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Volumn 369, Issue , 2007, Pages 345-363

Cryoelectron microscopy of icosahedral virus particles

(2)  Jiang, Wen a   Chiu, Wah a  

a NONE

Author keywords

3D reconstruction; Cryo EM; Cryoelectron microscopy; Icosahedral virus; Secondary structure elements; Structural fitting; Subnanometer resolution

Indexed keywords

MIRIDAE;

EID: 34548008824     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1385/1-59745-294-7:345     Document Type: Article
Times cited : (13)

References (58)
  • 1
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by fourier synthesis from electron micrographs
    • Crowther, R. A., Amos, L. A., Finch, J. T., De Rosier, D. J., and Klug, A. (1970) Three dimensional reconstructions of spherical viruses by fourier synthesis from electron micrographs. Nature 226, 421-425.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    De Rosier, D.J.4    Klug, A.5
  • 2
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by fourier synthesis from electron micrographs
    • Crowther, R. A. (1971) Procedures for three-dimensional reconstruction of spherical viruses by fourier synthesis from electron micrographs. Phil. Trans. Roy. Soc. Land. B. 261, 221-230.
    • (1971) Phil. Trans. Roy. Soc. Land. B , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 3
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Bottcher, B., Wynne, S. A., and Crowther, R. A. (1997) Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386, 88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 4
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway, J. F., Cheng, N., Zlotnick, A., Wingfield, P. T., Stahl, S. J., and Steven, A. C. (1997) Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 386, 91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 6
    • 0034814786 scopus 로고    scopus 로고
    • Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus
    • Zhou, Z. H., Baker, M. L., Jiang, W., Dougherty, M., Jakana, J., Dong, G., Lu, G., and Chiu, W. (2001) Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus. Nat. Struct. Biol. 8, 868-873.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 868-873
    • Zhou, Z.H.1    Baker, M.L.2    Jiang, W.3    Dougherty, M.4    Jakana, J.5    Dong, G.6    Lu, G.7    Chiu, W.8
  • 7
    • 14844325731 scopus 로고    scopus 로고
    • Electron cryomicroscopy of biological machines at subnanometer resolution
    • Chiu, W., Baker, M. L., Jiang, W., Dougherty, M., and Schmid, M. F. (2005) Electron cryomicroscopy of biological machines at subnanometer resolution. Structure 13, 363-372.
    • (2005) Structure , vol.13 , pp. 363-372
    • Chiu, W.1    Baker, M.L.2    Jiang, W.3    Dougherty, M.4    Schmid, M.F.5
  • 8
    • 0035906702 scopus 로고    scopus 로고
    • Bridging the information gap: Computational tools for intermediate resolution structure interpretation
    • Jiang, W., Baker, M. L., Ludtke, S. J., and Chiu, W. (2001) Bridging the information gap: computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 308, 1033-1044.
    • (2001) J. Mol. Biol , vol.308 , pp. 1033-1044
    • Jiang, W.1    Baker, M.L.2    Ludtke, S.J.3    Chiu, W.4
  • 9
    • 0036535896 scopus 로고    scopus 로고
    • Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches
    • Chiu, W., Baker, M. L., Jiang, W., and Zhou, Z. H. (2002) Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches. Curr. Opin. Struct. Biol. 12, 263-269.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 263-269
    • Chiu, W.1    Baker, M.L.2    Jiang, W.3    Zhou, Z.H.4
  • 10
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R., and Chiu, W. (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97.
    • (1999) J. Struct. Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 11
    • 0041561177 scopus 로고    scopus 로고
    • Semi-automated icosahedral particle reconstruction at sub-nanometer resolution
    • Jiang, W., Li, Z., Zhang, Z., Booth, C. R., Baker, M. L., and Chiu, W. (2001) Semi-automated icosahedral particle reconstruction at sub-nanometer resolution. J. Struct. Biol. 136, 214-225.
    • (2001) J. Struct. Biol , vol.136 , pp. 214-225
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Booth, C.R.4    Baker, M.L.5    Chiu, W.6
  • 14
    • 0024007766 scopus 로고
    • Cryo-electron microscopy of vitrified specimens
    • Dubochet, J., Adrian, M., Chang, J. J., et al. (1988) Cryo-electron microscopy of vitrified specimens. Q. Rev. Biophys. 21, 129-228.
    • (1988) Q. Rev. Biophys , vol.21 , pp. 129-228
    • Dubochet, J.1    Adrian, M.2    Chang, J.J.3
  • 15
    • 0013823053 scopus 로고
    • A new method of preparation of a self-perforated micro plastic grid and its application
    • Fukami, A. and Adachi, K. (1965) A new method of preparation of a self-perforated micro plastic grid and its application, J. Electron Microsc. 14, 112-118.
    • (1965) J. Electron Microsc , vol.14 , pp. 112-118
    • Fukami, A.1    Adachi, K.2
  • 16
    • 0023889015 scopus 로고
    • Containment system for the preparation of vitrified-hydrated virus specimens
    • Jeng, T. W., Talmon, Y., and Chiu, W. (1988) Containment system for the preparation of vitrified-hydrated virus specimens. J. Electron Microsc. Tech. 8, 343-348.
    • (1988) J. Electron Microsc. Tech , vol.8 , pp. 343-348
    • Jeng, T.W.1    Talmon, Y.2    Chiu, W.3
  • 17
    • 16644365074 scopus 로고    scopus 로고
    • A 9 Åsingle particle reconstruction from CCD captured images on a 200 kV electron cryomicroscope
    • Booth, C. R., Jiang, W., Baker, M. L., Zhou, Z. H., Ludtke, S. J., and Chiu, W. (2004) A 9 Åsingle particle reconstruction from CCD captured images on a 200 kV electron cryomicroscope. J. Struct. Biol. 147, 116-127.
    • (2004) J. Struct. Biol , vol.147 , pp. 116-127
    • Booth, C.R.1    Jiang, W.2    Baker, M.L.3    Zhou, Z.H.4    Ludtke, S.J.5    Chiu, W.6
  • 18
    • 20544468931 scopus 로고    scopus 로고
    • Automated molecular microscopy: The new Leginon system
    • Suloway, C., Pulokas, J., Fellmann, D., et al. (2005) Automated molecular microscopy: the new Leginon system. J. Struct. Biol. 151, 41-60.
    • (2005) J. Struct. Biol , vol.151 , pp. 41-60
    • Suloway, C.1    Pulokas, J.2    Fellmann, D.3
  • 19
    • 0035783259 scopus 로고    scopus 로고
    • Automated data collection with a Tecnai 12 electron microscope: Applications for molecular imaging by cryomicroscopy
    • Zhang, P., Beatty, A., Milne, J. L., and Subramaniam, S. (2001) Automated data collection with a Tecnai 12 electron microscope: applications for molecular imaging by cryomicroscopy. J. Struct. Biol. 135, 251-261.
    • (2001) J. Struct. Biol , vol.135 , pp. 251-261
    • Zhang, P.1    Beatty, A.2    Milne, J.L.3    Subramaniam, S.4
  • 20
    • 15444370401 scopus 로고    scopus 로고
    • Automated acquisition of cryo-electron micrographs for single particle reconstruction on an FEI Tecnai electron microscope
    • Lei, J. and Frank, J. (2005) Automated acquisition of cryo-electron micrographs for single particle reconstruction on an FEI Tecnai electron microscope. J. Struct. Biol. 150, 69-80.
    • (2005) J. Struct. Biol , vol.150 , pp. 69-80
    • Lei, J.1    Frank, J.2
  • 21
    • 19444365975 scopus 로고    scopus 로고
    • CryoEM structure at 9 Åresolution of an adenovirus vector targeted to hematopoietic cells
    • Saban, S. D., Nepomuceno, R. R., Gritton, L. D., Nemerow, G. R., and Stewart, P. L. (2005) CryoEM structure at 9 Åresolution of an adenovirus vector targeted to hematopoietic cells. J. Mol. Biol. 349, 526-537.
    • (2005) J. Mol. Biol , vol.349 , pp. 526-537
    • Saban, S.D.1    Nepomuceno, R.R.2    Gritton, L.D.3    Nemerow, G.R.4    Stewart, P.L.5
  • 22
    • 3142538754 scopus 로고    scopus 로고
    • Seeing GroEL at 6 Åresolution by single particle electron cryomicroscopy
    • Ludtke, S. J., Chen, D. H., Song, J. L., Chuang, D. T., and Chiu, W. (2004) Seeing GroEL at 6 Åresolution by single particle electron cryomicroscopy. Structure 12, 1129-1136.
    • (2004) Structure , vol.12 , pp. 1129-1136
    • Ludtke, S.J.1    Chen, D.H.2    Song, J.L.3    Chuang, D.T.4    Chiu, W.5
  • 23
    • 0344983355 scopus 로고    scopus 로고
    • Applications of a bilateral denoising filter in biological electron microscopy
    • Jiang, W., Baker, M. L., Wu, Q., Bajaj, C., and Chiu, W. (2003) Applications of a bilateral denoising filter in biological electron microscopy. J. Struct. Biol. 144, 114-122.
    • (2003) J. Struct. Biol , vol.144 , pp. 114-122
    • Jiang, W.1    Baker, M.L.2    Wu, Q.3    Bajaj, C.4    Chiu, W.5
  • 24
    • 0348077422 scopus 로고    scopus 로고
    • Automatic particle selection: Results of a comparative study
    • Zhu, Y., Carragher, B., Glaeser, R. M., et al. (2004) Automatic particle selection: results of a comparative study. J. Struct. Biol. 145, 3-14.
    • (2004) J. Struct. Biol , vol.145 , pp. 3-14
    • Zhu, Y.1    Carragher, B.2    Glaeser, R.M.3
  • 25
    • 0033787642 scopus 로고    scopus 로고
    • Local average intensity-based method for identifying spherical particles in electron micrographs
    • Kivioja, T., Ravantti, J., Verkhovsky, A., Ukkonen, E., and Bamford, D. (2000) Local average intensity-based method for identifying spherical particles in electron micrographs. J. Struct. Biol. 131, 126-134.
    • (2000) J. Struct. Biol , vol.131 , pp. 126-134
    • Kivioja, T.1    Ravantti, J.2    Verkhovsky, A.3    Ukkonen, E.4    Bamford, D.5
  • 26
    • 0002228874 scopus 로고
    • Phase contrast electron microscopy
    • Valdré, U, ed, Academic Press, New York, pp
    • Thon, F. (1971) Phase contrast electron microscopy, in Electron Microscopy in Material Sciences (Valdré, U., ed.), Academic Press, New York, pp. 571-625.
    • (1971) Electron Microscopy in Material Sciences , pp. 571-625
    • Thon, F.1
  • 27
    • 0000186608 scopus 로고
    • Measurement and compensation of de-focusing and aberrations by Fourier processing of electron micrographs
    • Erickson, H. P. and Klug, A. (1971) Measurement and compensation of de-focusing and aberrations by Fourier processing of electron micrographs. Phil. Trans. Roy. Soc. Loud. B. 261, 105-118.
    • (1971) Phil. Trans. Roy. Soc. Loud. B , vol.261 , pp. 105-118
    • Erickson, H.P.1    Klug, A.2
  • 28
    • 0014070124 scopus 로고
    • New knowledge on resolution and contrast in the electron microscope image
    • Hanszen, K. J. (1967) New knowledge on resolution and contrast in the electron microscope image. Naturwissenschaften 54, 125-133.
    • (1967) Naturwissenschaften , vol.54 , pp. 125-133
    • Hanszen, K.J.1
  • 29
    • 0035782663 scopus 로고    scopus 로고
    • Fourier amplitude decay of electron cryomicroscopic images of single particles and effects on structure determination
    • Saad, A., Ludtke, S. J., Jakana, J., Rixon, F. J., Tsuruta, H., and Chiu, W. (2001) Fourier amplitude decay of electron cryomicroscopic images of single particles and effects on structure determination. J. Struct. Biol. 133, 32-42.
    • (2001) J. Struct. Biol , vol.133 , pp. 32-42
    • Saad, A.1    Ludtke, S.J.2    Jakana, J.3    Rixon, F.J.4    Tsuruta, H.5    Chiu, W.6
  • 30
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., et al. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199.
    • (1996) J. Struct. Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3
  • 32
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Åin ice
    • Grigorieff, N. (1998) Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Åin ice. J. Mol. Biol. 277, 1033-1046.
    • (1998) J. Mol. Biol , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 33
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker, T. S. and Cheng, R. H. (1996) A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116, 120-130.
    • (1996) J. Struct. Biol , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 34
    • 5144235316 scopus 로고    scopus 로고
    • XMIPP: A new generation of an open-source image processing package for electron microscopy
    • Sorzano, C. O., Marabini, R., Velazquez-Muriel, J., et al. (2004) XMIPP: a new generation of an open-source image processing package for electron microscopy. J. Struct. Biol. 148, 194-204.
    • (2004) J. Struct. Biol , vol.148 , pp. 194-204
    • Sorzano, C.O.1    Marabini, R.2    Velazquez-Muriel, J.3
  • 35
    • 0036420061 scopus 로고    scopus 로고
    • IMIRS: A high-resolution 3D reconstruction package integrated with a relational image database
    • Liang, Y., Ke, E. Y., and Zhou, Z. H. (2002) IMIRS: a high-resolution 3D reconstruction package integrated with a relational image database. J. Struct. Biol. 137, 292-304.
    • (2002) J. Struct. Biol , vol.137 , pp. 292-304
    • Liang, Y.1    Ke, E.Y.2    Zhou, Z.H.3
  • 36
    • 31844435708 scopus 로고    scopus 로고
    • Structure of Epsilon 15 phage reveals organization of genome and DNA packaging/injection apparatus
    • Jiang, W., Chang, J., Jakana, J., Weigele, P., King, J., and Chiu, W. (2006) Structure of Epsilon 15 phage reveals organization of genome and DNA packaging/injection apparatus. Nature 439, 612-616.
    • (2006) Nature , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 37
    • 0000313739 scopus 로고
    • Exact filters for general geometry three dimensional reconstruction
    • Harauz, G. and van Heel, M. (1986) Exact filters for general geometry three dimensional reconstruction. Optik 73, 146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    van Heel, M.2
  • 38
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • van Heel, M. and Schatz, M. (2005) Fourier shell correlation threshold criteria. J. Struct. Biol. 151, 250-262.
    • (2005) J. Struct. Biol , vol.151 , pp. 250-262
    • van Heel, M.1    Schatz, M.2
  • 39
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. and Henderson, R. (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745.
    • (2003) J. Mol. Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 40
    • 0041347832 scopus 로고    scopus 로고
    • Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics
    • Baker, M. L., Jiang, W., Bowman, B. R., et al. (2003) Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics. J. Mol. Biol. 331, 447-456.
    • (2003) J. Mol. Biol , vol.331 , pp. 447-456
    • Baker, M.L.1    Jiang, W.2    Bowman, B.R.3
  • 41
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • Jiang, W., Li, Z., Zhang, Z., Baker, M. L., Prevelige, P. E., Jr., and Chiu, W. (2003) Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat. Struct. Biol. 10, 131-135.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige Jr., P.E.5    Chiu, W.6
  • 42
    • 36549009403 scopus 로고    scopus 로고
    • 365-385 1. Frank, J, ed, 1992 Electron Tomography: Three-Dimensional Imaging With the Transmission Electron Microscopy. Plenum Press, New York
    • 365-385 1. Frank, J. (ed.) (1992) Electron Tomography: Three-Dimensional Imaging With the Transmission Electron Microscopy. Plenum Press, New York.
  • 43
    • 2942608087 scopus 로고    scopus 로고
    • An improved strategy for automated electron microscopic tomography
    • Zheng, S. Q., Braunfeld, B. M., Sedat, W. J., and Agard, A. D. (2004) An improved strategy for automated electron microscopic tomography. J. Struct, Biol. 147, 10-22.
    • (2004) J. Struct, Biol , vol.147 , pp. 10-22
    • Zheng, S.Q.1    Braunfeld, B.M.2    Sedat, W.J.3    Agard, A.D.4
  • 44
    • 0000322501 scopus 로고    scopus 로고
    • Electron tomography of chromosome structure
    • Meyers, R. A, ed, John Wiley & Sons Ltd, Chichester, pp, Available at:, Accessed May 29, 2006
    • Engelhardt, P. (2000) Electron tomography of chromosome structure, in Encyclopedia of Analytical Chemistry vol. 6 (Meyers, R. A., ed.), John Wiley & Sons Ltd, Chichester, pp. 4948-4984. Available at: http://www.lce.hut.fi/∼engelhar/. Accessed May 29, 2006.
    • (2000) Encyclopedia of Analytical Chemistry , vol.6 , pp. 4948-4984
    • Engelhardt, P.1
  • 45
    • 36549013014 scopus 로고    scopus 로고
    • IMOD , Available at: URL:, Accessed May 29, 2006
    • IMOD (2005). Available at: URL: http://bio3d.colorado.edu/imod/. Accessed May 29, 2006.
    • (2005)
  • 47
    • 0035782662 scopus 로고    scopus 로고
    • Multiphase method for automatic alignment of transmission electron microscope images using markers
    • Brandt, S., Heikkonen, J., and Engelhardt, P. (2001) Multiphase method for automatic alignment of transmission electron microscope images using markers. J. Struct. Biol. 133, 10-22.
    • (2001) J. Struct. Biol , vol.133 , pp. 10-22
    • Brandt, S.1    Heikkonen, J.2    Engelhardt, P.3
  • 48
    • 0035783045 scopus 로고    scopus 로고
    • Automatic alignment of transmission electron microscope tilt-series without fiducial markers
    • Brandt, S., Heikkonen, J., and Engelhardt, P. (2001) Automatic alignment of transmission electron microscope tilt-series without fiducial markers. J. Struct. Biol. 136, 201-213.
    • (2001) J. Struct. Biol , vol.136 , pp. 201-213
    • Brandt, S.1    Heikkonen, J.2    Engelhardt, P.3
  • 49
    • 33744799156 scopus 로고    scopus 로고
    • Automatic TEM image alignment by trifocal geometry
    • Brandt, S.S. and Ziese, U. (2006) Automatic TEM image alignment by trifocal geometry. J. Microsc. (Oxford) 222, 1-4.
    • (2006) J. Microsc. (Oxford) , vol.222 , pp. 1-4
    • Brandt, S.S.1    Ziese, U.2
  • 52
    • 36549058558 scopus 로고    scopus 로고
    • BOB () Available at:, Accessed May 30, 2006
    • BOB (2005) Available at: http://www.ahpcrc.org/software/bob/. Accessed May 30, 2006.
    • (2005)
  • 53
    • 36549012093 scopus 로고    scopus 로고
    • Available at:, Accessed May 30, 2006
    • AnimaBob (2005) Available at: http://www.borg.umn.edu/~grant/AnimaBob/. Accessed May 30, 2006.
    • (2005)
    • AnimaBob1
  • 54
    • 36549011125 scopus 로고    scopus 로고
    • Available at:, Accessed May 30, 2006
    • Chimera (2005) Available at: http://www.cgl.ucsf.edu/chimera/. Accessed May 30, 2006.
    • (2005)
    • Chimera1
  • 55
    • 36549088910 scopus 로고    scopus 로고
    • VMD () Available at:, Accessed May 30, 2006
    • VMD (2005) Available at: http://www.ks.uiuc.edu/Research/vmd/. Accessed May 30, 2006.
    • (2005)
  • 56
    • 36549010333 scopus 로고    scopus 로고
    • SITUS () Available at:, Accessed May 30, 2006
    • SITUS (2005) Available at: http://situs.biomachina.org/. Accessed May 30, 2006.
    • (2005)
  • 57
    • 36549050193 scopus 로고    scopus 로고
    • Available at:, Accessed May 30, 2006
    • Vis5D (2005) Available at: http://www.ssec.wisc.edu/∼billh/vis5d. html. Accessed May 30, 2006.
    • Vis5D
  • 58
    • 36549084437 scopus 로고    scopus 로고
    • 3-Deep. IEEE Spectrum
    • April 22-27
    • Sullivan, A. (2005) 3-Deep. IEEE Spectrum, INT. April 22-27.
    • (2005) INT
    • Sullivan, A.1


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