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Volumn 141, Issue 6, 1998, Pages 1335-1347

Specific single or double proline substitutions in the 'spring-loaded' coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity

Author keywords

[No Author keywords available]

Indexed keywords

PROLINE; VIRUS HEMAGGLUTININ;

EID: 0032526413     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.6.1335     Document Type: Article
Times cited : (78)

References (57)
  • 1
    • 0028774339 scopus 로고
    • Influenza hemagglutinin: Kinetic control of protein function
    • Baker, D., and D. Agard. 1994. Influenza hemagglutinin: kinetic control of protein function. Structure. 2:907-910.
    • (1994) Structure , vol.2 , pp. 907-910
    • Baker, D.1    Agard, D.2
  • 2
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow, S.C., M. Lu, and P.S. Kim. 1995. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry. 34:14955-14962.
    • (1995) Biochemistry , vol.34 , pp. 14955-14962
    • Blacklow, S.C.1    Lu, M.2    Kim, P.S.3
  • 4
    • 0026744238 scopus 로고
    • A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization hut is essential for fusion
    • Bucklund, R., E. Malvoisin, P. Beauverger, and F. Wild. 1992. A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization hut is essential for fusion. J. Gen. Virol. 73:1703-1707.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1703-1707
    • Bucklund, R.1    Malvoisin, E.2    Beauverger, P.3    Wild, F.4
  • 5
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P.A., F.M. Hughson, J.J. Skehel, and D.C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature. 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 6
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C.M., and P.S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:823-832.
    • (1993) Cell. , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 7
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproleins
    • Chambers, P., C.R. Pringle, and AJ. Easton. 1990. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproleins. J. Gen. Virol. 71:3075-3080.
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 9
    • 0027266886 scopus 로고
    • Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprolein
    • Chen, S.S., C.N. Lee, W.R. Lee, K. McIntosh, and T.H. Lee. 1993. Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprolein. J. Virol. 67:3615-3619.
    • (1993) J. Virol. , vol.67 , pp. 3615-3619
    • Chen, S.S.1    Lee, C.N.2    Lee, W.R.3    McIntosh, K.4    Lee, T.H.5
  • 10
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli, T., S.L. Pelletier, Y.I. Henis, and J.M. White. 1996. Membrane fusion mediated by the influenza hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133:559-569.
    • (1996) J. Cell Biol. , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 11
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 A resolution
    • Fass, D., S.C. Harrison, and P.S. Kim. 1996. Retrovirus envelope domain at 1.7 A resolution. Nat. Struct. Biol. 3:465-469.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 12
    • 0029556891 scopus 로고
    • Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin
    • Fass, D., and P.S. Kim. 1995. Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin. Curr. Biol. 5:1377-1383.
    • (1995) Curr. Biol. , vol.5 , pp. 1377-1383
    • Fass, D.1    Kim, P.S.2
  • 13
    • 0030591276 scopus 로고    scopus 로고
    • Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses
    • Gallaher, W. R. 1996. Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses. Cell. 85:477-478.
    • (1996) Cell. , vol.85 , pp. 477-478
    • Gallaher, W.R.1
  • 14
    • 0026560161 scopus 로고
    • Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity
    • Godley, L., J. Peifer, D. Steinhauer, B. Ely, G. Shaw, R. Kaufmann, E. Suchanek, C. Pabo, J.J. Skehel, D.C. Wiley, and S. Wharton. 1992. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity. Cell. 68:635-645.
    • (1992) Cell. , vol.68 , pp. 635-645
    • Godley, L.1    Peifer, J.2    Steinhauer, D.3    Ely, B.4    Shaw, G.5    Kaufmann, R.6    Suchanek, E.7    Pabo, C.8    Skehel, J.J.9    Wiley, D.C.10    Wharton, S.11
  • 15
    • 0030768271 scopus 로고    scopus 로고
    • Structural studies on membrane-embedded influenza hemagglutinin and its fragments
    • Gray, C., and L.K. Tamm. 1997. Structural studies on membrane-embedded influenza hemagglutinin and its fragments. Prot. Sci. 6:1993-2006.
    • (1997) Prot. Sci. , vol.6 , pp. 1993-2006
    • Gray, C.1    Tamm, L.K.2
  • 16
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., R. Roth, H. Morisaki, R. Jahn, and J.E. Heuser. 1997. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell. 90:523-535.
    • (1997) Cell. , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 18
    • 0031440116 scopus 로고    scopus 로고
    • Activation of a retroviral membrane fusion protein: Soluble receptor-induced liposome binding of the ALSV envelope glycoprotein
    • Hernandez, L.D., R.R. Peters, S.E. DeLos, J.A.T. Young, D.A. Agard, and J.M. White. 1997. Activation of a retroviral membrane fusion protein: soluble receptor-induced liposome binding of the ALSV envelope glycoprotein. J. Cell Biol. 139:1455-1464.
    • (1997) J. Cell Biol. , vol.139 , pp. 1455-1464
    • Hernandez, L.D.1    Peters, R.R.2    DeLos, S.E.3    Young, J.A.T.4    Agard, D.A.5    White, J.M.6
  • 19
    • 0030753409 scopus 로고    scopus 로고
    • Structure-based identification of an inducer of the low pH conformational change in the influenza virus hemagglutinin: Irreversible inhibition of infectivity
    • Hoffman, L.R., I.D. Kuntz, and J.M. White. 1997. Structure-based identification of an inducer of the low pH conformational change in the influenza virus hemagglutinin: irreversible inhibition of infectivity. J. Virol. 71:8808-8820.
    • (1997) J. Virol. , vol.71 , pp. 8808-8820
    • Hoffman, L.R.1    Kuntz, I.D.2    White, J.M.3
  • 20
    • 0029257245 scopus 로고
    • Structural characterization of viral fusion proteins
    • Hughson, F.M. 1995. Structural characterization of viral fusion proteins. Curr. Biol. 5:265-274.
    • (1995) Curr. Biol. , vol.5 , pp. 265-274
    • Hughson, F.M.1
  • 21
    • 0030965051 scopus 로고    scopus 로고
    • Structural features of membrane fusion between influenza virus and liposomes as revealed by quick-freezing electron microscopy
    • Kanaseki, T., K. Kawasaki, M. Murata, Y. Ikeuchi, and S.-i. Ohnishi. 1997. Structural features of membrane fusion between influenza virus and liposomes as revealed by quick-freezing electron microscopy. J. Cell Biol. 137: 1041-1056.
    • (1997) J. Cell Biol. , vol.137 , pp. 1041-1056
    • Kanaseki, T.1    Kawasaki, K.2    Murata, M.3    Ikeuchi, Y.4    Ohnishi, S.-I.5
  • 22
    • 0026772024 scopus 로고
    • Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin
    • Kemble, G.W., D.L. Bodian, J. Rose, I.A. Wilson, and J.M. White. 1992. Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin. J. Virol. 66:4940-4950.
    • (1992) J. Virol. , vol.66 , pp. 4940-4950
    • Kemble, G.W.1    Bodian, D.L.2    Rose, J.3    Wilson, I.A.4    White, J.M.5
  • 23
    • 0027199871 scopus 로고
    • GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity
    • Kemble, G.W., Y. Henis, and J.M. White. 1993. GPI-and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity. J. Cell Biol. 122:1253-1265.
    • (1993) J. Cell Biol. , vol.122 , pp. 1253-1265
    • Kemble, G.W.1    Henis, Y.2    White, J.M.3
  • 24
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifuston, not complete fusion
    • Kemble, G.W., T. Danieli, and J.M. White. 1994. Lipid-anchored influenza hemagglutinin promotes hemifuston, not complete fusion. Cell. 76:383-391.
    • (1994) Cell. , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 25
    • 0029108852 scopus 로고
    • Membrane fusion and the alphavirus life cycle
    • Kielian, M. 1995. Membrane fusion and the alphavirus life cycle. Adv. Vir. Res. 45:113-151.
    • (1995) Adv. Vir. Res. , vol.45 , pp. 113-151
    • Kielian, M.1
  • 26
    • 0029665093 scopus 로고    scopus 로고
    • On the dynamics and conformation of the HA2 domain of the influenza virus hemagglutinin
    • Kim, C.-H., J.C. Macosko, Y.G. Yu, and Y.-K. Shin. 1996. On the dynamics and conformation of the HA2 domain of the influenza virus hemagglutinin. Biochemistry. 35:5359-5365.
    • (1996) Biochemistry , vol.35 , pp. 5359-5365
    • Kim, C.-H.1    Macosko, J.C.2    Yu, Y.G.3    Shin, Y.-K.4
  • 27
    • 0030953859 scopus 로고    scopus 로고
    • Transient changes of the conformation of hemagglutinin of influenza virus at low pH detected by time-resolved circular dichroism spectroscopy
    • Korte, T., K. Ludwig, M. Krumbiegel. D. Zirwert, G. Damaschun, and A. Hermann. 1997. Transient changes of the conformation of hemagglutinin of influenza virus at low pH detected by time-resolved circular dichroism spectroscopy. J. Biol. Chem. 272:9764-9770.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9764-9770
    • Korte, T.1    Ludwig, K.2    Krumbiegel, M.3    Zirwert, D.4    Damaschun, G.5    Hermann, A.6
  • 28
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., J.D. Roberts, and R.A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154: 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 30
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., S. Blacklow, and P.S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.2    Kim, P.S.3
  • 31
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. 1996. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21:375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 32
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science. 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 33
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K.T., and W.F. Degrado. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science. 250: 646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    Degrado, W.F.2
  • 35
    • 0025279843 scopus 로고
    • Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: Effects of acid presentment
    • Puri, A., F.P. Booy, R.W. Doms, J.M. White, and R. Blumenthal. 1990. Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid presentment. J. Virol. 64:3824-3932.
    • (1990) J. Virol. , vol.64 , pp. 3824-3932
    • Puri, A.1    Booy, F.P.2    Doms, R.W.3    White, J.M.4    Blumenthal, R.5
  • 36
  • 37
    • 0029944985 scopus 로고    scopus 로고
    • The "putative" leucine zipper region of murine leukemia virus transmembrane protein (P15e) is essential for viral infectivity
    • Ramsdale, E.E., S.M. Kingsman, and A.J. Kingsman. 1996. The "putative" leucine zipper region of murine leukemia virus transmembrane protein (P15e) is essential for viral infectivity. Virology. 220:100-108.
    • (1996) Virology , vol.220 , pp. 100-108
    • Ramsdale, E.E.1    Kingsman, S.M.2    Kingsman, A.J.3
  • 38
    • 0029132009 scopus 로고
    • Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein
    • Reitter, J.N., T. Sergel, and T.G. Morrison. 1995. Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein. J. Virol. 69: 5995-6004.
    • (1995) J. Virol. , vol.69 , pp. 5995-6004
    • Reitter, J.N.1    Sergel, T.2    Morrison, T.G.3
  • 39
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalilis virus at 2Å resolution
    • Rey, F.A., F.X. Heinz, C. Mandl, C. Kunz, and S.C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalilis virus at 2Å resolution. Nature. 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 40
    • 0030020733 scopus 로고    scopus 로고
    • The protein machinery of vesicle budding and fusion
    • Rothman, J.E. 1996. The protein machinery of vesicle budding and fusion. Prot. Sci. 5:185-194.
    • (1996) Prot. Sci. , vol.5 , pp. 185-194
    • Rothman, J.E.1
  • 42
    • 0023609501 scopus 로고
    • Effects of low pH on influenza virus. Activation and inactivation of the membrane fusion capacity of the hemagglutinin
    • Stegmann, T., F.P. Booy, and J. Wilschut. 1987. Effects of low pH on influenza virus. Activation and inactivation of the membrane fusion capacity of the hemagglutinin. J. Biol. Chem. 262:17744-17749.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17744-17749
    • Stegmann, T.1    Booy, F.P.2    Wilschut, J.3
  • 44
    • 0029828938 scopus 로고    scopus 로고
    • Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity
    • Steinhauer, D. A., J. Martin, Y.P. Lin, S.A. Wharton, M.B.A. Oldstone, J.J. Skehel, and D.C. Wiley. 1996. Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity. Proc. Natl. Acad. Sci. USA. 93:12873-12878.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12873-12878
    • Steinhauer, D.A.1    Martin, J.2    Lin, Y.P.3    Wharton, S.A.4    Oldstone, M.B.A.5    Skehel, J.J.6    Wiley, D.C.7
  • 45
    • 0028820162 scopus 로고
    • Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
    • Tatulian, S.A., P. Hinterdorfer, G. Baber, and L.K. Tamm. 1995. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO (Eur. Mol. Biol. Organ.) J. 14:5514-5523.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 46
    • 0019051305 scopus 로고
    • Influenza virus haemagglutinin. Structural predictions suggest that the fibrillar appearance is due to the presence of a coiled-coil
    • Ward, C.W., and T A. Dopheide. 1980. Influenza virus haemagglutinin. Structural predictions suggest that the fibrillar appearance is due to the presence of a coiled-coil. Aust. J. Biol. Sci. 33:449-455.
    • (1980) Aust. J. Biol. Sci. , vol.33 , pp. 449-455
    • Ward, C.W.1    Dopheide, T.A.2
  • 47
    • 0028774043 scopus 로고
    • Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs
    • Watowich, S.J., J.J. Skehel, and D.C. Wiley. 1994. Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs. Structure. 2:719-731.
    • (1994) Structure , vol.2 , pp. 719-731
    • Watowich, S.J.1    Skehel, J.J.2    Wiley, D.C.3
  • 48
    • 0028298880 scopus 로고
    • Evidence for H+-induced insertion of influenza hemagglutinin HA2 N-terminal segment into viral membrane
    • Weber, T., G. Paesold, C. Galli, R. Mischler, G. Semenza, and J. Brunner. 1994. Evidence for H+-induced insertion of influenza hemagglutinin HA2 N-terminal segment into viral membrane. J. Biol. Chem. 269:18353-18358.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18353-18358
    • Weber, T.1    Paesold, G.2    Galli, C.3    Mischler, R.4    Semenza, G.5    Brunner, J.6
  • 50
  • 53
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
    • White, J.M., and I.A. Wilson. 1987. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. J. Cell Biol. 105:2887-2896.
    • (1987) J. Cell Biol. , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 54
    • 0017647917 scopus 로고
    • Transfer of purified herpes virus thymidine kinase gene to cultured mouse cells
    • Wigler, M., S. Silverstein, L.-S. Lee, A. Pellicer, Y.-C. Cheng, and R. Axel. 1977. Transfer of purified herpes virus thymidine kinase gene to cultured mouse cells. Cell. 11:223-232.
    • (1977) Cell. , vol.11 , pp. 223-232
    • Wigler, M.1    Silverstein, S.2    Lee, L.-S.3    Pellicer, A.4    Cheng, Y.-C.5    Axel, R.6
  • 55
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C., J.W. Dubay, T. Greenwell, T. Baird, Jr., T.G. Oas, C. McDanal, E. Hunter, and T. Matthews. 1994a. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc. Natl. Acad. Sci. USA. 91:12676-12680.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird Jr., T.4    Oas, T.G.5    McDanal, C.6    Hunter, E.7    Matthews, T.8
  • 56
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C.T., D.C. Shugars, T.K. Greenwell, C.B. McDanal, and T.J. Matthews. 1994b. Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA. 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 57
    • 0030245704 scopus 로고    scopus 로고
    • Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection
    • Yao, Y., and R.W. Compans. 1996. Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection. Virology. 223:103-112.
    • (1996) Virology , vol.223 , pp. 103-112
    • Yao, Y.1    Compans, R.W.2


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