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Volumn 232, Issue 1, 1993, Pages 89-104

Translational repression by the bacteriophage T4 gene 32 protein involves specific recognition of an RNA pseudoknot structure

Author keywords

Protein: RNA interactions; Pseudoknots; Translational control

Indexed keywords


EID: 0027291857     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1993.1372     Document Type: Article
Times cited : (34)

References (53)
  • 1
    • 0014963741 scopus 로고
    • T4 bacteriophage gene 32: A structural protein in the replication and recombination of DNA
    • Alberts, B. M. & Frey, L. (1970). T4 bacteriophage gene 32: a structural protein in the replication and recombination of DNA. Nature (London), 227, 1313-1318.
    • (1970) Nature (London) , vol.227 , pp. 1313-1318
    • Alberts, B.M.1    Frey, L.2
  • 2
    • 0023673238 scopus 로고
    • Proposed structure for the zincbinding domains from transcription factor IIIA and related proteins
    • Berg, J. M. (1988). Proposed structure for the zincbinding domains from transcription factor IIIA and related proteins. Proc. Nacl. Acad. Sci., U.S.A. 85, 99-102.
    • (1988) Proc. Nacl. Acad. Sci., U.S.A. , vol.85 , pp. 99-102
    • Berg, J.M.1
  • 3
    • 0025255158 scopus 로고
    • Zinc fingers and other metal-binding domains
    • Berg, J. M. (1990). Zinc fingers and other metal-binding domains. J. Biol. Chem. 265, 6513-6516.
    • (1990) J. Biol. Chem , vol.265 , pp. 6513-6516
    • Berg, J.M.1
  • 4
    • 0018726495 scopus 로고
    • Purification of the T4 gene 32 protein free from detectable deoxyribonuclease activities
    • Bittner, M., Burke, R. L. & Alberts, B. M. (1979). Purification of the T4 gene 32 protein free from detectable deoxyribonuclease activities. J. Biol. Chem. 254, 9565-9572.
    • (1979) J. Biol. Chem , vol.254 , pp. 9565-9572
    • Bittner, M.1    Burke, R.L.2    Alberts, B.M.3
  • 5
    • 0024747886 scopus 로고
    • Transcription and messenger RNA processing upstream of bacteriophage T4 gene 32
    • Carpousis, A. J., Mudd, E. A. & Kriseh, H. M. (1989). Transcription and messenger RNA processing upstream of bacteriophage T4 gene 32. Mol. Gen. Genet. 219, 39-48.
    • (1989) Mol. Gen. Genet , vol.219 , pp. 39-48
    • Carpousis, A.J.1    Mudd, E.A.2    Kriseh, H.M.3
  • 6
    • 0023660747 scopus 로고
    • S4-aJpha mRNA translation regulation complex II. Secondary struc-tures of the RNA regulatory site in the presence and absence of S4
    • Deckman, I. C. & Draper, D. E. (1987). S4-aJpha mRNA translation regulation complex II. Secondary struc-tures of the RNA regulatory site in the presence and absence of S4. J. Mol. Biol. 196, 323-332.
    • (1987) J. Mol. Biol , vol.196 , pp. 323-332
    • Deckman, I.C.1    Draper, D.E.2
  • 7
    • 0025598002 scopus 로고
    • Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1
    • Darlix, J.-L, Gabus, C., Nugeyre, M.-T., Clavel, F. & Barre’-Sinoussi, F. (1990). Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1. J. Mol. Biol. 216, 689-699
    • (1990) J. Mol. Biol , vol.216 , pp. 689-699
    • Darlix, J.-L.1    Gabus, C.2    Nugeyre, M.-T.3    Clavel, F.4    Barre’-Sinoussi, F.5
  • 8
    • 0026632755 scopus 로고
    • Nucleic acid interactive properties of a peptide corresponding to the N-terminal zinc finger domain of HIV-1 nucleocapsid protein
    • Delahunty, M. D., South, T. L., Summers, M. F. & Karpel, R. L. (1992). Nucleic acid interactive properties of a peptide corresponding to the N-terminal zinc finger domain of HIV-1 nucleocapsid protein. Biochemistry, 31, 6461-6469
    • (1992) Biochemistry , vol.31 , pp. 6461-6469
    • Delahunty, M.D.1    South, T.L.2    Summers, M.F.3    Karpel, R.L.4
  • 9
    • 0015527105 scopus 로고
    • Characterization by electron microscopy of the complex formed between T4 bacteriophage gene 32 protein and DNA
    • Delius, H., Mantell, N. J. & Alberts, B. (1972). Characterization by electron microscopy of the complex formed between T4 bacteriophage gene 32 protein and DNA. J. Mol. Biol. 67, 341-350.
    • (1972) J. Mol. Biol. , vol.67 , pp. 341-350
    • Delius, H.1    Mantell, N.J.2    Alberts, B.3
  • 10
    • 0023316092 scopus 로고    scopus 로고
    • 3-D graphics modelling of the tRNA-like 3' end of turnip yellow mosaic virus RNA: Structural and functional implications
    • Dumas, P., Moras, D., Florentz, C., Giege, R., Verlaan, P., Van Belkum, A. & Pleij, C. W. A. (1987). 3-D graphics modelling of the tRNA-like 3' end of turnip yellow mosaic virus RNA: structural and functional implications. J. Biomol. Struct. Dynam. 4, 707-727.
    • J. Biomol. Struct. Dynam , vol.4 , pp. 707-727
    • Dumas, P.1    Moras, D.2    Florentz, C.3    Giege, R.4    Verlaan, P.5    Van Belkum, A.6    Pleij, C.W.7
  • 11
    • 0019878376 scopus 로고
    • Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis
    • Fried, M. & Crothers, D. M. (1981). Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis Nucl. Acids Res. 9, 6505-6525.
    • (1981) Nucl. Acids Res. , vol.9 , pp. 6505-6525
    • Fried, M.1    Crothers, D.M.2
  • 12
    • 0021321501 scopus 로고
    • Specificity of translational regulation by two DNA-binding proteins. J. Mol
    • Fulford, W. & Model, P. (1984). Specificity of translational regulation by two DNA-binding proteins. J. Mol. Biol. 173, 211-226.
    • (1984) Biol , vol.173 , pp. 211-226
    • Fulford, W.1    Model, P.2
  • 15
    • 0024477899 scopus 로고
    • NMR spectroscopy of 1330d(II)-substituted gene 32 protein
    • Giedroc, D. P., Johnson, B. A., Armitage, I. A. & Coleman, J. E. (1989). NMR spectroscopy of 1330d(II)-substituted gene 32 protein. Biochemistry, 28, 2410-2416.
    • (1989) Biochemistry , vol.28 , pp. 2410-2416
    • Giedroc, D.P.1    Johnson, B.A.2    Armitage, I.A.3    Coleman, J.E.4
  • 16
    • 0022346616 scopus 로고
    • The stability of bacteriophage T4 gene 32 mRNA: A 5' leader sequence that can stabilize mRNA transcripts
    • Gorski, K., Roch, J.-M., Prentki, P. & Krish, H. M. (1985). The stability of bacteriophage T4 gene 32 mRNA: a 5' leader sequence that can stabilize mRNA transcripts. Cell, 43, 461 -469.
    • (1985) Cell , vol.43
    • Gorski, K.1    Roch, J.-M.2    Prentki, P.3    Krish, H.M.4
  • 17
    • 0026078316 scopus 로고
    • Analysis of symmetry and three dimensional reconstruction of thin gp32*l crystals
    • Grant, R. A, Schmid, M. F. & Chiu, W. (1991). Analysis of symmetry and three dimensional reconstruction of thin gp32*l crystals. J. Mol. Biol, 217, 551-562.
    • (1991) J. Mol. Biol , vol.217 , pp. 551-562
    • Grant, R.A.1    Schmid, M.F.2    Chiu, W.3
  • 18
    • 0026647836 scopus 로고
    • The human immunodeficiency virus type 1 packaging signal and major splice donor region have a conserved stable secondary structure
    • Harrison, G. P. & Lever, A. M. (1992). The human immunodeficiency virus type 1 packaging signal and major splice donor region have a conserved stable secondary structure. J. Virol. 66, 4144-4153.
    • (1992) J. Virol , vol.66 , pp. 4144-4153
    • Harrison, G.P.1    Lever, A.M.2
  • 19
    • 0026632944 scopus 로고
    • RNA Packaging signal of human immunodeficiency virus type 1
    • Hayashi, T., Shioda, T, Twakura, Y. & Shibuta, H. (1992). RNA Packaging signal of human immunodeficiency virus type 1. Virology, 188, 590-599.
    • (1992) Virology , vol.188 , pp. 590-599
    • Hayashi, T.1    Shioda, T.2    Twakura, Y.3    Shibuta, H.4
  • 20
    • 0015243807 scopus 로고
    • Stimulation of T4 bacteriophage DNA polymerase by the protein product of T4 gene 32
    • Huberman, J. A., Kornberg, A. & Alberts, B. M, (1971). Stimulation of T4 bacteriophage DNA polymerase by the protein product of T4 gene 32. J. Mol. Biol. 62, 39-52.
    • (1971) J. Mol. Biol , vol.62 , pp. 39-52
    • Huberman, J.A.1    Kornberg, A.2    Alberts, B.M.3
  • 23
    • 0023772104 scopus 로고
    • Thermal denatura-tion of T4 gene 32 protein: Effects of zinc removal and substitution
    • Keating, K. M., Giedroc, D. P., Williams, K. R., Coleman, J. E. & Sturtevant, J. M. (1988). Thermal denatura-tion of T4 gene 32 protein: effects of zinc removal and substitution. Biochemistry, 27, 5240-5245.
    • (1988) Biochemistry , vol.27 , pp. 5240-5245
    • Keating, K.M.1    Giedroc, D.P.2    Williams, K.R.3    Coleman, J.E.4    Sturtevant, J.M.5
  • 24
    • 0019351776 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions
    • Kowalczykowski, S. C., Lonberg, N., Newport, J. W. & von Hippel, P, H. (1981). Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions. J. Mol. Biol. 145, 75-104.
    • (1981) J. Mol. Biol , vol.145 , pp. 75-104
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Von Hippel, P.4
  • 25
    • 0019904519 scopus 로고
    • Nucleotide sequences involved in bacteriophage T4 gene 32 translational self-regulation. IVoc
    • Krisch, H. M. & Allet, B. (1982). Nucleotide sequences involved in bacteriophage T4 gene 32 translational self-regulation. iVoc. Nacl. Acad. Sei., U.S.A. 79, 4937-4941.
    • (1982) Nacl. Acad. Sei., U.S.A. , vol.79 , pp. 4937-4941
    • Krisch, H.M.1    Allet, B.2
  • 26
    • 0021770897 scopus 로고
    • Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. Changes in mechanism as a function of sodium chloride concentration and other solution variables
    • Lohman, T. M. (1984). Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. Changes in mechanism as a function of sodium chloride concentration and other solution variables. Biochemistry, 23, 4656-4665.
    • (1984) Biochemistry , vol.23 , pp. 4656-4665
    • Lohman, T.M.1
  • 27
    • 0019774929 scopus 로고
    • Kinetics and mechanism of the association of the bacteriophage T4 gene 32 (Helix destabilizing) protein with single-stranded nucleic acids
    • Lohman, T. M. & Kowalczykowski, S. C. (1981). Kinetics and mechanism of the association of the bacteriophage T4 gene 32 (helix destabilizing) protein with single-stranded nucleic acids. J. Mol. Biol. 152, 67-109.
    • (1981) J. Mol. Biol , vol.152 , pp. 67-109
    • Lohman, T.M.1    Kowalczykowski, S.C.2
  • 28
    • 0022973884 scopus 로고
    • On the recognition of helical RNA by cobra vanom V! nuclease
    • bowman, H. B. & Draper, D. E. (1986). On the recognition of helical RNA by cobra vanom V! nuclease. J. Biol. Chem. 261, 5396-5403.
    • (1986) J. Biol. Chem , vol.261 , pp. 5396-5403
    • Bowman, H.B.1    Draper, D.E.2
  • 29
    • 0024278647 scopus 로고
    • Autogenous regulatory site on the bacteriophage T4 gene 32 messenger RNA
    • McPheeters, D. S., Stormo, G. D. & Gold, L. (1988). Autogenous regulatory site on the bacteriophage T4 gene 32 messenger RNA. J. Mol. Biol. 201, 517-535.
    • (1988) J. Mol. Biol , vol.201 , pp. 517-535
    • McPheeters, D.S.1    Stormo, G.D.2    Gold, L.3
  • 30
    • 0023801716 scopus 로고
    • Mutations in Rous sarcoma virus nucleocapsid protein pl2 (NC): Deletions of Cys-His boxes
    • Meric, C., GouIIIoud, E. & Spahr, P. F. (1988). Mutations in Rous sarcoma virus nucleocapsid protein pl2 (NC): deletions of Cys-His boxes. J. Virol. 62, 3328-3333.
    • (1988) J. Virol. , vol.62 , pp. 3328-3333
    • Meric, C.1    Gouiiioud, E.2    Spahr, P.F.3
  • 31
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • MIIIigan, J. F., Groege, D. R., Witherell, G. W. & Uhlenbeck, O. C. (1987). Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucl. Acids Res. 15, 8738-8792.
    • (1987) Nucl. Acids Res , vol.15 , pp. 8738-8792
    • Miiiigan, J.F.1    Groege, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 32
    • 0024117856 scopus 로고
    • Processing of unstable bacteriophage T4 gene 32 mRNAs into a stable species requires Escherichia coli ribonuclease E
    • Mudd, E. A, Prentki, P., Belin, D. & Krisch, H. M. (1988). Processing of unstable bacteriophage T4 gene 32 mRNAs into a stable species requires Escherichia coli ribonuclease E. EM BO J.7, 3601-3607.
    • (1988) EM BO J , vol.7 , pp. 3601-3607
    • Mudd, E.A.1    Prentki, P.2    Belin, D.3    Krisch, H.M.4
  • 33
    • 0025298946 scopus 로고
    • A novel function for zinc(TT) in a nucleic acid binding protein: Contribution of zinc(Tl) towards the cooperativity of bacteriophage T4 gene 32 binding
    • Nadler, S. G., Roberts, W. J., Shamoo, Y. & Williams, K. R. (1990). A novel function for zinc(TT) in a nucleic acid binding protein: contribution of zinc(Tl) towards the cooperativity of bacteriophage T4 gene 32 binding. J. Biol. Chem. 265, 10389-10394.
    • (1990) J. Biol. Chem , vol.265 , pp. 10389-10394
    • Nadler, S.G.1    Roberts, W.J.2    Shamoo, Y.3    Williams, K.R.4
  • 34
    • 0019349524 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids II. Specificitv of binding to DNA and RNA
    • Newport, J. W., Lonberg, N., Kowasczykowski, S. C. & von Hippel, P. H. (1981). Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids II. Specificitv of binding to DNA and RNA. J. Mol. Biol. 145 105-121.
    • (1981) J. Mol. Biol , vol.145 , pp. 105-121
    • Newport, J.W.1    Lonberg, N.2    Kowasczykowski, S.C.3    Von Hippel, P.H.4
  • 35
    • 0024457613 scopus 로고
    • Comparison of cooperative and isolated site binding of T4 gene 32 protein to ssDNA by *H NMR
    • Pan, T., King, G. C. & Coleman, J. E. (1989). Comparison of cooperative and isolated site binding of T4 gene 32 protein to ssDNA by *H NMR. Biochemistry, 28, 8833-8839.
    • (1989) Biochemistry , vol.28 , pp. 8833-8839
    • Pan, T.1    King, G.C.2    Coleman, J.E.3
  • 36
    • 0024026527 scopus 로고
    • Small finger protein of avian and murine retroviruses has nucleic acid annealing activity and positions the replication primer tRNA onto genomic RNA
    • Prats, A. O., Sarih, L., Gabus, C., Litvak, S., Keith, G. & Darlix, J. L. (1988). Small finger protein of avian and murine retroviruses has nucleic acid annealing activity and positions the replication primer tRNA onto genomic RNA. EMBO J. 7, 1777-1783
    • (1988) EMBO J , vol.7 , pp. 1777-1783
    • Prats, A.O.1    Sarih, L.2    Gabus, C.3    Litvak, S.4    Keith, G.5    Darlix, J.L.6
  • 37
    • 0023866603 scopus 로고
    • A pseudoknotted RNA oligonucleotide. Nature
    • Puglisi, J. D., Wyatt, J. R. & Tinoco, I., Jr. (1988). A pseudoknotted RNA oligonucleotide. Nature. (London), 331, 283-286.
    • (1988) (London) , vol.331 , pp. 283-286
    • Puglisi, J.D.1    Wyatt, J.R.2    Tinoco, I.3
  • 38
    • 0025108861 scopus 로고
    • Conformation of an RNA pseudoknot. J. Mol
    • Puglisi, J.D., Wyatt, J. R. & Tinoco, L, Jr. (1990). Conformation of an RNA pseudoknot. J. Mol. Biol. 214, 437-453.
    • (1990) Biol , vol.214 , pp. 437-453
    • Puglisi, J.D.1    Wyatt, J.R.2    Tinoco, L.3
  • 39
    • 0017137088 scopus 로고
    • Translational, autogenous regulation of gene 32 expression during bacteriophage T4 infection
    • Russel, M., Gold, L., Morrissett, H. & O’Earrell, P. Z, (1976). Translational, autogenous regulation of gene 32 expression during bacteriophage T4 infection. J. Biol. Chem. 251, 7263-7270.
    • (1976) J. Biol. Chem , vol.251 , pp. 7263-7270
    • Russel, M.1    Gold, L.2    Morrissett, H.3    O’earrell, P.Z.4
  • 40
    • 0003903343 scopus 로고
    • In, (Nolan, C., ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). In Molecular Cloning (Nolan, C., ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Molecular Cloning
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 41
    • 0022889372 scopus 로고
    • Cloning of T4 gene 32 and expression of the wild type protein under pL regulation in E. Coli
    • Shamoo, Y., Adari, H., Königsberg, W. H, Williams, K. R. & Chase, J. (1986). Cloning of T4 gene 32 and expression of the wild type protein under pL regulation in E. coli. Proc. Nacl. Acad. Sei., U.S.A. 83, 8844-8848.
    • (1986) Proc. Nacl. Acad. Sei., U.S.A. , vol.83 , pp. 8844-8848
    • Shamoo, Y.1    Adari, H.2    Königsberg, W.H.3    Williams, K.R.4    Chase, J.5
  • 42
    • 0023747813 scopus 로고
    • Photochemical crosslinking of bacteriophage T4 single-stranded DNA binding protein (Gp32) to oligo-p(dT)e: Identification of phenylalanine-138 as the site of crosslinking
    • e: identification of phenylalanine-138 as the site of crosslinking. Protein Struct. Funct. Genet. 4, 1-6.
    • (1988) Protein Struct. Funct. Genet , vol.4 , pp. 1-6
    • Shainoo, Y.1    Williams, K.R.2    Königsberg, W.H.3
  • 43
    • 0025901138 scopus 로고
    • A retrovirus-like zinc domain is essential for translational repression of bacteriophage T4 gene 32
    • Shamoo, Y., Webster, K. R., Williams, K. R. & Königsberg, W. H. (1991). A retrovirus-like zinc domain is essential for translational repression of bacteriophage T4 gene 32. J. Biol. Chem. 266, 7967-7970.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7967-7970
    • Shamoo, Y.1    Webster, K.R.2    Williams, K.R.3    Königsberg, W.H.4
  • 44
    • 0018289487 scopus 로고
    • T4 gene 32 protein trypsin-generated fragments: Fluorescence measurement of DNA-binding parameters
    • Spicer, E. K., Williams, K. R. & Königsberg, W. H. (1979). T4 gene 32 protein trypsin-generated fragments: fluorescence measurement of DNA-binding parameters. J. Biol. Chem. 254, 6433-6436.
    • (1979) J. Biol. Chem , vol.254 , pp. 6433-6436
    • Spicer, E.K.1    Williams, K.R.2    Königsberg, W.H.3
  • 45
    • 0017295709 scopus 로고
    • Conformational changes of transfer RNA. The role of magnesium (II)
    • Stein, A. & Crothers, D. M. (1976). Conformational changes of transfer RNA. The role of magnesium (II). Biochemistry, 15, 160-168.
    • (1976) Biochemistry , vol.15 , pp. 160-168
    • Stein, A.1    Crothers, D.M.2
  • 46
    • 0026075513 scopus 로고
    • An NMR characterizaton of the regA protein-binding site of bacteriophage T4 gene 44 mRNA
    • Szewczak, A. A., Webster, K. R., Spicer, E. K. & Moore, P. B. (1991). An NMR characterizaton of the regA protein-binding site of bacteriophage T4 gene 44 mRNA. J. Biol. Chem. 266, 17832-17837.
    • (1991) J. Biol. Chem , vol.266 , pp. 17832-17837
    • Szewczak, A.A.1    Webster, K.R.2    Spicer, E.K.3    Moore, P.B.4
  • 47
    • 0022429789 scopus 로고
    • The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA
    • Taylor, J. W., Ott, J. & Eckstein, R. (1985). The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA. Nucl. Acids Res. 13, 8764-8785.
    • (1985) Nucl. Acids Res , vol.13 , pp. 8764-8785
    • Taylor, J.W.1    Ott, J.2    Eckstein, R.3
  • 48
    • 0014014861 scopus 로고
    • Molecular mechanism of genetic recombination in bacteriophage. VI. A mutant defective in joining of DNA molecules
    • Tomizawa, J., Anraku, N. & Iwama, Y, (1966). Molecular mechanism of genetic recombination in bacteriophage. VI. A mutant defective in joining of DNA molecules. J. Mol. Biol. 21, 247-253.
    • (1966) J. Mol. Biol. , vol.21 , pp. 247-253
    • Tomizawa, J.1    Anraku, N.2    Iwama, Y.3
  • 51
    • 0024788334 scopus 로고
    • Bacteriophage T4 RegA protein binds to the Shine-Dalgarno region of gene 44 mRNA
    • Webster, K., Adari, H. Y. & Spicer, E. K. (1989). Bacteriophage T4 RegA protein binds to the Shine-Dalgarno region of gene 44 mRNA. Nucl. Acids Res. 17, 10047-10068.
    • (1989) Nucl. Acids Res , vol.17 , pp. 10047-10068
    • Webster, K.1    Adari, H.Y.2    Spicer, E.K.3
  • 52
    • 0015804484 scopus 로고
    • Requirements of a functional gene 32 product of bacteriophage T4 in UV repair
    • Wu, J. & Yeh, Y. (1973). Requirements of a functional gene 32 product of bacteriophage T4 in UV repair. J. Virol. 12, 758-765.
    • (1973) J. Virol , vol.12 , pp. 758-765
    • Wu, J.1    Yeh, Y.2


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