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Volumn 218, Issue 1, 2010, Pages 48-60

Ribosomal analysis of rapid rates of protein synthesis in the antarctic sea urchin sterechinus neumayeri

Author keywords

[No Author keywords available]

Indexed keywords

ECHINODERM; GENETIC ANALYSIS; HYPOTHESIS TESTING; MARINE ENVIRONMENT; MEASUREMENT METHOD; PROTEIN;

EID: 77952305439     PISSN: 00063185     EISSN: None     Source Type: Journal    
DOI: 10.1086/BBLv218n1p48     Document Type: Article
Times cited : (6)

References (55)
  • 2
    • 0014790788 scopus 로고
    • Rates of synthesis and degradation of protein in the sea urchin embryo
    • Berg, W. E., and D. H. Mertes. 1970. Rates of synthesis and degradation of protein in the sea urchin embryo. Exp. Cell Res. 60: 218-224.
    • (1970) Exp. Cell Res. , vol.60 , pp. 218-224
    • Berg, W.E.1    Mertes, D.H.2
  • 3
    • 0018406891 scopus 로고
    • Elevation of protein synthesis is a complex response to fertilisation
    • Brandis, J. W., and R. A. Raff. 1978. Elevation of protein synthesis is a complex response to fertilisation. Nature 278: 467-469.
    • (1978) Nature , vol.278 , pp. 467-469
    • Brandis, J.W.1    Raff, R.A.2
  • 4
    • 0018164785 scopus 로고
    • Translation of oogenetic mRNA in sea urchin eggs and embryos. Demonstration of a change in translational efficiency following fertilization
    • Brandis, J. W., and R. A. Raff. 1979. Translation of oogenetic mRNA in sea urchin eggs and embryos. Demonstration of a change in translational efficiency following fertilization. Dev. Biol. 67: 99-113.
    • (1979) Dev. Biol. , vol.67 , pp. 99-113
    • Brandis, J.W.1    Raff, R.A.2
  • 5
    • 0030970280 scopus 로고    scopus 로고
    • Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish
    • Chen, L. B., A. L. Devries, and C. H. C. Cheng. 1997. Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish. Proc. Natl. Acad. Sci. 94: 3811-3816.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 3811-3816
    • Chen, L.B.1    Devries, A.L.2    Cheng, C.H.C.3
  • 6
    • 0016756922 scopus 로고
    • Effect of reduced temperatures on protein synthesis in mouse L cells
    • Craig, N. 1975. Effect of reduced temperatures on protein synthesis in mouse L cells. Cell 4: 329-335.
    • (1975) Cell , vol.4 , pp. 329-335
    • Craig, N.1
  • 7
    • 0017225010 scopus 로고
    • Regulation of translation in rabbit reticulocytes and mouse L-cells; Comparison of the effects of temperature
    • Craig, N. 1976. Regulation of translation in rabbit reticulocytes and mouse L-cells; comparison of the effects of temperature. J. Cell. Physiol. 87: 157-166.
    • (1976) J. Cell. Physiol. , vol.87 , pp. 157-166
    • Craig, N.1
  • 9
    • 0034711208 scopus 로고    scopus 로고
    • Cold adaptation of microtubule assembly and dynamics: Structural interpretation of primary sequence changes present in the α-and β-tubulins of Antarctic fishes
    • Detrich, H. W., S. K. Parker, R. C. Williams, E. Nogales, and K. H. Downing. 2000. Cold adaptation of microtubule assembly and dynamics: structural interpretation of primary sequence changes present in the α-and β-tubulins of Antarctic fishes. J. Biol. Chem. 278: 37038-37047.
    • (2000) J. Biol. Chem. , vol.278 , pp. 37038-37047
    • Detrich, H.W.1    Parker, S.K.2    Williams, R.C.3    Nogales, E.4    Downing, K.H.5
  • 10
    • 0014078618 scopus 로고
    • Protein synthesis in sea urchin eggs: A "late" response to fertilization
    • Epel, D. 1967. Protein synthesis in sea urchin eggs: A "late" response to fertilization. Proc. Natl. Acad. Sci. 57: 899-906.
    • (1967) Proc. Natl. Acad. Sci. , vol.57 , pp. 899-906
    • Epel, D.1
  • 11
    • 0014966082 scopus 로고
    • Regulation of protein synthesis in mammalian cells. II. Inhibition of protein synthesis at the level of initiation during mitosis
    • Fan, H., and S. Penman. 1970. Regulation of protein synthesis in mammalian cells. II. Inhibition of protein synthesis at the level of initiation during mitosis. J. Mol. Biol. 50: 655-670.
    • (1970) J. Mol. Biol. , vol.50 , pp. 655-670
    • Fan, H.1    Penman, S.2
  • 12
    • 0030681366 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Molecular basis of cold adaptation
    • DOI 10.1007/s000180050103
    • Feller, G., and C. Gerday. 1997 . Psychrophilic enzymes: molecular basis of cold adaptation. Cell. Mol. Life Sci. 53: 830-841. (Pubitemid 27507534)
    • (1997) Cellular and Molecular Life Sciences , vol.53 , Issue.10 , pp. 830-841
    • Feller, G.1    Gerday, C.2
  • 13
    • 0034825983 scopus 로고    scopus 로고
    • Intrinsic versus extrinsic stabilization of enzymes: The interaction of solutes and temperature on A4-lactate dehydrogenase orthologs from warm-adapted and cold-adapted marine fishes
    • Fields, P. A., B. D. Wahlstrand, and G. Somero. 2001. Intrinsic versus extrinsic stabilization of enzymes: the interaction of solutes and temperature on A4-lactate dehydrogenase orthologs from warm-adapted and cold-adapted marine fishes. FEBS J. 268: 4497-4505.
    • (2001) FEBS J , vol.268 , pp. 4497-4505
    • Fields, P.A.1    Wahlstrand, B.D.2    Somero, G.3
  • 14
    • 33846829568 scopus 로고    scopus 로고
    • Protein metabolism in marine animals: The underlying mechanism of growth
    • Fraser, K. P. P., and A. D. Rogers. 2007. Protein metabolism in marine animals: the underlying mechanism of growth. Adv. Mar. Biol. 52: 267-362.
    • (2007) Adv. Mar. Biol. , vol.52 , pp. 267-362
    • Fraser, K.P.P.1    Rogers, A.D.2
  • 15
    • 0036795637 scopus 로고    scopus 로고
    • Low-temperature protein metabolism: Seasonal changes in protein synthesis and RNA dynamics in the Antarctic limpet Nacella concinna Strebel 1908
    • Fraser, K. P. P., A. Clarke, and L. S. Peck. 2002. Low-temperature protein metabolism: seasonal changes in protein synthesis and RNA dynamics in the Antarctic limpet Nacella concinna Strebel 1908. J. Exp. Biol. 205: 3077-3086.
    • (2002) J. Exp. Biol. , vol.205 , pp. 3077-3086
    • Fraser, K.P.P.1    Clarke, A.2    Peck, L.S.3
  • 16
    • 13444263703 scopus 로고    scopus 로고
    • Protein synthesis, RNA concentrations, nitrogen excretion, and metabolism vary seasonally in the Antarctic holothurian Heterocucumis steineni (Ludwig 1898)
    • Fraser, K. P. P., L. S. Peck, and A. Clarke. 2004. Protein synthesis, RNA concentrations, nitrogen excretion, and metabolism vary seasonally in the Antarctic holothurian Heterocucumis steineni (Ludwig 1898). Physiol. Biochem. Zool. 77: 556-569.
    • (2004) Physiol. Biochem. Zool. , vol.77 , pp. 556-569
    • Fraser, K.P.P.1    Peck, L.S.2    Clarke, A.3
  • 18
    • 49849112529 scopus 로고
    • Patterns and rates of protein synthesis in sea urchin embryos
    • Fry, B. J., and P. R. Gross. 1970. Patterns and rates of protein synthesis in sea urchin embryos. Dev. Biol. 21: 125-146.
    • (1970) Dev. Biol. , vol.21 , pp. 125-146
    • Fry, B.J.1    Gross, P.R.2
  • 20
    • 0019491506 scopus 로고
    • Protein synthesis, polyribosomes, and peptide elongation in early development of Strongylocentrotus purpuratus
    • Goustin, A. S., and F. H. Wilt. 1981. Protein synthesis, polyribosomes, and peptide elongation in early development of Strongylocentrotus purpuratus. Dev. Biol. 82: 32-40.
    • (1981) Dev. Biol. , vol.82 , pp. 32-40
    • Goustin, A.S.1    Wilt, F.H.2
  • 21
    • 0020493434 scopus 로고
    • Direct measurement of histone peptide elongation rate in cleaving sea urchin embryos
    • Goustin, A. S., and F. H. Wilt. 1982. Direct measurement of histone peptide elongation rate in cleaving sea urchin embryos. Biochim. Biophys. Acta 699: 22-27.
    • (1982) Biochim. Biophys. Acta , vol.699 , pp. 22-27
    • Goustin, A.S.1    Wilt, F.H.2
  • 22
    • 0032053157 scopus 로고    scopus 로고
    • Quiescence in Artemia franciscana embryos: Reversible arrest of metabolism and gene expression at low oxygen levels
    • Hand, S. C. 1996. Quiescence in Artemia franciscana embryos: reversible arrest of metabolism and gene expression at low oxygen levels. J. Exp. Biol. 201: 1233-1242.
    • (1996) J. Exp. Biol. , vol.201 , pp. 1233-1242
    • Hand, S.C.1
  • 23
    • 0001660493 scopus 로고
    • The relevance of whole-body protein metabolism to measured costs of maintenance and growth in Mytilus edulis
    • Hawkins, A. J. S., J. Widdows, and B. L. Bayne. 1989. The relevance of whole-body protein metabolism to measured costs of maintenance and growth in Mytilus edulis. Physiol. Zool. 62: 745-763.
    • (1989) Physiol. Zool. , vol.62 , pp. 745-763
    • Hawkins, A.J.S.1    Widdows, J.2    Bayne, B.L.3
  • 24
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey, J. W. B. 1991. Translational control in mammalian cells. Annu. Rev. Biochem. 60: 717-755.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.B.1
  • 25
    • 0018377032 scopus 로고
    • Efficiency of protein synthesis after fertilisation of sea urchin eggs
    • Hille, M. B., and A. A. Albers. 1979. Efficiency of protein synthesis after fertilisation of sea urchin eggs. Nature 278: 469-471.
    • (1979) Nature , vol.278 , pp. 469-471
    • Hille, M.B.1    Albers, A.A.2
  • 27
    • 0028100848 scopus 로고
    • Global arrest of translation during invertebrate quiescence
    • Hofmann, G. E., and S. C. Hand. 1992. Global arrest of translation during invertebrate quiescence. Proc. Natl. Acad. Sci. 91: 8492-8496.
    • (1992) Proc. Natl. Acad. Sci. , vol.91 , pp. 8492-8496
    • Hofmann, G.E.1    Hand, S.C.2
  • 28
    • 0002470291 scopus 로고
    • Protein turnover in ectotherms and its relationship to energetics
    • R. Gilles, ed. Springer-Verlag, New York.
    • Houlihan, D. F. 1991. Protein turnover in ectotherms and its relationship to energetics. Pp. 1-43 in Advances in Comparative and Environmental Physiology, R. Gilles, ed. Springer-Verlag, New York.
    • (1991) Advances in Comparative and Environmental Physiology , pp. 1-43
    • Houlihan, D.F.1
  • 29
    • 0015134638 scopus 로고
    • Efficiency of translation of messenger RNA before and after fertilization of sea urchin eggs
    • Humphreys, T. 1969. Efficiency of translation of messenger RNA before and after fertilization of sea urchin eggs. Dev. Biol. 26: 201-208.
    • (1969) Dev. Biol. , vol.26 , pp. 201-208
    • Humphreys, T.1
  • 30
    • 0015134638 scopus 로고
    • Measurements of messenger RNA entering polysomes upon fertilization of sea urchin eggs
    • Humphreys, T. 1971. Measurements of messenger RNA entering polysomes upon fertilization of sea urchin eggs. Dev. Biol. 26: 201-208.
    • (1971) Dev. Biol. , vol.26 , pp. 201-208
    • Humphreys, T.1
  • 31
    • 0141458030 scopus 로고    scopus 로고
    • Annual warming episodes in seawater temperatures in McMurdo Sound in relationship to endogenous ice in notothenioid fish
    • Hunt, B. M., K. Hoefling, and C. H. C. Cheng. 2003. Annual warming episodes in seawater temperatures in McMurdo Sound in relationship to endogenous ice in notothenioid fish. Antarct Sci. 15: 333-338.
    • (2003) Antarct Sci , vol.15 , pp. 333-338
    • Hunt, B.M.1    Hoefling, K.2    Cheng, C.H.C.3
  • 32
    • 0014116954 scopus 로고
    • Accumulation of newly synthesized RNA templates in a unique class of polyribosomes during em- bryogenesis
    • Infante, A. A., and M. Nemer. 1967. Accumulation of newly synthesized RNA templates in a unique class of polyribosomes during em- bryogenesis. Proc. Natl. Acad. Sci. 58: 681-688.
    • (1967) Proc. Natl. Acad. Sci. , vol.58 , pp. 681-688
    • Infante, A.A.1    Nemer, M.2
  • 33
    • 0017806336 scopus 로고
    • A test for masked message: The template activity of messenger ribonucleoportein particles isolated from sea urchin eggs
    • Jenkins, N. A., J. F. Kaumeyer, E. M. Young, and R. A. Raff. 1978. A test for masked message: the template activity of messenger ribonucleoportein particles isolated from sea urchin eggs. Dev. Biol. 63: 179-198.
    • (1978) Dev. Biol. , vol.63 , pp. 179-198
    • Jenkins, N.A.1    Kaumeyer, J.F.2    Young, E.M.3    Raff, R.A.4
  • 34
    • 1542376774 scopus 로고    scopus 로고
    • 4-lactate dehydrogenases of Pacific damselfishes (Chromis spp.)
    • Johns, G. C., and G. N. Somero. 2004. Evolutionary convergence in adaptation of proteins to temperature: A4-lactate dehydrogenases of Pacific damselfishes (Chromis spp.). Mol. Biol. Ecol. 21: 314-320.
    • (2004) Mol. Biol. Ecol. , vol.21 , pp. 314-320
    • Johns, G.C.1    Somero, G.N.2
  • 35
    • 0036934460 scopus 로고    scopus 로고
    • Metabolic cold adaptation in Antarctic fishes: Evidence from enzymatic activities of brain
    • Kawall, H. G., J. J. Torres, B. D. Sidell, and G. N. Somero. 2002. Metabolic cold adaptation in Antarctic fishes: evidence from enzymatic activities of brain. Mar. Biol. 140: 279-286.
    • (2002) Mar. Biol. , vol.140 , pp. 279-286
    • Kawall, H.G.1    Torres, J.J.2    Sidell, B.D.3    Somero, G.N.4
  • 36
    • 0036010758 scopus 로고    scopus 로고
    • Reversible suppression of protein synthesis in concert with polysome disaggregation during anoxia exposure in Littorina littorea
    • Larade, K., and K. B. Storey. 2002. Reversible suppression of protein synthesis in concert with polysome disaggregation during anoxia exposure in Littorina littorea. Mol. Cell. Biochem. 232: 121-127.
    • (2002) Mol. Cell. Biochem. , vol.232 , pp. 121-127
    • Larade, K.1    Storey, K.B.2
  • 37
    • 0002435281 scopus 로고
    • Oceanographic investigations in McMurdo Sound, Antarctica
    • Littlepage, J. L. 1965. Oceanographic investigations in McMurdo Sound, Antarctica. Antarct. Res. Ser. 5: 1-37.
    • (1965) Antarct. Res. Ser. , vol.5 , pp. 1-37
    • Littlepage, J.L.1
  • 38
    • 0035831272 scopus 로고    scopus 로고
    • High macromolecular synthesis with low metabolic cost in Antarctic sea urchin embryos
    • Marsh, A. G., R. E. Maxson, and D. T. Manahan. 2001. High macromolecular synthesis with low metabolic cost in Antarctic sea urchin embryos. Science 291: 1950-1952.
    • (2001) Science , vol.291 , pp. 1950-1952
    • Marsh, A.G.1    Maxson, R.E.2    Manahan, D.T.3
  • 39
    • 0020957479 scopus 로고
    • Polysome structure in sea urchin eggs and embryos: An electron microscopic analysis
    • Martin, K. A. and O. L. Miller. 1983. Polysome structure in sea urchin eggs and embryos: An electron microscopic analysis. Dev. Biol. 98: 338-348.
    • (1983) Dev. Biol. , vol.98 , pp. 338-348
    • Martin, K.A.1    Miller, O.L.2
  • 40
    • 31544442446 scopus 로고    scopus 로고
    • Fixed metabolic costs for highly variable rates of protein synthesis in sea urchin embryos and larvae
    • Pace, D. A., and D. T. Manahan. 2006. Fixed metabolic costs for highly variable rates of protein synthesis in sea urchin embryos and larvae. J. Exp. Biol. 209: 158-170.
    • (2006) J. Exp. Biol. , vol.209 , pp. 158-170
    • Pace, D.A.1    Manahan, D.T.2
  • 41
    • 35748954381 scopus 로고    scopus 로고
    • Efficiencies and costs of larval growth in different food environments (Asteroidea: Asterina miniata)
    • Pace, D. A., and D. T. Manahan. 2007a. Efficiencies and costs of larval growth in different food environments (Asteroidea: Asterina miniata). J. Exp. Mar. Biol. Ecol. 353: 89-106.
    • (2007) J. Exp. Mar. Biol. Ecol. , vol.353 , pp. 89-106
    • Pace, D.A.1    Manahan, D.T.2
  • 42
    • 34247552851 scopus 로고    scopus 로고
    • Cost of protein synthesis and energy allocation during development of Antarctic sea urchin embryos and larvae
    • Pace, D. A., and D. T. Manahan. 2007b. Cost of protein synthesis and energy allocation during development of Antarctic sea urchin embryos and larvae. Biol. Bull. 212: 115-129.
    • (2007) Biol. Bull. , vol.212 , pp. 115-129
    • Pace, D.A.1    Manahan, D.T.2
  • 43
    • 0034495927 scopus 로고    scopus 로고
    • Depression of protein synthesis during diapause in embryos of the annual killifish, Astrofundulus limnaeus
    • Podrabsky, J. E., and S. C. Hand. 2000. Depression of protein synthesis during diapause in embryos of the annual killifish, Astrofundulus limnaeus. Physiol. Biochem. Zool. 73: 799-800.
    • (2000) Physiol. Biochem. Zool. , vol.73 , pp. 799-800
    • Podrabsky, J.E.1    Hand, S.C.2
  • 44
    • 39149124482 scopus 로고    scopus 로고
    • Thermal limits and adaptation in marine Antarctic ectotherms: An integrative view
    • Portner, H. O., L. Peck, and G. Somero. 2007. Thermal limits and adaptation in marine Antarctic ectotherms: An integrative view. Philos. Trans. R. Soc. B: Biol. Sci. 362: 2233-2258.
    • (2007) Philos. Trans. R. Soc. B Biol. Sci. , vol.362 , pp. 2233-2258
    • Portner, H.O.1    Peck, L.2    Somero, G.3
  • 45
    • 0029067095 scopus 로고
    • Protein synthesis increases after fertilization of sea urchin eggs in the absence of an increase in intracellular pH
    • Rees, B. B., C. Patton, J. L. Grainger, and D. Epel. 1995. Protein synthesis increases after fertilization of sea urchin eggs in the absence of an increase in intracellular pH. Dev. Biol. 169: 683-698.
    • (1995) Dev. Biol. , vol.169 , pp. 683-698
    • Rees, B.B.1    Patton, C.2    Grainger, J.L.3    Epel, D.4
  • 46
    • 0017713093 scopus 로고
    • Absolute rates of protein synthesis in sea urchins with specific activity measurements of radioactive leucine and leucyl-tRNA
    • Regier, J. C., and F. C. Kafatos. 1977. Absolute rates of protein synthesis in sea urchins with specific activity measurements of radioactive leucine and leucyl-tRNA. Dev. Biol. 57: 270-283.
    • (1977) Dev. Biol. , vol.57 , pp. 270-283
    • Regier, J.C.1    Kafatos, F.C.2
  • 47
    • 0014448525 scopus 로고
    • Polyribosome formation and RNA synthesis in the early post-fertilization stages of the sea urchin egg
    • Rinaldi, A. M., and A. Monroe. 1969. Polyribosome formation and RNA synthesis in the early post-fertilization stages of the sea urchin egg. Dev. Biol. 19: 73-86.
    • (1969) Dev. Biol. , vol.19 , pp. 73-86
    • Rinaldi, A.M.1    Monroe, A.2
  • 48
    • 0034803288 scopus 로고    scopus 로고
    • The effects of temperature on metabolic rate and protein synthesis following a meal in the isopod Glyptonotus antarcticus Eights (1852)
    • Robertson, R. F., A. J. El-Haj, A. Clarke, and E. W. Taylor. 2001. The effects of temperature on metabolic rate and protein synthesis following a meal in the isopod Glyptonotus antarcticus Eights (1852) Polar Biol. 24: 677-686.
    • (2001) Polar Biol , vol.24 , pp. 677-686
    • Robertson, R.F.1    El-Haj, A.J.2    Clarke, A.3    Taylor, E.W.4
  • 49
    • 0028327825 scopus 로고
    • Energy metabolism and amino acid transport during early development of Antarctic and temperate echinoderms
    • Shilling F. M., and D. T. Manahan. 1994. Energy metabolism and amino acid transport during early development of Antarctic and temperate echinoderms. Biol. Bull. 187: 398-407.
    • (1994) Biol. Bull. , vol.187 , pp. 398-407
    • Shilling, F.M.1    Manahan, D.T.2
  • 50
    • 0001598579 scopus 로고
    • Protein metabolism and cold adaptation in Antarctic fishes
    • Smith, M. A., and A. E. Haschemeyer. 1980. Protein metabolism and cold adaptation in Antarctic fishes. Physiol. Zool. 53: 373-382.
    • (1980) Physiol. Zool. , vol.53 , pp. 373-382
    • Smith, M.A.1    Haschemeyer, A.E.2
  • 51
    • 0038745612 scopus 로고    scopus 로고
    • The protein synthesis machinery operates at the same expense in eurythermal and cold stenothermal pectinids
    • Storch, D., and H. O. Pörtner. 2003. The protein synthesis machinery operates at the same expense in eurythermal and cold stenothermal pectinids. Physiol. Biochem. Zool. 76: 28 -40.
    • (2003) Physiol. Biochem. Zool. , vol.76 , pp. 28-40
    • Storch, D.1    Pörtner, H.O.2
  • 52
    • 0033982036 scopus 로고    scopus 로고
    • Effect of temperature on the stability and activity of elongation factor 2 proteins from Antarctic and thermophilic methanogens
    • Thomas, T., and R. Cavicchioli. 2000. Effect of temperature on the stability and activity of elongation factor 2 proteins from Antarctic and thermophilic methanogens. J. Bacteriol. 182: 1328-1332.
    • (2000) J. Bacteriol. , vol.182 , pp. 1328-1332
    • Thomas, T.1    Cavicchioli, R.2
  • 53
    • 0035108129 scopus 로고    scopus 로고
    • Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens
    • Thomas, T., N. Kumar, and R. Cavicchioli. 2001. Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens. J Bac- teriol. 183: 1974-1982.
    • (2001) J Bac- Teriol , vol.183 , pp. 1974-1982
    • Thomas, T.1    Kumar, N.2    Cavicchioli, R.3
  • 55
    • 0019161074 scopus 로고
    • Dual ionic controls for the activation of protein synthesis at fertilization
    • Winkler, M. M., R. A. Steinhardt, J. L. Grainger, and L. Minning. 1980. Dual ionic controls for the activation of protein synthesis at fertilization. Nature 287: 558 -560.
    • (1980) Nature , vol.287 , pp. 558-560
    • Winkler, M.M.1    Steinhardt, R.A.2    Grainger, J.L.3    Minning, L.4


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