning probe microscopy revealed chromosome structures in eukaryotes and prokaryotes
    • Yoshimura SH, Kim J, Takeyasu K (2003) On-substrate lysis treatment combined with scanning probe microscopy revealed chromosome structures in eukaryotes and prokaryotes. J Electron Microsc (Tokyo) 52: 415-423.
    • (2003) J Electron Microsc (Tokyo) , vol.52 , pp. 415-423
    • Yoshimura, S.H.1    Kim, J.2    Takeyasu, K.3
  • 144
    • 24644446398 scopus 로고    scopus 로고
    • Ribo-gnome: The big world of small RNAs
    • Zamore PD, Haley B (2005) Ribo-gnome: the big world of small RNAs. Science 309: 1519-1524.
    • (2005) Science , vol.309 , pp. 1519-1524
    • Zamore, P.D.1    Haley, B.2
  • 145
    • 0032567080 scopus 로고    scopus 로고
    • Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling
    • Zhao K, Wang W, Rando OJ, Xue Y, Swiderek K, Kuo A, Crabtree GR (1998) Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell 95: 625-636.
    • (1998) Cell , vol.95 , pp. 625-636
    • Zhao, K.1    Wang, W.2    Rando, O.J.3    Xue, Y.4    Swiderek, K.5    Kuo, A.6    Crabtree, G.R.7
  • 146
    • 0037385490 scopus 로고    scopus 로고
    • Structures and interactions of the core histone tail domains
    • Zheng C, Hayes JJ (2003) Structures and interactions of the core histone tail domains. Biopolymers 68: 539-546.
    • (2003) Biopolymers , vol.68 , pp. 539-546
    • Zheng, C.1    Hayes, J.J.2


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