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Volumn 66, Issue 6, 1996, Pages 2523-2531

Binding of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase to Myelin: An in Vitro Study

Author keywords

2 ,3 cyclic nucleotide 3 phosphodiesterase; CXXX box; Detergent extraction; Isoprenylation; Myelin; Myelin skeleton

Indexed keywords

2',3' CYCLIC NUCLEOTIDE 3' PHOSPHODIESTERASE; CYSTEINE; ISOPRENOID; MYELIN; MYELIN PROTEIN;

EID: 0029951412     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66062523.x     Document Type: Article
Times cited : (22)

References (50)
  • 1
    • 0025339701 scopus 로고
    • 2′,3′-Cyclic nucleotide-3′-phosphodiesterase in the central nervous system is fatty-acylated by thioester linkage
    • Agrawal H. C., Sprinkle T. J., and Agrawal D. (1990) 2′,3′-Cyclic nucleotide-3′-phosphodiesterase in the central nervous system is fatty-acylated by thioester linkage. J. Biol. Chem. 265, 11849-11853.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11849-11853
    • Agrawal, H.C.1    Sprinkle, T.J.2    Agrawal, D.3
  • 2
    • 0027367040 scopus 로고
    • Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes
    • Ainger K., Avossa D., Morgan F., Hill S. J., Barry C., Barbarese E., and Carson J. H. (1993) Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes. J. Cell Biol. 123, 431-441.
    • (1993) J. Cell Biol. , vol.123 , pp. 431-441
    • Ainger, K.1    Avossa, D.2    Morgan, F.3    Hill, S.J.4    Barry, C.5    Barbarese, E.6    Carson, J.H.7
  • 3
    • 0028920240 scopus 로고
    • CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB
    • Armstrong S. A., Hannah V. C., Goldstein J. L., and Brown M. S. (1995) CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB. J. Biol. Chem. 270, 7864-7868.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7864-7868
    • Armstrong, S.A.1    Hannah, V.C.2    Goldstein, J.L.3    Brown, M.S.4
  • 4
    • 0023787396 scopus 로고
    • Immunocytochemical localization by electron microscopy of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in developing oligodendrocytes of normal and mutant brain
    • Braun P. E., Sandillon F., Edwards A., Matthieu J. M., and Privat A. (1988) Immunocytochemical localization by electron microscopy of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in developing oligodendrocytes of normal and mutant brain. J. Neurosci. 8, 3057-3066.
    • (1988) J. Neurosci. , vol.8 , pp. 3057-3066
    • Braun, P.E.1    Sandillon, F.2    Edwards, A.3    Matthieu, J.M.4    Privat, A.5
  • 5
    • 0025696732 scopus 로고
    • 2′,3′-Cyclic nucleotide 3′-phosphodiesterase has characteristics of cytoskeletal proteins. A hypothesis for its function
    • Braun P. E., Bambrick L. L., Edwards A. M., and Bernier L. (1990) 2′,3′-Cyclic nucleotide 3′-phosphodiesterase has characteristics of cytoskeletal proteins. A hypothesis for its function. Ann. NY Acad. Sci. 605, 55-65.
    • (1990) Ann. NY Acad. Sci. , vol.605 , pp. 55-65
    • Braun, P.E.1    Bambrick, L.L.2    Edwards, A.M.3    Bernier, L.4
  • 6
    • 0025786193 scopus 로고
    • Isoprenoid modification permits 2′,3′-cyclic nucleotide 3′-phosphodiesterase to bind to membranes
    • Braun P. E., De Angelis D., Shtybel W. W., and Bernier L. (1991) Isoprenoid modification permits 2′,3′-cyclic nucleotide 3′-phosphodiesterase to bind to membranes. J. Neurosci. Res. 30, 540-544.
    • (1991) J. Neurosci. Res. , vol.30 , pp. 540-544
    • Braun, P.E.1    De Angelis, D.2    Shtybel, W.W.3    Bernier, L.4
  • 7
    • 0024535322 scopus 로고
    • Differential ultrastructural localization of myelin basic protein, myelin/oligodendroglial glycoprotein, and 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the CNS of adult rats
    • Brunner C., Lassmann H., Waehneldt T. V., Matthieu J. M., and Linington C. (1989) Differential ultrastructural localization of myelin basic protein, myelin/oligodendroglial glycoprotein, and 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the CNS of adult rats. J. Neurochem. 52, 296-304.
    • (1989) J. Neurochem. , vol.52 , pp. 296-304
    • Brunner, C.1    Lassmann, H.2    Waehneldt, T.V.3    Matthieu, J.M.4    Linington, C.5
  • 8
    • 0027050783 scopus 로고
    • Biochemistry of protein prenylation
    • Casey P. J. (1992) Biochemistry of protein prenylation. J. Lipid Res. 33, 1731-1740.
    • (1992) J. Lipid Res. , vol.33 , pp. 1731-1740
    • Casey, P.J.1
  • 9
    • 0025948794 scopus 로고
    • Hypervariable C-terminal domain of rab proteins acts as a targeting signal
    • Chavrier P., Gorvel J. P., Stelzer E., Simons K., Gruenberg J., and Zerial M. (1991) Hypervariable C-terminal domain of rab proteins acts as a targeting signal. Nature 353, 769-772.
    • (1991) Nature , vol.353 , pp. 769-772
    • Chavrier, P.1    Gorvel, J.P.2    Stelzer, E.3    Simons, K.4    Gruenberg, J.5    Zerial, M.6
  • 10
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke S. (1992) Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem. 61, 355-386.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 11
    • 0020372097 scopus 로고
    • Synthesis and incorporation of myelin polypeptides into CNS myelin
    • Colman D. R., Kreibich G., Frey A. B., and Sabatini D. D. (1982) Synthesis and incorporation of myelin polypeptides into CNS myelin. J. Cell Biol. 95, 598-608.
    • (1982) J. Cell Biol. , vol.95 , pp. 598-608
    • Colman, D.R.1    Kreibich, G.2    Frey, A.B.3    Sabatini, D.D.4
  • 13
    • 0027026591 scopus 로고
    • Protein prenylation: More than just glue?
    • Cox A. D. and Der C. J. (1992) Protein prenylation: more than just glue? Curr. Opin. Cell Biol. 4, 1008-1016.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 1008-1016
    • Cox, A.D.1    Der, C.J.2
  • 14
    • 0026659959 scopus 로고
    • Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein
    • Cox A. D., Hisaka M. M., Buss J. E., and Der C. J. (1992) Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein. Mol. Cell. Biol. 12, 2606-2615.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2606-2615
    • Cox, A.D.1    Hisaka, M.M.2    Buss, J.E.3    Der, C.J.4
  • 15
    • 0028080453 scopus 로고
    • C-terminal CTII motif of 2′,3′-cyclic nucleotide 3′-phosphodiesterase undergoes carboxylmethylation
    • Cox M. E., Gao E. N., and Braun P. E. (1994) C-terminal CTII motif of 2′,3′-cyclic nucleotide 3′-phosphodiesterase undergoes carboxylmethylation. J. Neurosci. Res. 39, 513-518.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 513-518
    • Cox, M.E.1    Gao, E.N.2    Braun, P.E.3
  • 16
    • 0028099724 scopus 로고
    • Isoprenylation of brain 2′,3′-cyclic nucleotide 3′-phosphodiesterase modulates cell morphology
    • De Angelis D. A. and Braun P. E. (1994) Isoprenylation of brain 2′,3′-cyclic nucleotide 3′-phosphodiesterase modulates cell morphology. J. Neurosci. Res. 39, 386-397.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 386-397
    • De Angelis, D.A.1    Braun, P.E.2
  • 17
    • 0001772003 scopus 로고
    • Cellular and molecular characteristics of CNP suggest regulatory mechanism in myelinogenesis
    • Salvati S., ed, Plenum Press, New York
    • De Angelis D. A., Cox M., Gao E., and Braun P. (1994) Cellular and molecular characteristics of CNP suggest regulatory mechanism in myelinogenesis, in A Multidisciplinary Approach to Myelin Diseases (Salvati S., ed), pp. 49-58. Plenum Press, New York.
    • (1994) A Multidisciplinary Approach to Myelin Diseases , pp. 49-58
    • De Angelis, D.A.1    Cox, M.2    Gao, E.3    Braun, P.4
  • 18
    • 0024442564 scopus 로고
    • Organization of oligodendroglial membrane sheets. I: Association of myelin basic protein and 2′,3′-cyclic nucleotide 3′-phosphohydrolase with cytoskeleton
    • Dyer C. A. and Benjamins J. A. (1989) Organization of oligodendroglial membrane sheets. I: Association of myelin basic protein and 2′,3′-cyclic nucleotide 3′-phosphohydrolase with cytoskeleton. J. Neurosci. Res. 24, 201-211.
    • (1989) J. Neurosci. Res. , vol.24 , pp. 201-211
    • Dyer, C.A.1    Benjamins, J.A.2
  • 19
  • 20
    • 0024327316 scopus 로고
    • Characterization of a cytoskeletal matrix associated with myelin from rat brain
    • Gillespie C. S., Wilson R., Davidson A., and Brophy P. J. (1989) Characterization of a cytoskeletal matrix associated with myelin from rat brain. Biochem. J. 260, 689-696.
    • (1989) Biochem. J. , vol.260 , pp. 689-696
    • Gillespie, C.S.1    Wilson, R.2    Davidson, A.3    Brophy, P.J.4
  • 21
    • 0025137912 scopus 로고
    • Biosynthesis of the myelin 2′,3′-cyclic nucleotide 3′-phosphodiesterases
    • Gillespie C. S., Bernier L., Brophy P. J., and Colman D. R. (1990) Biosynthesis of the myelin 2′,3′-cyclic nucleotide 3′-phosphodiesterases. J. Neurochem. 54, 656-661.
    • (1990) J. Neurochem. , vol.54 , pp. 656-661
    • Gillespie, C.S.1    Bernier, L.2    Brophy, P.J.3    Colman, D.R.4
  • 22
    • 0028305164 scopus 로고
    • Molecular cloning and characterization of rat brain 2′,3′-cyclic nucleotide 3′-phosphodiesterase isoform 2
    • Gravel M., DeAngelis D., and Braun P. E. (1994) Molecular cloning and characterization of rat brain 2′,3′-cyclic nucleotide 3′-phosphodiesterase isoform 2. J. Neurosci. Res. 38, 243-247.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 243-247
    • Gravel, M.1    DeAngelis, D.2    Braun, P.E.3
  • 23
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock J. F., Magee A. I., Childs J. E., and Marshall C. J. (1989) All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57, 1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 24
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock J. F., Paterson H., and Marshall C. J. (1990) A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 63, 133-139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 25
    • 0026021456 scopus 로고
    • Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B)
    • Hancock J. F., Cadwallader K., and Marshall C. J. (1991) Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B). EMBO J. 10, 641-646.
    • (1991) EMBO J. , vol.10 , pp. 641-646
    • Hancock, J.F.1    Cadwallader, K.2    Marshall, C.J.3
  • 26
    • 85016731055 scopus 로고
    • Using PCR to engineer DNA
    • Erlich H. A., ed, Stockton Press, New York
    • Higushi R. (1989) Using PCR to engineer DNA, in PCR Technology (Erlich H. A., ed), pp. 61-70, Stockton Press, New York.
    • (1989) PCR Technology , pp. 61-70
    • Higushi, R.1
  • 27
    • 0024817731 scopus 로고
    • The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope
    • Holtz D., Tanaka R. A., Hartwig J., and McKeon F. (1989) The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope. Cell 59, 969-977.
    • (1989) Cell , vol.59 , pp. 969-977
    • Holtz, D.1    Tanaka, R.A.2    Hartwig, J.3    McKeon, F.4
  • 28
    • 0026726050 scopus 로고
    • Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases
    • Inglese J., Koch W. J., Caron M. G., and Lefkowitz R. J. (1992) Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases. Nature 359, 147-150.
    • (1992) Nature , vol.359 , pp. 147-150
    • Inglese, J.1    Koch, W.J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 29
    • 0029007102 scopus 로고
    • Regions outside of the CAAX motif influence the specificity of prenylation of G protein gamma subunits
    • Kaiman V. K., Erdman R. A., Maltese W. A., and Robishaw J. D. (1995) Regions outside of the CAAX motif influence the specificity of prenylation of G protein gamma subunits. J. Biol. Chem. 270, 14835-14841.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14835-14841
    • Kaiman, V.K.1    Erdman, R.A.2    Maltese, W.A.3    Robishaw, J.D.4
  • 30
    • 0021802577 scopus 로고
    • Biosynthesis and insertion of Wolfgram protein into optic nerve membranes
    • Karin N. J. and Waehneldt T. V. (1985) Biosynthesis and insertion of Wolfgram protein into optic nerve membranes. Neurochem. Res. 10, 897-907.
    • (1985) Neurochem. Res. , vol.10 , pp. 897-907
    • Karin, N.J.1    Waehneldt, T.V.2
  • 31
    • 0026731811 scopus 로고
    • rab GTP-binding proteins with three different carboxyl-terminal cysteine motifs are modified in vivo by 20-carbon isoprenoids
    • Kinsella B. T. and Maltese W. A. (1992) rab GTP-binding proteins with three different carboxyl-terminal cysteine motifs are modified in vivo by 20-carbon isoprenoids. J. Biol. Chem. 267, 3940-3945.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3940-3945
    • Kinsella, B.T.1    Maltese, W.A.2
  • 32
    • 0019140920 scopus 로고
    • Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in livers of mice treated with mevinolin, a competitive inhibitor of the reductase
    • Kita T., Brown M. S., and Goldstein J. L. (1980) Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in livers of mice treated with mevinolin, a competitive inhibitor of the reductase. J. Clin. Invest. 66, 1094-1100.
    • (1980) J. Clin. Invest. , vol.66 , pp. 1094-1100
    • Kita, T.1    Brown, M.S.2    Goldstein, J.L.3
  • 33
    • 0019406618 scopus 로고
    • Intracellular translocation of newly synthesized myelin proteins in the rat brain stem slices
    • Konat G. (1981) Intracellular translocation of newly synthesized myelin proteins in the rat brain stem slices. Exp. Neurol. 73, 254-266.
    • (1981) Exp. Neurol. , vol.73 , pp. 254-266
    • Konat, G.1
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0025649688 scopus 로고
    • Posttranslational modification of proteins by isoprenoids in mammalian cells
    • Maltese W. A. (1990) Posttranslational modification of proteins by isoprenoids in mammalian cells. FASEB J. 4, 3319-3328.
    • (1990) FASEB J. , vol.4 , pp. 3319-3328
    • Maltese, W.A.1
  • 36
    • 0015857284 scopus 로고
    • Myelination in rat brain: Method of myelin isolation
    • Norton W. T. and Poduslo S. E. (1973) Myelination in rat brain: method of myelin isolation. J. Neurochem. 21, 749-757.
    • (1973) J. Neurochem. , vol.21 , pp. 749-757
    • Norton, W.T.1    Poduslo, S.E.2
  • 37
  • 38
    • 0020635832 scopus 로고
    • Studies on subcellular fractions which are involved in myelin membrane assembly: Isolation from developing mouse brain and characterization by enzyme markers, electron microscopy, and electrophoresis
    • Pereyra P. M. and Braun P. E. (1983) Studies on subcellular fractions which are involved in myelin membrane assembly: isolation from developing mouse brain and characterization by enzyme markers, electron microscopy, and electrophoresis. J. Neurochem. 41, 957-973.
    • (1983) J. Neurochem. , vol.41 , pp. 957-973
    • Pereyra, P.M.1    Braun, P.E.2
  • 39
    • 0023898127 scopus 로고
    • Triton X-100 extractions of central nervous system myelin indicate a possible role for the minor myelin proteins in the stability in lamellae
    • Pereyra P. M., Horvath E., and Braun P. E. (1988) Triton X-100 extractions of central nervous system myelin indicate a possible role for the minor myelin proteins in the stability in lamellae. Neurochem. Res. 13, 583-595.
    • (1988) Neurochem. Res. , vol.13 , pp. 583-595
    • Pereyra, P.M.1    Horvath, E.2    Braun, P.E.3
  • 40
    • 0027193569 scopus 로고
    • The oligodendrocyte and its many cellular processes
    • Pfeiffer S. R., Warrington A. E., and Bansal R. (1993) The oligodendrocyte and its many cellular processes. Trends Cell Biol. 3, 191-197.
    • (1993) Trends Cell Biol. , vol.3 , pp. 191-197
    • Pfeiffer, S.R.1    Warrington, A.E.2    Bansal, R.3
  • 41
    • 0028196986 scopus 로고
    • Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers
    • Silvius J. R. and l'Heureux F. (1994) Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry 33, 3014-3022.
    • (1994) Biochemistry , vol.33 , pp. 3014-3022
    • Silvius, J.R.1    L'Heureux, F.2
  • 42
    • 0024600269 scopus 로고
    • 2′,3′-Cyclic nucleotide 3′-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system
    • Sprinkle T. J. (1989) 2′,3′-Cyclic nucleotide 3′-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system. Crit. Rev. Neurobiol. 4, 235-301.
    • (1989) Crit. Rev. Neurobiol. , vol.4 , pp. 235-301
    • Sprinkle, T.J.1
  • 43
    • 0025273261 scopus 로고
    • Expression of the oligodendrocyte marker 2′,3′-cyclic nucleotide 3′-phosphodiesterase in non-glial cells
    • Staugaitis S. M., Bernier L., Smith P. R., and Colman D. R. (1990) Expression of the oligodendrocyte marker 2′,3′-cyclic nucleotide 3′-phosphodiesterase in non-glial cells. J. Neurosci. Res. 25, 556-560.
    • (1990) J. Neurosci. Res. , vol.25 , pp. 556-560
    • Staugaitis, S.M.1    Bernier, L.2    Smith, P.R.3    Colman, D.R.4
  • 45
    • 0023678987 scopus 로고
    • Cellular and subcellular distribution of 2′,3′-cyclic nucleotide 3′-phosphodiesterase and its mRNA in the rat central nervous system
    • Trapp B. D., Bernier L., Andrews S. B., and Colman D. R. (1988) Cellular and subcellular distribution of 2′,3′-cyclic nucleotide 3′-phosphodiesterase and its mRNA in the rat central nervous system. J. Neurochem. 51, 859-868.
    • (1988) J. Neurochem. , vol.51 , pp. 859-868
    • Trapp, B.D.1    Bernier, L.2    Andrews, S.B.3    Colman, D.R.4
  • 46
    • 0001697547 scopus 로고
    • 2′,3′-Cyclic nucleotide 3′-phosphodiesterase: Molecular characterization and possible functional significance
    • Martensen R. E., ed, CRC Press, Boca Raton, Florida
    • Tsukada T. and Kurihara T. (1992) 2′,3′-Cyclic nucleotide 3′-phosphodiesterase: molecular characterization and possible functional significance, in Myelin: Biology and Chemistry (Martensen R. E., ed), pp. 449-480. CRC Press, Boca Raton, Florida.
    • (1992) Myelin: Biology and Chemistry , pp. 449-480
    • Tsukada, T.1    Kurihara, T.2
  • 47
    • 0027640552 scopus 로고
    • Transport and sorting of membrane lipids
    • van Meer G. (1993) Transport and sorting of membrane lipids. Curr. Opin. Cell Biol. 5, 661-673.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 661-673
    • Van Meer, G.1
  • 48
    • 0023925270 scopus 로고
    • Molecular structure, localization, and possible functions of the myelin-associated enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase
    • Vogel U. S. and Thompson R. J. (1988) Molecular structure, localization, and possible functions of the myelin-associated enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase. J. Neurochem. 50, 1667-1677.
    • (1988) J. Neurochem. , vol.50 , pp. 1667-1677
    • Vogel, U.S.1    Thompson, R.J.2
  • 49
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter P. and Blobel G. (1983) Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96, 83-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 83-93
    • Walter, P.1    Blobel, G.2
  • 50
    • 0024320814 scopus 로고
    • Role for the oligodendrocyte cytoskeleton in myelination
    • Wilson R. and Brophy P. J. (1989) Role for the oligodendrocyte cytoskeleton in myelination. J. Neurosci. Res. 22, 439-448.
    • (1989) J. Neurosci. Res. , vol.22 , pp. 439-448
    • Wilson, R.1    Brophy, P.J.2


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