메뉴 건너뛰기




Volumn 17, Issue 12, 2010, Pages 1500-1507

H2A.Z nucleosomes enriched over active genes are homotypic

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2A; HISTONE H2AZ;

EID: 78649884849     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1926     Document Type: Article
Times cited : (100)

References (55)
  • 1
    • 77949874234 scopus 로고    scopus 로고
    • Histone variants-ancient wrap artists of the epigenome
    • Talbert, P.B. & Henikoff, S. Histone variants-ancient wrap artists of the epigenome. Nat. Rev. Mol. Cell Biol. 11, 264-275 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 264-275
    • Talbert, P.B.1    Henikoff, S.2
  • 2
    • 0019011791 scopus 로고
    • Drosophila nucleosomes contain an unusual histone-like protein
    • Palmer, D., Snyder, L.A. & Blumenfeld, M. Drosophila nucleosomes contain an unusual histone-like protein. Proc. Natl. Acad. Sci. USA 77, 2671-2675 (1980).
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2671-2675
    • Palmer, D.1    Snyder, L.A.2    Blumenfeld, M.3
  • 3
    • 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 31, 367-374 (1982).
    • (1982) Cell , vol.31 , pp. 367-374
    • Wu, R.S.1    Tsai, S.2    Bonner, W.M.3
  • 4
    • 38949091078 scopus 로고    scopus 로고
    • H2A.Z: View from the top
    • Zlatanova, J. & Thakar, A. H2A.Z: view from the top. Structure 16, 166-179 (2008).
    • (2008) Structure , vol.16 , pp. 166-179
    • Zlatanova, J.1    Thakar, A.2
  • 5
    • 0029954395 scopus 로고    scopus 로고
    • Essential and nonessential histone H2A variants in Tetrahymena thermophila
    • Liu, X., Li, B. & Gorovsky, M. Essential and nonessential histone H2A variants in Tetrahymena thermophila. Mol. Cell. Biol. 16, 4305-4311 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4305-4311
    • Liu, X.1    Li, B.2    Gorovsky, M.3
  • 6
    • 6344277345 scopus 로고    scopus 로고
    • Unique residues on the H2A.Z containing nucleosome surface are important for Xenopus laevis development
    • Ridgway, P., Brown, K.D., Rangasamy, D., Svensson, U. & Tremethick, D.J. Unique residues on the H2A.Z containing nucleosome surface are important for Xenopus laevis development. J. Biol. Chem. 279, 43815-43820 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 43815-43820
    • Ridgway, P.1    Brown, K.D.2    Rangasamy, D.3    Svensson, U.4    Tremethick, D.J.5
  • 7
    • 0035822687 scopus 로고    scopus 로고
    • Histone variant H2A.Z is required for early mammalian development
    • Faast, R. et al. Histone variant H2A.Z is required for early mammalian development. Curr. Biol. 11, 1183-1187 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1183-1187
    • Faast, R.1
  • 8
    • 0027058961 scopus 로고
    • A histone variant, H2AvD, is essential in Drosophila melanogaster
    • van Daal, A. & Elgin, S.C. A histone variant, H2AvD, is essential in Drosophila melanogaster. Mol. Biol. Cell 3, 593-602 (1992).
    • (1992) Mol. Biol. Cell , vol.3 , pp. 593-602
    • Van Daal, A.1    Elgin, S.C.2
  • 9
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin
    • Kobor, M.S. et al. A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin. PLoS Biol. 2, E131 (2004).
    • (2004) PLoS Biol. , vol.2
    • Kobor, M.S.1
  • 10
    • 9144269660 scopus 로고    scopus 로고
    • A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1
    • Krogan, N.J. et al. A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1. Mol. Cell 12, 1565-1576 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1565-1576
    • Krogan, N.J.1
  • 11
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi, G. et al. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303, 343-348 (2004).
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1
  • 12
    • 43749099875 scopus 로고    scopus 로고
    • Nucleosome organization in the Drosophila genome
    • Mavrich, T.N. et al. Nucleosome organization in the Drosophila genome. Nature 453, 358-362 (2008).
    • (2008) Nature , vol.453 , pp. 358-362
    • Mavrich, T.N.1
  • 13
    • 34249026300 scopus 로고    scopus 로고
    • High-resolution profling of histone methylations in the human genome
    • Barski, A. et al. High-resolution profling of histone methylations in the human genome. Cell 129, 823-837 (2007).
    • (2007) Cell , vol.129 , pp. 823-837
    • Barski, A.1
  • 14
    • 55549141877 scopus 로고    scopus 로고
    • Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks
    • Zilberman, D., Coleman-Derr, D., Ballinger, T. & Henikoff, S. Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks. Nature 456, 125-129 (2008).
    • (2008) Nature , vol.456 , pp. 125-129
    • Zilberman, D.1    Coleman-Derr, D.2    Ballinger, T.3    Henikoff, S.4
  • 15
    • 76349103252 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe genome-wide nucleosome mapping reveals positioning mechanisms distinct from those of Saccharomyces cerevisiae
    • Lantermann, A.B. et al. Schizosaccharomyces pombe genome-wide nucleosome mapping reveals positioning mechanisms distinct from those of Saccharomyces cerevisiae. Nat. Struct. Mol. Biol. 17, 251-257 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 251-257
    • Lantermann, A.B.1
  • 16
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • Suto, R.K., Clarkson, M.J., Tremethick, D.J. & Luger, K. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat. Struct. Biol. 7, 1121-1124 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 18
    • 33745842279 scopus 로고    scopus 로고
    • Analysis of human histone H2AZ deposition in vivo argues against its direct role in epigenetic templating mechanisms
    • Viens, A. et al. Analysis of human histone H2AZ deposition in vivo argues against its direct role in epigenetic templating mechanisms. Mol. Cell. Biol. 26, 5325-5335 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5325-5335
    • Viens, A.1
  • 19
    • 2642515598 scopus 로고    scopus 로고
    • A new fuorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome
    • Park, Y.J., Dyer, P.N., Tremethick, D.J. & Luger, K. A new fuorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome. J. Biol. Chem. 279, 24274-24282 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 24274-24282
    • Park, Y.J.1    Dyer, P.N.2    Tremethick, D.J.3    Luger, K.4
  • 20
    • 0027716843 scopus 로고
    • Effects of histone acetylation, ubiquitination and variants on nucleosome stability
    • Li, W., Nagaraja, S., Delcuve, G.P., Hendzel, M.J. & Davie, J.R. Effects of histone acetylation, ubiquitination and variants on nucleosome stability. Biochem. J. 296, 737-744 (1993).
    • (1993) Biochem. J. , vol.296 , pp. 737-744
    • Li, W.1    Nagaraja, S.2    Delcuve, G.P.3    Hendzel, M.J.4    Davie, J.R.5
  • 21
    • 33746015346 scopus 로고    scopus 로고
    • H2A.Z stabilizes chromatin in a way that is dependent on core histone acetylation
    • Thambirajah, A.A. et al. H2A.Z stabilizes chromatin in a way that is dependent on core histone acetylation. J. Biol. Chem. 281, 20036-20044 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 20036-20044
    • Thambirajah, A.A.1
  • 22
    • 77952378219 scopus 로고    scopus 로고
    • Histone variant H2A.Z inhibits transcription in reconstituted nucleosomes
    • Thakar, A., Gupta, P., McAllister, W.T. & Zlatanova, J. Histone variant H2A.Z inhibits transcription in reconstituted nucleosomes. Biochemistry 49, 4018-4026 (2010).
    • (2010) Biochemistry , vol.49 , pp. 4018-4026
    • Thakar, A.1    Gupta, P.2    McAllister, W.T.3    Zlatanova, J.4
  • 23
    • 66649092628 scopus 로고    scopus 로고
    • Acetylation of vertebrate H2A.Z and its effect on the structure of the nucleosome
    • Ishibashi, T. et al. Acetylation of vertebrate H2A.Z and its effect on the structure of the nucleosome. Biochemistry 48, 5007-5017 (2009).
    • (2009) Biochemistry , vol.48 , pp. 5007-5017
    • Ishibashi, T.1
  • 24
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • Malik, H.S. & Henikoff, S. Phylogenomics of the nucleosome. Nat. Struct. Biol. 10, 882-891 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 25
    • 34250745886 scopus 로고    scopus 로고
    • Nucleosome stability mediated by histone variants H3.3 and H2A.Z
    • Jin, C. & Felsenfeld, G. Nucleosome stability mediated by histone variants H3.3 and H2A.Z. Genes Dev. 21, 1519-1529 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1519-1529
    • Jin, C.1    Felsenfeld, G.2
  • 26
    • 0037264483 scopus 로고    scopus 로고
    • Single-strand-specifc nucleases
    • Desai, N.A. & Shankar, V. Single-strand-specifc nucleases. FEMS Microbiol. Rev. 26, 457-491 (2003).
    • (2003) FEMS Microbiol. Rev. , vol.26 , pp. 457-491
    • Desai, N.A.1    Shankar, V.2
  • 27
    • 0024977414 scopus 로고
    • Five intermediate complexes in transcription initiation by RNA polymerase II
    • Buratowski, S., Hahn, S., Guarente, L. & Sharp, P.A. Five intermediate complexes in transcription initiation by RNA polymerase II. Cell 56, 549-561 (1989).
    • (1989) Cell , vol.56 , pp. 549-561
    • Buratowski, S.1    Hahn, S.2    Guarente, L.3    Sharp, P.A.4
  • 28
    • 0030804783 scopus 로고    scopus 로고
    • RNA polymerase II stalled at a thymine dimer: Footprint and effect on excision repair
    • Selby, C.P., Drapkin, R., Reinberg, D. & Sancar, A. RNA polymerase II stalled at a thymine dimer: Footprint and effect on excision repair. Nucleic Acids Res. 25, 787-793 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 787-793
    • Selby, C.P.1    Drapkin, R.2    Reinberg, D.3    Sancar, A.4
  • 29
    • 61849170193 scopus 로고    scopus 로고
    • Genome-wide profling of salt fractions maps physical properties of chromatin
    • Henikoff, S., Henikoff, J.G., Sakai, A., Loeb, G.B. & Ahmad, K. Genome-wide profling of salt fractions maps physical properties of chromatin. Genome Res. 19, 460-469 (2009).
    • (2009) Genome Res. , vol.19 , pp. 460-469
    • Henikoff, S.1    Henikoff, J.G.2    Sakai, A.3    Loeb, G.B.4    Ahmad, K.5
  • 30
    • 0019011791 scopus 로고
    • Drosophila nucleosomes contain an unusual histone-like protein
    • Palmer, D., Snyder, L.A. & Blumenfeld, M. Drosophila nucleosomes contain an unusual histone-like protein. Proc. Natl. Acad. Sci. USA 77, 2671-2675 (1980).
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2671-2675
    • Palmer, D.1    Snyder, L.A.2    Blumenfeld, M.3
  • 31
    • 69949132191 scopus 로고    scopus 로고
    • Chromatin organization marks exon-intron structure
    • Schwartz, S., Meshorer, E. & Ast, G. Chromatin organization marks exon-intron structure. Nat. Struct. Mol. Biol. 16, 990-995 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 990-995
    • Schwartz, S.1    Meshorer, E.2    Ast, G.3
  • 32
    • 36249027156 scopus 로고    scopus 로고
    • Recognition of trimethylated histone h3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing
    • Sims, R.J. et al. Recognition of trimethylated histone h3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. Mol. Cell 28, 665-676 (2007).
    • (2007) Mol. Cell , vol.28 , pp. 665-676
    • Sims, R.J.1
  • 33
    • 69949124307 scopus 로고    scopus 로고
    • Nucleosome positioning as a determinant of exon recognition
    • Tilgner, H. et al. Nucleosome positioning as a determinant of exon recognition. Nat. Struct. Mol. Biol. 16, 996-1001 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 996-1001
    • Tilgner, H.1
  • 34
    • 0021250601 scopus 로고
    • Differential salt fractionation of active and inactive genomic domains in chicken erythrocyte
    • Rocha, E., Davie, J.R., van Holde, K.E. & Weintraub, H. Differential salt fractionation of active and inactive genomic domains in chicken erythrocyte. J. Biol. Chem. 259, 8558-8563 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 8558-8563
    • Rocha, E.1    Davie, J.R.2    Van Holde, K.E.3    Weintraub, H.4
  • 35
    • 0025166038 scopus 로고
    • Postinitiation transcriptional control in Drosophila melanogaster
    • Rougvie, A.E. & Lis, J.T. Postinitiation transcriptional control in Drosophila melanogaster. Mol. Cell 10, 6041-6045 (1990).
    • (1990) Mol. Cell , vol.10 , pp. 6041-6045
    • Rougvie, A.E.1    Lis, J.T.2
  • 36
    • 36549061004 scopus 로고    scopus 로고
    • RNA polymerase is poised for activation across the genome
    • Muse, G.W. et al. RNA polymerase is poised for activation across the genome. Nat. Genet. 39, 1507-1511 (2007).
    • (2007) Nat. Genet. , vol.39 , pp. 1507-1511
    • Muse, G.W.1
  • 37
    • 77951920690 scopus 로고    scopus 로고
    • C-Myc regulates transcriptional pause release
    • Rahl, P.B. et al. c-Myc regulates transcriptional pause release. Cell 141, 432-445 (2010).
    • (2010) Cell , vol.141 , pp. 432-445
    • Rahl, P.B.1
  • 38
    • 68149158205 scopus 로고    scopus 로고
    • Labile H3.3+H2A.Z nucleosomes mark 'nucleosome-free regions
    • Henikoff, S. Labile H3.3+H2A.Z nucleosomes mark 'nucleosome-free regions'. Nat. Genet. 41, 865-866 (2009).
    • (2009) Nat. Genet. , vol.41 , pp. 865-866
    • Henikoff, S.1
  • 39
    • 68149150830 scopus 로고    scopus 로고
    • H3.3/H2A.Z double variant-containing nucleosomes mark 'nucleosome-free regions' of active promoters and other regulatory regions in the human genome
    • Jin, C. et al. H3.3/H2A.Z double variant-containing nucleosomes mark 'nucleosome-free regions' of active promoters and other regulatory regions in the human genome. Nat. Genet. 41, 941-945 (2009).
    • (2009) Nat. Genet. , vol.41 , pp. 941-945
    • Jin, C.1
  • 40
    • 0036203807 scopus 로고    scopus 로고
    • Nucleosome remodeling induced by RNA polymerase II: Loss of the H2A/H2B dimer during transcription
    • Kireeva, M.L. et al. Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription. Mol. Cell 9, 541-552 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 541-552
    • Kireeva, M.L.1
  • 41
    • 77951169141 scopus 로고    scopus 로고
    • Chromatin remodeling by imitation switch (ISWI) class ATP-dependent remodelers is stimulated by histone variant H2A.Z
    • Goldman, J.A., Garlick, J.D. & Kingston, R.E. Chromatin remodeling by imitation switch (ISWI) class ATP-dependent remodelers is stimulated by histone variant H2A.Z. J. Biol. Chem. 285, 4645-4651 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 4645-4651
    • Goldman, J.A.1    Garlick, J.D.2    Kingston, R.E.3
  • 42
    • 0026713778 scopus 로고
    • What happens to nucleosomes during transcription?
    • van Holde, K.E., Lohr, D.E. & Robert, C. What happens to nucleosomes during transcription? J. Biol. Chem. 267, 2837-2840 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 2837-2840
    • Van Holde, K.E.1    Lohr, D.E.2    Robert, C.3
  • 43
    • 38849132828 scopus 로고    scopus 로고
    • The functional response of upstream DNA to dynamic supercoiling in vivo
    • Kouzine, F., Sanford, S., Elisha-Feil, Z. & Levens, D. The functional response of upstream DNA to dynamic supercoiling in vivo. Nat. Struct. Mol. Biol. 15, 146-154 (2008).
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 146-154
    • Kouzine, F.1    Sanford, S.2    Elisha-Feil, Z.3    Levens, D.4
  • 44
    • 34250803868 scopus 로고    scopus 로고
    • Nucleosome chiral transition under positive torsional stress in single chromatin fbers
    • Bancaud, A. et al. Nucleosome chiral transition under positive torsional stress in single chromatin fbers. Mol. Cell 27, 135-147 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 135-147
    • Bancaud, A.1
  • 45
    • 0030028981 scopus 로고    scopus 로고
    • Differential control of transcription-induced and overall DNA supercoiling by eukaryotic topoisomerases in vitro
    • Wang, Z. & Droge, P. Differential control of transcription-induced and overall DNA supercoiling by eukaryotic topoisomerases in vitro. EMBO J. 15, 581-589 (1996).
    • (1996) EMBO J. , vol.15 , pp. 581-589
    • Wang, Z.1    Droge, P.2
  • 46
    • 34147206187 scopus 로고    scopus 로고
    • Backtracking determines the force sensitivity of RNAP II in a factor-dependent manner
    • Galburt, E.A. et al. Backtracking determines the force sensitivity of RNAP II in a factor-dependent manner. Nature 446, 820-823 (2007).
    • (2007) Nature , vol.446 , pp. 820-823
    • Galburt, E.A.1
  • 47
    • 34047111213 scopus 로고    scopus 로고
    • Translational and rotational settings of H2A.Z nucleosomes across the Saccharomyces cerevisiae genome
    • Albert, I. et al. Translational and rotational settings of H2A.Z nucleosomes across the Saccharomyces cerevisiae genome. Nature 446, 572-576 (2007).
    • (2007) Nature , vol.446 , pp. 572-576
    • Albert, I.1
  • 49
    • 0036712095 scopus 로고    scopus 로고
    • DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis
    • Madigan, J.P., Chotkowski, H.L. & Glaser, R.L. DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis. Nucleic Acids Res. 30, 3698-3705 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3698-3705
    • Madigan, J.P.1    Chotkowski, H.L.2    Glaser, R.L.3
  • 50
    • 27144510368 scopus 로고    scopus 로고
    • Genome-scale profling of histone H3.3 replacement patterns
    • Mito, Y., Henikoff, J.G. & Henikoff, S. Genome-scale profling of histone H3.3 replacement patterns. Nat. Genet. 37, 1090-1097 (2005).
    • (2005) Nat. Genet. , vol.37 , pp. 1090-1097
    • Mito, Y.1    Henikoff, J.G.2    Henikoff, S.3
  • 51
    • 61849170193 scopus 로고    scopus 로고
    • Genome-wide profling of salt fractions maps physical properties of chromatin
    • Henikoff, S., Henikoff, J.G., Sakai, A., Loeb, G.B. & Ahmad, K. Genome-wide profling of salt fractions maps physical properties of chromatin. Genome Res. 19, 460-469 (2009).
    • (2009) Genome Res. , vol.19 , pp. 460-469
    • Henikoff, S.1    Henikoff, J.G.2    Sakai, A.3    Loeb, G.B.4    Ahmad, K.5
  • 52
    • 77957729191 scopus 로고    scopus 로고
    • Baculovirus-encoded protein expression for epigenomic profling in Drosophila cells
    • Bryson, T.D., Weber, C.M. & Henikoff, S. Baculovirus-encoded protein expression for epigenomic profling in Drosophila cells. Fly (Austin) 4, 258-265 (2010).
    • (2010) Fly (Austin) , vol.4 , pp. 258-265
    • Bryson, T.D.1    Weber, C.M.2    Henikoff, S.3
  • 53
    • 67149086996 scopus 로고    scopus 로고
    • Extensive demethylation of repetitive elements during seed development underlies gene imprinting
    • Gehring, M., Bubb, K. & Henikoff, S. Extensive demethylation of repetitive elements during seed development underlies gene imprinting. Science 324, 1447-1451 (2009).
    • (2009) Science , vol.324 , pp. 1447-1451
    • Gehring, M.1    Bubb, K.2    Henikoff, S.3
  • 54
    • 33750442876 scopus 로고    scopus 로고
    • Large-scale turnover of functional transcription factor binding sites in Drosophila
    • Moses, A.M. et al. Large-scale turnover of functional transcription factor binding sites in Drosophila. PLOS Comput. Biol. 2, e130 (2006).
    • (2006) PLOS Comput. Biol. , vol.2
    • Moses, A.M.1
  • 55
    • 33745225872 scopus 로고    scopus 로고
    • Genome-wide analysis of Polycomb targets in Drosophila melanogaster
    • Schwartz, Y.B. et al. Genome-wide analysis of Polycomb targets in Drosophila melanogaster. Nat. Genet. 38, 700-705 (2006).
    • (2006) Nat. Genet. , vol.38 , pp. 700-705
    • Schwartz, Y.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.