메뉴 건너뛰기




Volumn 1819, Issue 3-4, 2012, Pages 196-210

Assembling chromatin: The long and winding road

Author keywords

Assembly; Chaperone; Chromatin; Factor; Histone; Replication

Indexed keywords

ANTISILENCING FUNCTION 1 PROTEIN; CHAPERONE; CHROMATIN ASSEMBLY FACTOR 1; DNA; HISTONE H2A; HISTONE H2AZ; HISTONE H2B; HISTONE H3; HISTONE H4; MESSENGER RNA; NUCLEOPLASMIN; NUCLEOSOME ASSEMBLY PROTEIN 1; UNCLASSIFIED DRUG;

EID: 84857119394     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2011.07.005     Document Type: Article
Times cited : (70)

References (340)
  • 1
    • 0000546369 scopus 로고
    • Ultractructure of inactive chromatin
    • Woodcock C.L.F. Ultractructure of inactive chromatin. J. Cell Biol. 1973, 59:A368.
    • (1973) J. Cell Biol. , vol.59
    • Woodcock, C.L.F.1
  • 2
    • 0141887600 scopus 로고
    • Spheroid chromatin units (v bodies)
    • Olins A.L., Olins D.E. Spheroid chromatin units (v bodies). J. Cell Biol. 1973, 59:A252.
    • (1973) J. Cell Biol. , vol.59
    • Olins, A.L.1    Olins, D.E.2
  • 3
    • 0015964401 scopus 로고
    • Spheroid chromatin units (v bodies)
    • Olins A.L., Olins D.E. Spheroid chromatin units (v bodies). Science 1974, 183:330-332.
    • (1974) Science , vol.183 , pp. 330-332
    • Olins, A.L.1    Olins, D.E.2
  • 4
    • 0015977368 scopus 로고
    • Mechanism of DNA replication in Drosophila chromosomes: structure of replication forks and evidence for bidirectionality
    • Kriegstein H.J., Hogness D.S. Mechanism of DNA replication in Drosophila chromosomes: structure of replication forks and evidence for bidirectionality. Proc. Natl. Acad. Sci. U. S. A. 1974, 71:135-139.
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 135-139
    • Kriegstein, H.J.1    Hogness, D.S.2
  • 5
    • 0017739173 scopus 로고
    • Electron microscopic analysis of chromatin replication in the cellular blastoderm Drosophila melanogaster embryo
    • McKnight S.L., Miller O.L. Electron microscopic analysis of chromatin replication in the cellular blastoderm Drosophila melanogaster embryo. Cell 1977, 12:795-804.
    • (1977) Cell , vol.12 , pp. 795-804
    • McKnight, S.L.1    Miller, O.L.2
  • 6
    • 0003903126 scopus 로고
    • Springer-Verlag, New York
    • van Holde K.E. Chromatin 1988, Springer-Verlag, New York.
    • (1988) Chromatin
    • van Holde, K.E.1
  • 7
    • 0141995062 scopus 로고    scopus 로고
    • Chromatin history: our view from the bridge
    • Olins D.E., Olins A.L. Chromatin history: our view from the bridge. Nat. Rev. Mol. Cell Biol. 2003, 4:809-814.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 809-814
    • Olins, D.E.1    Olins, A.L.2
  • 9
    • 0017189157 scopus 로고
    • Rapid assembly of newly synthesized DNA into chromatin subunits prior to joining to small DNA replication intermediates
    • Hildebrand C.E., Walters R.A. Rapid assembly of newly synthesized DNA into chromatin subunits prior to joining to small DNA replication intermediates. Biochem. Biophys. Res. Commun. 1976, 73:157-163.
    • (1976) Biochem. Biophys. Res. Commun. , vol.73 , pp. 157-163
    • Hildebrand, C.E.1    Walters, R.A.2
  • 10
    • 0016833975 scopus 로고
    • Assembly of DNA and protein during replication in HeLa cells
    • Seale R.L. Assembly of DNA and protein during replication in HeLa cells. Nature 1975, 255:247-249.
    • (1975) Nature , vol.255 , pp. 247-249
    • Seale, R.L.1
  • 11
    • 0016013262 scopus 로고
    • The assembly of newly replicated DNA into chromatin
    • Weintraub H. The assembly of newly replicated DNA into chromatin. Cold Spring Harb. Symp. Quant. Biol. 1974, 38:247-256.
    • (1974) Cold Spring Harb. Symp. Quant. Biol. , vol.38 , pp. 247-256
    • Weintraub, H.1
  • 12
    • 0016699355 scopus 로고
    • Effects of cycloheximide on chromatin biosynthesis
    • Seale R.L., Simpson R.T. Effects of cycloheximide on chromatin biosynthesis. J. Mol. Biol. 1975, 94:479-501.
    • (1975) J. Mol. Biol. , vol.94 , pp. 479-501
    • Seale, R.L.1    Simpson, R.T.2
  • 13
    • 0015786441 scopus 로고
    • Chromatin sub-structure. The digestion of chromatin DNA at regularly spaced sites by a nuclear deoxyribonuclease
    • Hewish D.R., Burgoyne L.A. Chromatin sub-structure. The digestion of chromatin DNA at regularly spaced sites by a nuclear deoxyribonuclease. Biochem. Biophys. Res. Commun. 1973, 52:504-510.
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 504-510
    • Hewish, D.R.1    Burgoyne, L.A.2
  • 14
    • 0015919073 scopus 로고
    • Properties of nuclease-resistant fragments of calf thymus chromatin
    • Rill R., Van Holde K.E. Properties of nuclease-resistant fragments of calf thymus chromatin. J. Biol. Chem. 1973, 248:1080-1083.
    • (1973) J. Biol. Chem. , vol.248 , pp. 1080-1083
    • Rill, R.1    Van Holde, K.E.2
  • 15
    • 0016144734 scopus 로고
    • Subunit structure of chromatin
    • Noll M. Subunit structure of chromatin. Nature 1974, 251:249-251.
    • (1974) Nature , vol.251 , pp. 249-251
    • Noll, M.1
  • 17
    • 0017897683 scopus 로고
    • Nucleosomes associated with newly replicated DNA have an altered conformation
    • Seale R.L. Nucleosomes associated with newly replicated DNA have an altered conformation. Proc. Natl. Acad. Sci. U. S. A. 1978, 75:2717-2721.
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 2717-2721
    • Seale, R.L.1
  • 18
    • 0018036390 scopus 로고
    • Assembly of newly replicated chromatin
    • Worcel A., Han S., Wong M.L. Assembly of newly replicated chromatin. Cell 1978, 15:969-977.
    • (1978) Cell , vol.15 , pp. 969-977
    • Worcel, A.1    Han, S.2    Wong, M.L.3
  • 19
    • 0018875030 scopus 로고
    • Maturation of newly replicated chromatin of simian virus 40 and its host cell
    • Klempnauer K.H., Fanning E., Otto B., Knippers R. Maturation of newly replicated chromatin of simian virus 40 and its host cell. J. Mol. Biol. 1980, 136:359-374.
    • (1980) J. Mol. Biol. , vol.136 , pp. 359-374
    • Klempnauer, K.H.1    Fanning, E.2    Otto, B.3    Knippers, R.4
  • 20
    • 0019888640 scopus 로고
    • Dual nature of newly replicated chromatin: evidence for nucleosomal and non-nucleosomal DNA at the site of native replication forks
    • Annunziato A.T., Schindler R.K., Thomas C.A., Seale R.L. Dual nature of newly replicated chromatin: evidence for nucleosomal and non-nucleosomal DNA at the site of native replication forks. J. Biol. Chem. 1981, 256:11880-11886.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11880-11886
    • Annunziato, A.T.1    Schindler, R.K.2    Thomas, C.A.3    Seale, R.L.4
  • 21
    • 0019871821 scopus 로고
    • Structure of chromatin at deoxyribonucleic acid replication forks: location of the first nucleosomes on newly synthesized simian virus 40 deoxyribonucleic acid
    • Herman T.M., DePamphilis M.L., Wassarman P.M. Structure of chromatin at deoxyribonucleic acid replication forks: location of the first nucleosomes on newly synthesized simian virus 40 deoxyribonucleic acid. Biochemistry 1981, 20:621-630.
    • (1981) Biochemistry , vol.20 , pp. 621-630
    • Herman, T.M.1    DePamphilis, M.L.2    Wassarman, P.M.3
  • 22
    • 0019841419 scopus 로고
    • Structure of chromatin at deoxyribonucleic acid replication forks: prenucleosomal deoxyribonucleic acid is rapidly excised from replicating simian virus 40 chromosomes by micrococcal nuclease
    • Cusick M.E., Herman T.M., DePamphilis M.L., Wassarman P.M. Structure of chromatin at deoxyribonucleic acid replication forks: prenucleosomal deoxyribonucleic acid is rapidly excised from replicating simian virus 40 chromosomes by micrococcal nuclease. Biochemistry 1981, 20:6648-6658.
    • (1981) Biochemistry , vol.20 , pp. 6648-6658
    • Cusick, M.E.1    Herman, T.M.2    DePamphilis, M.L.3    Wassarman, P.M.4
  • 23
    • 0018823801 scopus 로고
    • Replication of eukaryotic chromosomes: a close-up of the replication fork
    • DePamphilis M.L., Wassarman P.M. Replication of eukaryotic chromosomes: a close-up of the replication fork. Annu. Rev. Biochem. 1980, 49:627-666.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 627-666
    • DePamphilis, M.L.1    Wassarman, P.M.2
  • 24
    • 0022457421 scopus 로고
    • Structure of replicating simian virus chromosomes
    • Sogo J.M., Stahl H., Koller T., Knippers R. Structure of replicating simian virus chromosomes. J. Mol. Biol. 1986, 189:189-204.
    • (1986) J. Mol. Biol. , vol.189 , pp. 189-204
    • Sogo, J.M.1    Stahl, H.2    Koller, T.3    Knippers, R.4
  • 25
    • 0017629182 scopus 로고
    • Assembly of SV40 and polyoma minichromosomes during replication
    • Cremisi C., Chestier A., Yaniv M. Assembly of SV40 and polyoma minichromosomes during replication. Cold Spring Harb. Symp. Quant. Biol. 1978, 42(Pt 1):409-416.
    • (1978) Cold Spring Harb. Symp. Quant. Biol. , vol.42 , Issue.PART 1 , pp. 409-416
    • Cremisi, C.1    Chestier, A.2    Yaniv, M.3
  • 26
    • 0018434015 scopus 로고
    • DNA-histone interaction in the vicinity of replication points
    • Schlaeger E.J., Knippers R. DNA-histone interaction in the vicinity of replication points. Nucleic Acids Res. 1979, 6:645-656.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 645-656
    • Schlaeger, E.J.1    Knippers, R.2
  • 27
    • 0020491951 scopus 로고
    • Maturation of nucleosomal and nonnucleosomal components of nascent chromatin: differential requirement for concurrent protein synthesis
    • Annunziato A.T., Seale R.L. Maturation of nucleosomal and nonnucleosomal components of nascent chromatin: differential requirement for concurrent protein synthesis. Biochemistry 1982, 21:5431-5438.
    • (1982) Biochemistry , vol.21 , pp. 5431-5438
    • Annunziato, A.T.1    Seale, R.L.2
  • 28
    • 0021321016 scopus 로고
    • Two-stage maturation process for newly replicated chromatin
    • Smith P.A., Jackson V., Chalkley R. Two-stage maturation process for newly replicated chromatin. Biochemistry 1984, 23:1576-1581.
    • (1984) Biochemistry , vol.23 , pp. 1576-1581
    • Smith, P.A.1    Jackson, V.2    Chalkley, R.3
  • 29
    • 0021093461 scopus 로고
    • Structure of chromatin at deoxyribonucleic acid replication forks: nuclease hypersensitivity results from both prenucleosomal deoxyribonucleic acid and an immature chromatin structure
    • Cusick M.E., Lee K.S., DePamphilis M.L., Wassarman P.M. Structure of chromatin at deoxyribonucleic acid replication forks: nuclease hypersensitivity results from both prenucleosomal deoxyribonucleic acid and an immature chromatin structure. Biochemistry 1983, 22:3873-3884.
    • (1983) Biochemistry , vol.22 , pp. 3873-3884
    • Cusick, M.E.1    Lee, K.S.2    DePamphilis, M.L.3    Wassarman, P.M.4
  • 30
    • 0017054307 scopus 로고
    • Cooperative alignment of nu bodies during chromosome replication in the presence of cycloheximide
    • Weintraub H. Cooperative alignment of nu bodies during chromosome replication in the presence of cycloheximide. Cell 1976, 9:419-422.
    • (1976) Cell , vol.9 , pp. 419-422
    • Weintraub, H.1
  • 31
    • 0017054798 scopus 로고
    • Studies on the mode of segregation of histone nu bodies during replication in HeLa cells
    • Seale R.L. Studies on the mode of segregation of histone nu bodies during replication in HeLa cells. Cell 1976, 9:423-429.
    • (1976) Cell , vol.9 , pp. 423-429
    • Seale, R.L.1
  • 32
    • 0025984349 scopus 로고
    • Transfer of nucleosomes from parental to replicated chromatin
    • Krude T., Knippers R. Transfer of nucleosomes from parental to replicated chromatin. Mol. Cell. Biol. 1991, 11:6257-6267.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6257-6267
    • Krude, T.1    Knippers, R.2
  • 33
    • 0016723918 scopus 로고
    • Processing of newly synthesized histone molecules
    • Ruiz-Carrillo A., Wangh L.J., Allfrey V.G. Processing of newly synthesized histone molecules. Science 1975, 190:117-128.
    • (1975) Science , vol.190 , pp. 117-128
    • Ruiz-Carrillo, A.1    Wangh, L.J.2    Allfrey, V.G.3
  • 35
    • 0021112111 scopus 로고
    • Histone hyperacetylation has little effect on the higher order folding of chromatin
    • McGhee J.D., Nickol J.M., Felsenfeld G., Rau D.C. Histone hyperacetylation has little effect on the higher order folding of chromatin. Nucleic Acids Res. 1983, 11:4065-4075.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 4065-4075
    • McGhee, J.D.1    Nickol, J.M.2    Felsenfeld, G.3    Rau, D.C.4
  • 36
    • 0023777121 scopus 로고
    • Treatment with sodium butyrate inhibits the complete condensation of interphase chromatin
    • Annunziato A.T., Frado L.-L.Y., Seale R.L., Woodcock C.L.F. Treatment with sodium butyrate inhibits the complete condensation of interphase chromatin. Chromosoma (Berl) 1988, 96:132-138.
    • (1988) Chromosoma (Berl) , vol.96 , pp. 132-138
    • Annunziato, A.T.1    Frado, L.-L.Y.2    Seale, R.L.3    Woodcock, C.L.F.4
  • 37
    • 0025217826 scopus 로고
    • Histone acetylation reduces the capacity of H1 histones to condense transcriptionally active/competent chromatin
    • Ridsdale J.A., Hendzel M.J., Delcuve G.P., Davie J.R. Histone acetylation reduces the capacity of H1 histones to condense transcriptionally active/competent chromatin. J. Biol. Chem. 1990, 265:5150-5156.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5150-5156
    • Ridsdale, J.A.1    Hendzel, M.J.2    Delcuve, G.P.3    Davie, J.R.4
  • 38
    • 0020478939 scopus 로고
    • Accessibility of newly synthesized chromatin to histone acetylase
    • Cousens L.S., Alberts B.M. Accessibility of newly synthesized chromatin to histone acetylase. J. Biol. Chem. 1982, 257:3945-3949.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3945-3949
    • Cousens, L.S.1    Alberts, B.M.2
  • 39
    • 0021112684 scopus 로고
    • Histone deacetylation is required for the maturation of newly replicated chromatin
    • Annunziato A.T., Seale R.L. Histone deacetylation is required for the maturation of newly replicated chromatin. J. Biol. Chem. 1983, 258:12675-12684.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12675-12684
    • Annunziato, A.T.1    Seale, R.L.2
  • 40
    • 0024323875 scopus 로고
    • Influence of histone acetylation on the solubility, H1 content and DNase I sensitivity of newly assembled chromatin
    • Perry C.A., Annunziato A.T. Influence of histone acetylation on the solubility, H1 content and DNase I sensitivity of newly assembled chromatin. Nucleic Acids Res. 1989, 17:4275-4291.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4275-4291
    • Perry, C.A.1    Annunziato, A.T.2
  • 41
    • 0025946135 scopus 로고
    • Histone acetylation reduces H1-mediated nucleosome interactions during chromatin assembly
    • Perry C.A., Annunziato A.T. Histone acetylation reduces H1-mediated nucleosome interactions during chromatin assembly. Exp. Cell Res. 1991, 196:337-345.
    • (1991) Exp. Cell Res. , vol.196 , pp. 337-345
    • Perry, C.A.1    Annunziato, A.T.2
  • 42
    • 0023900774 scopus 로고
    • Erythroid-specific gene chromatin has an altered association with linker histones
    • Ridsdale J.A., Rattner J.B., Davie J.R. Erythroid-specific gene chromatin has an altered association with linker histones. Nucleic Acids Res. 1988, 16:5915-5926.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 5915-5926
    • Ridsdale, J.A.1    Rattner, J.B.2    Davie, J.R.3
  • 44
    • 0024532966 scopus 로고
    • Metabolic behaviors of the core histones in proliferating Friend cells
    • Tsvetkov S., Ivanova E., Djondjurov L. Metabolic behaviors of the core histones in proliferating Friend cells. Exp. Cell Res. 1989, 180:94-105.
    • (1989) Exp. Cell Res. , vol.180 , pp. 94-105
    • Tsvetkov, S.1    Ivanova, E.2    Djondjurov, L.3
  • 45
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y. Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell 2004, 116:51-61.
    • (2004) Cell , vol.116 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 46
    • 27144453690 scopus 로고    scopus 로고
    • ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA
    • English C.M., Maluf N.K., Tripet B., Churchill M.E., Tyler J.K. ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA. Biochemistry 2005, 44:13673-13682.
    • (2005) Biochemistry , vol.44 , pp. 13673-13682
    • English, C.M.1    Maluf, N.K.2    Tripet, B.3    Churchill, M.E.4    Tyler, J.K.5
  • 48
    • 16844384065 scopus 로고    scopus 로고
    • Split decision: what happens to nucleosomes during DNA replication?
    • Annunziato A.T. Split decision: what happens to nucleosomes during DNA replication?. J. Biol. Chem. 2005, 280:12065-12068.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12065-12068
    • Annunziato, A.T.1
  • 49
    • 0025098652 scopus 로고
    • In vitro replication through nucleosomes without histone displacement
    • Bonne-Andrea C., Wong M.L., Alberts B.M. In vitro replication through nucleosomes without histone displacement. Nature 1990, 343:719-726.
    • (1990) Nature , vol.343 , pp. 719-726
    • Bonne-Andrea, C.1    Wong, M.L.2    Alberts, B.M.3
  • 50
    • 0025138502 scopus 로고
    • Conservative segregation of tetrameric units of H3 and H4 histones during nucleosome replication
    • Yamasu K., Senshu T. Conservative segregation of tetrameric units of H3 and H4 histones during nucleosome replication. J. Biochem. (Tokyo) 1990, 107:15-20.
    • (1990) J. Biochem. (Tokyo) , vol.107 , pp. 15-20
    • Yamasu, K.1    Senshu, T.2
  • 51
    • 0018891793 scopus 로고
    • Incorporation of exogenous pyrene-labeled histone into Physarum chromatin: a system for studying changes in nucleosomes assembled in vivo
    • Prior C.P., Cantor C.R., Johnson E.M., Allfrey V.G. Incorporation of exogenous pyrene-labeled histone into Physarum chromatin: a system for studying changes in nucleosomes assembled in vivo. Cell 1980, 20:597-608.
    • (1980) Cell , vol.20 , pp. 597-608
    • Prior, C.P.1    Cantor, C.R.2    Johnson, E.M.3    Allfrey, V.G.4
  • 52
    • 0021256401 scopus 로고
    • Conservative segregation of nucleosome core histones
    • Leffak I.M. Conservative segregation of nucleosome core histones. Nature 1984, 307:82-85.
    • (1984) Nature , vol.307 , pp. 82-85
    • Leffak, I.M.1
  • 53
    • 0025134076 scopus 로고
    • In vivo studies on the dynamics of histone-DNA interaction: evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both
    • Jackson V. In vivo studies on the dynamics of histone-DNA interaction: evidence for nucleosome dissolution during replication and transcription and a low level of dissolution independent of both. Biochemistry 1990, 29:719-731.
    • (1990) Biochemistry , vol.29 , pp. 719-731
    • Jackson, V.1
  • 54
    • 77950462427 scopus 로고    scopus 로고
    • Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly
    • Xu M., Long C., Chen X., Huang C., Chen S., Zhu B. Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly. Science 2010, 328:94-98.
    • (2010) Science , vol.328 , pp. 94-98
    • Xu, M.1    Long, C.2    Chen, X.3    Huang, C.4    Chen, S.5    Zhu, B.6
  • 55
    • 79951992242 scopus 로고    scopus 로고
    • Splitting of H3-H4 tetramers at transcriptionally active genes undergoing dynamic histone exchange
    • Katan-Khaykovich Y., Struhl K. Splitting of H3-H4 tetramers at transcriptionally active genes undergoing dynamic histone exchange. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:1296-1301.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 1296-1301
    • Katan-Khaykovich, Y.1    Struhl, K.2
  • 56
    • 0034677955 scopus 로고    scopus 로고
    • Histone octamer dissociation is not required for in vitro replication of simian virus 40 minichromosomes
    • Vestner B., Waldmann T., Gruss C. Histone octamer dissociation is not required for in vitro replication of simian virus 40 minichromosomes. J. Biol. Chem. 2000, 275:8190-8195.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8190-8195
    • Vestner, B.1    Waldmann, T.2    Gruss, C.3
  • 57
    • 37549049820 scopus 로고    scopus 로고
    • Regulation of replication fork progression through histone supply and demand
    • Groth A., Corpet A., Cook A.J.L., Roche D., Bartek J., Lukas J., Almouzni G. Regulation of replication fork progression through histone supply and demand. Science 2007, 318:1928-1931.
    • (2007) Science , vol.318 , pp. 1928-1931
    • Groth, A.1    Corpet, A.2    Cook, A.J.L.3    Roche, D.4    Bartek, J.5    Lukas, J.6    Almouzni, G.7
  • 59
    • 0018714973 scopus 로고
    • The asymmetric segregation of parental nucleosomes during chrosome replication
    • Seidman M.M., Levine A.J., Weintraub H. The asymmetric segregation of parental nucleosomes during chrosome replication. Cell 1979, 18:439-449.
    • (1979) Cell , vol.18 , pp. 439-449
    • Seidman, M.M.1    Levine, A.J.2    Weintraub, H.3
  • 60
    • 0021610687 scopus 로고
    • Dispersive segregation of nucleosomes during replication of simian virus 40 chromosomes
    • Cusick M.F., DePamphilis M.L., Wassarman P.M. Dispersive segregation of nucleosomes during replication of simian virus 40 chromosomes. J. Mol. Biol. 1984, 178:249-271.
    • (1984) J. Mol. Biol. , vol.178 , pp. 249-271
    • Cusick, M.F.1    DePamphilis, M.L.2    Wassarman, P.M.3
  • 61
    • 0026516913 scopus 로고
    • Nonconservative segregation of parental nucleosomes during simian virus-40 chromosome replication invitro
    • Sugasawa K., Ishimi Y., Eki T., Hurwitz J., Kikuchi A., Hanaoka F. Nonconservative segregation of parental nucleosomes during simian virus-40 chromosome replication invitro. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:1055-1059.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 1055-1059
    • Sugasawa, K.1    Ishimi, Y.2    Eki, T.3    Hurwitz, J.4    Kikuchi, A.5    Hanaoka, F.6
  • 62
    • 0020110769 scopus 로고
    • Nucleosome segregation at a defined mammalian chromosomal site
    • Roufa D.J., Marchionni M.A. Nucleosome segregation at a defined mammalian chromosomal site. Proc. Natl. Acad. Sci. U. S. A. 1982, 79:1810-1814.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 1810-1814
    • Roufa, D.J.1    Marchionni, M.A.2
  • 64
    • 0019888031 scopus 로고
    • A reevaluation of new histone deposition on replicating chromatin
    • Jackson V., Chalkley R. A reevaluation of new histone deposition on replicating chromatin. J. Biol. Chem. 1981, 256:5095-5103.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5095-5103
    • Jackson, V.1    Chalkley, R.2
  • 65
    • 0020134132 scopus 로고
    • Assembly of new histones into nucleosomes and their distribution in replicating chromatin
    • Russev G., Hancock R. Assembly of new histones into nucleosomes and their distribution in replicating chromatin. Proc. Natl. Acad. Sci. U. S. A. 1982, 79:3143-3147.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 3143-3147
    • Russev, G.1    Hancock, R.2
  • 66
    • 0020488589 scopus 로고
    • Distribution of the core histones H2A.H2B.H3 and H4 during cell replication
    • Fowler E., Farb R., El-Saidy S. Distribution of the core histones H2A.H2B.H3 and H4 during cell replication. Nucleic Acids Res. 1982, 10:735-748.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 735-748
    • Fowler, E.1    Farb, R.2    El-Saidy, S.3
  • 67
    • 0022367261 scopus 로고
    • Histone segregation on replicating chromatin
    • Jackson V., Chalkley R. Histone segregation on replicating chromatin. Biochemistry 1985, 24:6930-6938.
    • (1985) Biochemistry , vol.24 , pp. 6930-6938
    • Jackson, V.1    Chalkley, R.2
  • 68
    • 0017715478 scopus 로고
    • Conservative assembly and segregation of nucleosomal histones
    • Leffak I.M., Grainger R., Weintraub H. Conservative assembly and segregation of nucleosomal histones. Cell 1977, 12:837-845.
    • (1977) Cell , vol.12 , pp. 837-845
    • Leffak, I.M.1    Grainger, R.2    Weintraub, H.3
  • 69
    • 0021759602 scopus 로고
    • Presence of nucleosomes within irregularly cleaved fragments of newly replicated chromatin
    • Annunziato A.T., Seale R.L. Presence of nucleosomes within irregularly cleaved fragments of newly replicated chromatin. Nucleic Acids Res. 1984, 12:6179-6196.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 6179-6196
    • Annunziato, A.T.1    Seale, R.L.2
  • 70
    • 0019952141 scopus 로고
    • Nucleosome segregation in chromatin replicated in the presence of cycloheximide
    • Pospelov V., Russev G., Vassilev L., Tsanev R. Nucleosome segregation in chromatin replicated in the presence of cycloheximide. J. Mol. Biol. 1982, 156:79-91.
    • (1982) J. Mol. Biol. , vol.156 , pp. 79-91
    • Pospelov, V.1    Russev, G.2    Vassilev, L.3    Tsanev, R.4
  • 71
    • 0025931653 scopus 로고
    • Emetine allows identification of origins of mammalian DNA replication by Imbalanced DNA synthesis, not through conservative nucleosome segregation
    • Burhans W.C., Vassilev L.T., Wu J., Sogo J.M., Nallaseth F.S., Depamphilis M.L. Emetine allows identification of origins of mammalian DNA replication by Imbalanced DNA synthesis, not through conservative nucleosome segregation. EMBO J. 1991, 10:4351-4360.
    • (1991) EMBO J. , vol.10 , pp. 4351-4360
    • Burhans, W.C.1    Vassilev, L.T.2    Wu, J.3    Sogo, J.M.4    Nallaseth, F.S.5    Depamphilis, M.L.6
  • 72
    • 0037126597 scopus 로고    scopus 로고
    • Nucleosome positioning at the replication fork
    • Lucchini R., Wellinger R.E., Sogo J.M. Nucleosome positioning at the replication fork. EMBO J. 2001, 20:7294-7302.
    • (2001) EMBO J. , vol.20 , pp. 7294-7302
    • Lucchini, R.1    Wellinger, R.E.2    Sogo, J.M.3
  • 74
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • Malik H.S., Henikoff S. Phylogenomics of the nucleosome. Nat. Struct. Biol. 2003, 10:882-891.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 76
    • 58149522909 scopus 로고    scopus 로고
    • Making copies of chromatin: the challenge of nucleosomal organization and epigenetic information
    • Corpet A., Almouzni G. Making copies of chromatin: the challenge of nucleosomal organization and epigenetic information. Trends Cell Biol. 2009, 19:29-41.
    • (2009) Trends Cell Biol. , vol.19 , pp. 29-41
    • Corpet, A.1    Almouzni, G.2
  • 77
    • 77954817543 scopus 로고    scopus 로고
    • Chromatin as a potential carrier of heritable information
    • Kaufman P.D., Rando O.J. Chromatin as a potential carrier of heritable information. Curr. Opin. Cell Biol. 2010, 22:284-290.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 284-290
    • Kaufman, P.D.1    Rando, O.J.2
  • 78
    • 0027715686 scopus 로고
    • Parental nucleosomes segregated to newly replicated chromatin are underacetylated relative to those assembled de novo
    • Perry C.A., Allis C.D., Annunziato A.T. Parental nucleosomes segregated to newly replicated chromatin are underacetylated relative to those assembled de novo. Biochemistry 1993, 32:13615-13623.
    • (1993) Biochemistry , vol.32 , pp. 13615-13623
    • Perry, C.A.1    Allis, C.D.2    Annunziato, A.T.3
  • 80
    • 47249157351 scopus 로고    scopus 로고
    • Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry
    • Pesavento J.J., Bullock C.R., LeDuc R.D., Mizzen C.A., Kelleher N.L. Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry. J. Biol. Chem. 2008, 283:14927-14937.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14927-14937
    • Pesavento, J.J.1    Bullock, C.R.2    LeDuc, R.D.3    Mizzen, C.A.4    Kelleher, N.L.5
  • 81
    • 69849087056 scopus 로고    scopus 로고
    • Establishment of histone modifications after chromatin assembly
    • Scharf A.N., Barth T.K., Imhof A. Establishment of histone modifications after chromatin assembly. Nucleic Acids Res. 2009, 37:5032-5040.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5032-5040
    • Scharf, A.N.1    Barth, T.K.2    Imhof, A.3
  • 82
    • 0015704859 scopus 로고
    • Enzymatic modifications and their possible roles in regulating the binding of basic proteins to DNA and in controlling chromosomal structure
    • Louie A.J., Candido E.P.M., Dixon G. Enzymatic modifications and their possible roles in regulating the binding of basic proteins to DNA and in controlling chromosomal structure. Cold Spring Harb. Symp. Quant. Biol. 1974, 38:808-819.
    • (1974) Cold Spring Harb. Symp. Quant. Biol. , vol.38 , pp. 808-819
    • Louie, A.J.1    Candido, E.P.M.2    Dixon, G.3
  • 84
    • 0022650761 scopus 로고
    • Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena: evidence for functionally distinct H4 acetylation sites
    • Chicoine L.G., Schulman I.G., Richman R., Cook R.G., Allis C.D. Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena: evidence for functionally distinct H4 acetylation sites. J. Biol. Chem. 1986, 261:1071-1076.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1071-1076
    • Chicoine, L.G.1    Schulman, I.G.2    Richman, R.3    Cook, R.G.4    Allis, C.D.5
  • 85
    • 0018395286 scopus 로고
    • The modification of stored histones H3 and H4 during the oogenesis and early development of Xenopus laevis
    • Woodland H.R. The modification of stored histones H3 and H4 during the oogenesis and early development of Xenopus laevis. Dev. Biol. 1979, 68:360-370.
    • (1979) Dev. Biol. , vol.68 , pp. 360-370
    • Woodland, H.R.1
  • 86
    • 0027429520 scopus 로고
    • Chromatin transitions during early Xenopus embryogenesis - changes in histone-H4 acetylation and in linker histone type
    • Dimitrov S., Almouzni G., Dasso M., Wolffe A.P. Chromatin transitions during early Xenopus embryogenesis - changes in histone-H4 acetylation and in linker histone type. Dev. Biol. 1993, 160:214-227.
    • (1993) Dev. Biol. , vol.160 , pp. 214-227
    • Dimitrov, S.1    Almouzni, G.2    Dasso, M.3    Wolffe, A.P.4
  • 87
    • 0021738672 scopus 로고
    • Levels of histone H4 diacetylation decrease dramatically during sea urchin embryonic development and correlate with cell doubling rate
    • Chambers S.A.M., Shaw B.R. Levels of histone H4 diacetylation decrease dramatically during sea urchin embryonic development and correlate with cell doubling rate. J. Biol. Chem. 1984, 259:13458-13463.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13458-13463
    • Chambers, S.A.M.1    Shaw, B.R.2
  • 89
    • 0021765422 scopus 로고
    • Patterns of histone acetylation in Physarum polycephalum: H2A and H2B acetylation is functionally distinct from H3 and H4 acetylation
    • Waterborg J.H., Matthews J.H. Patterns of histone acetylation in Physarum polycephalum: H2A and H2B acetylation is functionally distinct from H3 and H4 acetylation. Eur. J. Biochem. 1984, 142:329-335.
    • (1984) Eur. J. Biochem. , vol.142 , pp. 329-335
    • Waterborg, J.H.1    Matthews, J.H.2
  • 91
    • 0033710367 scopus 로고    scopus 로고
    • Role of histone acetylation in the assembly and modulation of chromatin structures
    • Annunziato A.T., Hansen J.C. Role of histone acetylation in the assembly and modulation of chromatin structures. Gene Expr. 2000, 9:37-61.
    • (2000) Gene Expr. , vol.9 , pp. 37-61
    • Annunziato, A.T.1    Hansen, J.C.2
  • 92
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • Shahbazian M.D., Grunstein M. Functions of site-specific histone acetylation and deacetylation. Annu. Rev. Biochem. 2007, 76:75-100.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 93
    • 0025093599 scopus 로고
    • Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation
    • Megee P.C., Morgan B.A., Mittman B.A., Smith M.M. Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science 1990, 247:841-845.
    • (1990) Science , vol.247 , pp. 841-845
    • Megee, P.C.1    Morgan, B.A.2    Mittman, B.A.3    Smith, M.M.4
  • 94
    • 0032499747 scopus 로고    scopus 로고
    • Deposition-related sites K5/K12 in histone H4 are not required for nucleosome deposition in yeast
    • Ma X.J., Wu J.S., Altheim B.A., Schultz M.C., Grunstein M. Deposition-related sites K5/K12 in histone H4 are not required for nucleosome deposition in yeast. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:6693-6698.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6693-6698
    • Ma, X.J.1    Wu, J.S.2    Altheim, B.A.3    Schultz, M.C.4    Grunstein, M.5
  • 95
    • 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.Z., 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. 1998, 17:3155-3167.
    • (1998) EMBO J. , vol.17 , pp. 3155-3167
    • Zhang, W.Z.1    Bone, J.R.2    Edmondson, D.G.3    Turner, B.M.4    Roth, S.Y.5
  • 96
    • 34547099863 scopus 로고    scopus 로고
    • Mutational analysis of H3 and H4N termini reveals distinct roles in nuclear import
    • Blackwell J.S., Wilkinson S.T., Mosammaparast N., Pemberton L.F. Mutational analysis of H3 and H4N termini reveals distinct roles in nuclear import. J. Biol. Chem. 2007, 282:20142-20150.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20142-20150
    • Blackwell, J.S.1    Wilkinson, S.T.2    Mosammaparast, N.3    Pemberton, L.F.4
  • 97
    • 8644251883 scopus 로고    scopus 로고
    • Yeast chromatin assembly complex 1 protein excludes nonacetylatable forms of histone H4 from chromatin and the nucleus
    • Glowczewski L., Waterborg J.H., Berman J.G. Yeast chromatin assembly complex 1 protein excludes nonacetylatable forms of histone H4 from chromatin and the nucleus. Mol. Cell. Biol. 2004, 24:10180-10192.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10180-10192
    • Glowczewski, L.1    Waterborg, J.H.2    Berman, J.G.3
  • 98
    • 78751531687 scopus 로고    scopus 로고
    • H4 replication-dependent diacetylation and Hat1 promote S-phase chromatin assembly in vivo
    • Ejlassi-Lassallette A., Mocquard E., Arnaud M.C., Thiriet C. H4 replication-dependent diacetylation and Hat1 promote S-phase chromatin assembly in vivo. Mol. Biol. Cell 2011, 22:245-255.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 245-255
    • Ejlassi-Lassallette, A.1    Mocquard, E.2    Arnaud, M.C.3    Thiriet, C.4
  • 99
    • 0028104174 scopus 로고
    • Human CENP-A contains a histone H3 related histone fold domain that 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 that is required for targeting to the centromere. J. Cell Biol. 1994, 127:581-592.
    • (1994) J. Cell Biol. , vol.127 , pp. 581-592
    • Sullivan, K.F.1    Hechenberger, M.2    Masri, K.3
  • 101
    • 17344375688 scopus 로고    scopus 로고
    • Human histone gene organization: nonregular arrangement within a large cluster
    • Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D. Human histone gene organization: nonregular arrangement within a large cluster. Genomics 1997, 40:314-322.
    • (1997) Genomics , vol.40 , pp. 314-322
    • Albig, W.1    Kioschis, P.2    Poustka, A.3    Meergans, K.4    Doenecke, D.5
  • 102
    • 0038203126 scopus 로고    scopus 로고
    • Aberrant expression pattern of replication-dependent histone H3 subtype genes in human tumor cell lines
    • Koessler H., Doenecke D., Albig W. Aberrant expression pattern of replication-dependent histone H3 subtype genes in human tumor cell lines. DNA Cell Biol. 2003, 22:233-241.
    • (2003) DNA Cell Biol. , vol.22 , pp. 233-241
    • Koessler, H.1    Doenecke, D.2    Albig, W.3
  • 104
    • 0030589491 scopus 로고    scopus 로고
    • Testis-specific expression of a novel human H3 histone gene
    • Witt O., Albig W., Doenecke D. Testis-specific expression of a novel human H3 histone gene. Exp. Cell Res. 1996, 229:301-306.
    • (1996) Exp. Cell Res. , vol.229 , pp. 301-306
    • Witt, O.1    Albig, W.2    Doenecke, D.3
  • 105
    • 0019865207 scopus 로고
    • Separation of basal histone synthesis from S-phase histone synthesis in dividing cells
    • Wu R.S., Bonner W.M. Separation of basal histone synthesis from S-phase histone synthesis in dividing cells. Cell 1981, 27:321-330.
    • (1981) Cell , vol.27 , pp. 321-330
    • Wu, R.S.1    Bonner, W.M.2
  • 106
    • 0020358561 scopus 로고
    • Patterns of histone variant synthesis can distinguish G0 from G1 cells
    • Wu R.S., Tsai S., Bonner W.M. Patterns of histone variant synthesis can distinguish G0 from G1 cells. Cell 1982, 31:367-374.
    • (1982) Cell , vol.31 , pp. 367-374
    • Wu, R.S.1    Tsai, S.2    Bonner, W.M.3
  • 107
    • 0017365534 scopus 로고
    • Non-allelic variants of histones 2a, 2b and 3 in mammals
    • Franklin S.G., Zweidler A. Non-allelic variants of histones 2a, 2b and 3 in mammals. Nature 1977, 266:273-275.
    • (1977) Nature , vol.266 , pp. 273-275
    • Franklin, S.G.1    Zweidler, A.2
  • 108
    • 0024588670 scopus 로고
    • Expression of a mouse replacement histone H3.3 gene with a highly conserved 3' noncoding region during SV40- and polyoma-induced Go to S-phase transition
    • Hraba-Renevey S., Kress M. Expression of a mouse replacement histone H3.3 gene with a highly conserved 3' noncoding region during SV40- and polyoma-induced Go to S-phase transition. Nucleic Acids Res. 1989, 17:2449-2461.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 2449-2461
    • Hraba-Renevey, S.1    Kress, M.2
  • 110
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly
    • Ahmad K., Henikoff S. The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol. Cell 2002, 9:1191-1200.
    • (2002) Mol. Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 112
    • 17044394787 scopus 로고    scopus 로고
    • Transcriptional activation triggers deposition and removal of the histone variant H3.3
    • Schwartz B.E., Ahmad K. Transcriptional activation triggers deposition and removal of the histone variant H3.3. Gene Dev. 2005, 19:804-814.
    • (2005) Gene Dev. , vol.19 , pp. 804-814
    • Schwartz, B.E.1    Ahmad, K.2
  • 114
    • 23744460663 scopus 로고    scopus 로고
    • Variant histone H3.3 is deposited at sites of nucleosomal displacement throughout transcribed genes while active histone modifications show a promoter-proximal bias
    • Wirbelauer C., Bell O., Schubeler D. Variant histone H3.3 is deposited at sites of nucleosomal displacement throughout transcribed genes while active histone modifications show a promoter-proximal bias. Gene Dev. 2005, 19:1761-1766.
    • (2005) Gene Dev. , vol.19 , pp. 1761-1766
    • Wirbelauer, C.1    Bell, O.2    Schubeler, D.3
  • 115
    • 27144510368 scopus 로고    scopus 로고
    • Genome-scale profiling of histone H3.3 replacement patterns
    • Mito Y., Henikoff J.G., Henikoff S. Genome-scale profiling of histone H3.3 replacement patterns. Nat. Genet. 2005, 37:1090-1097.
    • (2005) Nat. Genet. , vol.37 , pp. 1090-1097
    • Mito, Y.1    Henikoff, J.G.2    Henikoff, S.3
  • 116
    • 31144445949 scopus 로고    scopus 로고
    • Dynamic regulation of replication independent deposition of histone H3 in fission yeast
    • Choi E.S., Shin J.A., Kim H.S., Jang Y.K. Dynamic regulation of replication independent deposition of histone H3 in fission yeast. Nucleic Acid Res. 2005, 33:7102-7110.
    • (2005) Nucleic Acid Res. , vol.33 , pp. 7102-7110
    • Choi, E.S.1    Shin, J.A.2    Kim, H.S.3    Jang, Y.K.4
  • 117
    • 0029938745 scopus 로고    scopus 로고
    • Nucleosome assembly: the CAF and the HAT
    • Kaufman P.D. Nucleosome assembly: the CAF and the HAT. Cure. Opin. Biol. 1996, 8:369-373.
    • (1996) Cure. Opin. Biol. , vol.8 , pp. 369-373
    • Kaufman, P.D.1
  • 118
    • 0036091117 scopus 로고    scopus 로고
    • Chromatin assembly - cooperation between histone chaperones and ATP-dependent nucleosome remodeling machines
    • Tyler J.K. Chromatin assembly - cooperation between histone chaperones and ATP-dependent nucleosome remodeling machines. Eur. J. Biochem. 2002, 269:2268-2274.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2268-2274
    • Tyler, J.K.1
  • 119
    • 1542298307 scopus 로고    scopus 로고
    • Histone chaperones, a supporting role in the limelight
    • Loyola A., Almouzni G. Histone chaperones, a supporting role in the limelight. BBA Gene Struct. Express 2004, 1677:3-11.
    • (2004) BBA Gene Struct. Express , vol.1677 , pp. 3-11
    • Loyola, A.1    Almouzni, G.2
  • 121
    • 0036135016 scopus 로고    scopus 로고
    • Chromatin assembly factor I mutants defective for PCNA binding require Asf1/Hir proteins for silencing
    • Krawitz D.C., Kama T., Kaufman P.D. Chromatin assembly factor I mutants defective for PCNA binding require Asf1/Hir proteins for silencing. Mol. Cell. Biol. 2002, 22:614-625.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 614-625
    • Krawitz, D.C.1    Kama, T.2    Kaufman, P.D.3
  • 124
    • 77953955724 scopus 로고    scopus 로고
    • The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3
    • Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A. The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 2010, 24:1-13.
    • (2010) Genes Dev. , vol.24 , pp. 1-13
    • Drane, P.1    Ouararhni, K.2    Depaux, A.3    Shuaib, M.4    Hamiche, A.5
  • 125
    • 77956282773 scopus 로고    scopus 로고
    • Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
    • Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D. Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:14075-14080.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 14075-14080
    • Lewis, P.W.1    Elsaesser, S.J.2    Noh, K.M.3    Stadler, S.C.4    Allis, C.D.5
  • 126
    • 0037058948 scopus 로고    scopus 로고
    • Histone H3 variants specify modes of chromatin assembly
    • Ahmad K., Henikoff S. Histone H3 variants specify modes of chromatin assembly. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:16477-16484.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16477-16484
    • Ahmad, K.1    Henikoff, S.2
  • 127
    • 11144355550 scopus 로고    scopus 로고
    • SWRred not shaken: mixing the histones
    • Korber P., Horz W. SWRred not shaken: mixing the histones. Cell 2004, 117:5-7.
    • (2004) Cell , vol.117 , pp. 5-7
    • Korber, P.1    Horz, W.2
  • 128
    • 69249216438 scopus 로고    scopus 로고
    • At the right place at the right time: novel CENP-A binding proteins shed light on centromere assembly
    • Silva M.C., Jansen L.E. At the right place at the right time: novel CENP-A binding proteins shed light on centromere assembly. Chromosoma 2009, 118:567-574.
    • (2009) Chromosoma , vol.118 , pp. 567-574
    • Silva, M.C.1    Jansen, L.E.2
  • 129
    • 77956184148 scopus 로고    scopus 로고
    • The histone shuffle: histone chaperones in an energetic dance
    • Das C., Tyler J.K., Churchill M.E. The histone shuffle: histone chaperones in an energetic dance. Trends Biochem. Sci. 2010, 35:476-489.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 476-489
    • Das, C.1    Tyler, J.K.2    Churchill, M.E.3
  • 130
    • 79957865318 scopus 로고    scopus 로고
    • Cell cycle dynamics of histone variants at the centromere, a model for chromosomal landmarks
    • Boyarchuk E., Montes de Oca R., Almouzni G. Cell cycle dynamics of histone variants at the centromere, a model for chromosomal landmarks. Curr. Opin. Cell Biol. 2011, 23:1-11.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 1-11
    • Boyarchuk, E.1    Montes de Oca, R.2    Almouzni, G.3
  • 132
    • 0018525174 scopus 로고
    • Modification of histones immediately following synthesis
    • Sealy L., Chalkley R. Modification of histones immediately following synthesis. Arch. Biochem. Biophys. 1979, 197:78-82.
    • (1979) Arch. Biochem. Biophys. , vol.197 , pp. 78-82
    • Sealy, L.1    Chalkley, R.2
  • 133
    • 33749657892 scopus 로고    scopus 로고
    • PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state
    • Loyola A., Bonaldi T., Roche D., Imhof A., Almouzni G. PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state. Mol. Cell 2006, 24:309-316.
    • (2006) Mol. Cell , vol.24 , pp. 309-316
    • Loyola, A.1    Bonaldi, T.2    Roche, D.3    Imhof, A.4    Almouzni, G.5
  • 134
    • 77649268110 scopus 로고    scopus 로고
    • Replication stress interferes with histone recycling and predeposition marking of new histones
    • Jasencakova Z., Scharf A.N., Ask K., Corpet A., Imhof A., Almouzni G., Groth A. Replication stress interferes with histone recycling and predeposition marking of new histones. Mol. Cell 2010, 37:736-743.
    • (2010) Mol. Cell , vol.37 , pp. 736-743
    • Jasencakova, Z.1    Scharf, A.N.2    Ask, K.3    Corpet, A.4    Imhof, A.5    Almouzni, G.6    Groth, A.7
  • 136
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
    • Li Q., Zhou H., Wurtele H., Davies B., Horazdovsky B., Verreault A., Zhang Z. Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 2008, 134:244-255.
    • (2008) Cell , vol.134 , pp. 244-255
    • Li, Q.1    Zhou, H.2    Wurtele, H.3    Davies, B.4    Horazdovsky, B.5    Verreault, A.6    Zhang, Z.7
  • 137
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • Chen C.C., Carson J.J., Feser J., Tamburini B., Zabaronick S., Linger J., Tyler J.K. Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 2008, 134:231-243.
    • (2008) Cell , vol.134 , pp. 231-243
    • Chen, C.C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5    Linger, J.6    Tyler, J.K.7
  • 139
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto H., Hawke D., Kobayashi R., Verreault A. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 2005, 436:294-298.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 141
    • 70450223335 scopus 로고    scopus 로고
    • A negatively charged residue in place of histone H3K56 supports chromatin assembly factor association but not genotoxic stress resistance
    • Erkmann J.A., Kaufman P.D. A negatively charged residue in place of histone H3K56 supports chromatin assembly factor association but not genotoxic stress resistance. DNA Repair (Amst) 2009, 8:1371-1379.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 1371-1379
    • Erkmann, J.A.1    Kaufman, P.D.2
  • 143
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das C., Lucia M.S., Hansen K.C., Tyler J.K. CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 2009, 459:113-117.
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 145
    • 67650409769 scopus 로고    scopus 로고
    • Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells
    • Tjeertes J.V., Miller K.M., Jackson S.P. Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells. EMBO J. 2009, 28:1878-1889.
    • (2009) EMBO J. , vol.28 , pp. 1878-1889
    • Tjeertes, J.V.1    Miller, K.M.2    Jackson, S.P.3
  • 146
    • 67650462882 scopus 로고    scopus 로고
    • A histone code for the DNA damage response in mammalian cells?
    • Corpet A., Almouzni G. A histone code for the DNA damage response in mammalian cells?. EMBO J. 2009, 28:1828-1830.
    • (2009) EMBO J. , vol.28 , pp. 1828-1830
    • Corpet, A.1    Almouzni, G.2
  • 147
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan J., Pu M., Zhang Z., Lou Z. Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 2009, 8:1747-1753.
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4
  • 148
    • 0017164570 scopus 로고
    • Deposition of histone onto the replicating chromosome: newly synthesized histone is not found near the replication fork
    • Jackson V., Granner D., Chalkley R. Deposition of histone onto the replicating chromosome: newly synthesized histone is not found near the replication fork. Proc. Natl. Acad. Sci. U. S. A. 1976, 73:2266-2269.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2266-2269
    • Jackson, V.1    Granner, D.2    Chalkley, R.3
  • 149
    • 0017129675 scopus 로고
    • Temporal relationships of chromatin protein synthesis, DNA synthesis, and assembly of deoxyribonucleoprotein
    • Seale R.L. Temporal relationships of chromatin protein synthesis, DNA synthesis, and assembly of deoxyribonucleoprotein. Proc. Natl. Acad. Sci. U. S. A. 1976, 73:2270-2274.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2270-2274
    • Seale, R.L.1
  • 150
    • 0017899059 scopus 로고
    • Assembly of new nucleosomal histones and new DNA into chromatin
    • Hancock R. Assembly of new nucleosomal histones and new DNA into chromatin. Proc. Natl. Acad. Sci. U. S. A. 1978, 75:2130-2134.
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 2130-2134
    • Hancock, R.1
  • 152
    • 0019351449 scopus 로고
    • A new method for the isolation of replicative chromatin: selective deposition of histone on both new and old DNA
    • Jackson V., Chalkley R. A new method for the isolation of replicative chromatin: selective deposition of histone on both new and old DNA. Cell 1981, 23:121-134.
    • (1981) Cell , vol.23 , pp. 121-134
    • Jackson, V.1    Chalkley, R.2
  • 153
    • 0018022824 scopus 로고
    • Preferential association of newly synthesized H3 and H4 histones with newly replicated DNA
    • Senshu T., Fukuda M., Ohashi M. Preferential association of newly synthesized H3 and H4 histones with newly replicated DNA. J. Biochem. (Tokyo) 1978, 84:985-988.
    • (1978) J. Biochem. (Tokyo) , vol.84 , pp. 985-988
    • Senshu, T.1    Fukuda, M.2    Ohashi, M.3
  • 154
    • 0019023551 scopus 로고
    • Isolation of newly replicated chromatin by using shallow metrizamide gradients
    • Murphy R.F., Wallace R.B., Bonner J. Isolation of newly replicated chromatin by using shallow metrizamide gradients. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:3336-3340.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 3336-3340
    • Murphy, R.F.1    Wallace, R.B.2    Bonner, J.3
  • 155
    • 0019888372 scopus 로고
    • Formation of hybrid nucleosomes cantaining new and old histones
    • Russev G., Hancock R. Formation of hybrid nucleosomes cantaining new and old histones. Nucleic Acids Res. 1981, 9:4129-4137.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 4129-4137
    • Russev, G.1    Hancock, R.2
  • 156
    • 0021865469 scopus 로고
    • Fractionation of newly replicated nucleosomes by density labeling and rate zonal centrifugation for the analysis of the deposition sites of newly synthesized nucleosomal core histones
    • Senshu T., Yamasu K., Ohsawa T. Fractionation of newly replicated nucleosomes by density labeling and rate zonal centrifugation for the analysis of the deposition sites of newly synthesized nucleosomal core histones. Eur. J. Biochem. 1985, 150:575-5780.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 575-5780
    • Senshu, T.1    Yamasu, K.2    Ohsawa, T.3
  • 157
    • 0017741826 scopus 로고
    • Preferential association of newly synthesized histones with replicating SV40 DNA
    • Cremisi C., Chestier A., Yaniv M. Preferential association of newly synthesized histones with replicating SV40 DNA. Cell 1977, 12:947-951.
    • (1977) Cell , vol.12 , pp. 947-951
    • Cremisi, C.1    Chestier, A.2    Yaniv, M.3
  • 158
    • 0019333799 scopus 로고
    • Sequential assembly of newly synthesized histones on replicating SV40 DNA
    • Cremisi C., Yaniv M. Sequential assembly of newly synthesized histones on replicating SV40 DNA. Biochem. Biophys. Res. Commun. 1980, 92:1117-1123.
    • (1980) Biochem. Biophys. Res. Commun. , vol.92 , pp. 1117-1123
    • Cremisi, C.1    Yaniv, M.2
  • 159
    • 0017674014 scopus 로고
    • Electron microscopic analysis of chromosome metabolism in the Drosophila melanogaster embryo
    • McKnight S.L., Bustin M., Miller O.L. Electron microscopic analysis of chromosome metabolism in the Drosophila melanogaster embryo. Cold Spring Harb. Symp. Quant. Biol. 1978, 42(Pt 2):741-754.
    • (1978) Cold Spring Harb. Symp. Quant. Biol. , vol.42 , Issue.PART 2 , pp. 741-754
    • McKnight, S.L.1    Bustin, M.2    Miller, O.L.3
  • 160
    • 0017860932 scopus 로고
    • Nascent DNA in nucleosome like structures from chromatin
    • Levy A., Jakob K.M. Nascent DNA in nucleosome like structures from chromatin. Cell 1978, 14:259-267.
    • (1978) Cell , vol.14 , pp. 259-267
    • Levy, A.1    Jakob, K.M.2
  • 161
    • 0019888448 scopus 로고
    • The sites of deposition of newly synthesized histone
    • Jackson V., Marshall S., Chalkley R. The sites of deposition of newly synthesized histone. Nucleic Acids Res. 1981, 9:4563-4581.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 4563-4581
    • Jackson, V.1    Marshall, S.2    Chalkley, R.3
  • 162
    • 0020490906 scopus 로고
    • Association of newly synthesized histones with replicating and nonreplicating regions of chromatin
    • Annunziato A.T., Schindler R.K., Riggs M.G., Seale R.L. Association of newly synthesized histones with replicating and nonreplicating regions of chromatin. J. Biol. Chem. 1982, 257:8507-8515.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8507-8515
    • Annunziato, A.T.1    Schindler, R.K.2    Riggs, M.G.3    Seale, R.L.4
  • 163
    • 0021112529 scopus 로고
    • Chromatin assembled in the presence of cytosine arabinoside has a short nucleosome repeat
    • Leffak I.M. Chromatin assembled in the presence of cytosine arabinoside has a short nucleosome repeat. Nucleic Acids Res. 1983, 11:5451-5466.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 5451-5466
    • Leffak, I.M.1
  • 164
    • 0023845207 scopus 로고
    • Nonrandom assembly of chromatin during hydroxyurea inhibition of DNA synthesis
    • Leffak M. Nonrandom assembly of chromatin during hydroxyurea inhibition of DNA synthesis. Biochemistry 1988, 27:686-691.
    • (1988) Biochemistry , vol.27 , pp. 686-691
    • Leffak, M.1
  • 165
    • 0022546114 scopus 로고
    • Assembly of active chromatin
    • Kumar S., Leffak M. Assembly of active chromatin. Biochemistry 1986, 25:2055-2060.
    • (1986) Biochemistry , vol.25 , pp. 2055-2060
    • Kumar, S.1    Leffak, M.2
  • 166
    • 0022393483 scopus 로고
    • Histone synthesis and deposition in the G1 and S phases of hepatoma tissue culture cells
    • Jackson V., Chalkley R. Histone synthesis and deposition in the G1 and S phases of hepatoma tissue culture cells. Biochemistry 1985, 24:6921-6930.
    • (1985) Biochemistry , vol.24 , pp. 6921-6930
    • Jackson, V.1    Chalkley, R.2
  • 167
    • 0023945277 scopus 로고
    • Deposition of newly synthesized histones: hybrid nucleosomes are not tandemly arranged on daughter DNA strands
    • Jackson V. Deposition of newly synthesized histones: hybrid nucleosomes are not tandemly arranged on daughter DNA strands. Biochemistry 1988, 27:2109-2120.
    • (1988) Biochemistry , vol.27 , pp. 2109-2120
    • Jackson, V.1
  • 168
    • 0023248714 scopus 로고
    • Deposition of newly synthesized histones: new histones H2A and H2B do not deposit in the same nucleosome with new histones H3 and H4
    • Jackson V. Deposition of newly synthesized histones: new histones H2A and H2B do not deposit in the same nucleosome with new histones H3 and H4. Biochemistry 1987, 26:2315-2325.
    • (1987) Biochemistry , vol.26 , pp. 2315-2325
    • Jackson, V.1
  • 169
    • 0023277045 scopus 로고
    • Deposition of newly synthesized histones: misinterpretations due to cross-linking density-labeled proteins with Lomant's reagent
    • Jackson V. Deposition of newly synthesized histones: misinterpretations due to cross-linking density-labeled proteins with Lomant's reagent. Biochemistry 1987, 26:2325-2334.
    • (1987) Biochemistry , vol.26 , pp. 2325-2334
    • Jackson, V.1
  • 170
    • 0023316479 scopus 로고
    • Reassembly of nucleosomal histone octamers during replication of chromatin
    • Yamasu K., Senshu T. Reassembly of nucleosomal histone octamers during replication of chromatin. J. Biochem. 1987, 101:1041-1049.
    • (1987) J. Biochem. , vol.101 , pp. 1041-1049
    • Yamasu, K.1    Senshu, T.2
  • 171
    • 0022423470 scopus 로고
    • Histone H1 and HMG 14/17 are deposited nonrandomly in the nucleus
    • Leffak M., Trempe J.P. Histone H1 and HMG 14/17 are deposited nonrandomly in the nucleus. Nucleic Acids Res. 1985, 13:4853-4869.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 4853-4869
    • Leffak, M.1    Trempe, J.P.2
  • 172
    • 0029946736 scopus 로고    scopus 로고
    • Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays
    • Ito T., Bulger M., Kobayashi R., Kadonaga J.T. Drosophila NAP-1 is a core histone chaperone that functions in ATP-facilitated assembly of regularly spaced nucleosomal arrays. Mol. Cell. Biol. 1996, 16:3112-3124.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3112-3124
    • Ito, T.1    Bulger, M.2    Kobayashi, R.3    Kadonaga, J.T.4
  • 173
    • 0031026487 scopus 로고    scopus 로고
    • Histones in transit: cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells
    • Chang L., Loranger S.S., Mizzen C., Ernst S.G., Allis C.D., Annunziato A.T. Histones in transit: cytosolic histone complexes and diacetylation of H4 during nucleosome assembly in human cells. Biochemistry 1997, 36:469-480.
    • (1997) Biochemistry , vol.36 , pp. 469-480
    • Chang, L.1    Loranger, S.S.2    Mizzen, C.3    Ernst, S.G.4    Allis, C.D.5    Annunziato, A.T.6
  • 174
    • 0021796444 scopus 로고
    • Exchange of histones H1, H2A, and H2B in vivo
    • Louters L., Chalkley R. Exchange of histones H1, H2A, and H2B in vivo. Biochemistry 1985, 24:3080-3085.
    • (1985) Biochemistry , vol.24 , pp. 3080-3085
    • Louters, L.1    Chalkley, R.2
  • 175
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura H., Cook P.R. Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B. J. Cell Biol. 2001, 153:1341-1353.
    • (2001) J. Cell Biol. , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 176
    • 0025089206 scopus 로고
    • Nucleosomal histones of transcriptionally active/competent chromatin preferentially exchange with newly synthesized histones in quiescent chicken erythrocytes
    • Hendzel M.J., Davie J.R. Nucleosomal histones of transcriptionally active/competent chromatin preferentially exchange with newly synthesized histones in quiescent chicken erythrocytes. Biochem. J. 1990, 271:67-73.
    • (1990) Biochem. J. , vol.271 , pp. 67-73
    • Hendzel, M.J.1    Davie, J.R.2
  • 177
    • 0027743318 scopus 로고
    • Analysis of nucleosome assembly and histone exchange using antibodies specific for acetylated H4
    • Perry C.A., Dadd C.A., Allis C.D., Annunziato A.T. Analysis of nucleosome assembly and histone exchange using antibodies specific for acetylated H4. Biochemistry 1993, 32:13605-13614.
    • (1993) Biochemistry , vol.32 , pp. 13605-13614
    • Perry, C.A.1    Dadd, C.A.2    Allis, C.D.3    Annunziato, A.T.4
  • 178
    • 15444376394 scopus 로고    scopus 로고
    • Replication-independent core histone dynamics at transcriptionally active loci in vivo
    • Thiriet C., Hayes J.J. Replication-independent core histone dynamics at transcriptionally active loci in vivo. Gene Dev. 2005, 19:677-682.
    • (2005) Gene Dev. , vol.19 , pp. 677-682
    • Thiriet, C.1    Hayes, J.J.2
  • 179
    • 34247328546 scopus 로고    scopus 로고
    • Histone dynamics during transcription: exchange of H2A/H2B dimers and H3/H4 tetramers during pol II elongation
    • Thiriet C., Hayes J.J. Histone dynamics during transcription: exchange of H2A/H2B dimers and H3/H4 tetramers during pol II elongation. Results Probl. Cell Differ. 2006, 41:77-90.
    • (2006) Results Probl. Cell Differ. , vol.41 , pp. 77-90
    • Thiriet, C.1    Hayes, J.J.2
  • 180
    • 0033582544 scopus 로고    scopus 로고
    • Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin
    • Shibahara K., Stillman B. Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin. Cell 1999, 96:575-585.
    • (1999) Cell , vol.96 , pp. 575-585
    • Shibahara, K.1    Stillman, B.2
  • 182
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi G., Shen X.T., Landry J., Wu W.H., Sen S., Wu C. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 2004, 303:343-348.
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.T.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 184
    • 0016687530 scopus 로고
    • Electron microscopic and biochemical evidence that chromatin structure is a repeating unit
    • Oudet P., Gross-Bellard M., Chambon P. Electron microscopic and biochemical evidence that chromatin structure is a repeating unit. Cell 1975, 4:281-300.
    • (1975) Cell , vol.4 , pp. 281-300
    • Oudet, P.1    Gross-Bellard, M.2    Chambon, P.3
  • 185
    • 0017133394 scopus 로고
    • The organization of histones and DNA in chromatin: evidence for an arginine-rich histone kernel
    • Camerini-Otero R.D., Sollner-Webb B., Felsenfeld G. The organization of histones and DNA in chromatin: evidence for an arginine-rich histone kernel. Cell 1976, 8:333-347.
    • (1976) Cell , vol.8 , pp. 333-347
    • Camerini-Otero, R.D.1    Sollner-Webb, B.2    Felsenfeld, G.3
  • 186
    • 0017762802 scopus 로고
    • Reconstitution of chromatin core particles
    • Tatchell K., Van Holde K.E. Reconstitution of chromatin core particles. Biochemistry 1977, 16:5295-5303.
    • (1977) Biochemistry , vol.16 , pp. 5295-5303
    • Tatchell, K.1    Van Holde, K.E.2
  • 187
    • 0017590015 scopus 로고
    • Ultrastructure of chromatin subunits during unfolding, histone depletion, and reconstitution
    • Woodcock C.L., Frado L.L. Ultrastructure of chromatin subunits during unfolding, histone depletion, and reconstitution. Cold Spring Harb. Symp. Quant. Biol. 1978, 42(Pt 1):43-55.
    • (1978) Cold Spring Harb. Symp. Quant. Biol. , vol.42 , Issue.PART 1 , pp. 43-55
    • Woodcock, C.L.1    Frado, L.L.2
  • 188
    • 79953228495 scopus 로고    scopus 로고
    • Histones, histone chaperones and nucleosome assembly
    • Burgess R.J., Zhang Z. Histones, histone chaperones and nucleosome assembly. Protein Cell 2010, 1:607-612.
    • (2010) Protein Cell , vol.1 , pp. 607-612
    • Burgess, R.J.1    Zhang, Z.2
  • 189
    • 38949202272 scopus 로고    scopus 로고
    • Histone chaperones: 30years from isolation to elucidation of the mechanisms of nucleosome assembly and disassembly
    • Eitoku M., Sato L., Senda T., Horikoshi M. Histone chaperones: 30years from isolation to elucidation of the mechanisms of nucleosome assembly and disassembly. Cell. Mol. Life Sci. 2008, 65:414-444.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 414-444
    • Eitoku, M.1    Sato, L.2    Senda, T.3    Horikoshi, M.4
  • 191
    • 0031957859 scopus 로고    scopus 로고
    • A topological approach to nucleosome structure and dynamics: the linking number paradox and other issues
    • Prunell A. A topological approach to nucleosome structure and dynamics: the linking number paradox and other issues. Biophys. J. 1998, 74:2531-2544.
    • (1998) Biophys. J. , vol.74 , pp. 2531-2544
    • Prunell, A.1
  • 192
    • 0019211644 scopus 로고
    • DNA is assembled into globular supranucleosomal chromatin structures by nuclear contents of amphibian oocytes
    • Scheer U., Sommerville J., Muller U. DNA is assembled into globular supranucleosomal chromatin structures by nuclear contents of amphibian oocytes. Exp. Cell Res. 1980, 129:115-126.
    • (1980) Exp. Cell Res. , vol.129 , pp. 115-126
    • Scheer, U.1    Sommerville, J.2    Muller, U.3
  • 193
    • 1642489179 scopus 로고
    • Extracts of Drosophila embryos mediate chromatin assembly in vitro
    • Nelson T., Hsieh T.S., Brutlag D. Extracts of Drosophila embryos mediate chromatin assembly in vitro. Proc. Natl. Acad. Sci. U. S. A. 1979, 76:5510-5514.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 5510-5514
    • Nelson, T.1    Hsieh, T.S.2    Brutlag, D.3
  • 194
    • 0029618706 scopus 로고
    • Assembly of regularly spaced nucleosome arrays by Drosophila chromatin assembly factor 1 and a 56-kDa histone-binding protein
    • Bulger M., Ito T., Kamakaka R.T., Kadonaga J.T. Assembly of regularly spaced nucleosome arrays by Drosophila chromatin assembly factor 1 and a 56-kDa histone-binding protein. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:11726-11730.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11726-11730
    • Bulger, M.1    Ito, T.2    Kamakaka, R.T.3    Kadonaga, J.T.4
  • 195
    • 0017330474 scopus 로고
    • The synthesis and storage of histones during the oogenesis of Xenopus laevis
    • Woodland H.R., Adamson E.D. The synthesis and storage of histones during the oogenesis of Xenopus laevis. Dev. Biol. 1977, 57:118-135.
    • (1977) Dev. Biol. , vol.57 , pp. 118-135
    • Woodland, H.R.1    Adamson, E.D.2
  • 196
    • 0017617464 scopus 로고
    • Assembly of SV40 chromatin in a cell-free system from Xenopus eggs
    • Laskey R.A., Mills A.D., Morris N.R. Assembly of SV40 chromatin in a cell-free system from Xenopus eggs. Cell 1977, 10:237-243.
    • (1977) Cell , vol.10 , pp. 237-243
    • Laskey, R.A.1    Mills, A.D.2    Morris, N.R.3
  • 197
    • 0017881614 scopus 로고
    • Selective DNA conservation and chromatin assembly after injection of SV40 DNA into Xenopus oocytes
    • Wyllie A.H., Laskey R.A., Finch J., Gurdon J.B. Selective DNA conservation and chromatin assembly after injection of SV40 DNA into Xenopus oocytes. Dev. Biol. 1978, 64:178-188.
    • (1978) Dev. Biol. , vol.64 , pp. 178-188
    • Wyllie, A.H.1    Laskey, R.A.2    Finch, J.3    Gurdon, J.B.4
  • 198
    • 0018221572 scopus 로고
    • Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
    • Laskey R.A., Honda B.M., Mills A.D., Finch J.T. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature 1978, 275:416-420.
    • (1978) Nature , vol.275 , pp. 416-420
    • Laskey, R.A.1    Honda, B.M.2    Mills, A.D.3    Finch, J.T.4
  • 199
    • 0018959726 scopus 로고
    • Assembly of nucleosomes: the reaction involving X. laevis nucleoplasmin
    • Earnshaw W.C., Honda B.M., Laskey R.A., Thomas J.O. Assembly of nucleosomes: the reaction involving X. laevis nucleoplasmin. Cell 1980, 21:373-383.
    • (1980) Cell , vol.21 , pp. 373-383
    • Earnshaw, W.C.1    Honda, B.M.2    Laskey, R.A.3    Thomas, J.O.4
  • 200
    • 0023053350 scopus 로고
    • Xenopus nucleoplasmin: egg vs. oocyte
    • Sealy L., Cotten M., Chalkley R. Xenopus nucleoplasmin: egg vs. oocyte. Biochemistry 1986, 25:3064-3072.
    • (1986) Biochemistry , vol.25 , pp. 3064-3072
    • Sealy, L.1    Cotten, M.2    Chalkley, R.3
  • 201
    • 0342547994 scopus 로고
    • Immunological identification and localization of the predominant nuclear protein of the amphibian oocyte nucleus
    • Krohne G., Franke W.W. Immunological identification and localization of the predominant nuclear protein of the amphibian oocyte nucleus. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:1034-1038.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 1034-1038
    • Krohne, G.1    Franke, W.W.2
  • 202
    • 0019120765 scopus 로고
    • A major soluble acidic protein located in nuclei of diverse vertebrate species
    • Krohne G., Franke W.W. A major soluble acidic protein located in nuclei of diverse vertebrate species. Exp. Cell Res. 1980, 129:167-189.
    • (1980) Exp. Cell Res. , vol.129 , pp. 167-189
    • Krohne, G.1    Franke, W.W.2
  • 203
    • 0021076839 scopus 로고
    • Two-dimensional gel analysis of the fate of oocyte nuclear proteins in the development of Xenopus laevis
    • Dreyer C., Hausen P. Two-dimensional gel analysis of the fate of oocyte nuclear proteins in the development of Xenopus laevis. Dev. Biol. 1983, 100:412-425.
    • (1983) Dev. Biol. , vol.100 , pp. 412-425
    • Dreyer, C.1    Hausen, P.2
  • 204
    • 0016430929 scopus 로고
    • Protein migration into nuclei. II. Frog oocyte nuclei accumulate a class of microinjected oocyte nuclear proteins and exclude a class of microinjected oocyte cytoplasmic proteins
    • Bonner W.M. Protein migration into nuclei. II. Frog oocyte nuclei accumulate a class of microinjected oocyte nuclear proteins and exclude a class of microinjected oocyte cytoplasmic proteins. J. Cell Biol. 1975, 64:431-437.
    • (1975) J. Cell Biol. , vol.64 , pp. 431-437
    • Bonner, W.M.1
  • 205
    • 0017835239 scopus 로고
    • Intracellular migration of nuclear proteins in Xenopus oocytes
    • De Robertis E.M., Longthorne R.F., Gurdon J.B. Intracellular migration of nuclear proteins in Xenopus oocytes. Nature 1978, 272:254-256.
    • (1978) Nature , vol.272 , pp. 254-256
    • De Robertis, E.M.1    Longthorne, R.F.2    Gurdon, J.B.3
  • 206
    • 0020159426 scopus 로고
    • Soluble acidic complexes containing histones H3 and H4 in nuclei of Xenopus laevis oocytes
    • Kleinschmidt J.A., Franke W.W. Soluble acidic complexes containing histones H3 and H4 in nuclei of Xenopus laevis oocytes. Cell 1982, 29:799-809.
    • (1982) Cell , vol.29 , pp. 799-809
    • Kleinschmidt, J.A.1    Franke, W.W.2
  • 207
    • 0022006731 scopus 로고
    • Co-existence of two different types of soluble histone complexes in nuclei of Xenopus laevis oocytes
    • Kleinschmidt J.A., Fortkamp E., Krohne G., Zentgraf H., Franke W.W. Co-existence of two different types of soluble histone complexes in nuclei of Xenopus laevis oocytes. J. Biol. Chem. 1985, 260:1166-1176.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1166-1176
    • Kleinschmidt, J.A.1    Fortkamp, E.2    Krohne, G.3    Zentgraf, H.4    Franke, W.W.5
  • 208
    • 0023663912 scopus 로고
    • Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus oocytes
    • Dilworth S.M., Black S.J., Laskey R.L. Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus oocytes. Cell 1987, 51:1009-1018.
    • (1987) Cell , vol.51 , pp. 1009-1018
    • Dilworth, S.M.1    Black, S.J.2    Laskey, R.L.3
  • 209
    • 0025266048 scopus 로고
    • Nucleosome assembly in vitro: separate transfer and synergistic interaction of native histone complexes purified from nuclei of Xenopus laevis oocytes
    • Kleinschmidt J.A., Seiter A., Zentgraf H. Nucleosome assembly in vitro: separate transfer and synergistic interaction of native histone complexes purified from nuclei of Xenopus laevis oocytes. EMBO J. 1990, 9:1309-1318.
    • (1990) EMBO J. , vol.9 , pp. 1309-1318
    • Kleinschmidt, J.A.1    Seiter, A.2    Zentgraf, H.3
  • 210
    • 33846597441 scopus 로고    scopus 로고
    • New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones
    • Frehlick L.J., Eirin-Lopez J.M., Ausio J. New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones. Bioessays 2007, 29:49-59.
    • (2007) Bioessays , vol.29 , pp. 49-59
    • Frehlick, L.J.1    Eirin-Lopez, J.M.2    Ausio, J.3
  • 211
    • 1942502859 scopus 로고    scopus 로고
    • The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly
    • Ai X., Parthun M.R. The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly. Mol. Cell 2004, 14:195-205.
    • (2004) Mol. Cell , vol.14 , pp. 195-205
    • Ai, X.1    Parthun, M.R.2
  • 213
    • 33748929687 scopus 로고    scopus 로고
    • The PLZF-like protein TRA-4 cooperates with the Gli-like transcription factor TRA-1 to promote female development in C. elegans
    • Grote P., Conradt B. The PLZF-like protein TRA-4 cooperates with the Gli-like transcription factor TRA-1 to promote female development in C. elegans. Dev. Cell 2006, 11:561-573.
    • (2006) Dev. Cell , vol.11 , pp. 561-573
    • Grote, P.1    Conradt, B.2
  • 214
    • 0026472435 scopus 로고
    • Sequence and localization of human NASP: conservation of a Xenopus histone-binding protein
    • O'Rand M.G., Richardson R.T., Zimmerman L.J., Widgren E.E. Sequence and localization of human NASP: conservation of a Xenopus histone-binding protein. Dev. Biol. 1992, 154:37-44.
    • (1992) Dev. Biol. , vol.154 , pp. 37-44
    • O'Rand, M.G.1    Richardson, R.T.2    Zimmerman, L.J.3    Widgren, E.E.4
  • 217
    • 51049086205 scopus 로고    scopus 로고
    • SNASP, a histone H1-specific eukaryotic chaperone dimer that facilitates chromatin assembly
    • Finn R.M., Browne K., Hodgson K.C., Ausio J. sNASP, a histone H1-specific eukaryotic chaperone dimer that facilitates chromatin assembly. Biophys. J. 2008, 95:1314-1325.
    • (2008) Biophys. J. , vol.95 , pp. 1314-1325
    • Finn, R.M.1    Browne, K.2    Hodgson, K.C.3    Ausio, J.4
  • 218
    • 54549118247 scopus 로고    scopus 로고
    • Expanded binding specificity of the human histone chaperone NASP
    • Wang H., Walsh S.T., Parthun M.R. Expanded binding specificity of the human histone chaperone NASP. Nucleic Acids Res. 2008, 36:5763-5772.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5763-5772
    • Wang, H.1    Walsh, S.T.2    Parthun, M.R.3
  • 220
    • 0020282938 scopus 로고
    • Properties of the chromatin assembled on DNA injected into Xenopus oocytes and eggs
    • Gargiulo G., Wasserman W., Worcel A. Properties of the chromatin assembled on DNA injected into Xenopus oocytes and eggs. Cold Spring Harb. Symp. Quant. Biol. 1983, 47(Pt 1):549-556.
    • (1983) Cold Spring Harb. Symp. Quant. Biol. , vol.47 , Issue.PART 1 , pp. 549-556
    • Gargiulo, G.1    Wasserman, W.2    Worcel, A.3
  • 221
    • 0022363877 scopus 로고
    • Structure of the two distinct types of minichromosomes that are assembled on DNA injected in Xenopus oocytes
    • Ryoji M., Worcel A. Structure of the two distinct types of minichromosomes that are assembled on DNA injected in Xenopus oocytes. Cell 1985, 40:923-932.
    • (1985) Cell , vol.40 , pp. 923-932
    • Ryoji, M.1    Worcel, A.2
  • 222
    • 0002727389 scopus 로고    scopus 로고
    • Chromatin structure and DNA replication: implications for transcriptional activity
    • Cold Spring Harbor Laboratory Press, New York, M.L. DePamphilis (Ed.)
    • Wolffe A.P. Chromatin structure and DNA replication: implications for transcriptional activity. DNA Replication in Eukaryotic Cells 1996, 271-293. Cold Spring Harbor Laboratory Press, New York. M.L. DePamphilis (Ed.).
    • (1996) DNA Replication in Eukaryotic Cells , pp. 271-293
    • Wolffe, A.P.1
  • 223
    • 0014682838 scopus 로고
    • The replication of purified DNA introduced into living egg cytoplasm
    • Gurdon J.B., Birnstiel M.L., Speight V.A. The replication of purified DNA introduced into living egg cytoplasm. Biochim. Biophys. Acta 1969, 174:614-628.
    • (1969) Biochim. Biophys. Acta , vol.174 , pp. 614-628
    • Gurdon, J.B.1    Birnstiel, M.L.2    Speight, V.A.3
  • 224
    • 0017845120 scopus 로고
    • DNA synthesis in a multi-enzyme system from Xenopus laevis eggs
    • Benbow R.M., Krauss M.R., Reeder R.H. DNA synthesis in a multi-enzyme system from Xenopus laevis eggs. Cell 1978, 13:307-318.
    • (1978) Cell , vol.13 , pp. 307-318
    • Benbow, R.M.1    Krauss, M.R.2    Reeder, R.H.3
  • 225
    • 0019878183 scopus 로고
    • Replication of SV40 chromatin in extracts from eggs of Xenopus laevis
    • Richter A., Otto B., Knippers R. Replication of SV40 chromatin in extracts from eggs of Xenopus laevis. Nucleic Acids Res. 1981, 9:3793-37807.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 3793-37807
    • Richter, A.1    Otto, B.2    Knippers, R.3
  • 226
    • 0022981734 scopus 로고
    • Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs
    • Blow J.J., Laskey R.A. Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs. Cell 1986, 47:577-587.
    • (1986) Cell , vol.47 , pp. 577-587
    • Blow, J.J.1    Laskey, R.A.2
  • 227
    • 0021003728 scopus 로고
    • Induction of chromosome replication during maturation of amphibian oocytes
    • Laskey R.A., Harland R.M., Mechali M. Induction of chromosome replication during maturation of amphibian oocytes. CIBA Found. Symp. 1983, 98:25-43.
    • (1983) CIBA Found. Symp. , vol.98 , pp. 25-43
    • Laskey, R.A.1    Harland, R.M.2    Mechali, M.3
  • 228
    • 0020417651 scopus 로고
    • DNA synthesis in a cell-free system from Xenopus eggs: priming and elongation on single-stranded DNA in vitro
    • Mechali M., Harland R.M. DNA synthesis in a cell-free system from Xenopus eggs: priming and elongation on single-stranded DNA in vitro. Cell 1982, 30:93-101.
    • (1982) Cell , vol.30 , pp. 93-101
    • Mechali, M.1    Harland, R.M.2
  • 229
    • 0023975123 scopus 로고
    • Assembly of spaced chromatin promoted by DNA synthesis in extracts from Xenopus eggs
    • Almouzni G., Méchali M. Assembly of spaced chromatin promoted by DNA synthesis in extracts from Xenopus eggs. EMBO J. 1988, 665-672.
    • (1988) EMBO J. , pp. 665-672
    • Almouzni, G.1    Méchali, M.2
  • 231
    • 0018267908 scopus 로고
    • Effect of inhibition of DNA synthesis on histone synthesis and deposition
    • Nadeau P., Oliver D.R., Chalkley R. Effect of inhibition of DNA synthesis on histone synthesis and deposition. Biochemistry 1978, 17:4885-4893.
    • (1978) Biochemistry , vol.17 , pp. 4885-4893
    • Nadeau, P.1    Oliver, D.R.2    Chalkley, R.3
  • 232
    • 0019304757 scopus 로고
    • Histone exchange in chromatin of hydroxyurea-blocked Ehrlich ascites tumour cells
    • Russev G., Vassilev L., Tsanev R. Histone exchange in chromatin of hydroxyurea-blocked Ehrlich ascites tumour cells. Nature 1980, 285:584-586.
    • (1980) Nature , vol.285 , pp. 584-586
    • Russev, G.1    Vassilev, L.2    Tsanev, R.3
  • 233
    • 0021774173 scopus 로고
    • In vitro exchange of nucleosomal histones H2A and H2B
    • Louters L., Chalkley R. In vitro exchange of nucleosomal histones H2A and H2B. Biochemistry 1984, 23:547-552.
    • (1984) Biochemistry , vol.23 , pp. 547-552
    • Louters, L.1    Chalkley, R.2
  • 234
    • 0023793586 scopus 로고
    • Kinetics of accumulation and depletion of soluble newly synthesized histone in the reciprocal regulation of histone and DNA synthesis
    • Bonner W.M., Wu R.S., Panusz H.T., Muneses C. Kinetics of accumulation and depletion of soluble newly synthesized histone in the reciprocal regulation of histone and DNA synthesis. Biochemistry 1988, 27:6542-6550.
    • (1988) Biochemistry , vol.27 , pp. 6542-6550
    • Bonner, W.M.1    Wu, R.S.2    Panusz, H.T.3    Muneses, C.4
  • 235
    • 0018539353 scopus 로고
    • Fate of newly synthesized histones shortly after interruption of DNA replication
    • Senshu T., Ohashi M. Fate of newly synthesized histones shortly after interruption of DNA replication. J. Biochem. 1979, 86:1259-1267.
    • (1979) J. Biochem. , vol.86 , pp. 1259-1267
    • Senshu, T.1    Ohashi, M.2
  • 236
    • 0019198648 scopus 로고
    • Two-dimensional gel analysis of histones in acid extracts of nuclei, cells, and tissues
    • Bonner W.M., West M.H., Stedman J.D. Two-dimensional gel analysis of histones in acid extracts of nuclei, cells, and tissues. Eur. J. Biochem. 1980, 109:17-23.
    • (1980) Eur. J. Biochem. , vol.109 , pp. 17-23
    • Bonner, W.M.1    West, M.H.2    Stedman, J.D.3
  • 237
    • 0019024068 scopus 로고
    • Involvement of cytoplasmic soluble fraction in the assembly of nucleosome-like materials under near physiological conditions
    • Senshu T., Yamada F. Involvement of cytoplasmic soluble fraction in the assembly of nucleosome-like materials under near physiological conditions. J. Biochem. 1980, 87:1659-1668.
    • (1980) J. Biochem. , vol.87 , pp. 1659-1668
    • Senshu, T.1    Yamada, F.2
  • 238
    • 0020816370 scopus 로고
    • A protein which facilitates the assembly of nucleosome-like structures in vitro in mammalian cells
    • Ishimi Y., Yasuda H., Hirosumi J., Hanaoka F., Yamada M.-a. A protein which facilitates the assembly of nucleosome-like structures in vitro in mammalian cells. J. Biochem. 1983, 94:735-744.
    • (1983) J. Biochem. , vol.94 , pp. 735-744
    • Ishimi, Y.1    Yasuda, H.2    Hirosumi, J.3    Hanaoka, F.4    Yamada, M.-A.5
  • 239
    • 0021470855 scopus 로고
    • Purification and initial characterization of a protein which facilitates assembly of nucleosome-like structure from mammalian cells
    • Ishimi Y., Hirosumi J., Sato W., Sugasawa K., Yokota S., Hanoaoka F., Yamada M.-a. Purification and initial characterization of a protein which facilitates assembly of nucleosome-like structure from mammalian cells. Eur. J. Biochem. 1984, 142:431-439.
    • (1984) Eur. J. Biochem. , vol.142 , pp. 431-439
    • Ishimi, Y.1    Hirosumi, J.2    Sato, W.3    Sugasawa, K.4    Yokota, S.5    Hanoaoka, F.6    Yamada, M.-A.7
  • 240
    • 0023105676 scopus 로고
    • Binding mode of nucleosome-assembly protein (AP-I) and histones
    • Ishimi Y., Kojima M., Yamada M., Hanaoka F. Binding mode of nucleosome-assembly protein (AP-I) and histones. Eur. J. Biochem. 1987, 162:19-24.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 19-24
    • Ishimi, Y.1    Kojima, M.2    Yamada, M.3    Hanaoka, F.4
  • 241
    • 0025816844 scopus 로고
    • Identification and molecular cloning of yeast homolog of nucleosome assembly protein-I which facilitates nucleosome assembly invitro
    • Ishimi Y., Kikuchi A. Identification and molecular cloning of yeast homolog of nucleosome assembly protein-I which facilitates nucleosome assembly invitro. J. Biol. Chem. 1991, 266:7025-7029.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7025-7029
    • Ishimi, Y.1    Kikuchi, A.2
  • 242
    • 0019890073 scopus 로고
    • Ribonucleic acid and other polyanions facilitate chromatin assembly in vitro
    • Nelson T., Wiegand R., Brutlag D. Ribonucleic acid and other polyanions facilitate chromatin assembly in vitro. Biochemistry 1981, 20:2594-2601.
    • (1981) Biochemistry , vol.20 , pp. 2594-2601
    • Nelson, T.1    Wiegand, R.2    Brutlag, D.3
  • 243
    • 0018531367 scopus 로고
    • Acidic polypeptides can assemble both histones and chromatin in vitro at physiological ionic strength
    • Stein A., Whitlock J.P., Bina M. Acidic polypeptides can assemble both histones and chromatin in vitro at physiological ionic strength. Proc. Natl. Acad. Sci. U. S. A. 1979, 76:5000-5004.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 5000-5004
    • Stein, A.1    Whitlock, J.P.2    Bina, M.3
  • 244
    • 33750693058 scopus 로고    scopus 로고
    • Structure and function of nucleosome assembly proteins
    • Park Y.J., Luger K. Structure and function of nucleosome assembly proteins. Biochem. Cell Biol. 2006, 84:549-558.
    • (2006) Biochem. Cell Biol. , vol.84 , pp. 549-558
    • Park, Y.J.1    Luger, K.2
  • 245
    • 34247619728 scopus 로고    scopus 로고
    • Nap1: taking a closer look at a juggler protein of extraordinary skills
    • Zlatanova J., Seebart C., Tomschik M. Nap1: taking a closer look at a juggler protein of extraordinary skills. FASEB J. 2007, 21:1294-1310.
    • (2007) FASEB J. , vol.21 , pp. 1294-1310
    • Zlatanova, J.1    Seebart, C.2    Tomschik, M.3
  • 246
    • 0034724563 scopus 로고    scopus 로고
    • NAP-2: Histone chaperone function and phosphorylation state through the cell cycle
    • Rodriguez P., Pelletier J., Price G.B., ZannisHadjopoulos M. NAP-2: Histone chaperone function and phosphorylation state through the cell cycle. J. Mol. Biol. 2000, 298:225-238.
    • (2000) J. Mol. Biol. , vol.298 , pp. 225-238
    • Rodriguez, P.1    Pelletier, J.2    Price, G.B.3    ZannisHadjopoulos, M.4
  • 248
    • 0028799432 scopus 로고
    • Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer
    • Walter P.P., Owenhughes T.A., Cote J., Workman J.L. Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer. Mol. Cell. Biol. 1995, 15:6178-6187.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6178-6187
    • Walter, P.P.1    Owenhughes, T.A.2    Cote, J.3    Workman, J.L.4
  • 249
    • 16844366808 scopus 로고    scopus 로고
    • Histone release during transcription: displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress
    • Levchenko V., Jackson B., Jackson V. Histone release during transcription: displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress. Biochemistry 2005, 44:5357-5372.
    • (2005) Biochemistry , vol.44 , pp. 5357-5372
    • Levchenko, V.1    Jackson, B.2    Jackson, V.3
  • 250
    • 12544258222 scopus 로고    scopus 로고
    • Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding
    • Park Y.J., Chodaparambil J.V., Bao Y.H., McBryant S.J., Luger K. Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding. J. Biol. Chem. 2005, 280:1817-1825.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1817-1825
    • Park, Y.J.1    Chodaparambil, J.V.2    Bao, Y.H.3    McBryant, S.J.4    Luger, K.5
  • 252
    • 0037011167 scopus 로고    scopus 로고
    • A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B
    • Mosammaparast N., Ewart C.S., Pemberton L.F. A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B. EMBO J. 2002, 21:6527-6538.
    • (2002) EMBO J. , vol.21 , pp. 6527-6538
    • Mosammaparast, N.1    Ewart, C.S.2    Pemberton, L.F.3
  • 254
    • 26444474558 scopus 로고    scopus 로고
    • Interaction of heterochromatin protein 2 with HP1 defines a novel HP1-binding domain
    • Stephens G.E., Slawson E.E., Craig C.A., Elgin S.C.R. Interaction of heterochromatin protein 2 with HP1 defines a novel HP1-binding domain. Biochemistry USA 2005, 44:13394-13403.
    • (2005) Biochemistry USA , vol.44 , pp. 13394-13403
    • Stephens, G.E.1    Slawson, E.E.2    Craig, C.A.3    Elgin, S.C.R.4
  • 255
    • 0037295514 scopus 로고    scopus 로고
    • Knock-out targeting of the Drosophila Nap1 gene and examination of DNA repair tracts in the recombination products
    • Lankenau S., Barnickel T., Marhold J., Lyko F., Mechler B.M., Lankenau D.H. Knock-out targeting of the Drosophila Nap1 gene and examination of DNA repair tracts in the recombination products. Genetics 2003, 163:611-623.
    • (2003) Genetics , vol.163 , pp. 611-623
    • Lankenau, S.1    Barnickel, T.2    Marhold, J.3    Lyko, F.4    Mechler, B.M.5    Lankenau, D.H.6
  • 258
    • 26644467244 scopus 로고    scopus 로고
    • NAP1 modulates binding of linker histone H1 to chromatin and induces an extended chromatin fiber conformation
    • Kepert J.F., Mazurkiewicz J., Heuvelman G.L., Toth K.F., Rippe K. NAP1 modulates binding of linker histone H1 to chromatin and induces an extended chromatin fiber conformation. J. Biol. Chem. 2005, 280:34063-34072.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34063-34072
    • Kepert, J.F.1    Mazurkiewicz, J.2    Heuvelman, G.L.3    Toth, K.F.4    Rippe, K.5
  • 260
    • 0020501854 scopus 로고
    • Initiation of simian virus 40 DNA replication in vitro
    • Ariga H., Sugano S. Initiation of simian virus 40 DNA replication in vitro. J. Virol. 1983, 48:481-491.
    • (1983) J. Virol. , vol.48 , pp. 481-491
    • Ariga, H.1    Sugano, S.2
  • 262
    • 0021830055 scopus 로고
    • Replication and supercoiling of simian virus 40 DNA in cell extracts from human cells
    • Stillman B.W., Gluzman Y. Replication and supercoiling of simian virus 40 DNA in cell extracts from human cells. Mol. Cell. Biol. 1985, 5:2051-2060.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 2051-2060
    • Stillman, B.W.1    Gluzman, Y.2
  • 263
    • 0022519177 scopus 로고
    • Chromatin assembly during DNA replication in vitro
    • Stillman B. Chromatin assembly during DNA replication in vitro. Cell 1986, 45:555-565.
    • (1986) Cell , vol.45 , pp. 555-565
    • Stillman, B.1
  • 264
    • 0024372060 scopus 로고
    • Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro
    • Smith S., Stillman B. Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro. Cell 1989, 58:15-25.
    • (1989) Cell , vol.58 , pp. 15-25
    • Smith, S.1    Stillman, B.2
  • 265
    • 0026062937 scopus 로고
    • Immunological characterization of chromatin assembly factor-I, a human cell factor required for chromatin assembly during DNA replication in vitro
    • Smith S., Stillman B. Immunological characterization of chromatin assembly factor-I, a human cell factor required for chromatin assembly during DNA replication in vitro. J. Biol. Chem. 1991, 266:12041-12047.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12041-12047
    • Smith, S.1    Stillman, B.2
  • 266
    • 0026079369 scopus 로고
    • Stepwise assembly of chromatin during dna replication in vitro
    • Smith S., Stillman B. Stepwise assembly of chromatin during dna replication in vitro. EMBO J. 1991, 10:971-980.
    • (1991) EMBO J. , vol.10 , pp. 971-980
    • Smith, S.1    Stillman, B.2
  • 267
    • 0015964440 scopus 로고
    • Identification of a distinction between cytoplasmic histone synthesis and subsequent histone deposition
    • Oliver D., Granner D., Chalkley R. Identification of a distinction between cytoplasmic histone synthesis and subsequent histone deposition. Biochemistry 1974, 13:746-749.
    • (1974) Biochemistry , vol.13 , pp. 746-749
    • Oliver, D.1    Granner, D.2    Chalkley, R.3
  • 268
    • 0029011919 scopus 로고
    • The p150 and p60 subunits of chromatin assembly factor I: A molecular link between newly synthesized histones and DNA replication
    • Kaufman P.D., Kobayashi R., Kessler N., Stillman B. The p150 and p60 subunits of chromatin assembly factor I: A molecular link between newly synthesized histones and DNA replication. Cell 1995, 81:1105-1114.
    • (1995) Cell , vol.81 , pp. 1105-1114
    • Kaufman, P.D.1    Kobayashi, R.2    Kessler, N.3    Stillman, B.4
  • 269
    • 0030272047 scopus 로고    scopus 로고
    • Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
    • Verreault A., Kaufman P.D., Kobayashi R., Stillman B. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 1996, 87:95-104.
    • (1996) Cell , vol.87 , pp. 95-104
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 270
    • 0034608938 scopus 로고    scopus 로고
    • The N-terminal domains of histones H3 and H4 are not necessary for chromatin assembly factor-1-mediated nucleosome assembly onto replicated DNA in vitro
    • Shibahara K., Verreault A., Stillman B. The N-terminal domains of histones H3 and H4 are not necessary for chromatin assembly factor-1-mediated nucleosome assembly onto replicated DNA in vitro. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:7766-7771.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7766-7771
    • Shibahara, K.1    Verreault, A.2    Stillman, B.3
  • 271
    • 0030042971 scopus 로고    scopus 로고
    • Postreplicative chromatin assembly by Drosophila and human chromatin assembly factor 1
    • Kamakaka R.T., Bulger M., Kaufman P.D., Stillman B., Kadonaga J.T. Postreplicative chromatin assembly by Drosophila and human chromatin assembly factor 1. Mol. Cell. Biol. 1996, 16:810-817.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 810-817
    • Kamakaka, R.T.1    Bulger, M.2    Kaufman, P.D.3    Stillman, B.4    Kadonaga, J.T.5
  • 273
    • 0031043134 scopus 로고    scopus 로고
    • Ultraviolet radiation sensitivity and reduction of telomeric silencing Saccharomyces cerevisiae cells lacking chromatin assembly factor-I
    • Kaufman P.D., Kobayashi R., Stillman B. Ultraviolet radiation sensitivity and reduction of telomeric silencing Saccharomyces cerevisiae cells lacking chromatin assembly factor-I. Gene Dev. 1997, 11:345-357.
    • (1997) Gene Dev. , vol.11 , pp. 345-357
    • Kaufman, P.D.1    Kobayashi, R.2    Stillman, B.3
  • 274
    • 0031049284 scopus 로고    scopus 로고
    • RLF2, a subunit of yeast chromatin assembly factor-I, is required for telomeric chromatin function in vivo
    • Enomoto S., Mccunezierath P.D., Geraminejad M., Sanders M.A., Berman J. RLF2, a subunit of yeast chromatin assembly factor-I, is required for telomeric chromatin function in vivo. Gene Dev. 1997, 11:358-370.
    • (1997) Gene Dev. , vol.11 , pp. 358-370
    • Enomoto, S.1    Mccunezierath, P.D.2    Geraminejad, M.3    Sanders, M.A.4    Berman, J.5
  • 275
    • 0030696045 scopus 로고    scopus 로고
    • The yeast Cac1 protein is required for the stable inheritance of transcriptionally repressed chromatin at telomeres
    • Monson E.K., Debruin D., Zakian V.A. The yeast Cac1 protein is required for the stable inheritance of transcriptionally repressed chromatin at telomeres. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:13081-13086.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13081-13086
    • Monson, E.K.1    Debruin, D.2    Zakian, V.A.3
  • 276
    • 0031985051 scopus 로고    scopus 로고
    • Chromatin assembly factor I contributes to the maintenance, but not the re-establishment, of silencing at the yeast silent mating loci
    • Enomoto S., Berman J. Chromatin assembly factor I contributes to the maintenance, but not the re-establishment, of silencing at the yeast silent mating loci. Gene Dev. 1998, 12:219-232.
    • (1998) Gene Dev. , vol.12 , pp. 219-232
    • Enomoto, S.1    Berman, J.2
  • 277
    • 0032912468 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae chromatin assembly factor-I in repair of ultraviolet radiation damage in vivo
    • Game J.C., Kaufman P.D. Role of Saccharomyces cerevisiae chromatin assembly factor-I in repair of ultraviolet radiation damage in vivo. Genetics 1999, 151:485-497.
    • (1999) Genetics , vol.151 , pp. 485-497
    • Game, J.C.1    Kaufman, P.D.2
  • 279
    • 0141530885 scopus 로고    scopus 로고
    • Local action of the chromatin assembly factor CAF-1 at sites of nucleotide excision repair in vivo
    • Green C.M., Almouzni G. Local action of the chromatin assembly factor CAF-1 at sites of nucleotide excision repair in vivo. EMBO J. 2003, 22:5163-5174.
    • (2003) EMBO J. , vol.22 , pp. 5163-5174
    • Green, C.M.1    Almouzni, G.2
  • 280
    • 0033212963 scopus 로고    scopus 로고
    • Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins
    • Murzina N., Verreault A., Laue E., Stillman B. Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins. Mol. Cell 1999, 4:529-540.
    • (1999) Mol. Cell , vol.4 , pp. 529-540
    • Murzina, N.1    Verreault, A.2    Laue, E.3    Stillman, B.4
  • 281
    • 0037405867 scopus 로고    scopus 로고
    • The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1
    • Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R. The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1. Mol. Cell. Biol. 2003, 23:3226-3236.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3226-3236
    • Reese, B.E.1    Bachman, K.E.2    Baylin, S.B.3    Rountree, M.R.4
  • 282
    • 33845571860 scopus 로고    scopus 로고
    • Heterochromatin protein 2 interacts with Nap-1 and NURF: A link between heterochromatin-induced gene silencing and the chromatin remodeling machinery in Drosophila
    • Stephens G.E., Xiao H., Lankenau D.H., Wu C., Elgin S.C.R. Heterochromatin protein 2 interacts with Nap-1 and NURF: A link between heterochromatin-induced gene silencing and the chromatin remodeling machinery in Drosophila. Biochemistry 2006, 45:14990-14999.
    • (2006) Biochemistry , vol.45 , pp. 14990-14999
    • Stephens, G.E.1    Xiao, H.2    Lankenau, D.H.3    Wu, C.4    Elgin, S.C.R.5
  • 284
    • 33747792063 scopus 로고    scopus 로고
    • The replication kinase Cdc7-Dbf4 promotes the interaction of the p150 subunit of chromatin assembly factor 1 with proliferating cell nuclear antigen
    • Gerard A., Koundrioukoff S., Ramillon V., Sergere J.C., Mailand N., Quivy J.P., Almouzni G.V. The replication kinase Cdc7-Dbf4 promotes the interaction of the p150 subunit of chromatin assembly factor 1 with proliferating cell nuclear antigen. EMBO Rep. 2006, 7:817-823.
    • (2006) EMBO Rep. , vol.7 , pp. 817-823
    • Gerard, A.1    Koundrioukoff, S.2    Ramillon, V.3    Sergere, J.C.4    Mailand, N.5    Quivy, J.P.6    Almouzni, G.V.7
  • 285
    • 0037291295 scopus 로고    scopus 로고
    • Defective S phase chromatin assembly causes DNA damage, activation of the S phase checkpoint, and S phase arrest
    • Ye X.F., Franco A.A., Santos H., Nelson D.M., Kaufman P.D., Adams P.D. Defective S phase chromatin assembly causes DNA damage, activation of the S phase checkpoint, and S phase arrest. Mol. Cell 2003, 11:341-351.
    • (2003) Mol. Cell , vol.11 , pp. 341-351
    • Ye, X.F.1    Franco, A.A.2    Santos, H.3    Nelson, D.M.4    Kaufman, P.D.5    Adams, P.D.6
  • 286
    • 0142091385 scopus 로고    scopus 로고
    • Chromatin assembly factor 1 is essential and couples chromatin assembly to DNA replication in vivo
    • Hoek M., Stillman B. Chromatin assembly factor 1 is essential and couples chromatin assembly to DNA replication in vivo. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:12183-12188.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12183-12188
    • Hoek, M.1    Stillman, B.2
  • 287
    • 1642312883 scopus 로고    scopus 로고
    • Silencing of chromatin assembly factor 1 in human cells leads to cell death and loss of chromatin assembly during DNA synthesis
    • Nabatiyan A., Krude T. Silencing of chromatin assembly factor 1 in human cells leads to cell death and loss of chromatin assembly during DNA synthesis. Mol. Cell. Biol. 2004, 24:2853-2862.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2853-2862
    • Nabatiyan, A.1    Krude, T.2
  • 288
    • 33846128464 scopus 로고    scopus 로고
    • Essential role of chromatin assembly factor-1-mediated rapid nucleosome assembly for DNA replication and cell division in vertebrate cells
    • Takami Y., Ono T., Fukagawa T., Shibahara K., Nakayama T. Essential role of chromatin assembly factor-1-mediated rapid nucleosome assembly for DNA replication and cell division in vertebrate cells. Mol. Biol. Cell 2007, 18:129-141.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 129-141
    • Takami, Y.1    Ono, T.2    Fukagawa, T.3    Shibahara, K.4    Nakayama, T.5
  • 290
    • 0030862060 scopus 로고    scopus 로고
    • Two new S-phase-specific genes from Saccharomyces cerevisiae
    • Le S., Davis C., Konopka J.B., Sternglanz R. Two new S-phase-specific genes from Saccharomyces cerevisiae. Yeast 1997, 13:1029-1042.
    • (1997) Yeast , vol.13 , pp. 1029-1042
    • Le, S.1    Davis, C.2    Konopka, J.B.3    Sternglanz, R.4
  • 293
    • 0034100123 scopus 로고    scopus 로고
    • A human homologue of yeast anti-silencing factor has histone chaperone activity
    • Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M. A human homologue of yeast anti-silencing factor has histone chaperone activity. Genes Cells 2000, 5:221-233.
    • (2000) Genes Cells , vol.5 , pp. 221-233
    • Munakata, T.1    Adachi, N.2    Yokoyama, N.3    Kuzuhara, T.4    Horikoshi, M.5
  • 294
    • 0036163533 scopus 로고    scopus 로고
    • Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro
    • Umehara T., Chimura T., Ichikawa N., Horikoshi M. Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro. Genes Cells 2002, 7:59-73.
    • (2002) Genes Cells , vol.7 , pp. 59-73
    • Umehara, T.1    Chimura, T.2    Ichikawa, N.3    Horikoshi, M.4
  • 295
    • 8644256711 scopus 로고    scopus 로고
    • Activation of the DNA damage checkpoint in yeast lacking the histone chaperone anti-silencing function 1
    • Ramey C.J., Howar S., Adkins M., Linger J., Spicer J., Tyler J.K. Activation of the DNA damage checkpoint in yeast lacking the histone chaperone anti-silencing function 1. Mol. Cell. Biol. 2004, 24:10313-10327.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10313-10327
    • Ramey, C.J.1    Howar, S.2    Adkins, M.3    Linger, J.4    Spicer, J.5    Tyler, J.K.6
  • 296
    • 0035206962 scopus 로고    scopus 로고
    • Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1
    • Yamaki M., Umehara T., Chimura T., Horikoshi M. Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1. Genes Cells 2001, 6:1043-1054.
    • (2001) Genes Cells , vol.6 , pp. 1043-1054
    • Yamaki, M.1    Umehara, T.2    Chimura, T.3    Horikoshi, M.4
  • 297
    • 0025840592 scopus 로고
    • Associative behavior of the histone (H3-H4)2 tetramer - dependence on ionic environment
    • Baxevanis A.D., Godfrey J.E., Moudrianakis E.N. Associative behavior of the histone (H3-H4)2 tetramer - dependence on ionic environment. Biochemistry 1991, 30:8817-8823.
    • (1991) Biochemistry , vol.30 , pp. 8817-8823
    • Baxevanis, A.D.1    Godfrey, J.E.2    Moudrianakis, E.N.3
  • 298
    • 0029053420 scopus 로고
    • Thermodynamic studies of the core histones: Ionic strength and pH dependence of H2A-H2B dimer stability
    • Karantza V., Baxevanis A.D., Freire E., Moudrianakis E.N. Thermodynamic studies of the core histones: Ionic strength and pH dependence of H2A-H2B dimer stability. Biochemistry 1995, 34:5988-5996.
    • (1995) Biochemistry , vol.34 , pp. 5988-5996
    • Karantza, V.1    Baxevanis, A.D.2    Freire, E.3    Moudrianakis, E.N.4
  • 299
    • 0038661090 scopus 로고    scopus 로고
    • Equilibrium folding of the core histones: the H3-H4 tetramer is less stable than the H2A-H2B dimer
    • Banks D.D., Gloss L.M. Equilibrium folding of the core histones: the H3-H4 tetramer is less stable than the H2A-H2B dimer. Biochemistry Usa 2003, 42:6827-6839.
    • (2003) Biochemistry Usa , vol.42 , pp. 6827-6839
    • Banks, D.D.1    Gloss, L.M.2
  • 300
    • 33644866511 scopus 로고    scopus 로고
    • Chromatin assembly: a basic recipe with various flavours
    • Polo S.E., Almouzni G. Chromatin assembly: a basic recipe with various flavours. Curr. Opin. Genet. Dev. 2006, 16:104-111.
    • (2006) Curr. Opin. Genet. Dev. , vol.16 , pp. 104-111
    • Polo, S.E.1    Almouzni, G.2
  • 301
    • 33847226680 scopus 로고    scopus 로고
    • Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
    • Natsume R., Eitoku M., Akai Y., Sano N., Horikoshi M., Senda T. Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4. Nature 2007, 446:338-341.
    • (2007) Nature , vol.446 , pp. 338-341
    • Natsume, R.1    Eitoku, M.2    Akai, Y.3    Sano, N.4    Horikoshi, M.5    Senda, T.6
  • 302
    • 0036250827 scopus 로고    scopus 로고
    • Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway
    • Mello J.A., Sillje H.H.W., Roche D.M.J., Kirschner D.B., Nigg E.A., Almouzni G. Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway. EMBO Rep. 2002, 3:329-334.
    • (2002) EMBO Rep. , vol.3 , pp. 329-334
    • Mello, J.A.1    Sillje, H.H.W.2    Roche, D.M.J.3    Kirschner, D.B.4    Nigg, E.A.5    Almouzni, G.6
  • 305
    • 33846574739 scopus 로고    scopus 로고
    • Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics
    • Antczak A.J., Tsubota T., Kaufman P.D., Berger J.M. Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics. BMC Struct. Biol. 2006, 6:26-37.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 26-37
    • Antczak, A.J.1    Tsubota, T.2    Kaufman, P.D.3    Berger, J.M.4
  • 309
    • 34347258162 scopus 로고    scopus 로고
    • The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3
    • Han J.H., Zhou H., Li Z.Z., Xu R.M., Zhang Z.G. The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3. J. Biol. Chem. 2007, 282:14158-14164.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14158-14164
    • Han, J.H.1    Zhou, H.2    Li, Z.Z.3    Xu, R.M.4    Zhang, Z.G.5
  • 311
    • 22344434704 scopus 로고    scopus 로고
    • Histone deposition protein Asf1 maintains DNA replisome integrity and interacts with replication factor C
    • Franco A.A., Lam W.M., Burgers P.M., Kaufman P.D. Histone deposition protein Asf1 maintains DNA replisome integrity and interacts with replication factor C. Gene Dev. 2005, 19:1365-1375.
    • (2005) Gene Dev. , vol.19 , pp. 1365-1375
    • Franco, A.A.1    Lam, W.M.2    Burgers, P.M.3    Kaufman, P.D.4
  • 312
    • 33645835466 scopus 로고    scopus 로고
    • The histone chaperone ASF1 localizes to active DNA replication forks to mediate efficient DNA replication
    • Schulz L.L., Tyler J.K. The histone chaperone ASF1 localizes to active DNA replication forks to mediate efficient DNA replication. FASEB J. 2006, 20:488-490.
    • (2006) FASEB J. , vol.20 , pp. 488-490
    • Schulz, L.L.1    Tyler, J.K.2
  • 313
    • 12344321682 scopus 로고    scopus 로고
    • Human Asf1 regulates the flow of S phase histones during replicational stress
    • Groth A., Ray-Gallet D., Quivy J.P., Lukas J., Bartek J., Almouzni G. Human Asf1 regulates the flow of S phase histones during replicational stress. Mol. Cell 2005, 17:301-311.
    • (2005) Mol. Cell , vol.17 , pp. 301-311
    • Groth, A.1    Ray-Gallet, D.2    Quivy, J.P.3    Lukas, J.4    Bartek, J.5    Almouzni, G.6
  • 314
    • 44349161775 scopus 로고    scopus 로고
    • In vivo study of the nucleosome assembly functions of ASF1 histone chaperones in human cells
    • Galvani A., Courbeyrette R., Agez M., Ochsenbein F., Mann C., Thuret J.Y. In vivo study of the nucleosome assembly functions of ASF1 histone chaperones in human cells. Mol. Cell. Biol. 2008, 28:3672-3685.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3672-3685
    • Galvani, A.1    Courbeyrette, R.2    Agez, M.3    Ochsenbein, F.4    Mann, C.5    Thuret, J.Y.6
  • 315
    • 0023478786 scopus 로고
    • Trans-acting regulatory mutations that alter transcription of Saccharomyces cerevisiae histone genes
    • Osley M.A., Lycan D. Trans-acting regulatory mutations that alter transcription of Saccharomyces cerevisiae histone genes. Mol. Cell. Biol. 1987, 7:4204-4210.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4204-4210
    • Osley, M.A.1    Lycan, D.2
  • 316
    • 0025998566 scopus 로고
    • Histone regulatory (hir) mutations suppress delta insertion alleles in Saccharomyces cerevisiae
    • Sherwood P.W., Osley M.A. Histone regulatory (hir) mutations suppress delta insertion alleles in Saccharomyces cerevisiae. Genetics 1991, 128:729-738.
    • (1991) Genetics , vol.128 , pp. 729-738
    • Sherwood, P.W.1    Osley, M.A.2
  • 317
    • 0027391029 scopus 로고
    • Characterization of HIR1 and HIR2, two genes required for regulation of histone gene transcription in Saccharomyces cerevisiae
    • Sherwood P.W., Tsang S.V., Osley M.A. Characterization of HIR1 and HIR2, two genes required for regulation of histone gene transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 1993, 13:28-38.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 28-38
    • Sherwood, P.W.1    Tsang, S.V.2    Osley, M.A.3
  • 318
    • 0027731681 scopus 로고
    • Isolation of a putative transcriptional regulator from the region of 22q11 deleted in DiGeorge syndrome, Shprintzen syndrome and familial congenital heart disease
    • Halford S., Wadey R., Roberts C., Daw S.C., Whiting J.A., O'Donnell H., Dunham I., Bentley D., Lindsay E., Baldini A., et al. Isolation of a putative transcriptional regulator from the region of 22q11 deleted in DiGeorge syndrome, Shprintzen syndrome and familial congenital heart disease. Hum. Mol. Genet. 1993, 2:2099-2107.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 2099-2107
    • Halford, S.1    Wadey, R.2    Roberts, C.3    Daw, S.C.4    Whiting, J.A.5    O'Donnell, H.6    Dunham, I.7    Bentley, D.8    Lindsay, E.9    Baldini, A.10
  • 319
    • 0029038946 scopus 로고
    • A human homolog of the S. cerevisiae HIR1 and HIR2 transcriptional repressors cloned from the DiGeorge syndrome critical region
    • Lamour V., Lecluse Y., Desmaze C., Spector M., Bodescot M., Aurias A., Osley M.A., Lipinski M. A human homolog of the S. cerevisiae HIR1 and HIR2 transcriptional repressors cloned from the DiGeorge syndrome critical region. Hum. Mol. Genet. 1995, 4:791-799.
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 791-799
    • Lamour, V.1    Lecluse, Y.2    Desmaze, C.3    Spector, M.4    Bodescot, M.5    Aurias, A.6    Osley, M.A.7    Lipinski, M.8
  • 320
    • 0031858054 scopus 로고    scopus 로고
    • Hir proteins are required for position-dependent gene silencing in Saccharomyces cerevisiae in the absence of chromatin assembly factor I
    • Kaufman P.D., Cohen J.L., Osley M.A. Hir proteins are required for position-dependent gene silencing in Saccharomyces cerevisiae in the absence of chromatin assembly factor I. Mol. Cell. Biol. 1998, 18:4793-4806.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4793-4806
    • Kaufman, P.D.1    Cohen, J.L.2    Osley, M.A.3
  • 321
    • 0031713666 scopus 로고    scopus 로고
    • HIRA, a mammalian homologue of Saccharomyces cerevisiae transcriptional co-repressors, interacts with Pax3
    • Magnaghi P., Roberts C., Lorain S., Lipinski M., Scambler P.J. HIRA, a mammalian homologue of Saccharomyces cerevisiae transcriptional co-repressors, interacts with Pax3. Nat. Genet. 1998, 20:74-77.
    • (1998) Nat. Genet. , vol.20 , pp. 74-77
    • Magnaghi, P.1    Roberts, C.2    Lorain, S.3    Lipinski, M.4    Scambler, P.J.5
  • 323
    • 27644515513 scopus 로고    scopus 로고
    • The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus
    • Loppin B., Bonnefoy E., Anselme C., Laurencon A., Karr T.L., Couble P. The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus. Nature 2005, 437:1386-1390.
    • (2005) Nature , vol.437 , pp. 1386-1390
    • Loppin, B.1    Bonnefoy, E.2    Anselme, C.3    Laurencon, A.4    Karr, T.L.5    Couble, P.6
  • 324
    • 35948990898 scopus 로고    scopus 로고
    • The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization
    • Bonnefoy E., Orsi G.A., Couble P., Loppin B. The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization. PLoS Genet. 2007, 3:1991-2006.
    • (2007) PLoS Genet. , vol.3 , pp. 1991-2006
    • Bonnefoy, E.1    Orsi, G.A.2    Couble, P.3    Loppin, B.4
  • 325
    • 0036124470 scopus 로고    scopus 로고
    • Targeted mutagenesis of the Hira gene results in gastrulation defects and patterning abnormalities of mesoendodermal derivatives prior to early embryonic lethality
    • Roberts C., Sutherland H.F., Farmer H., Kimber W., Halford S., Carey A., Brickman J.M., Wynshaw-Boris A., Scambler P.J. Targeted mutagenesis of the Hira gene results in gastrulation defects and patterning abnormalities of mesoendodermal derivatives prior to early embryonic lethality. Mol. Cell. Biol. 2002, 22:2318-2328.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2318-2328
    • Roberts, C.1    Sutherland, H.F.2    Farmer, H.3    Kimber, W.4    Halford, S.5    Carey, A.6    Brickman, J.M.7    Wynshaw-Boris, A.8    Scambler, P.J.9
  • 326
    • 0035799281 scopus 로고    scopus 로고
    • Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing
    • Sharp J.A., Fouts E.T., Krawitz D.C., Kaufman P.D. Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing. Curr. Biol. 2001, 11:463-473.
    • (2001) Curr. Biol. , vol.11 , pp. 463-473
    • Sharp, J.A.1    Fouts, E.T.2    Krawitz, D.C.3    Kaufman, P.D.4
  • 327
    • 0034977802 scopus 로고    scopus 로고
    • Yeast ASF1 protein is required for cell cycle regulation of histone gene transcription
    • Sutton A., Bucaria J., Osley M.A., Sternglanz R. Yeast ASF1 protein is required for cell cycle regulation of histone gene transcription. Genetics 2001, 158:587-596.
    • (2001) Genetics , vol.158 , pp. 587-596
    • Sutton, A.1    Bucaria, J.2    Osley, M.A.3    Sternglanz, R.4
  • 333
    • 21844465956 scopus 로고    scopus 로고
    • Histone dynamics in living cells revealed by photobleaching
    • Kimura H. Histone dynamics in living cells revealed by photobleaching. DNA Repair 2005, 4:939-950.
    • (2005) DNA Repair , vol.4 , pp. 939-950
    • Kimura, H.1
  • 336
    • 78751536862 scopus 로고    scopus 로고
    • Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome
    • Luk E., Ranjan A., Fitzgerald P.C., Mizuguchi G., Huang Y., Wei D., Wu C. Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome. Cell 2010, 143:725-736.
    • (2010) Cell , vol.143 , pp. 725-736
    • Luk, E.1    Ranjan, A.2    Fitzgerald, P.C.3    Mizuguchi, G.4    Huang, Y.5    Wei, D.6    Wu, C.7
  • 337
    • 33846663256 scopus 로고    scopus 로고
    • Continuous histone H2B and transcription-dependent histone H3 exchange in yeast cells outside of replication
    • Jamai A., Imoberdorf R.M., Strubin M. Continuous histone H2B and transcription-dependent histone H3 exchange in yeast cells outside of replication. Mol. Cell 2007, 25:345-355.
    • (2007) Mol. Cell , vol.25 , pp. 345-355
    • Jamai, A.1    Imoberdorf, R.M.2    Strubin, M.3
  • 338
    • 33749048664 scopus 로고
    • Genetical implications of the structure of deoxyribonucleic acid
    • Watson J.D., Crick F.H. Genetical implications of the structure of deoxyribonucleic acid. Nature 1953, 171:964-967.
    • (1953) Nature , vol.171 , pp. 964-967
    • Watson, J.D.1    Crick, F.H.2
  • 339
    • 70449713419 scopus 로고    scopus 로고
    • Mechanisms of epigenetic inheritance: copying of polycomb repressed chromatin
    • Francis N.J. Mechanisms of epigenetic inheritance: copying of polycomb repressed chromatin. Cell Cycle 2009, 8:3521-3526.
    • (2009) Cell Cycle , vol.8 , pp. 3521-3526
    • Francis, N.J.1
  • 340
    • 63049138876 scopus 로고    scopus 로고
    • Polycomb proteins remain bound to chromatin and DNA during DNA replication in vitro
    • Francis N.J., Follmer N.E., Simon M.D., Aghia G., Butler J.D. Polycomb proteins remain bound to chromatin and DNA during DNA replication in vitro. Cell 2009, 137:110-122.
    • (2009) Cell , vol.137 , pp. 110-122
    • Francis, N.J.1    Follmer, N.E.2    Simon, M.D.3    Aghia, G.4    Butler, J.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.