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Volumn 1, Issue , 2003, Pages

Oolemmal proteomics - Identification of highly abundant heat shock proteins and molecular chaperones in the mature mouse egg and their localization on the plasma membrane

Author keywords

[No Author keywords available]

Indexed keywords

ANAZOLENE SODIUM; AVIDIN; CALNEXIN; CALRETICULIN; CHAPERONE; EGG PROTEIN; GLUCOSE REGULATED PROTEIN 78; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MEMBRANE PROTEIN; PROTEIN ANTIBODY; PROTEIN DISULFIDE ISOMERASE; GLUCOSE REGULATED PROTEINS; GLUCOSE-REGULATED PROTEINS; MOLECULAR CHAPERONE GRP78;

EID: 0346445420     PISSN: 14777827     EISSN: None     Source Type: Journal    
DOI: 10.1187/1477-7827-1-27     Document Type: Article
Times cited : (91)

References (55)
  • 3
    • 0036197618 scopus 로고    scopus 로고
    • Analysis of the roles of RGD-binding integrins, alpha(4)/alpha(9) integrins, alpha(6) integrins, and CD9 in the interaction of the fertilin beta (ADAM2) disintegrin domain with the mouse egg membrane
    • Zhu X, Evans JP: Analysis of the roles of RGD-binding integrins, alpha(4)/alpha(9) integrins, alpha(6) integrins, and CD9 in the interaction of the fertilin beta (ADAM2) disintegrin domain with the mouse egg membrane. Biol Reprod 2002, 66:1193-202.
    • (2002) Biol. Reprod. , vol.66 , pp. 1193-1202
    • Zhu, X.1    Evans, J.P.2
  • 4
    • 0031193325 scopus 로고    scopus 로고
    • Characterization of the binding of recombinant mouse sperm fertilin beta subunit to mouse eggs: Evidence for adhesive activity via an egg beta1 integrin-mediated interaction
    • Evans JP, Kopf GS, Schultz RM: Characterization of the binding of recombinant mouse sperm fertilin beta subunit to mouse eggs: evidence for adhesive activity via an egg beta1 integrin-mediated interaction. Dev Biol 1997, 187:79-93.
    • (1997) Dev. Biol. , vol.187 , pp. 79-93
    • Evans, J.P.1    Kopf, G.S.2    Schultz, R.M.3
  • 5
    • 0034640885 scopus 로고    scopus 로고
    • Normal fertilization occurs with eggs lacking the integrin alpha6beta1 and is CD9-dependent
    • Miller BJ, Georges-Labouesse E, Primakoff P, Myles DG: Normal fertilization occurs with eggs lacking the integrin alpha6beta1 and is CD9-dependent. J Cell Biol 2000, 149:1289-96.
    • (2000) J. Cell Biol. , vol.149 , pp. 1289-1296
    • Miller, B.J.1    Georges-Labouesse, E.2    Primakoff, P.3    Myles, D.G.4
  • 6
    • 0037150651 scopus 로고    scopus 로고
    • Penetration, adhesion, and fusion in mammalian sperm-egg interaction
    • Primakoff P, Myles DG: Penetration, adhesion, and fusion in mammalian sperm-egg interaction. Science 2002, 296:2183-5.
    • (2002) Science , vol.296 , pp. 2183-2185
    • Primakoff, P.1    Myles, D.G.2
  • 8
    • 0033559614 scopus 로고    scopus 로고
    • Treatment of mouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) protein clusters from the egg surface and inhibits sperm-oolemma binding and fusion
    • Coonrod SA, Naaby-Hansen S, Shetty J, Shibahara H, Chen M, White JM, Herr JC: Treatment of mouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) protein clusters from the egg surface and inhibits sperm-oolemma binding and fusion. Dev Biol 1999, 207:334-49.
    • (1999) Dev. Biol. , vol.207 , pp. 334-349
    • Coonrod, S.A.1    Naaby-Hansen, S.2    Shetty, J.3    Shibahara, H.4    Chen, M.5    White, J.M.6    Herr, J.C.7
  • 10
    • 0030132728 scopus 로고    scopus 로고
    • P-selectin is expressed on the oolemma of human and hamster oocytes following sperm adhesion and is also detected on the equatorial region of acrosome-reacted human spermatozoa
    • Fusi FM, Montesano M, Bernocchi N, Panzeri C, Ferrara F, Villa A, Bronson RA: P-selectin is expressed on the oolemma of human and hamster oocytes following sperm adhesion and is also detected on the equatorial region of acrosome-reacted human spermatozoa. Mol Hum Reprod 1996, 2:341-7.
    • (1996) Mol. Hum. Reprod. , vol.2 , pp. 341-347
    • Fusi, F.M.1    Montesano, M.2    Bernocchi, N.3    Panzeri, C.4    Ferrara, F.5    Villa, A.6    Bronson, R.A.7
  • 11
    • 0022978442 scopus 로고
    • Immunofluorescent localization of immunoglobulins on the cell surface of mouse oocytes and preimplantation embryos
    • Wiley LM, Obasaju MF: Immunofluorescent localization of immunoglobulins on the cell surface of mouse oocytes and preimplantation embryos. J In Vitro Fert Embryo Transf 1986, 3:319-25.
    • (1986) J. In. Vitro. Fert. Embryo. Transf. , vol.3 , pp. 319-325
    • Wiley, L.M.1    Obasaju, M.F.2
  • 12
    • 0025780480 scopus 로고
    • Complement component C1q and its receptor are involved in the interaction of human sperm with zona-free hamster eggs
    • Fusi F, Bronson RA, Hong Y, Ghebrehiwet B: Complement component C1q and its receptor are involved in the interaction of human sperm with zona-free hamster eggs. Mol Reprod Dev 1991, 29:180-8.
    • (1991) Mol. Reprod. Dev. , vol.29 , pp. 180-188
    • Fusi, F.1    Bronson, R.A.2    Hong, Y.3    Ghebrehiwet, B.4
  • 13
    • 0027444742 scopus 로고
    • The role of complement component C3b and its receptors in sperm-oocyte interaction
    • Anderson DJ, Abbott AF, Jack RM: The role of complement component C3b and its receptors in sperm-oocyte interaction. Proc Natl Acad Sci U S A 1993, 90:10051-5.
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 10051-10055
    • Anderson, D.J.1    Abbott, A.F.2    Jack, R.M.3
  • 14
    • 0026553566 scopus 로고
    • Monoclonal antibodies identify Fc gamma receptors on unfertilized human oocytes but not spermatozoa
    • Bronson RA, Fusi FM, Fleit HB: Monoclonal antibodies identify Fc gamma receptors on unfertilized human oocytes but not spermatozoa. J Reprod Immunol 1992, 21:293-307.
    • (1992) J. Reprod. Immunol. , vol.21 , pp. 293-307
    • Bronson, R.A.1    Fusi, F.M.2    Fleit, H.B.3
  • 15
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S: The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 1993, 27:437-96.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 16
    • 0031055601 scopus 로고    scopus 로고
    • Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" Molecular chaperones
    • Wiest DL, Bhandoola A, Punt J, Kreibich G, McKean D, Singer A: Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones. Proc Natl Acad Sci U S A 1997, 94:1884-9.
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 1884-1889
    • Wiest, D.L.1    Bhandoola, A.2    Punt, J.3    Kreibich, G.4    McKean, D.5    Singer, A.6
  • 17
    • 0029072799 scopus 로고
    • The molecular chaperone calnexin is expressed on the surface of immature thymocytes in association with clonotype-independent CD3 complexes
    • Wiest DL, Burgess WH, McKean D, Kearse KP, Singer A: The molecular chaperone calnexin is expressed on the surface of immature thymocytes in association with clonotype-independent CD3 complexes. Embo J 1995, 14:3425-33.
    • (1995) Embo J. , vol.14 , pp. 3425-3433
    • Wiest, D.L.1    Burgess, W.H.2    McKean, D.3    Kearse, K.P.4    Singer, A.5
  • 18
    • 0345035504 scopus 로고    scopus 로고
    • Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved
    • Robert J, Menoret A, Cohen N: Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved. J Immunol 1999, 163:4133-9.
    • (1999) J. Immunol. , vol.163 , pp. 4133-4139
    • Robert, J.1    Menoret, A.2    Cohen, N.3
  • 19
    • 0030611753 scopus 로고    scopus 로고
    • The Ig alpha/Igbeta heterodimer on mu-negative proB cells is competent for transducing signals to induce early B cell differentiation
    • Nagata K, Nakamura T, Kitamura F, Kuramochi S, Taki S, Campbell KS, Karasuyama H: The Ig alpha/Igbeta heterodimer on mu-negative proB cells is competent for transducing signals to induce early B cell differentiation. Immunity 1997, 7:559-70.
    • (1997) Immunity , vol.7 , pp. 559-570
    • Nagata, K.1    Nakamura, T.2    Kitamura, F.3    Kuramochi, S.4    Taki, S.5    Campbell, K.S.6    Karasuyama, H.7
  • 20
    • 0034680917 scopus 로고    scopus 로고
    • Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum
    • Okazaki Y, Ohno H, Takase K, Ochiai T, Saito T: Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum. J Biol Chem 2000, 275:35751-8.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35751-35758
    • Okazaki, Y.1    Ohno, H.2    Takase, K.3    Ochiai, T.4    Saito, T.5
  • 22
    • 0028953056 scopus 로고
    • A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells
    • Multhoff G, Botzler C, Wiesnet M, Muller E, Meier T, Wilmanns W, Issels RD: A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. Int J Cancer 1995, 61:272-9.
    • (1995) Int. J. Cancer , vol.61 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Muller, E.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7
  • 23
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini M, Heltai S, Zocchi MR, Rugarli C: Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 1992, 51:613-9.
    • (1992) Int. J. Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 24
    • 0031869555 scopus 로고    scopus 로고
    • Differential Hsp70 plasma-membrane expression on primary human tumors and metastases in mice with severe combined immunodeficiency
    • Botzler C, Schmidt J, Luz A, Jennen L, Issels R, Multhoff G: Differential Hsp70 plasma-membrane expression on primary human tumors and metastases in mice with severe combined immunodeficiency. Int J Cancer 1998, 77:942-8.
    • (1998) Int. J. Cancer , vol.77 , pp. 942-948
    • Botzler, C.1    Schmidt, J.2    Luz, A.3    Jennen, L.4    Issels, R.5    Multhoff, G.6
  • 25
    • 0034680794 scopus 로고    scopus 로고
    • Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea S, Orr AW, Pallero MA, Eggleton P, Murphy-Ullrich JE: Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J Biol Chem 2000, 275:36358-68.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36358-36368
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy-Ullrich, J.E.5
  • 26
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White TK, Zhu Q, Tanzer ML: Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading. J Biol Chem 1995, 270:15926-9.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15926-15929
    • White, T.K.1    Zhu, Q.2    Tanzer, M.L.3
  • 27
    • 0029144477 scopus 로고
    • Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex DW, Chen K, Swiatkowska M: Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 1995, 86:2168-73.
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1    Chen, K.2    Swiatkowska, M.3
  • 29
  • 30
    • 0026689538 scopus 로고
    • Heavy chain binding protein (BiP/GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase
    • Takemoto H, Yoshimori T, Yamamoto A, Miyata Y, Yahara I, Inoue K, Tashiro Y: Heavy chain binding protein (BiP/GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase. Arch Biochem Biophys 1992, 296:129-36.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 129-136
    • Takemoto, H.1    Yoshimori, T.2    Yamamoto, A.3    Miyata, Y.4    Yahara, I.5    Inoue, K.6    Tashiro, Y.7
  • 31
    • 0034900520 scopus 로고    scopus 로고
    • Major histocompatibility class one molecule associates with glucose regulated protein (GRP) 78 on the cell surface
    • Triantafilou M, Fradelizi D, Triantafilou K: Major histocompatibility class one molecule associates with glucose regulated protein (GRP) 78 on the cell surface. Hum Immunol 2001, 62:764-70.
    • (2001) Hum. Immunol. , vol.62 , pp. 764-770
    • Triantafilou, M.1    Fradelizi, D.2    Triantafilou, K.3
  • 32
    • 0021526790 scopus 로고
    • Xenopus hsp 70 genes are constitutively expressed in injected oocytes
    • Bienz M: Xenopus hsp 70 genes are constitutively expressed in injected oocytes. Embo J 1984, 3:2477-83.
    • (1984) Embo J. , vol.3 , pp. 2477-2483
    • Bienz, M.1
  • 33
    • 0020156128 scopus 로고
    • The heat-shock response in Xenopus oocytes is controlled at the translational level
    • Bienz M, Gurdon JB: The heat-shock response in Xenopus oocytes is controlled at the translational level. Cell 1982, 29:811-9.
    • (1982) Cell , vol.29 , pp. 811-819
    • Bienz, M.1    Gurdon, J.B.2
  • 34
    • 0027438122 scopus 로고
    • Constitutive expression of a somatic heat-inducible hsp70 gene during amphibian oogenesis
    • Billoud B, Rodriguez-Martin ML, Berard L, Moreau N, Angelier N: Constitutive expression of a somatic heat-inducible hsp70 gene during amphibian oogenesis. Development 1993, 119:921-32.
    • (1993) Development , vol.119 , pp. 921-932
    • Billoud, B.1    Rodriguez-Martin, M.L.2    Berard, L.3    Moreau, N.4    Angelier, N.5
  • 35
    • 0035260778 scopus 로고    scopus 로고
    • Expression and localisation of heat shock protein 70 in cultured bovine oocytes and embryos
    • Kawarsky SJ, King WA: Expression and localisation of heat shock protein 70 in cultured bovine oocytes and embryos. Zygote 2001, 9:39-50.
    • (2001) Zygote , vol.9 , pp. 39-50
    • Kawarsky, S.J.1    King, W.A.2
  • 36
    • 0028923673 scopus 로고
    • Evidence for a 90 kDa heat-shock protein gene expression in the amphibian oocyte
    • Coumailleau P, Billoud B, Sourrouille P, Moreau N, Angelier N: Evidence for a 90 kDa heat-shock protein gene expression in the amphibian oocyte. Dev Biol 1995, 168:247-58.
    • (1995) Dev. Biol. , vol.168 , pp. 247-258
    • Coumailleau, P.1    Billoud, B.2    Sourrouille, P.3    Moreau, N.4    Angelier, N.5
  • 37
    • 0023414744 scopus 로고
    • Lack of heat-shock response in preovulatory mouse oocytes
    • Curci A, Bevilacqua A, Mangia F: Lack of heat-shock response in preovulatory mouse oocytes. Dev Biol 1987, 123:154-60.
    • (1987) Dev. Biol. , vol.123 , pp. 154-160
    • Curci, A.1    Bevilacqua, A.2    Mangia, F.3
  • 38
    • 0025796846 scopus 로고
    • Regulation of hsp70 mRNA levels during oocyte maturation and zygotic gene activation in the mouse
    • Manejwala FM, Logan CY, Schultz RM: Regulation of hsp70 mRNA levels during oocyte maturation and zygotic gene activation in the mouse. Dev Biol 1991, 144:301-8.
    • (1991) Dev. Biol. , vol.144 , pp. 301-308
    • Manejwala, F.M.1    Logan, C.Y.2    Schultz, R.M.3
  • 39
    • 0020616421 scopus 로고
    • Heat shock proteins, first major products of zygotic gene activity in mouse embryo
    • Bensaude O, Babinet C, Morange M, Jacob F: Heat shock proteins, first major products of zygotic gene activity in mouse embryo. Nature 1983, 305:331-3.
    • (1983) Nature , vol.305 , pp. 331-333
    • Bensaude, O.1    Babinet, C.2    Morange, M.3    Jacob, F.4
  • 40
    • 0028796917 scopus 로고
    • Expression of the HSP 70.1 gene, a landmark of early zygotic activity in the mouse embryo, is restricted to the first burst of transcription
    • Christians E, Campion E, Thompson EM, Renard JP: Expression of the HSP 70.1 gene, a landmark of early zygotic activity in the mouse embryo, is restricted to the first burst of transcription. Development 1995, 121:113-22.
    • (1995) Development , vol.121 , pp. 113-122
    • Christians, E.1    Campion, E.2    Thompson, E.M.3    Renard, J.P.4
  • 41
    • 0034848309 scopus 로고    scopus 로고
    • The effects of antibodies to heat shock protein 70 in fertilization and embryo development
    • Matwee C, Kamaruddin M, Betts DH, Basrur PK, King WA: The effects of antibodies to heat shock protein 70 in fertilization and embryo development. Mol Hum Reprod 2001, 7:829-37.
    • (2001) Mol. Hum. Reprod. , vol.7 , pp. 829-837
    • Matwee, C.1    Kamaruddin, M.2    Betts, D.H.3    Basrur, P.K.4    King, W.A.5
  • 42
    • 0027416845 scopus 로고
    • Sea urchin egg receptor for sperm: Sequence similarity of binding domain and hsp70
    • Foltz KR, Partin JS, Lennarz WJ: Sea urchin egg receptor for sperm: sequence similarity of binding domain and hsp70. Science 1993, 259:1421-5.
    • (1993) Science , vol.259 , pp. 1421-1425
    • Foltz, K.R.1    Partin, J.S.2    Lennarz, W.J.3
  • 43
    • 0028269937 scopus 로고
    • Presence of inositol 1,4,5-trisphosphate receptor, calreticulin, and calsequestrin in eggs of sea urchins and Xenopus laevis
    • Parys JB, McPherson SM, Mathews L, Campbell KP, Longo FJ: Presence of inositol 1,4,5-trisphosphate receptor, calreticulin, and calsequestrin in eggs of sea urchins and Xenopus laevis. Dev Biol 1994, 161:466-76.
    • (1994) Dev. Biol. , vol.161 , pp. 466-476
    • Parys, J.B.1    McPherson, S.M.2    Mathews, L.3    Campbell, K.P.4    Longo, F.J.5
  • 45
    • 0028141914 scopus 로고
    • ERcalcistorin/protein disulfide isomerase (PDI). Sequence determination and expression of a cDNA clone encoding a calcium storage protein with PDI activity from endoplasmic reticulum of the sea urchin egg
    • Lucero HA, Lebeche D, Kaminer B: ERcalcistorin/protein disulfide isomerase (PDI). Sequence determination and expression of a cDNA clone encoding a calcium storage protein with PDI activity from endoplasmic reticulum of the sea urchin egg. J Biol Chem 1994, 269:23112-9.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23112-23119
    • Lucero, H.A.1    Lebeche, D.2    Kaminer, B.3
  • 48
    • 0024185105 scopus 로고
    • 'Catalysts' for polyacrylamide gel polymerization and detection of proteins by silver staining
    • Hochstrasser DF, Merril CR: 'Catalysts' for polyacrylamide gel polymerization and detection of proteins by silver staining. Appl Theor Electrophor 1988, 1:35-40.
    • (1988) Appl. Theor. Electrophor. , vol.1 , pp. 35-40
    • Hochstrasser, D.F.1    Merril, C.R.2
  • 49
    • 0025668558 scopus 로고
    • Comprehensive two-dimensional gel protein databases offer a global approach to the analysis of human cells: The transformed amnion cells (AMA) master database and its link to genome DNA sequence data
    • Celis JE, Gesser B, Rasmussen HH, Madsen P, Leffers H, Dejgaard K, Honore B, Olsen E, Ratz G, Lauridsen JB, et al.: Comprehensive two-dimensional gel protein databases offer a global approach to the analysis of human cells: the transformed amnion cells (AMA) master database and its link to genome DNA sequence data. Electrophoresis 1990, 11:989-1071.
    • (1990) Electrophoresis , vol.11 , pp. 989-1071
    • Celis, J.E.1    Gesser, B.2    Rasmussen, H.H.3    Madsen, P.4    Leffers, H.5    Dejgaard, K.6    Honore, B.7    Olsen, E.8    Ratz, G.9    Lauridsen, J.B.10
  • 51
    • 0032776580 scopus 로고    scopus 로고
    • Studies on heat shock proteins in sea urchin development
    • Giudice G, Sconzo G, Roccheri MC: Studies on heat shock proteins in sea urchin development. Dev Growth Differ 1999, 41:375-80.
    • (1999) Dev. Growth Differ. , vol.41 , pp. 375-380
    • Giudice, G.1    Sconzo, G.2    Roccheri, M.C.3
  • 52
    • 0033664329 scopus 로고    scopus 로고
    • The distribution of heat shock proteins in the nervous system of the unstressed mouse embryo suggests a role in neuronal and non-neuronal differentiation
    • Loones MT, Chang Y, Morange M: The distribution of heat shock proteins in the nervous system of the unstressed mouse embryo suggests a role in neuronal and non-neuronal differentiation. Cell Stress Chaperones 2000, 5:291-305.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 291-305
    • Loones, M.T.1    Chang, Y.2    Morange, M.3
  • 54
    • 0031682263 scopus 로고    scopus 로고
    • Expression of cell death regulatory genes and limited apoptosis induction in avian blastodermal cells
    • Muscarella DE, Rachlinski MK, Bloom SE: Expression of cell death regulatory genes and limited apoptosis induction in avian blastodermal cells. Mol Reprod Dev 1998, 51:130-42.
    • (1998) Mol. Reprod. Dev. , vol.51 , pp. 130-142
    • Muscarella, D.E.1    Rachlinski, M.K.2    Bloom, S.E.3


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