메뉴 건너뛰기




Volumn 249, Issue 3, 1997, Pages 895-904

Structural properties of chimeric peptides containing a T-cell epitope linked to a fusion peptide and their importance for in vivo induction of cytotoxic T-cell responses

Author keywords

Conformation; Fusion peptide; Immunogenicity; Microspectrofluorometry; T cell epitope

Indexed keywords

CHIMERIC PROTEIN; EPITOPE; HYBRID PROTEIN; SYNTHETIC PEPTIDE;

EID: 0030682479     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00895.x     Document Type: Article
Times cited : (11)

References (56)
  • 1
    • 0026492542 scopus 로고
    • Membrane fusion
    • While, J. M. (1992) Membrane fusion, Science 258, 917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • While, J.M.1
  • 3
    • 0023652302 scopus 로고
    • Ability of the Hydrophobic fusion related domain of a paramyxovirus F protein to act as a membrane anchor
    • Paterson, R. G. & Lamb, R. A. (1987) Ability of the Hydrophobic fusion related domain of a paramyxovirus F protein to act as a membrane anchor, Cell 48, 441-452.
    • (1987) Cell , vol.48 , pp. 441-452
    • Paterson, R.G.1    Lamb, R.A.2
  • 4
    • 0029159058 scopus 로고
    • Preparation and characterization of antisense oligonucleotide-peptide hybrids containing viral fusion peptides
    • Soukchareun, S., Tregear, G. W. & Haralambidis, J. (1995) Preparation and characterization of antisense oligonucleotide-peptide hybrids containing viral fusion peptides, Bioconjugate Chem. 6, 43-53.
    • (1995) Bioconjugate Chem. , vol.6 , pp. 43-53
    • Soukchareun, S.1    Tregear, G.W.2    Haralambidis, J.3
  • 5
    • 0029155732 scopus 로고
    • The induction of respiratory syncytial virus-specific cytotoxic T-cell responses following immunization with a synthetic peptide containing a fusion peptide linked to a cytotoxic T lymphocyte epitope
    • Hsu, S. C., Shaw, D. M. & Steward, M. W. (1995) The induction of respiratory syncytial virus-specific cytotoxic T-cell responses following immunization with a synthetic peptide containing a fusion peptide linked to a cytotoxic T lymphocyte epitope, Immunology 85, 347-350.
    • (1995) Immunology , vol.85 , pp. 347-350
    • Hsu, S.C.1    Shaw, D.M.2    Steward, M.W.3
  • 7
    • 0029310528 scopus 로고
    • T-cell immunotherapy of tumors by adoptive transfer of cytotoxic T lymphocytes and by vaccination with minimal essentiel epitopes
    • Melief, C. J. M. & Kast, W. M. (1995) T-cell immunotherapy of tumors by adoptive transfer of cytotoxic T lymphocytes and by vaccination with minimal essentiel epitopes, Immunol. Rev. 146, 167-177.
    • (1995) Immunol. Rev. , vol.146 , pp. 167-177
    • Melief, C.J.M.1    Kast, W.M.2
  • 8
    • 0027468145 scopus 로고
    • The biochemistry and cell biology of antigen processing and presentation
    • Germain, R. M. & Margolies, D. H. (1993) The biochemistry and cell biology of antigen processing and presentation, Annu. Rev. Immunol. 11, 403-450.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 403-450
    • Germain, R.M.1    Margolies, D.H.2
  • 9
    • 43949164161 scopus 로고
    • Can soluble antigens induce CD8+ cytotoxic T-cell responses? a paradox revisited
    • Raychaudhuri, S. & Morrow, W. J. W. (1993) Can soluble antigens induce CD8+ cytotoxic T-cell responses? A paradox revisited, Immunol. Today 914, 344-348.
    • (1993) Immunol. Today , vol.914 , pp. 344-348
    • Raychaudhuri, S.1    Morrow, W.J.W.2
  • 10
    • 0029012652 scopus 로고
    • Delivery of protein antigen to the major histocompatibility complex class I-restricted antigen presentation pathway
    • Zhou, F. & Huang, L. (1995) Delivery of protein antigen to the major histocompatibility complex class I-restricted antigen presentation pathway, J. Drug Targ. 3, 91-109.
    • (1995) J. Drug Targ. , vol.3 , pp. 91-109
    • Zhou, F.1    Huang, L.2
  • 11
    • 0026603218 scopus 로고
    • Processing of exogenous liposome-encapsulated antigens in vivo generated class I MHC-restricted T cell responses
    • Collins, D. S., Findlay, K. & Harding, C. V. (1992) Processing of exogenous liposome-encapsulated antigens in vivo generated class I MHC-restricted T cell responses, J. Immunol. 148, 3336-3341.
    • (1992) J. Immunol. , vol.148 , pp. 3336-3341
    • Collins, D.S.1    Findlay, K.2    Harding, C.V.3
  • 12
    • 0030581353 scopus 로고    scopus 로고
    • Linkage of a fusion peptide to a CTL epitope from the nucleocapsid of measles virus enables incorporation into IS-COMs and induction of CTL responses following intranasal immunisation
    • Hsu, S. C., Schadeck, E. B., Delmas, A., Shaw, D. M. & Steward, M. W. (1996) Linkage of a fusion peptide to a CTL epitope from the nucleocapsid of measles virus enables incorporation into IS-COMs and induction of CTL responses following intranasal immunisation, Vaccine 14, 1159-1166.
    • (1996) Vaccine , vol.14 , pp. 1159-1166
    • Hsu, S.C.1    Schadeck, E.B.2    Delmas, A.3    Shaw, D.M.4    Steward, M.W.5
  • 13
    • 0026091287 scopus 로고
    • Efficiency of peptides and lipopeptides for in vivo priming of virus-specific cytotoxic T cells
    • Schild, H., Deres, K., Wiesmuller, K. H., Jung, G. & Rammensee, H. G. (1991) Efficiency of peptides and lipopeptides for in vivo priming of virus-specific cytotoxic T cells, Eur. J. Immunol. 21, 2649-2654.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 2649-2654
    • Schild, H.1    Deres, K.2    Wiesmuller, K.H.3    Jung, G.4    Rammensee, H.G.5
  • 19
    • 0015931593 scopus 로고
    • P-Alkoxybenzyl alcohol resin and p-alkoxybenzyloxycarbonylhydrazide resin for solid phase synthesis of protected fragments
    • Wang, S. S. (1973) p-Alkoxybenzyl alcohol resin and p-alkoxybenzyloxycarbonylhydrazide resin for solid phase synthesis of protected fragments, J. Am. Chem. Soc. 95, 1328-1333.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 1328-1333
    • Wang, S.S.1
  • 20
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • King, D. S., Fields, C. G. & Fields, G. B. (1990) A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis, Int. J. Pept. Protein Res. 36, 255-266.
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 21
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides
    • Kaiser, E., Coleseott, R. L., Bossinger, C. D. & Cook, P. I. (1970) Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides, Anal. Biochem. 34, 595-598.
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Coleseott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 22
    • 0030835498 scopus 로고    scopus 로고
    • Incorporation of ethidium bromide in the Drosophila salivary gland approached by microspectrofluorometry: Evidence for the presence of both free and bound dye in the nuclei of cells in viable conditions
    • Favard, C. Pager, J., Locker, D. & Vigny, P. (1997) Incorporation of ethidium bromide in the Drosophila salivary gland approached by microspectrofluorometry: evidence for the presence of both free and bound dye in the nuclei of cells in viable conditions, Eur: Biophys. J. 25, 225-237.
    • (1997) Eur: Biophys. J. , vol.25 , pp. 225-237
    • Favard, C.1    Pager, J.2    Locker, D.3    Vigny, P.4
  • 23
    • 0027256817 scopus 로고
    • Immunization of mice with vaccinia virus-M2 recombinant induces epitope-specific and cross-reactive Kd-restricted CD8+ cytotoxic T cells
    • Kulkarni, A. B., Morse, H. C. III, Bennick, J. R., Yewdell, J. W. & Murphy, B. R. (1993) Immunization of mice with vaccinia virus-M2 recombinant induces epitope-specific and cross-reactive Kd-restricted CD8+ cytotoxic T cells, J. Virol. 67, 4086-4092.
    • (1993) J. Virol. , vol.67 , pp. 4086-4092
    • Kulkarni, A.B.1    Morse III, H.C.2    Bennick, J.R.3    Yewdell, J.W.4    Murphy, B.R.5
  • 24
    • 0026739624 scopus 로고
    • T-helper epitopes enhance the cytotoxic response of mice immunized with MHC class I-restricted malaria peptides
    • Widmann, C., Romero, P., Maryanski, J. L., Corradin, G. & Valmori, D. (1992) T-helper epitopes enhance the cytotoxic response of mice immunized with MHC class I-restricted malaria peptides. J. Immunol. Methods 155, 95-99.
    • (1992) J. Immunol. Methods , vol.155 , pp. 95-99
    • Widmann, C.1    Romero, P.2    Maryanski, J.L.3    Corradin, G.4    Valmori, D.5
  • 25
    • 0346766751 scopus 로고
    • Fluorescence of dansyl amino acids in organicsolvents and protein solution
    • Chen, R. F. (1967) Fluorescence of dansyl amino acids in organicsolvents and protein solution, Arch. Biochem. Biophys. 120, 609-620.
    • (1967) Arch. Biochem. Biophys. , vol.120 , pp. 609-620
    • Chen, R.F.1
  • 26
    • 0016846155 scopus 로고
    • Multichannel microspectrofluorometry for topographic and spectral analysis of NAD(P)H fluorescence in single living cells
    • Kohen, E., Hirschberg, J. G., Kohen, C., Wouters, A., Pearson, A., Salmon, J. M. & Thorell, B. (1975) Multichannel microspectrofluorometry for topographic and spectral analysis of NAD(P)H fluorescence in single living cells, Biochim. Biochim. Biophys. Acta 396, 149-154.
    • (1975) Biochim. Biochim. Biophys. Acta , vol.396 , pp. 149-154
    • Kohen, E.1    Hirschberg, J.G.2    Kohen, C.3    Wouters, A.4    Pearson, A.5    Salmon, J.M.6    Thorell, B.7
  • 27
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C. (1990) Protein secondary structure and circular dichroism: a practical guide, Proteins 7, 205-214.
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson, W.C.1
  • 28
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. & Fasman, D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, D.2
  • 29
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sönnichsen, F. D., Van Eyk, J. E., Hodges, R. H. & Sykes, B. D. (1992) Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide, Biochemistry 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.H.3    Sykes, B.D.4
  • 32
    • 0030068733 scopus 로고    scopus 로고
    • Use of intrinsic and extrinsic helper epitopes for in vivo induction of anti-hepatitis C virus cytotoxic T lymphocytes (CTL) with CTL epitope peptide vaccines
    • Shirai, M., Chen, M., Arichi, T., Masaki, T., Nishioka, M., Newman, M., Nakazawa, T., Feinstone, S. M. & Berzofsky, J. A. (1996) Use of intrinsic and extrinsic helper epitopes for in vivo induction of anti-hepatitis C virus cytotoxic T lymphocytes (CTL) with CTL epitope peptide vaccines, J. Infect. Dis. 173, 24-31.
    • (1996) J. Infect. Dis. , vol.173 , pp. 24-31
    • Shirai, M.1    Chen, M.2    Arichi, T.3    Masaki, T.4    Nishioka, M.5    Newman, M.6    Nakazawa, T.7    Feinstone, S.M.8    Berzofsky, J.A.9
  • 33
    • 0028972123 scopus 로고
    • Long-lasting anti-viral cytotoxic T lymphocytes induced in vivo with chimeric-multirestricted lipopeptides
    • Sauzet, J. P., Déprez, B., Martinon, F., Guillet, J. F., Gras-Masse, H. & Gomard, E. (1995) Long-lasting anti-viral cytotoxic T lymphocytes induced in vivo with chimeric-multirestricted lipopeptides, Vaccine 13, 1339-1345.
    • (1995) Vaccine , vol.13 , pp. 1339-1345
    • Sauzet, J.P.1    Déprez, B.2    Martinon, F.3    Guillet, J.F.4    Gras-Masse, H.5    Gomard, E.6
  • 34
    • 0026645243 scopus 로고
    • Membrane destabilization by N-terminal peptides of viral envelope proteins
    • Düzgünes, N. & Shavnin, S. A. (1992) Membrane destabilization by N-terminal peptides of viral envelope proteins, J. Memhr. Biol. 128, 71-80.
    • (1992) J. Memhr. Biol. , vol.128 , pp. 71-80
    • Düzgünes, N.1    Shavnin, S.A.2
  • 35
    • 0029915994 scopus 로고    scopus 로고
    • Interaction of fusiogenic synthetic peptide with phospholipid bilayers: Orientation of the peptide α-helix and binding isotherm
    • Ishiguro, R., Matsumoto, M. & Takahashi, S. (1996) Interaction of fusiogenic synthetic peptide with phospholipid bilayers: orientation of the peptide α-helix and binding isotherm, Biochemistry 35, 4976-4983.
    • (1996) Biochemistry , vol.35 , pp. 4976-4983
    • Ishiguro, R.1    Matsumoto, M.2    Takahashi, S.3
  • 37
    • 0025735564 scopus 로고
    • Effects of the 'fusion peptide' from measles virus on the structure of N-methyl dioleoylphosphatidylethanolamine membranes and their fusion with Sendai virus
    • Yeagle, P. L., Epand, R. M., Richardson, C. D. & Flanagan, T. D. (1991) Effects of the 'fusion peptide' from measles virus on the structure of N-methyl dioleoylphosphatidylethanolamine membranes and their fusion with Sendai virus, Biochim. Biophys. Acta 1065, 49-53.
    • (1991) Biochim. Biophys. Acta , vol.1065 , pp. 49-53
    • Yeagle, P.L.1    Epand, R.M.2    Richardson, C.D.3    Flanagan, T.D.4
  • 38
    • 0017112098 scopus 로고
    • Conformation of immunoglobulin M: Characterization of anti-ε-1-dimethylamino-5-naphthalenesulfonyl-L-lysine immunoglobulin M antibodies from horse, pig and shark
    • Holowka, D. A. & Cathou, R. E. (1976) Conformation of immunoglobulin M: Characterization of anti-ε-1-dimethylamino-5-naphthalenesulfonyl-L-lysine immunoglobulin M antibodies from horse, pig and shark, Biochemistry 15, 3373-3379.
    • (1976) Biochemistry , vol.15 , pp. 3373-3379
    • Holowka, D.A.1    Cathou, R.E.2
  • 39
    • 0028133498 scopus 로고
    • Influence of the conformation of a macromolecule on the generation of T-epitope: A study with model polypeptides
    • Lacassie, E., Delmas, A. & Trudelle, Y. (1994) Influence of the conformation of a macromolecule on the generation of T-epitope: a study with model polypeptides, FEBS Lett. 349, 380-384.
    • (1994) FEBS Lett. , vol.349 , pp. 380-384
    • Lacassie, E.1    Delmas, A.2    Trudelle, Y.3
  • 41
    • 0029973314 scopus 로고    scopus 로고
    • Quaternary structure of a carrier protein influences antigenicity and immunogenicity of an inserted T cell determinant
    • Janssen, R., Wauben, M. H. M. & Tommassen, J. (1996) Quaternary structure of a carrier protein influences antigenicity and immunogenicity of an inserted T cell determinant, Int. J. Immunol. 8, 829-836.
    • (1996) Int. J. Immunol. , vol.8 , pp. 829-836
    • Janssen, R.1    Wauben, M.H.M.2    Tommassen, J.3
  • 42
    • 0022322597 scopus 로고
    • Design and characterization of peptides with amphihilic β-strand structures
    • Ostermann, D. G. & Kaiser, E. T. (1985) Design and characterization of peptides with amphihilic β-strand structures, J. Cell. Biochem. 29, 57-72.
    • (1985) J. Cell. Biochem. , vol.29 , pp. 57-72
    • Ostermann, D.G.1    Kaiser, E.T.2
  • 43
    • 0030937833 scopus 로고    scopus 로고
    • Capture and processing of exogenous antigens for presentation on MHC molecules
    • Walts, C. (1997) Capture and processing of exogenous antigens for presentation on MHC molecules, Annu. Rev. Immunol. 15, 821-850.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 821-850
    • Walts, C.1
  • 44
    • 0029917002 scopus 로고    scopus 로고
    • Processing and delivery of peptides presented by MHC class I molecules
    • Lehner, P. J. & Cresswell, P. (1996) Processing and delivery of peptides presented by MHC class I molecules, Curr. Opin. Immunol. 8, 59-67.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 59-67
    • Lehner, P.J.1    Cresswell, P.2
  • 45
    • 0031042309 scopus 로고    scopus 로고
    • Cooperative alpha-helix formation of beta-lactoglobulin and melittin induced by hexafluoroisopropanol
    • Hirota, N., Mizuno, K. & Goto, Y. (1996) Cooperative alpha-helix formation of beta-lactoglobulin and melittin induced by hexafluoroisopropanol, Protein Sci. 6, 416-421.
    • (1996) Protein Sci. , vol.6 , pp. 416-421
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 46
    • 0030593499 scopus 로고    scopus 로고
    • Native β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat
    • Schönbrunner, N., Wey, J., Engels, J., Georg, H. & Kiefhaber, T. (1996) Native β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat, J. Mol. Biol. 260, 432-445.
    • (1996) J. Mol. Biol. , vol.260 , pp. 432-445
    • Schönbrunner, N.1    Wey, J.2    Engels, J.3    Georg, H.4    Kiefhaber, T.5
  • 47
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation
    • Rabenstein, M. & Shin, Y. K. (1995) A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation, Biochemistry 34, 13 390-13 397.
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.K.2
  • 48
    • 0028840940 scopus 로고
    • Structure and topology of the influenza virus fusion peptide in lipid bilayers
    • Lüneberg, J., Martin, I., Nüßler, F., Ruysschaert, J. M. & Herrmann, A. (1995) Structure and topology of the influenza virus fusion peptide in lipid bilayers, Biochemistry 270, 27 606-27 617.
    • (1995) Biochemistry , vol.270 , pp. 27606-27617
    • Lüneberg, J.1    Martin, I.2    Nüßler, F.3    Ruysschaert, J.M.4    Herrmann, A.5
  • 50
    • 0029153215 scopus 로고
    • Peptides in membranes: Helicity and hydrophobicity
    • Deber, C. M. & Li, S. C. (1995) Peptides in membranes: helicity and hydrophobicity, Biopolymers 37, 295-318.
    • (1995) Biopolymers , vol.37 , pp. 295-318
    • Deber, C.M.1    Li, S.C.2
  • 51
    • 0024095276 scopus 로고
    • Detective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen
    • Townsend, A., Bastin, J., Gould, K., Brownlee, G., Andrew, M., Coupar, B., Boyle, D., Chan, S. & Smith, G. (1988) Detective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen, J. Exp. Med. 168, 1211-1224.
    • (1988) J. Exp. Med. , vol.168 , pp. 1211-1224
    • Townsend, A.1    Bastin, J.2    Gould, K.3    Brownlee, G.4    Andrew, M.5    Coupar, B.6    Boyle, D.7    Chan, S.8    Smith, G.9
  • 52
    • 0030977234 scopus 로고    scopus 로고
    • Targeting of HIV-1 antigens for rapid intracellular degradation enhances cytotoxic T lymphocytes (CTL) recognition and the induction of de novo CTL responses in vivo after immunization
    • Tobery, T. W. & Siliciano, R. F. (1997) Targeting of HIV-1 antigens for rapid intracellular degradation enhances cytotoxic T lymphocytes (CTL) recognition and the induction of de novo CTL responses in vivo after immunization, J. Exp. Med. 185, 909-920.
    • (1997) J. Exp. Med. , vol.185 , pp. 909-920
    • Tobery, T.W.1    Siliciano, R.F.2
  • 53
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • Rafalski, M., Lear, J. D. & Degrade, W. F. (1990) Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41, Biochemistry 29, 7917-7922.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    Degrade, W.F.3
  • 54
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicules: Different structural requirements for fusion and leakage
    • Nieva, J. L., Nir, S., Muga, A., Goni, F. M. & Wilschut, J. (1994) Interaction of the HIV-1 fusion peptide with phospholipid vesicules: different structural requirements for fusion and leakage, Biochemistry 33, 3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 55
    • 0028850506 scopus 로고
    • Processing of exogenous heat-aggregated (denatured) and particulate (native) hepatitis B surface antigen for class-I restricted epitope presentation
    • Schirmbeck, R., Böhm, W., Melber, K. & Reimann, J. (1995) Processing of exogenous heat-aggregated (denatured) and particulate (native) hepatitis B surface antigen for class-I restricted epitope presentation, J. Immunol. 155, 4676-4684.
    • (1995) J. Immunol. , vol.155 , pp. 4676-4684
    • Schirmbeck, R.1    Böhm, W.2    Melber, K.3    Reimann, J.4
  • 56
    • 0029032060 scopus 로고
    • MHC class-I restricted processing of transmembrane proteins: Mechanism and biological significance
    • Siliciano, R. F. & Soloski, M. J. (1995) MHC class-I restricted processing of transmembrane proteins: mechanism and biological significance, J. Immunol. 155, 2-5.
    • (1995) J. Immunol. , vol.155 , pp. 2-5
    • Siliciano, R.F.1    Soloski, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.