메뉴 건너뛰기




Volumn 143, Issue 3, 1998, Pages 849-859

Dystrophic muscle in mice chimeric for expression of α5 integrin

Author keywords

Apoptosis; Chimeric mice; Integrin 5 1; Muscular dystrophy

Indexed keywords

INTEGRIN;

EID: 0032476651     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.3.849     Document Type: Article
Times cited : (95)

References (62)
  • 1
    • 0024359871 scopus 로고
    • Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration matrix assembly, and cytoskeletal organization
    • Akiyaa, S.K., S.S. Yamad, W.T. Chen, and K. Yamada. 1989. Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration matrix assembly, and cytoskeletal organization. J. Cell Biol. 109:863-875.
    • (1989) J. Cell Biol. , vol.109 , pp. 863-875
    • Akiyaa, S.K.1    Yamad, S.S.2    Chen, W.T.3    Yamada, K.4
  • 3
    • 0027433289 scopus 로고
    • α7β1 integrin is a component of the myotendinous junction on skeletal muscle
    • Bao, Z.Z., M. Lakonishok, S. Kaufman, and A.F. Horwitz. 1993. α7β1 integrin is a component of the myotendinous junction on skeletal muscle. J. Cell Sci. 106:579-589.
    • (1993) J. Cell Sci. , vol.106 , pp. 579-589
    • Bao, Z.Z.1    Lakonishok, M.2    Kaufman, S.3    Horwitz, A.F.4
  • 5
    • 0027262541 scopus 로고
    • PS2 integrin requirements in Drosophila embryo and wing morphogenesis
    • Brabant, M.C., and D.L. Brower. 1993. PS2 integrin requirements in Drosophila embryo and wing morphogenesis. Dev. Biol. 157:49-59.
    • (1993) Dev. Biol. , vol.157 , pp. 49-59
    • Brabant, M.C.1    Brower, D.L.2
  • 6
    • 0000742810 scopus 로고
    • Production and analysis of chimeric mice
    • E.J. Robertson, editor. IRL Press, Oxford, UK
    • Bradley, A. 1987. Production and analysis of chimeric mice. In Teratocarcinomas and Embyonic Stem Cells: A Practical Approach. E.J. Robertson, editor. IRL Press, Oxford, UK. 113-151.
    • (1987) Teratocarcinomas and Embyonic Stem Cells: A Practical Approach , pp. 113-151
    • Bradley, A.1
  • 7
    • 0031440110 scopus 로고    scopus 로고
    • Genetic analysis of β1 integrin function: Confirmed, new and revised roles for a crucial family of cell adhesion molecules
    • Brakebusch, C., E. Hirsch, A. Potocnik, and R. Faessler. 1997. Genetic analysis of β1 integrin function: confirmed, new and revised roles for a crucial family of cell adhesion molecules. J. Cell Sci. 110:2895-2904.
    • (1997) J. Cell Sci. , vol.110 , pp. 2895-2904
    • Brakebusch, C.1    Hirsch, E.2    Potocnik, A.3    Faessler, R.4
  • 9
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell, K.P. 1995. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell. 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 10
    • 0021270360 scopus 로고
    • Chick myotendinous antigen. I. A monoclonal antibody as a marker for tendon and muscle morphogenesis
    • Chiquet, M., and D.M. Fambrough. 1984. Chick myotendinous antigen. I. A monoclonal antibody as a marker for tendon and muscle morphogenesis. J. Cell Biol. 98:1926-1936.
    • (1984) J. Cell Biol. , vol.98 , pp. 1926-1936
    • Chiquet, M.1    Fambrough, D.M.2
  • 11
    • 0021891053 scopus 로고
    • The in vitro development of blastoeyst-derived embryonic stem cell lines: Formation of visceral yolk sac, blood islands and myocardium
    • Doetschman, T.C., H. Eistetter, M. Katz, W. Schmidt, and R. Kemler. 1985. The in vitro development of blastoeyst-derived embryonic stem cell lines: formation of visceral yolk sac, blood islands and myocardium. J. Embryol. Exp. Morphol. 87:27-45.
    • (1985) J. Embryol. Exp. Morphol. , vol.87 , pp. 27-45
    • Doetschman, T.C.1    Eistetter, H.2    Katz, M.3    Schmidt, W.4    Kemler, R.5
  • 12
    • 0026481012 scopus 로고
    • Expression of α1 integrin, a laminin-collagen receptor, during myogenesis and neurogenesis in the avian embryo
    • Duband, J.L., A.M. Belkin, J. Syfrig, J.P. Thiery, and V.E. Koteliansky. 1992. Expression of α1 integrin, a laminin-collagen receptor, during myogenesis and neurogenesis in the avian embryo. Development (Camb.). 116:585-600.
    • (1992) Development (Camb.) , vol.116 , pp. 585-600
    • Duband, J.L.1    Belkin, A.M.2    Syfrig, J.3    Thiery, J.P.4    Koteliansky, V.E.5
  • 14
    • 0027481216 scopus 로고
    • α5 integrin is a critical component of adhesion plaques in myogenesis
    • Enomoto, M.I., D. Boettinger, and A.S. Menko. 1993. α5 integrin is a critical component of adhesion plaques in myogenesis. Dev. Biol. 155:180-197.
    • (1993) Dev. Biol. , vol.155 , pp. 180-197
    • Enomoto, M.I.1    Boettinger, D.2    Menko, A.S.3
  • 15
    • 0028979154 scopus 로고
    • Consequences of the lack of β1 integrin gene expression in mice
    • Faessler, R., and M. Meyer. 1995. Consequences of the lack of β1 integrin gene expression in mice. Genes Dev. 9:1896-1908.
    • (1995) Genes Dev. , vol.9 , pp. 1896-1908
    • Faessler, R.1    Meyer, M.2
  • 16
    • 0025362679 scopus 로고
    • Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (α5β1) antibodies
    • Fogerty, F.J., S.K. Akiyama, K.M. Yamada, and D.F. Mosher. 1990. Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (α5β1) antibodies. J. Cell Biol. 111:699-708.
    • (1990) J. Cell Biol. , vol.111 , pp. 699-708
    • Fogerty, F.J.1    Akiyama, S.K.2    Yamada, K.M.3    Mosher, D.F.4
  • 17
    • 0028057613 scopus 로고
    • Disruption of epithelial cell matrix interactions induces apoptosis
    • Frisch, S.M., and H. Francis. 1994. Disruption of epithelial cell matrix interactions induces apoptosis. J. Cell Biol. 124:619-626.
    • (1994) J. Cell Biol. , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 18
    • 0027379724 scopus 로고
    • Defects in mesodermal migration and vascular development in fibronectin-deficient mice
    • George, E.L., E.N. Georges, R.S. Patel-King, H. Rayburn, and R.O. Hynes. 1993. Defects in mesodermal migration and vascular development in fibronectin-deficient mice. Development (Camb.). 119:1079-1091.
    • (1993) Development (Camb.) , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 19
    • 0028361337 scopus 로고
    • Integrin-mediated adhesion and signaling in tumorigenesis
    • Giancotti, F.G., and F. Mainiero. 1994. Integrin-mediated adhesion and signaling in tumorigenesis. Biochim. Biophys. Acta. 1198:47-64.
    • (1994) Biochim. Biophys. Acta , vol.1198 , pp. 47-64
    • Giancotti, F.G.1    Mainiero, F.2
  • 20
    • 0025214421 scopus 로고
    • Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells
    • Giancotti, F.G., and E. Ruoslahti. 1990. Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell. 60:849-859.
    • (1990) Cell , vol.60 , pp. 849-859
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 21
    • 0030700763 scopus 로고    scopus 로고
    • Mesodermal defects and cranial neural crest apoptosis in α5 integrin-null embryos
    • Goh, K.L., J.T. Yang, and R.O. Hynes. 1997. Mesodermal defects and cranial neural crest apoptosis in α5 integrin-null embryos. Development (Camb.). 124:4309-4319.
    • (1997) Development (Camb.) , vol.124 , pp. 4309-4319
    • Goh, K.L.1    Yang, J.T.2    Hynes, R.O.3
  • 22
    • 0025266739 scopus 로고
    • Retroviral expression of alternatively spliced forms of rat fibronectin
    • Guan, J.L., J.E. Trevithick, and R.O. Hynes. 1990. Retroviral expression of alternatively spliced forms of rat fibronectin. J. Cell Biol. 110:833-847.
    • (1990) J. Cell Biol. , vol.110 , pp. 833-847
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 24
    • 0030809116 scopus 로고    scopus 로고
    • Altered expression of the α7β1 integrin in human and murine muscular dystrophies
    • Hodges, B.L., Y.K. Hayashi, I. Nonaka, W. Wang, K. Arahata, and S.J. Kaufman. 1997. Altered expression of the α7β1 integrin in human and murine muscular dystrophies. J. Cell Sci. 110:2873-2881.
    • (1997) J. Cell Sci. , vol.110 , pp. 2873-2881
    • Hodges, B.L.1    Hayashi, Y.K.2    Nonaka, I.3    Wang, W.4    Arahata, K.5    Kaufman, S.J.6
  • 25
    • 0004043397 scopus 로고
    • Springer-Verlag, New York
    • Hynes, R.O. 1990. Fibronectin. Springer-Verlag, New York. 546 pp.
    • (1990) Fibronectin
    • Hynes, R.O.1
  • 26
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes, R.O. 1992. Integrins: versatility, modulation and signaling in cell adhesion. Cell. 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 27
    • 0026503656 scopus 로고
    • Contact and adhesive specificities in the associations, migrations and targeting of cells and axons
    • Hynes, R.O., and A.D. Lander. 1992. Contact and adhesive specificities in the associations, migrations and targeting of cells and axons. Cell. 68:303-322.
    • (1992) Cell , vol.68 , pp. 303-322
    • Hynes, R.O.1    Lander, A.D.2
  • 28
    • 0023785195 scopus 로고
    • Myoblast migration specifically inhibited in the chick embryo by grafted CSAT hybridoma cells secreting an anti-integrin antibody
    • Jaffredo, T., A.F. Horwitz, C.A. Buck, P.M. Rong, and F. Dieterlen-Lievre. 1988. Myoblast migration specifically inhibited in the chick embryo by grafted CSAT hybridoma cells secreting an anti-integrin antibody. Development (Camb.). 103:431-446.
    • (1988) Development (Camb.) , vol.103 , pp. 431-446
    • Jaffredo, T.1    Horwitz, A.F.2    Buck, C.A.3    Rong, P.M.4    Dieterlen-Lievre, F.5
  • 29
    • 0002055279 scopus 로고
    • The diversity of muscle fiber types and its origin during development
    • A.G. Engel and C. Franzini-Armstrong, editors. McGraw-Hill, New York
    • Kelly, A.M., and N.A. Rubinstein. 1994. The diversity of muscle fiber types and its origin during development. In Myology. A.G. Engel and C. Franzini-Armstrong, editors. McGraw-Hill, New York. 119-133.
    • (1994) Myology , pp. 119-133
    • Kelly, A.M.1    Rubinstein, N.A.2
  • 30
    • 0025185115 scopus 로고
    • Cell adhesion molecules in myogenesis
    • Knudsen, K.A. 1990. Cell adhesion molecules in myogenesis. Curr. Opin. Cell Biol. 2:902-906.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 902-906
    • Knudsen, K.A.1
  • 31
    • 0028817970 scopus 로고
    • Visualization of dystrophic muscle fibers in Mdx mouse by vital staining with evans blue: Evidence of apoptosis in dystrophin-deficient muscle
    • Matsuda, R., A. Nishikawa, and H. Tanaka. 1995. Visualization of dystrophic muscle fibers in Mdx mouse by vital staining with evans blue: evidence of apoptosis in dystrophin-deficient muscle. J. Biochem. 118:959-964.
    • (1995) J. Biochem. , vol.118 , pp. 959-964
    • Matsuda, R.1    Nishikawa, A.2    Tanaka, H.3
  • 32
    • 0017699553 scopus 로고
    • Surface distribution of lets protein in relation to the cytoskeleton of normal and transformed cells
    • Mautner, V., and R.O. Hynes. 1977. Surface distribution of lets protein in relation to the cytoskeleton of normal and transformed cells. J. Cell Biol. 75: 743-768.
    • (1977) J. Cell Biol. , vol.75 , pp. 743-768
    • Mautner, V.1    Hynes, R.O.2
  • 35
    • 0023649186 scopus 로고
    • Occupation of the extracellular matrix receptor, integrin, is a control point for myogenic differentiation
    • Menko, A.S., and D. Boettiger. 1987. Occupation of the extracellular matrix receptor, integrin, is a control point for myogenic differentiation. Cell. 51:51-57.
    • (1987) Cell , vol.51 , pp. 51-57
    • Menko, A.S.1    Boettiger, D.2
  • 37
    • 0025743718 scopus 로고
    • Down regulation of the chicken α5β1 integrin fibronectin receptor during development
    • Muschler, J.L., and A.F. Horwitz. 1991. Down regulation of the chicken α5β1 integrin fibronectin receptor during development. Development (Camb.). 113:327-337.
    • (1991) Development (Camb.) , vol.113 , pp. 327-337
    • Muschler, J.L.1    Horwitz, A.F.2
  • 38
    • 0024534377 scopus 로고
    • Changes in integrin receptors on oncogenically transformed cells
    • Plantefaber, L.C., and R.O. Hynes. 1989. Changes in integrin receptors on oncogenically transformed cells. Cell. 56:281-290.
    • (1989) Cell , vol.56 , pp. 281-290
    • Plantefaber, L.C.1    Hynes, R.O.2
  • 39
    • 0022000778 scopus 로고
    • Identification and isolation of a 140 Kd cell surface glycoprotein with properties expected of a fibronectin receptor
    • Pytela, R., M.D. Piershbacher, and E. Ruoslahti. 1994. Identification and isolation of a 140 Kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell. 40:191-198.
    • (1994) Cell , vol.40 , pp. 191-198
    • Pytela, R.1    Piershbacher, M.D.2    Ruoslahti, E.3
  • 40
    • 0028264320 scopus 로고
    • Primary mouse myoblast purification, characterization, and transplantation for cell-mediated gene therapy
    • Rando, T.A., and H.M. Blau. 1994. Primary mouse myoblast purification, characterization, and transplantation for cell-mediated gene therapy. J. Cell Biol. 125:1275-1284.
    • (1994) J. Cell Biol. , vol.125 , pp. 1275-1284
    • Rando, T.A.1    Blau, H.M.2
  • 41
    • 0030635069 scopus 로고    scopus 로고
    • Methods for myoblast transplantation
    • Rando, T.A., and H.M. Blau. 1997. Methods for myoblast transplantation. Methods Cell Biol. 52:261-272.
    • (1997) Methods Cell Biol. , vol.52 , pp. 261-272
    • Rando, T.A.1    Blau, H.M.2
  • 43
    • 0026708853 scopus 로고
    • Roles for the integrin VLA-4 and its counter receptor VCAM-1 in myogenesis
    • Rosen, G.D., J.R. Sanes, R. LaChance, J.M. Cunningham, J. Roman, and D.C. Dean. 1992. Roles for the integrin VLA-4 and its counter receptor VCAM-1 in myogenesis. Cell. 69:1107-1119.
    • (1992) Cell , vol.69 , pp. 1107-1119
    • Rosen, G.D.1    Sanes, J.R.2    LaChance, R.3    Cunningham, J.M.4    Roman, J.5    Dean, D.C.6
  • 46
    • 0002270650 scopus 로고
    • The extracellular matrix
    • A.G. Engel and C. Franzini-Armstrong, editors. McGraw-Hill, New York
    • Sanes, J.R. 1994. The extracellular matrix. In Myology. A.G. Engel and C. Franzini-Armstrong, editors. McGraw-Hill, New York. 242-260.
    • (1994) Myology , pp. 242-260
    • Sanes, J.R.1
  • 47
    • 0029664439 scopus 로고    scopus 로고
    • Integrin α subunit ratios, cytoplasmic domains and growth factor synergy regulate muscle proliferation and differentiation
    • Sastry, S.K., M. Lakonishok, D.A. Thomas, J. Muschler, and A.F. Horwitz. 1996. Integrin α subunit ratios, cytoplasmic domains and growth factor synergy regulate muscle proliferation and differentiation. J. Cell Biol. 133:169-184.
    • (1996) J. Cell Biol. , vol.133 , pp. 169-184
    • Sastry, S.K.1    Lakonishok, M.2    Thomas, D.A.3    Muschler, J.4    Horwitz, A.F.5
  • 48
    • 0025729036 scopus 로고
    • Increased tumorigenicity of fibronectin receptor deficient Chinese hamster ovary cell variants
    • Schreiner, C., M. Fisher, and S. Hussein, and R.L. Juliano. 1991. Increased tumorigenicity of fibronectin receptor deficient Chinese hamster ovary cell variants. Cancer Res. 51:1738-1740.
    • (1991) Cancer Res. , vol.51 , pp. 1738-1740
    • Schreiner, C.1    Fisher, M.2    Hussein, S.3    Juliano, R.L.4
  • 49
    • 0030051130 scopus 로고    scopus 로고
    • Tenascin-C expression in dystrophin-related muscular dystrophy
    • Settles, D.L., R.A. Cihak, and H.P. Erickson. 1996. Tenascin-C expression in dystrophin-related muscular dystrophy. Muscle Nerve. 19:147-154.
    • (1996) Muscle Nerve. , vol.19 , pp. 147-154
    • Settles, D.L.1    Cihak, R.A.2    Erickson, H.P.3
  • 50
    • 0025730216 scopus 로고
    • Lymphocyte interactions with extracellular matrix
    • Shimizu, Y., and S. Shaw. 1991. Lymphocyte interactions with extracellular matrix. FASEB (Fed. Am. Soc. Exp. Biol.) J. 5:2292-2299.
    • (1991) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.5 , pp. 2292-2299
    • Shimizu, Y.1    Shaw, S.2
  • 51
    • 0032518992 scopus 로고    scopus 로고
    • A test of the role of α5 integrin/fibronectin interactions in tumorigenesis
    • Taverna, D., M. Ullman-Cullerè, H. Rayburn, R.T. Bronson, and R.O. Hynes. 1998. A test of the role of α5 integrin/fibronectin interactions in tumorigenesis. Cancer Res. 58:848-853.
    • (1998) Cancer Res. , vol.58 , pp. 848-853
    • Taverna, D.1    Ullman-Cullerè, M.2    Rayburn, H.3    Bronson, R.T.4    Hynes, R.O.5
  • 54
    • 0028979701 scopus 로고
    • Integrin α5β1 expression negatively regulates growth: Reversal by attachment to fibronectin
    • Varner, J.A., D.A. Emerson, and R.L. Juliano. 1995. Integrin α5β1 expression negatively regulates growth: reversal by attachment to fibronectin. Mol. Biol Cell. 6:725-740.
    • (1995) Mol. Biol Cell. , vol.6 , pp. 725-740
    • Varner, J.A.1    Emerson, D.A.2    Juliano, R.L.3
  • 55
    • 0025153883 scopus 로고
    • A role for integrin in the formation of sarcomeric cytoarchiteclure
    • Volk, T., L.I. Fessler, and J.H. Fessler. 1990. A role for integrin in the formation of sarcomeric cytoarchiteclure. Cell. 63:525-536.
    • (1990) Cell , vol.63 , pp. 525-536
    • Volk, T.1    Fessler, L.I.2    Fessler, J.H.3
  • 56
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb, Z., P.M. Tremble, O. Behrendtsen, E. Crowley, and C.H. Damsky. 1989. Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J. Cell Biol. 109:877-889.
    • (1989) J. Cell Biol. , vol.109 , pp. 877-889
    • Werb, Z.1    Tremble, P.M.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 57
    • 0027243387 scopus 로고
    • Integrin α subunit mRNAs are differentially expressed in early Xenopus embryos
    • Whittaker, C.A., and D.W. DeSimone. 1993. Integrin α subunit mRNAs are differentially expressed in early Xenopus embryos. Development (Camb.). 117:1239-1249.
    • (1993) Development (Camb.) , vol.117 , pp. 1239-1249
    • Whittaker, C.A.1    DeSimone, D.W.2
  • 58
    • 0029957287 scopus 로고    scopus 로고
    • Fibronectin receptor functions in embryonic cells deficient in α5β1 integrin can be replaced by αv integrins
    • Yang, J.T., and R.O. Hynes. 1996. Fibronectin receptor functions in embryonic cells deficient in α5β1 integrin can be replaced by αv integrins. Mol. Biol. Cell. 7:1737-1748.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1737-1748
    • Yang, J.T.1    Hynes, R.O.2
  • 59
    • 0027371908 scopus 로고
    • Embryonic mesodermal defects in α5 integrin-deficient mice
    • Yang, J.T., H. Rayburn, and R.O. Hynes. 1993. Embryonic mesodermal defects in α5 integrin-deficient mice. Development (Camb.). 119:1093-1105.
    • (1993) Development (Camb.) , vol.119 , pp. 1093-1105
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3
  • 60
    • 0029826158 scopus 로고    scopus 로고
    • Genetic analysis of α4 integrin functions in the development of mouse skeletal muscle
    • Yang, J.T., T.A. Rando, W.A. Mohler, H. Rayburn, H.M. Blau, and R.O. Hynes. 1996. Genetic analysis of α4 integrin functions in the development of mouse skeletal muscle. J. Cell Biol. 135:829-835.
    • (1996) J. Cell Biol. , vol.135 , pp. 829-835
    • Yang, J.T.1    Rando, T.A.2    Mohler, W.A.3    Rayburn, H.4    Blau, H.M.5    Hynes, R.O.6
  • 61
    • 0029661978 scopus 로고    scopus 로고
    • α7 integrin mediates cell adhesion and migration on specific laminin isoforms
    • Yao, C.C., B.L. Ziober, R.M. Squillace, and R.H. Kramer. 1996. α7 integrin mediates cell adhesion and migration on specific laminin isoforms. J. Biol. Chem. 271:25598-25603.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25598-25603
    • Yao, C.C.1    Ziober, B.L.2    Squillace, R.M.3    Kramer, R.H.4
  • 62
    • 0028983407 scopus 로고
    • The α5β1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression
    • Zhang, Z., K. Vuori, J.C. Reed, and E. Ruoslahti. 1995. The α5β1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression. Proc. Natl. Acad. Sci. USA. 92:6161-6165.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6161-6165
    • Zhang, Z.1    Vuori, K.2    Reed, J.C.3    Ruoslahti, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.