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Volumn 15, Issue 3, 1996, Pages 548-561

Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin

Author keywords

B4 HMG1 nucleosome Xenopus; Chromatin histone

Indexed keywords

DEOXYRIBONUCLEASE I; DNA; HIGH MOBILITY GROUP PROTEIN; HISTONE; HISTONE H1; HYDROXYL RADICAL; MICROCOCCAL NUCLEASE;

EID: 0030064348     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00387.x     Document Type: Article
Times cited : (149)

References (106)
  • 1
    • 0025144029 scopus 로고
    • Efficient large-scale purification of non-histone chromosomal proteins HMG1 and HMG2 by using polybuffer exchanger PBE94
    • Adachi, Y., Mizuno, S. and Yoshida, M. (1990) Efficient large-scale purification of non-histone chromosomal proteins HMG1 and HMG2 by using polybuffer exchanger PBE94. J. Chromatogr., 530, 39-46.
    • (1990) J. Chromatogr. , vol.530 , pp. 39-46
    • Adachi, Y.1    Mizuno, S.2    Yoshida, M.3
  • 2
    • 0019157001 scopus 로고
    • The structure of histone H1 and its location in chromatin
    • Allan, J., Hartman, P.G., Crane-Robinson, C. and Aviles, F.X. (1980) The structure of histone H1 and its location in chromatin. Nature, 288, 675-679.
    • (1980) Nature , vol.288 , pp. 675-679
    • Allan, J.1    Hartman, P.G.2    Crane-Robinson, C.3    Aviles, F.X.4
  • 3
    • 0029070956 scopus 로고
    • Homology model building of the HMG-1 box structural domain
    • Baxevanis, A.D., Bryant, S.H. and Landsman, D. (1995) Homology model building of the HMG-1 box structural domain. Nucleic Acids Res., 23, 1604-1613.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1604-1613
    • Baxevanis, A.D.1    Bryant, S.H.2    Landsman, D.3
  • 4
    • 0021112557 scopus 로고
    • Detection by chemical cross-linking of the interaction between high mobility group protein 1 and histone oligomers in free solution
    • Bernues, J., Querol, E., Martinez, P., Barris, A., Espel, E. and Llobevas, J. (1983) Detection by chemical cross-linking of the interaction between high mobility group protein 1 and histone oligomers in free solution. J. Biol. Chem., 258, 11020-11024.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11020-11024
    • Bernues, J.1    Querol, E.2    Martinez, P.3    Barris, A.4    Espel, E.5    Llobevas, J.6
  • 5
    • 0028043678 scopus 로고
    • Prokaryotic H1 and eukaryotic HMG1: A kinked relationship
    • Bianchi, M.E. (1994) Prokaryotic H1 and eukaryotic HMG1: a kinked relationship. Mol. Microbiol., 14, 1-5.
    • (1994) Mol. Microbiol. , vol.14 , pp. 1-5
    • Bianchi, M.E.1
  • 6
    • 0024584528 scopus 로고
    • Specific recognition of cruciform DNA by nuclear protein HMG1
    • Bianchi, M.E., Beltrame, M. and Paonessa, G. (1989) Specific recognition of cruciform DNA by nuclear protein HMG1. Science, 243, 1056-1059.
    • (1989) Science , vol.243 , pp. 1056-1059
    • Bianchi, M.E.1    Beltrame, M.2    Paonessa, G.3
  • 7
    • 0026609275 scopus 로고
    • The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins
    • Bianchi, M.E., Falciola, L., Ferrari, S. and Lilley, D.M.J. (1992) The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins. EMBO J., 11, 1055-1063.
    • (1992) EMBO J. , vol.11 , pp. 1055-1063
    • Bianchi, M.E.1    Falciola, L.2    Ferrari, S.3    Lilley, D.M.J.4
  • 8
    • 1842299187 scopus 로고
    • Rat liver HMG1: A physiological nucleosome assembly factor
    • Bonne-Andrea, C., Harper, F., Sobczak, J. and DeRecondo, M. (1984) Rat liver HMG1: a physiological nucleosome assembly factor. EMBO J., 3, 1193-1199.
    • (1984) EMBO J. , vol.3 , pp. 1193-1199
    • Bonne-Andrea, C.1    Harper, F.2    Sobczak, J.3    DeRecondo, M.4
  • 9
    • 0018866555 scopus 로고
    • Points of contact between histone H1 and the histone octamer
    • Boulikas, T., Wiseman, J.M. and Garrard, W.T. (1980) Points of contact between histone H1 and the histone octamer. Proc. Natl Acad. Sci. USA, 77, 127-131.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 127-131
    • Boulikas, T.1    Wiseman, J.M.2    Garrard, W.T.3
  • 10
    • 0025323711 scopus 로고
    • Structural features of the HMG chromosomal proteins and their genes
    • Bustin, M., Lehn, D.A. and Landsman, D. (1990) Structural features of the HMG chromosomal proteins and their genes. Biochim. Biophys. Acta, 1049, 231-243.
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 231-243
    • Bustin, M.1    Lehn, D.A.2    Landsman, D.3
  • 11
    • 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. and Felsenfeld, G. (1976) The organization of histones and DNA in chromatin: evidence for an arginine-rich histone kernel. Cell, 8, 333-347.
    • (1976) Cell , vol.8 , pp. 333-347
    • Camerini-Otero, R.D.1    Sollner-Webb, B.2    Felsenfeld, G.3
  • 12
    • 0027518437 scopus 로고
    • Post-translational cleavage of a histone H1-like protein in the sperm of Mytilus
    • Carlos, S., Hunt, D.F., Rocchini, C., Arnott, D.P. and Ausio, J. (1993) Post-translational cleavage of a histone H1-like protein in the sperm of Mytilus. J. Biol. Chem., 268, 195-199.
    • (1993) J. Biol. Chem. , vol.268 , pp. 195-199
    • Carlos, S.1    Hunt, D.F.2    Rocchini, C.3    Arnott, D.P.4    Ausio, J.5
  • 13
    • 0028950413 scopus 로고
    • HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG
    • Churchill, M.E.A., Jones, D.N.M., Glaser, T., Hefner, H., Searles, M.A. and Travers, A.A. (1995) HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG. EMBO J., 14, 1264-1275
    • (1995) EMBO J. , vol.14 , pp. 1264-1275
    • Churchill, M.E.A.1    Jones, D.N.M.2    Glaser, T.3    Hefner, H.4    Searles, M.A.5    Travers, A.A.6
  • 14
    • 0022470051 scopus 로고
    • Salt-dependent co-operative interaction of histone H1 with linker DNA
    • Clark, D.J. and Thomas, J.O. (1986) Salt-dependent co-operative interaction of histone H1 with linker DNA. J. Mol. Biol., 187, 569-580.
    • (1986) J. Mol. Biol. , vol.187 , pp. 569-580
    • Clark, D.J.1    Thomas, J.O.2
  • 15
    • 0027270989 scopus 로고
    • Cocrystal structure of the HNF-3/forkhead DNA recognition motif resembles histone H5
    • Clark, K.L., Halay, E.D., Lai, E. and Burley, S.K. (1993) Cocrystal structure of the HNF-3/forkhead DNA recognition motif resembles histone H5. Nature, 364, 412-420.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 16
    • 0028587368 scopus 로고
    • Nuclear assembly is independent of linker histones
    • Dasso, M., Dimitrov, S. and Wolffe, A.P. (1994) Nuclear assembly is independent of linker histones. Proc. Natl Acad. Sci. USA, 91, 12477-12481.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12477-12481
    • Dasso, M.1    Dimitrov, S.2    Wolffe, A.P.3
  • 17
    • 0023391097 scopus 로고
    • The globular domain of histone H5 is internally located in the 30 nm chromatin fiber: An immunochemical study
    • Dimitrov, S.I., Russanova, V. and Pashev, I. (1987) The globular domain of histone H5 is internally located in the 30 nm chromatin fiber: an immunochemical study. EMBO J., 6, 2387-2392.
    • (1987) EMBO J. , vol.6 , pp. 2387-2392
    • Dimitrov, S.I.1    Russanova, V.2    Pashev, I.3
  • 18
    • 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. and Wolffe, A.P. (1993) Chromatin transitions during early Xenopus embryogenesis: changes in histone H4 acetylation and in linker histone type. Dev. Biol., 160, 214-227.
    • (1993) Dev. Biol. , vol.160 , pp. 214-227
    • Dimitrov, S.1    Almouzni, G.2    Dasso, M.3    Wolffe, A.P.4
  • 19
    • 0028015742 scopus 로고
    • Remodeling sperm chromatin in Xenopus laevis egg extracts: The role of core histone phosphorylation and linker histone B4 in chromatin assembly
    • Dimitrov, S., Dasso, M.C. and Wolffe, A.P. (1994) Remodeling sperm chromatin in Xenopus laevis egg extracts: the role of core histone phosphorylation and linker histone B4 in chromatin assembly. J. Cell Biol., 126, 591-601.
    • (1994) J. Cell Biol. , vol.126 , pp. 591-601
    • Dimitrov, S.1    Dasso, M.C.2    Wolffe, A.P.3
  • 20
    • 0025311114 scopus 로고
    • DNA and protein determinants of nucleosome positioning on sea urchin 5S rRNA gene sequences in vitro
    • Dong, F., Hansen, J.C. and van Holde, K.E. (1990) DNA and protein determinants of nucleosome positioning on sea urchin 5S rRNA gene sequences in vitro. Proc. Natl Acad. Sci. USA, 87, 5724-5728.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5724-5728
    • Dong, F.1    Hansen, J.C.2    Van Holde, K.E.3
  • 21
    • 0028303884 scopus 로고
    • The high mobility protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein
    • Ge, H. and Roeder, R.G. (1994) The high mobility protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein. J. Biol. Chem., 269, 17136-17140.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17136-17140
    • Ge, H.1    Roeder, R.G.2
  • 22
    • 0017886022 scopus 로고
    • Evidence for the close proximity of histones H1 and H3 in chromatin of intact nuclei
    • Glotov, B.O., Itkes, A.V., Nikolaev, L.G. and Severin, E.S. (1978) Evidence for the close proximity of histones H1 and H3 in chromatin of intact nuclei. FEBS Lett., 91, 149-152.
    • (1978) FEBS Lett. , vol.91 , pp. 149-152
    • Glotov, B.O.1    Itkes, A.V.2    Nikolaev, L.G.3    Severin, E.S.4
  • 23
    • 49449120940 scopus 로고
    • The presence of high mobility group non-histone proteins in isolated nucleosomes
    • Goodwin, G.H., Woodhead, L. and Johns, E.W. (1977) The presence of high mobility group non-histone proteins in isolated nucleosomes. FEBS Lett., 73, 85-88.
    • (1977) FEBS Lett. , vol.73 , pp. 85-88
    • Goodwin, G.H.1    Woodhead, L.2    Johns, E.W.3
  • 24
    • 0001095880 scopus 로고
    • The induction of DNA synthesis in frog egg cytoplasm
    • Graham, C.F., Arms, K. and Gurdon, J.B. (1966) The induction of DNA synthesis in frog egg cytoplasm. Dev. Biol., 14, 349-381.
    • (1966) Dev. Biol. , vol.14 , pp. 349-381
    • Graham, C.F.1    Arms, K.2    Gurdon, J.B.3
  • 25
    • 0025727615 scopus 로고
    • Isolation and characterization of maize cDNAs encoding a high-mobility-group protein displaying a HMG-box
    • Grasser, K.D. and Feix, G. (1991) Isolation and characterization of maize cDNAs encoding a high-mobility-group protein displaying a HMG-box. Nucleic Acids Res., 19, 2573-2577.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2573-2577
    • Grasser, K.D.1    Feix, G.2
  • 26
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R., Giese, K. and Pagel, J. (1994) HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet., 10, 94-100.
    • (1994) Trends Genet. , vol.10 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 27
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in E.coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan, K.L. and Dixon, J.E. (1991) Eukaryotic proteins expressed in E.coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem., 192, 262-267
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 28
    • 0028657623 scopus 로고
    • Molecular basis of mammalian sexual determination: Activation of Mullerian inhibiting substance gene expression by SRY
    • Hagg, C.M., King, C.-Y., Ukiyama, E., Falsafi, S., Hagg, T.N., Donahoe, P.K. and Weiss, M.A. (1994) Molecular basis of mammalian sexual determination: activation of Mullerian inhibiting substance gene expression by SRY. Science, 266, 1494-1500.
    • (1994) Science , vol.266 , pp. 1494-1500
    • Hagg, C.M.1    King, C.-Y.2    Ukiyama, E.3    Falsafi, S.4    Hagg, T.N.5    Donahoe, P.K.6    Weiss, M.A.7
  • 29
    • 0025165918 scopus 로고
    • New fold back transposable element TFB1 found in histone genes of the midge Chironornus thummi
    • Hankeln, T. and Schmidt, E.R. (1990) New fold back transposable element TFB1 found in histone genes of the midge Chironornus thummi. J. Mol. Biol., 215, 447-482.
    • (1990) J. Mol. Biol. , vol.215 , pp. 447-482
    • Hankeln, T.1    Schmidt, E.R.2
  • 30
    • 0024508029 scopus 로고
    • Tetrahymena HMG nonhistone chromosomal protein. Isolation and amino acid sequence lacking the N- and C-terminal domains of vertebrate HMG 1
    • Hayashi, T., Hayashi, H. and Iwai, K. (1989) Tetrahymena HMG nonhistone chromosomal protein. Isolation and amino acid sequence lacking the N- and C-terminal domains of vertebrate HMG 1. J. Biochem., 105, 577-581.
    • (1989) J. Biochem. , vol.105 , pp. 577-581
    • Hayashi, T.1    Hayashi, H.2    Iwai, K.3
  • 31
    • 0026570858 scopus 로고
    • Histones H2A/H2B inhibit the interaction of TFIIIA with 5S DNA in a nucleosome
    • Hayes, J.J. and Wolffe, A.P. (1992) Histones H2A/H2B inhibit the interaction of TFIIIA with 5S DNA in a nucleosome. Proc. Natl Acad. Sci. USA, 89, 1229-1233.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 1229-1233
    • Hayes, J.J.1    Wolffe, A.P.2
  • 32
    • 0027248504 scopus 로고
    • Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome
    • Hayes, J.J. and Wolffe, A.P. (1993) Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome. Proc. Natl Acad. Sci. USA, 90, 6415-6419.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6415-6419
    • Hayes, J.J.1    Wolffe, A.P.2
  • 34
    • 0026010309 scopus 로고
    • Histone contributions to the structure of DNA in the nucleosome
    • Hayes, J.J., Clark, D.J. and Wolffe, A.P. (1991) Histone contributions to the structure of DNA in the nucleosome. Proc. Natl Acad. Sci. USA, 88, 6829-6833.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6829-6833
    • Hayes, J.J.1    Clark, D.J.2    Wolffe, A.P.3
  • 35
    • 0028031310 scopus 로고
    • Histone domains required to assemble a chromatosome including the Xenopus borealis somatic 5S rRNA gene
    • Hayes, J.J., Pruss, D. and Wolffe, A.P. (1994) Histone domains required to assemble a chromatosome including the Xenopus borealis somatic 5S rRNA gene. Proc. Natl Acad. Sci. USA, 91, 7817-7821.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7817-7821
    • Hayes, J.J.1    Pruss, D.2    Wolffe, A.P.3
  • 36
    • 0027272359 scopus 로고
    • Absence of somatic histone H1 in oocytes and preblastula embryos of Xenopus laevis
    • Hock, R., Moorman, A., Fischer, D. and Scheer, U. (1993) Absence of somatic histone H1 in oocytes and preblastula embryos of Xenopus laevis. Dev. Biol., 158, 510-522.
    • (1993) Dev. Biol. , vol.158 , pp. 510-522
    • Hock, R.1    Moorman, A.2    Fischer, D.3    Scheer, U.4
  • 37
    • 0024351482 scopus 로고
    • Electrophoretic analyses of nucleosomes and other protein-DNA complexes
    • Huang, S.-Y. and Garrard, W.T. (1989) Electrophoretic analyses of nucleosomes and other protein-DNA complexes. Methods Enzymol., 170, 116-141.
    • (1989) Methods Enzymol. , vol.170 , pp. 116-141
    • Huang, S.-Y.1    Garrard, W.T.2
  • 38
    • 0019318249 scopus 로고
    • Isolation and separation of chicken erythrocyte high mobility group non-histone chromatin proteins by chromatography on phosphocellulose
    • Isackson, P.J., Debold, W.A. and Reeck, G.R. (1980) Isolation and separation of chicken erythrocyte high mobility group non-histone chromatin proteins by chromatography on phosphocellulose. FEBS Lett., 119, 337-342.
    • (1980) FEBS Lett. , vol.119 , pp. 337-342
    • Isackson, P.J.1    Debold, W.A.2    Reeck, G.R.3
  • 39
    • 0019883147 scopus 로고
    • Circular dichroism, thermal denaturation and deoxyribonuclease 1 digestion studies of nucleosomes highly enriched in high mobility group protein HMG1 and HMG2
    • Jackson, J.B. and Rill, R.L. (1981) Circular dichroism, thermal denaturation and deoxyribonuclease 1 digestion studies of nucleosomes highly enriched in high mobility group protein HMG1 and HMG2. Biochemistry, 20, 1042-1046.
    • (1981) Biochemistry , vol.20 , pp. 1042-1046
    • Jackson, J.B.1    Rill, R.L.2
  • 40
    • 0018294176 scopus 로고
    • Chromatin fractionation procedure that yields nucleosomes containing near-stoichiometric amounts of high mobility group non histone chromosomal proteins
    • Jackson, J.B., Pollock, J.M.Jr and Rill, R.L. (1979) Chromatin fractionation procedure that yields nucleosomes containing near-stoichiometric amounts of high mobility group non histone chromosomal proteins. Biochemistry, 18, 3739-3748.
    • (1979) Biochemistry , vol.18 , pp. 3739-3748
    • Jackson, J.B.1    Pollock Jr., J.M.2    Rill, R.L.3
  • 41
    • 0023762972 scopus 로고
    • Full length cDNA sequence for bovine high mobility group 1 (HMG1) protein
    • Kaplan, D.J. and Duncan, C.H. (1988) Full length cDNA sequence for bovine high mobility group 1 (HMG1) protein. Nucleic Acids Res., 16, 10375-10375.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10375-10375
    • Kaplan, D.J.1    Duncan, C.H.2
  • 42
    • 0028129851 scopus 로고
    • HMG-X, a Xenopus gene encoding a HMG1 homolog, is abundantly expressed in the developing nervous system
    • Kinoshita, M., Hatada, S., Arashima, M. and Noda, M. (1994) HMG-X, a Xenopus gene encoding a HMG1 homolog, is abundantly expressed in the developing nervous system. FEBS Lett., 352, 191-196.
    • (1994) FEBS Lett. , vol.352 , pp. 191-196
    • Kinoshita, M.1    Hatada, S.2    Arashima, M.3    Noda, M.4
  • 43
    • 0020550415 scopus 로고
    • High mobility group proteins of amphibian oocytes: A large storage pool of a soluble high mobility group-1-like protein and involvement in transcriptional events
    • Kleinschmidt, J.A., Scheer, U., Dabauville, M.-C., Bustin, M. and Franke, W.W. (1983) High mobility group proteins of amphibian oocytes: a large storage pool of a soluble high mobility group-1-like protein and involvement in transcriptional events. J. Cell Biol., 97, 838-848.
    • (1983) J. Cell Biol. , vol.97 , pp. 838-848
    • Kleinschmidt, J.A.1    Scheer, U.2    Dabauville, M.-C.3    Bustin, M.4    Franke, W.W.5
  • 44
    • 0025239027 scopus 로고
    • Duplicated NHP6 genes of Saccharomyces cerevisiae encode proteins homologous to bovine high-mobility-group protein 1
    • Kolodrubetz, D. and Burgum, A. (1990) Duplicated NHP6 genes of Saccharomyces cerevisiae encode proteins homologous to bovine high-mobility-group protein 1. J. Biol. Chem., 265, 3234-3239.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3234-3239
    • Kolodrubetz, D.1    Burgum, A.2
  • 45
    • 0025309738 scopus 로고
    • Isolation and characterization of a Drosophila hydei histone DNA repeat unit
    • Kremer, H. and Hennig, W. (1990) Isolation and characterization of a Drosophila hydei histone DNA repeat unit. Nucleic Acids Res., 18, 1573-1580.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1573-1580
    • Kremer, H.1    Hennig, W.2
  • 46
    • 0025836057 scopus 로고
    • A negative regulator of HO transcription, SIN1 (SPT2), is a non specific DNA binding protein related to HMG1
    • Kruger, W. and Herskowitz, I. (1991) A negative regulator of HO transcription, SIN1 (SPT2), is a non specific DNA binding protein related to HMG1. Mol. Cell. Biol., 11, 4135-4146.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4135-4146
    • Kruger, W.1    Herskowitz, I.2
  • 47
    • 0026659070 scopus 로고
    • DNA-protein interactions. HMG has DNA wrapped up
    • Lilley, D.M. (1992) DNA-protein interactions. HMG has DNA wrapped up. Nature, 357, 282-283.
    • (1992) Nature , vol.357 , pp. 282-283
    • Lilley, D.M.1
  • 48
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components
    • Lohka, M.J. and Masui, Y. (1983) Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science, 220, 719-721.
    • (1983) Science , vol.220 , pp. 719-721
    • Lohka, M.J.1    Masui, Y.2
  • 49
    • 0021176610 scopus 로고
    • Roles of the cytosol and cytoplasmic particles in nuclear envelope assembly and sperm pronuclear formation in cell-free preparations from amphibian eggs
    • Lohka, M.J. and Masui, Y. (1984) Roles of the cytosol and cytoplasmic particles in nuclear envelope assembly and sperm pronuclear formation in cell-free preparations from amphibian eggs. J. Cell Biol., 98, 1222-1230.
    • (1984) J. Cell Biol. , vol.98 , pp. 1222-1230
    • Lohka, M.J.1    Masui, Y.2
  • 52
    • 0025916330 scopus 로고
    • Chromatosome positioning on assembled long chromatin: Linker histones affect nucleosome placement on 5S DNA
    • Meersseman, G., Pennings, S. and Bradbury, E.M. (1991) Chromatosome positioning on assembled long chromatin: linker histones affect nucleosome placement on 5S DNA. J. Mol. Biol., 220, 89-100.
    • (1991) J. Mol. Biol. , vol.220 , pp. 89-100
    • Meersseman, G.1    Pennings, S.2    Bradbury, E.M.3
  • 53
    • 0028211484 scopus 로고
    • HMG-D, the Drosophila melanogaster homologue of HMG1 protein, is associated with early embryonic chromatin in the place of histone H1
    • Ner, S.S. and Travers, A.A. (1994) HMG-D, the Drosophila melanogaster homologue of HMG1 protein, is associated with early embryonic chromatin in the place of histone H1. EMBO J., 13, 1817-1822.
    • (1994) EMBO J. , vol.13 , pp. 1817-1822
    • Ner, S.S.1    Travers, A.A.2
  • 54
  • 55
    • 0020407569 scopus 로고
    • A major developmental transition in early Xenopus embryos. 1. Characterization and timing of cellular changes at the mid blastula stage
    • Newport, J.W. and Kirschner, M.W. (1982a) A major developmental transition in early Xenopus embryos. 1. Characterization and timing of cellular changes at the mid blastula stage. Cell, 30, 675-686.
    • (1982) Cell , vol.30 , pp. 675-686
    • Newport, J.W.1    Kirschner, M.W.2
  • 56
    • 0020460737 scopus 로고
    • A major developmental transition in early Xenopus embryos. II. Control of the onset of transcription
    • Newport, J.W. and Kirschner, M.W. (1982b) A major developmental transition in early Xenopus embryos. II. Control of the onset of transcription. Cell, 30, 687-696.
    • (1982) Cell , vol.30 , pp. 687-696
    • Newport, J.W.1    Kirschner, M.W.2
  • 57
    • 0028954144 scopus 로고
    • Methylation at CpG sequences does not influence histone H1 binding to a nucleosome including a Xenopus borealis 5S rRNA gene
    • Nightingale, K. and Wolffe, A.P. (1995) Methylation at CpG sequences does not influence histone H1 binding to a nucleosome including a Xenopus borealis 5S rRNA gene. J. Biol. Chem., 270, 4197-1200.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4197-11200
    • Nightingale, K.1    Wolffe, A.P.2
  • 58
    • 23444445850 scopus 로고
    • Chromosome condensation in Xenopus mitotic extracts without histone H1
    • Ohsumi, K., Katagiri, C. and Kishimoto, T. (1993) Chromosome condensation in Xenopus mitotic extracts without histone H1. Science, 262, 2033-2035.
    • (1993) Science , vol.262 , pp. 2033-2035
    • Ohsumi, K.1    Katagiri, C.2    Kishimoto, T.3
  • 59
    • 0023651437 scopus 로고
    • Nucleotide sequence of rat liver HMG1 cDNA
    • Paonessa, G., Frank, R. and Cortese, R. (1987) Nucleotide sequence of rat liver HMG1 cDNA. Nucleic Acids Res., 15, 9077-9077.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 9077-9077
    • Paonessa, G.1    Frank, R.2    Cortese, R.3
  • 60
    • 0027216519 scopus 로고
    • The non specific DNA-binding and bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures
    • Paull, T.T., Haykinson, M.J. and Johnson, R.C. (1993) The non specific DNA-binding and bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures. Genes Dev., 7, 1521-1534.
    • (1993) Genes Dev. , vol.7 , pp. 1521-1534
    • Paull, T.T.1    Haykinson, M.J.2    Johnson, R.C.3
  • 61
    • 0022423480 scopus 로고
    • Isolation and sequence of cDNA clones coding for a member of the family of high mobility group proteins (HMG-T) in trout, and analysis of HMG-T-mRNAs in trout tissues
    • Pentecost, B.T., Wright, J.M. and Dixon, G.H. (1985) Isolation and sequence of cDNA clones coding for a member of the family of high mobility group proteins (HMG-T) in trout, and analysis of HMG-T-mRNAs in trout tissues. Nucleic Acids Res., 13, 4871-4888.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 4871-4888
    • Pentecost, B.T.1    Wright, J.M.2    Dixon, G.H.3
  • 62
    • 0026630997 scopus 로고
    • Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts
    • Philpott, A. and Leno, G.H. (1992) Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts. Cell, 69, 759-767.
    • (1992) Cell , vol.69 , pp. 759-767
    • Philpott, A.1    Leno, G.H.2
  • 63
    • 0028046675 scopus 로고
    • Cloning and characterization of seven human forkhead proteins: Binding site specificity and DNA bending
    • Pierrou, S., Hellquist, M., Samuelsson, L., Enerback, S. and Carlsson, P. (1994) Cloning and characterization of seven human forkhead proteins: binding site specificity and DNA bending. EMBO J., 13, 5002-5014.
    • (1994) EMBO J. , vol.13 , pp. 5002-5014
    • Pierrou, S.1    Hellquist, M.2    Samuelsson, L.3    Enerback, S.4    Carlsson, P.5
  • 64
    • 0026569275 scopus 로고
    • Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin
    • Pil, P.M. and Lippard, S.J. (1992) Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin. Science, 256, 234-236.
    • (1992) Science , vol.256 , pp. 234-236
    • Pil, P.M.1    Lippard, S.J.2
  • 65
    • 0029152586 scopus 로고
    • Nucleosomal anatomy - Where are the histones?
    • Pruss, D., Hayes, J.J. and Wolffe, A.P.L (1995) Nucleosomal anatomy - where are the histones? BioEssays, 17, 161-170.
    • (1995) BioEssays , vol.17 , pp. 161-170
    • Pruss, D.1    Hayes, J.J.2    Wolffe, A.P.L.3
  • 66
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, J.T., Graziano, V., Lee, P.L. and Sweet, R.M. (1993) Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature, 362, 219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 68
    • 0027993040 scopus 로고
    • The DNA sequence specificity of HMG boxes lies in the minor wing of the structure
    • Read, C.M., Cary, P.D., Preston, N.S., Luenicek-Allen, M. and Crane-Robinson, C. (1994) The DNA sequence specificity of HMG boxes lies in the minor wing of the structure. EMBO J., 13, 5369-5646.
    • (1994) EMBO J. , vol.13 , pp. 5369-5646
    • Read, C.M.1    Cary, P.D.2    Preston, N.S.3    Luenicek-Allen, M.4    Crane-Robinson, C.5
  • 69
    • 0019907207 scopus 로고
    • Domain structure in high molecular weight high mobility group non histone chromatin proteins
    • Reeck, G.R., Isackson, P.J. and Teller, D.C. (1982) Domain structure in high molecular weight high mobility group non histone chromatin proteins. Nature, 300, 76-78.
    • (1982) Nature , vol.300 , pp. 76-78
    • Reeck, G.R.1    Isackson, P.J.2    Teller, D.C.3
  • 70
    • 0022476944 scopus 로고
    • Mechanism of chromatin assembly in Xenopus oocytes
    • Ruberti, I. and Worcel, A. (1986) Mechanism of chromatin assembly in Xenopus oocytes. J. Mol. Biol., 189, 457-476.
    • (1986) J. Mol. Biol. , vol.189 , pp. 457-476
    • Ruberti, I.1    Worcel, A.2
  • 71
    • 0019133371 scopus 로고
    • A comparison of histone variants in different rat tissues
    • Russanova, V., Venkov, C. and Tsanev, R. (1980) A comparison of histone variants in different rat tissues. Cell Differ., 9, 339-350.
    • (1980) Cell Differ. , vol.9 , pp. 339-350
    • Russanova, V.1    Venkov, C.2    Tsanev, R.3
  • 73
    • 0020198155 scopus 로고
    • The binding sites for large and small high mobility group (HMG) proteins: Studies on HMG-nucleosome interactions in vitro
    • Schröter, H. and Bode, J. (1982) The binding sites for large and small high mobility group (HMG) proteins: studies on HMG-nucleosome interactions in vitro. Eur. J. Biochem., 127, 429-436.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 429-436
    • Schröter, H.1    Bode, J.2
  • 74
    • 0024401923 scopus 로고
    • High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA
    • Sheflin, L.G. and Spaulding, S.W. (1989) High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA. Biochemistry, 28, 5658-5664.
    • (1989) Biochemistry , vol.28 , pp. 5658-5664
    • Sheflin, L.G.1    Spaulding, S.W.2
  • 75
    • 0025285226 scopus 로고
    • Primary structure of non histone chromosomal protein HMG2 revealed by the nucleotide sequence
    • Shirakawa, H., Tsuda, K.-I. and Yoshida, M. (1990) Primary structure of non histone chromosomal protein HMG2 revealed by the nucleotide sequence. Biochemistry, 29, 4419-4423.
    • (1990) Biochemistry , vol.29 , pp. 4419-4423
    • Shirakawa, H.1    Tsuda, K.-I.2    Yoshida, M.3
  • 76
    • 0029078364 scopus 로고
    • Activation of the TFIID-TFIIA complex with HMG2
    • Shykind, B.M., Kim, J. and Sharp, P.A. (1995) Activation of the TFIID-TFIIA complex with HMG2. Genes Dev., 9, 1354-1365.
    • (1995) Genes Dev. , vol.9 , pp. 1354-1365
    • Shykind, B.M.1    Kim, J.2    Sharp, P.A.3
  • 77
    • 0018266771 scopus 로고
    • Structure of the chromatosome, a chromatin core particle containing 160 base pairs of DNA and all the histones
    • Simpson, R.T. (1978) Structure of the chromatosome, a chromatin core particle containing 160 base pairs of DNA and all the histones. Biochemistry, 17, 5524-5531.
    • (1978) Biochemistry , vol.17 , pp. 5524-5531
    • Simpson, R.T.1
  • 78
    • 0024100359 scopus 로고
    • Expression of a histone HI-like protein is restricted to early Xenopus development
    • Smith, R.C., Dworkin-Rastl, E. and Dworkin, M.D. (1988) Expression of a histone HI-like protein is restricted to early Xenopus development. Genes Dev., 2, 1284-1295.
    • (1988) Genes Dev. , vol.2 , pp. 1284-1295
    • Smith, R.C.1    Dworkin-Rastl, E.2    Dworkin, M.D.3
  • 79
    • 0026682636 scopus 로고
    • Sequence of a cDNA encoding chicken high mobility group protein 2
    • Sparrow, D.B. and Wells, J.R.E. (1992) Sequence of a cDNA encoding chicken high mobility group protein 2. Gene, 114, 289-290.
    • (1992) Gene , vol.114 , pp. 289-290
    • Sparrow, D.B.1    Wells, J.R.E.2
  • 80
    • 0026775596 scopus 로고
    • Nucleotide sequence of a mouse cDNA encoding the non histone chromosomal high mobility group protein 2 (HMG-2)
    • Stalzenburg, F. Dinkl, E. and Grummt, F. (1992) Nucleotide sequence of a mouse cDNA encoding the non histone chromosomal high mobility group protein 2 (HMG-2). Nucleic Acids Res., 20, 4927-4927.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4927-4927
    • Stalzenburg, F.1    Dinkl, E.2    Grummt, F.3
  • 81
    • 0028359704 scopus 로고
    • DNA looping by the HMG box domains of HMG1 and modulation of DNA binding by the acidic COOH-terminal domain
    • Stros, M., Stokrova, J. and Thomas, J.O. (1994) DNA looping by the HMG box domains of HMG1 and modulation of DNA binding by the acidic COOH-terminal domain. Nucleic Acids Res., 22, 1044-1051.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1044-1051
    • Stros, M.1    Stokrova, J.2    Thomas, J.O.3
  • 82
    • 0021112328 scopus 로고
    • Genomic organisation, DNA sequence and expression of chicken embryonic
    • Sugarman, B.J., Dodgson, J.B. and Engel, J.D. (1983) Genomic organisation, DNA sequence and expression of chicken embryonic. J. Biol. Chem., 258, 9005-9016.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9005-9016
    • Sugarman, B.J.1    Dodgson, J.B.2    Engel, J.D.3
  • 83
    • 0025222080 scopus 로고
    • Xenopus Y-box transcription factors: Molecular cloning, functional analysis and developmental regulation
    • Tafuri, S.R. and Wolffe, A.P. (1990) Xenopus Y-box transcription factors: molecular cloning, functional analysis and developmental regulation. Proc. Natl Acad. Sci. USA, 87, 9028-9032.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9028-9032
    • Tafuri, S.R.1    Wolffe, A.P.2
  • 84
    • 0017762802 scopus 로고
    • Reconstitution of chromatin core particles
    • Tatchell, K. and van Holde, K.E. (1977) Reconstitution of chromatin core particles. Biochemistry, 16, 5295-5303.
    • (1977) Biochemistry , vol.16 , pp. 5295-5303
    • Tatchell, K.1    Van Holde, K.E.2
  • 85
    • 0029117147 scopus 로고
    • Two mutations in the HMG box with very different structural consequences provide insights into the nature of binding to four-way junction DNA
    • Teo, S.H., Grasser, K.D., Hardman, C.H., Broadhurst, R.W., Lane, E.D. and Thomas, J.O. (1995) Two mutations in the HMG box with very different structural consequences provide insights into the nature of binding to four-way junction DNA. EMBO J., 14, 3844-3853.
    • (1995) EMBO J. , vol.14 , pp. 3844-3853
    • Teo, S.H.1    Grasser, K.D.2    Hardman, C.H.3    Broadhurst, R.W.4    Lane, E.D.5    Thomas, J.O.6
  • 86
    • 0026597552 scopus 로고
    • Cooperative binding of the globular domains of histones H1 and H5 to DNA
    • Thomas, J.O., Rees, C. and Finch, J.T. (1992) Cooperative binding of the globular domains of histones H1 and H5 to DNA. Nucleic Acids Res., 20, 187-194.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 187-194
    • Thomas, J.O.1    Rees, C.2    Finch, J.T.3
  • 87
    • 0017382546 scopus 로고
    • Two dimensional electrophoretic analysis of polynucleosomes
    • Todd, R.D. and Garrard, W.T. (1977) Two dimensional electrophoretic analysis of polynucleosomes. J. Biol. Chem., 252, 4729-4738.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4729-4738
    • Todd, R.D.1    Garrard, W.T.2
  • 88
    • 0028226799 scopus 로고
    • DNA chaperones: A solution to a persistence problem
    • Travers, A.A., Ner, S.S. and Churchill, M.E.A. (1994) DNA chaperones: a solution to a persistence problem. Cell, 77, 167-170.
    • (1994) Cell , vol.77 , pp. 167-170
    • Travers, A.A.1    Ner, S.S.2    Churchill, M.E.A.3
  • 89
    • 0022826752 scopus 로고
    • High mobility group proteins 1 and 2 stimulate transcription in vitro by RNA polymerases II and III
    • Tremethick, D.J. and Molloy, P.L. (1986) High mobility group proteins 1 and 2 stimulate transcription in vitro by RNA polymerases II and III. J. Biol. Chem., 261, 6986-6996.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6986-6996
    • Tremethick, D.J.1    Molloy, P.L.2
  • 90
    • 0023705812 scopus 로고
    • Primary structure of non histone protein HMG1 revealed by the nucleotide sequence
    • Tsuda, K.-I., Kikuchi, M., Mori, K., Waga, S. and Yoshida, M. (1988) Primary structure of non histone protein HMG1 revealed by the nucleotide sequence. Biochemistry, 27, 6159-6163.
    • (1988) Biochemistry , vol.27 , pp. 6159-6163
    • Tsuda, K.-I.1    Kikuchi, M.2    Mori, K.3    Waga, S.4    Yoshida, M.5
  • 91
    • 0028127302 scopus 로고
    • Core histone acetylation does not block linker histone binding to a nucleosome including a Xenopus borealis 5S rRNA gene
    • Ura, K., Wolffe, A.P. and Hayes, J.J. (1994) Core histone acetylation does not block linker histone binding to a nucleosome including a Xenopus borealis 5S rRNA gene. J. Biol. Chem., 269, 27171-27174.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27171-27174
    • Ura, K.1    Wolffe, A.P.2    Hayes, J.J.3
  • 92
    • 0029091306 scopus 로고
    • A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: Restriction by linker histones
    • Ura, K., Hayes, J.J. and Wolffe, A.P. (1995) A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: restriction by linker histones. EMBO J., 14, 3752-3765.
    • (1995) EMBO J. , vol.14 , pp. 3752-3765
    • Ura, K.1    Hayes, J.J.2    Wolffe, A.P.3
  • 93
    • 0003903126 scopus 로고
    • Springer-Verlag, New York
    • van Holde, K.E. (1988) Chromatin. Springer-Verlag, New York.
    • (1988) Chromatin
    • Van Holde, K.E.1
  • 95
    • 0017238172 scopus 로고
    • Heterogeneity of chromatin subunits in vitro and location of histone H1
    • Varshavsky, A.J., Bakayev, V.V. and Georgiev, G.P. (1976) Heterogeneity of chromatin subunits in vitro and location of histone H1. Nucleic Acids Res., 3, 477-479.
    • (1976) Nucleic Acids Res. , vol.3 , pp. 477-479
    • Varshavsky, A.J.1    Bakayev, V.V.2    Georgiev, G.P.3
  • 96
    • 0024561316 scopus 로고
    • Non histone proteins HMG1 and HMG2 suppress the nucleosome assembly at physiological ionic strength
    • Waga, S., Mizuno, S. and Yoshida, M. (1989) Non histone proteins HMG1 and HMG2 suppress the nucleosome assembly at physiological ionic strength. Biochim. Biophys. Acta, 1007, 209-219.
    • (1989) Biochim. Biophys. Acta , vol.1007 , pp. 209-219
    • Waga, S.1    Mizuno, S.2    Yoshida, M.3
  • 97
    • 0026704583 scopus 로고
    • A high-mobility-group protein and its DNAs from Drosophila melanogaster
    • Wagner, C.R., Hamana, K. and Elgin, S.C.R. (1992) A high-mobility-group protein and its DNAs from Drosophila melanogaster. Mol. Cell. Biol., 12, 1915-1923.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1915-1923
    • Wagner, C.R.1    Hamana, K.2    Elgin, S.C.R.3
  • 99
    • 0020211154 scopus 로고
    • Active chromatin of oocytes injected with somatic cell nuclei or cloned DNA
    • Weisbrod, S., Wickens, M.P., Whytock, S. and Gurdon, J.B. (1982) Active chromatin of oocytes injected with somatic cell nuclei or cloned DNA. Dev. Biol., 94, 216-229.
    • (1982) Dev. Biol. , vol.94 , pp. 216-229
    • Weisbrod, S.1    Wickens, M.P.2    Whytock, S.3    Gurdon, J.B.4
  • 100
    • 0024590341 scopus 로고
    • A human placental cDNA clone that encodes non histone chromosomal protein HMG-1
    • Wen, L., Huang, J.K., Johnson, B.H. and Reeck, G.R. (1989) A human placental cDNA clone that encodes non histone chromosomal protein HMG-1. Nucleic Acids Res., 17, 1197-1214.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1197-1214
    • Wen, L.1    Huang, J.K.2    Johnson, B.H.3    Reeck, G.R.4
  • 101
    • 0029075461 scopus 로고
    • Molecular basis of human 46X.Y sex reversal revealed from the three dimensional solution structure of the human SRY-DNA complex
    • Werner, M.H., Huth, J.R., Gronenborn, A.M. and Clore, G.M. (1995) Molecular basis of human 46X.Y sex reversal revealed from the three dimensional solution structure of the human SRY-DNA complex. Cell, 81, 705-717.
    • (1995) Cell , vol.81 , pp. 705-717
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 102
    • 0026794748 scopus 로고
    • Insect proteins homologous to mammalian high-mobility-group protein 1: Characterization and DNA-binding properties
    • Wisniewski, J.R. and Schulze, E. (1992) Insect proteins homologous to mammalian high-mobility-group protein 1: characterization and DNA-binding properties. J. Biol. Chem., 267, 17170-17177.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17170-17177
    • Wisniewski, J.R.1    Schulze, E.2
  • 103
    • 0024977888 scopus 로고
    • Transcriptional activation of Xenopus class III genes in chromatin isolated from sperm and somatic nuclei
    • Wolffe, A.P. (1989a) Transcriptional activation of Xenopus class III genes in chromatin isolated from sperm and somatic nuclei. Nucleic Acids Res., 17, 767-780.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 767-780
    • Wolffe, A.P.1
  • 104
    • 0024414257 scopus 로고
    • Dominant and specific repression of Xenopus oocyte 5S RNA genes and satellite 1 DNA by histone H1
    • Wolffe, A.P. (1989b) Dominant and specific repression of Xenopus oocyte 5S RNA genes and satellite 1 DNA by histone H1. EMBO J., 8, 527-537.
    • (1989) EMBO J. , vol.8 , pp. 527-537
    • Wolffe, A.P.1
  • 105
    • 0000215015 scopus 로고
    • Transcription factor interactions with model nucleosomal templates
    • Wolffe, A.P. and Hayes, J.J. (1993) Transcription factor interactions with model nucleosomal templates. Methods Mol. Genet., 2, 314-330.
    • (1993) Methods Mol. Genet. , vol.2 , pp. 314-330
    • Wolffe, A.P.1    Hayes, J.J.2
  • 106
    • 0026770702 scopus 로고
    • Nucleotide sequence of a mouse cDNA encoding the non-histone chromosomal high mobility group protein-1 (HMG1)
    • Yotov, W.V. and St-Arnaud, R. (1992) Nucleotide sequence of a mouse cDNA encoding the non-histone chromosomal high mobility group protein-1 (HMG1). Nucleic Acids Res., 20, 3516-3516.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3516-3516
    • Yotov, W.V.1    St-Arnaud, R.2


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