메뉴 건너뛰기




Volumn 383, Issue 9, 2002, Pages 1407-1413

Degradation of extracellular matrix protein tenascin-C by cathepsin B: An interaction involved in the progression of gliomas

Author keywords

Cathepsin; Cysteine protease; Glioma; Immunohistochemistry; Tenascin C

Indexed keywords

CATHEPSIN B; COLLAGEN TYPE 1; ENZYME PRECURSOR; FIBRIN; LIPOCORTIN 2; MATRIX PROTEIN; PROCATHEPSIN B; TENASCIN; TETRAMER; UNCLASSIFIED DRUG;

EID: 0036754586     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.159     Document Type: Article
Times cited : (93)

References (56)
  • 1
    • 0024547527 scopus 로고
    • Tenascin mediates cell attachment through an RGD-dependent receptor
    • Bourdon, M.A., and Ruoslahti, E. (1989). Tenascin mediates cell attachment through an RGD-dependent receptor. J. Cell Biol. 108, 1149-1155.
    • (1989) J. Cell Biol , vol.108 , pp. 1149-1155
    • Bourdon, M.A.1    Ruoslahti, E.2
  • 2
    • 0029384013 scopus 로고
    • Expression of tenascin in tumors of the esophagus, small intestine and colo-rectum
    • Broll, R., Meyer, S., Neuber, M., and Bruch, H-P. 1995). Expression of tenascin in tumors of the esophagus, small intestine and colo-rectum. Gen. Diagn. Pathol. 141, 111-119.
    • (1995) Gen. Diagn. Pathol , vol.141 , pp. 111-119
    • Broll, R.1    Meyer, S.2    Neuber, M.3    Bruch, H.-P.4
  • 3
    • 0028362876 scopus 로고
    • Requirement of vascular integrin αvβ3 for angiogenesis
    • Brooks, P. C., Clark, R. F., and Cheresh, D. A. (1994). Requirement of vascular integrin αvβ3 for angiogenesis. Science 264, 569-571.
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.F.2    Cheresh, D.A.3
  • 5
    • 0022972814 scopus 로고
    • Tenascin: An extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis
    • Chiquet-Ehrismann, R., Mackie, E. J., Pearson, C. A., and Sakakura, T. (1986). Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell 47, 131-139.
    • (1986) Cell , vol.47 , pp. 131-139
    • Chiquet-Ehrismann, R.1    Mackie, E.J.2    Pearson, C.A.3    Sakakura, T.4
  • 6
    • 0029379601 scopus 로고
    • The complexity in regulating the expression of tenascins
    • Chiquet-Ehrismann, R., Hagios, C., and Schenk, S. (1995). The complexity in regulating the expression of tenascins. Bioassays 17, 873-878.
    • (1995) Bioassays , vol.17 , pp. 873-878
    • Chiquet-Ehrismann, R.1    Hagios, C.2    Schenk, S.3
  • 8
    • 0028305739 scopus 로고
    • Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C
    • Chung, C. Y., and Erickson, H. P. (1994). Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J. Cell Biol. 126, 539-548.
    • (1994) J. Cell Biol , vol.126 , pp. 539-548
    • Chung, C.Y.1    Erickson, H.P.2
  • 10
    • 0345215170 scopus 로고    scopus 로고
    • Utilization of a soluble integrin-alkaline phosphatase chimera to characterize integrin α8β1 receptor interactions with tenascin: Murine α8β1 binds to the RGD site in tenascin-C fragments, but not to native tenascin-C
    • Denda, S., Muller, U., Crossin K. L., Erickson, H. P., and Reichardt, L. (1998). Utilization of a soluble integrin-alkaline phosphatase chimera to characterize integrin α8β1 receptor interactions with tenascin: murine α8β1 binds to the RGD site in tenascin-C fragments, but not to native tenascin-C. Biochemistry 37, 5464-5474.
    • (1998) Biochemistry , vol.37 , pp. 5464-5474
    • Denda, S.1    Muller, U.2    Crossin, K.L.3    Erickson, H.P.4    Reichardt, L.5
  • 11
    • 6844250127 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases
    • d'Ortho, M. P., Will, H., Atkinson, S., Butler, G., Messent, A., Gavrilovic, J., Smith, B., Timpl, R., Zardi, L., and Murphy, G. (1997). Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur. J. Biochem. 250, 751-757.
    • (1997) Eur. J. Biochem , vol.250 , pp. 751-757
    • d'Ortho, M.P.1    Will, H.2    Atkinson, S.3    Butler, G.4    Messent, A.5    Gavrilovic, J.6    Smith, B.7    Timpl, R.8    Zardi, L.9    Murphy, G.10
  • 12
    • 0026575258 scopus 로고
    • Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues
    • Emmert-Buck, M. R., Karustis, D. G., Day, N. A., Honn, K. V., and Sloane, B. F. (1992). Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues. Biochem. J. 282, 273-278.
    • (1992) J. Biochem , vol.282 , pp. 273-278
    • Emmert-Buck, M.R.1    Karustis, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 14
    • 0027685702 scopus 로고
    • Tenascin-C, tenascin-R and tenascin-X: A family of talented proteins in search of functions
    • Erickson, H. P. (1993). Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions. Curr. Opin. Cell Biol. 5, 869-876.
    • (1993) Curr. Opin. Cell Biol , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 15
    • 0024441046 scopus 로고
    • Tenascin: An extra-cellular matrix protein prominent in specialized embryonic tissues and tumors
    • Erickson, H. P., and Bourdon, M. A. (1989). Tenascin: an extra-cellular matrix protein prominent in specialized embryonic tissues and tumors. Annu. Rev. Cell Biol. 5, 71-92.
    • (1989) Annu. Rev. Cell Biol , vol.5 , pp. 71-92
    • Erickson, H.P.1    Bourdon, M.A.2
  • 16
    • 0003126050 scopus 로고    scopus 로고
    • Molecular regulation, membrane association and secretion of tumor cathepsin B
    • Frosch, B. A., Berquin, I., Emmert-Buck, M. R., Moin, K., and Sloane, B. F (1999). Molecular regulation, membrane association and secretion of tumor cathepsin B. APMIS 107, 28-37.
    • (1999) APMIS , vol.107 , pp. 28-37
    • Frosch, B.A.1    Berquin, I.2    Emmert-Buck, M.R.3    Moin, K.4    Sloane, B.F.5
  • 17
    • 0031065191 scopus 로고    scopus 로고
    • Plasmin-induced proteolysis of tenascin-C: Modulation by T lymphocyte-derived urokinase-type plasminogen activator and effect on T lymphocyte adhesion, activation, and cell clustering
    • Gundersen, D., Tran-Thang, C., Sorda, B., Mourali, F, and Ruegg, C. (1997). Plasmin-induced proteolysis of tenascin-C: modulation by T lymphocyte-derived urokinase-type plasminogen activator and effect on T lymphocyte adhesion, activation, and cell clustering. J. Immunol. 158, 1051-1060.
    • (1997) J. Immunol , vol.158 , pp. 1051-1060
    • Gundersen, D.1    Tran-Thang, C.2    Sorda, B.3    Mourali, F.4    Ruegg, C.5
  • 18
    • 0027256757 scopus 로고
    • Expression of tenascin in human gliomas: Its relation to histological malignancy, tumor dedifferentiation and angiogenesis
    • Higuchi, M., Ohnishi, T., Arita, N., Hiraga, S., and Hayakawa, T. (1993). Expression of tenascin in human gliomas: its relation to histological malignancy, tumor dedifferentiation and angiogenesis. Acta Neuropathol. 85, 481-487.
    • (1993) Acta Neuropathol , vol.85 , pp. 481-487
    • Higuchi, M.1    Ohnishi, T.2    Arita, N.3    Hiraga, S.4    Hayakawa, T.5
  • 19
    • 0025609303 scopus 로고
    • Differential distribution of tenascin in the normal, hyperplastic, and neoplastic breast
    • Howeedy, A. A., Virtanen, I., Laitinen, L., Gould, M. S., Koukolis, G. K., and Gould, V. E. (1990). Differential distribution of tenascin in the normal, hyperplastic, and neoplastic breast. Lab. Invest. 63, 798-806.
    • (1990) Lab. Invest , vol.63 , pp. 798-806
    • Howeedy, A.A.1    Virtanen, I.2    Laitinen, L.3    Gould, M.S.4    Koukolis, G.K.5    Gould, V.E.6
  • 20
    • 0030476255 scopus 로고    scopus 로고
    • Expression of tenascin in invasion border of early breast cancer correlates with higher risk of distant metastasis
    • Jahkola, T., Toivonen, T., von Smitten, K., Blomqvist, C., and Virtanen, I. (1996). Expression of tenascin in invasion border of early breast cancer correlates with higher risk of distant metastasis. Int. J. Cancer 69, 445-447.
    • (1996) Int. J. Cancer , vol.69 , pp. 445-447
    • Jahkola, T.1    Toivonen, T.2    von Smitten, K.3    Blomqvist, C.4    Virtanen, I.5
  • 21
    • 0032189621 scopus 로고    scopus 로고
    • Expression of tenascin-C in intraductal carcinoma of human breast: Relationship to invasion
    • Jahkola, T., Toivonen, T., Nordling, S., von Smitten, K., and Virtanen, I. (1998). Expression of tenascin-C in intraductal carcinoma of human breast: relationship to invasion. Eur. J. Cancer 11, 1687-1692.
    • (1998) Eur. J. Cancer , vol.11 , pp. 1687-1692
    • Jahkola, T.1    Toivonen, T.2    Nordling, S.3    von Smitten, K.4    Virtanen, I.5
  • 22
    • 0030657742 scopus 로고    scopus 로고
    • Tenascin-C expression in the cyst wall and fluid of human brain tumors correlates with angiogenesis
    • Jallo, G. I., Friedlander, D. R., Kelly, P. J., Wisoff, J. H., Grumet, M., and Zagzag, D. (1997). Tenascin-C expression in the cyst wall and fluid of human brain tumors correlates with angiogenesis. Neurosurgery 41, 1052-1059.
    • (1997) Neurosurgery , vol.41 , pp. 1052-1059
    • Jallo, G.I.1    Friedlander, D.R.2    Kelly, P.J.3    Wisoff, J.H.4    Grumet, M.5    Zagzag, D.6
  • 23
    • 0033635695 scopus 로고    scopus 로고
    • Expression of tenascin-C in astrocytic tumors: Its relevance to proliferation and angiogenesis
    • Kim, C.H., Bak, K.H., Kim, Y.S., Kim, J.M., Ko, Y., Oh, S.J., Kim, K.M., and Hong, E.K. (2000). Expression of tenascin-C in astrocytic tumors: its relevance to proliferation and angiogenesis. Surg. Neurol. 54, 235-240.
    • (2000) Surg. Neurol , vol.54 , pp. 235-240
    • Kim, C.H.1    Bak, K.H.2    Kim, Y.S.3    Kim, J.M.4    Ko, Y.5    Oh, S.J.6    Kim, K.M.7    Hong, E.K.8
  • 24
    • 0025827485 scopus 로고
    • Tenascin in normal, reactive, hyperplastic, and neoplastic tissues: Biologic and pathologic implications
    • Koukoulis, G. K., Gould, V. E., Bhattacharyya, A., Could, J. E. Howeedy, A. A., and Virtanen, I. (1991). Tenascin in normal, reactive, hyperplastic, and neoplastic tissues: biologic and pathologic implications. Hum. Pathol. 22, 636-643.
    • (1991) Hum. Pathol , vol.22 , pp. 636-643
    • Koukoulis, G.K.1    Gould, V.E.2    Bhattacharyya, A.3    Could, J.E.4    Howeedy, A.A.5    Virtanen, I.6
  • 27
    • 0033567263 scopus 로고    scopus 로고
    • Exocytosis of active cathepsin B: Enzyme activity at pH 7.0, inhibition and molecular mass
    • Linebaugh, B.E., Sameni, M., Day, N.A., Sloane, B.F., and Keppler, D. (1999). Exocytosis of active cathepsin B: enzyme activity at pH 7.0, inhibition and molecular mass. Eur. J. Biochem. 264, 100-109.
    • (1999) Eur. J. Biochem , vol.264 , pp. 100-109
    • Linebaugh, B.E.1    Sameni, M.2    Day, N.A.3    Sloane, B.F.4    Keppler, D.5
  • 28
    • 0022555838 scopus 로고
    • Biochemical interactions of tumor cells with the basement membrane
    • Liotta, L. A., Rao, C. N., and Wewer, U. M. (1986). Biochemical interactions of tumor cells with the basement membrane. Annu. Rev. Biochem. 55, 1037-1057.
    • (1986) Annu. Rev. Biochem , vol.55 , pp. 1037-1057
    • Liotta, L.A.1    Rao, C.N.2    Wewer, U.M.3
  • 29
    • 0024215607 scopus 로고
    • Induction of tenascin in healing wounds
    • Mackie, E. J., Thesleff, I., and Liverani, D. (1988a). Induction of tenascin in healing wounds. J. Cell Biol. 107, 2757-2767.
    • (1988) J. Cell Biol , vol.107 , pp. 2757-2767
    • Mackie, E.J.1    Thesleff, I.2    Liverani, D.3
  • 30
    • 0023867432 scopus 로고
    • The distribution of tenascin coincides with pathways of neural crest cell migration
    • Mackie, E.J., Tucker, R. P., Halfer, W., Chiquet-Ehrismann, R., and Epperlein, H. H. (1988b). The distribution of tenascin coincides with pathways of neural crest cell migration. Development 102, 237-250.
    • (1988) Development , vol.102 , pp. 237-250
    • Mackie, E.J.1    Tucker, R.P.2    Halfer, W.3    Chiquet-Ehrismann, R.4    Epperlein, H.H.5
  • 31
    • 0034725119 scopus 로고    scopus 로고
    • Procathepsin B interacts with the annexin II tetramer on the surface of tumor cells
    • Mai, J., Finley, R. L., Waisman, D. M., and Sloane, B. F. (2000a). Procathepsin B interacts with the annexin II tetramer on the surface of tumor cells. J. Biol. Chem. 275, 12806-12812.
    • (2000) J. Biol. Chem , vol.275 , pp. 12806-12812
    • Mai, J.1    Finley, R.L.2    Waisman, D.M.3    Sloane, B.F.4
  • 32
    • 0034615565 scopus 로고    scopus 로고
    • Cell surface complex of cathepsin B/annexin II tetramer in malignant progression
    • Mai, J., Waisman, D. M., and Sloane, B. F. (2000b). Cell surface complex of cathepsin B/annexin II tetramer in malignant progression. Biochim. Biophys. Acta 1477, 215-230.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 215-230
    • Mai, J.1    Waisman, D.M.2    Sloane, B.F.3
  • 33
    • 0022969477 scopus 로고
    • Tumor invasion through the human amniotic membrane: Requirement for a proteinase cascade
    • Mignatti, P., Robbins, E., and Rifkin, D. B. (1986). Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell 47, 487-498.
    • (1986) Cell , vol.47 , pp. 487-498
    • Mignatti, P.1    Robbins, E.2    Rifkin, D.B.3
  • 34
    • 0029097797 scopus 로고
    • Immunolocalization of cathepsin B in human glioma: Implications for tumor invasion and angiogenesis
    • Mikkelsen, T., Yan, P. S., Ho, K. L., Sameni, M., Sloane, B. F., and Rosenblum, M. L. (1995). Immunolocalization of cathepsin B in human glioma: implications for tumor invasion and angiogenesis. J. Neurosurg. 83, 285-290.
    • (1995) J. Neurosurg , vol.83 , pp. 285-290
    • Mikkelsen, T.1    Yan, P.S.2    Ho, K.L.3    Sameni, M.4    Sloane, B.F.5    Rosenblum, M.L.6
  • 35
    • 0026729645 scopus 로고
    • Human tumour cathepsin B: Comparison with normal human liver cathepsin B
    • Moin, K., Day, N. A., Sameni, M., Hasnain, S., Hirama, T., and Sloane, B. F. (1992). Human tumour cathepsin B: comparison with normal human liver cathepsin B. Biochem. J. 285, 427-434.
    • (1992) Biochem. J , vol.285 , pp. 427-434
    • Moin, K.1    Day, N.A.2    Sameni, M.3    Hasnain, S.4    Hirama, T.5    Sloane, B.F.6
  • 36
    • 0025777905 scopus 로고
    • Comparative analysis of the expression of the extracellular matrix protein tenascin in normal human fetal, adult and tumor tissues
    • Natali, P.G., Nicotra, M. R., and Bigotti, A. (1991). Comparative analysis of the expression of the extracellular matrix protein tenascin in normal human fetal, adult and tumor tissues. Int. J. Cancer 47, 811-816.
    • (1991) Int. J. Cancer , vol.47 , pp. 811-816
    • Natali, P.G.1    Nicotra, M.R.2    Bigotti, A.3
  • 37
    • 0026425707 scopus 로고
    • Qualitative and quantitative changes of human tenascin expression in transformed lung fibroblast and lung tumor tissues: Comparison with fibronectin
    • Oyama, F., Hirohashi, S., Shimosato, Y., Titani, K., and Sekiguchi, K. (1991). Qualitative and quantitative changes of human tenascin expression in transformed lung fibroblast and lung tumor tissues: comparison with fibronectin. Cancer Res. 51, 4876-4881.
    • (1991) Cancer Res , vol.51 , pp. 4876-4881
    • Oyama, F.1    Hirohashi, S.2    Shimosato, Y.3    Titani, K.4    Sekiguchi, K.5
  • 38
    • 0031554904 scopus 로고    scopus 로고
    • Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen
    • Podobnik, M., Kuhelj, R., Turk, V., and Turk, D. (1997). Crystal structure of the wild-type human procathepsin B at 2.5 Å resolution reveals the native active site of a papain-like cysteine protease zymogen. J. Mol. Biol. 271, 774-788.
    • (1997) J. Mol. Biol , vol.271 , pp. 774-788
    • Podobnik, M.1    Kuhelj, R.2    Turk, V.3    Turk, D.4
  • 40
    • 0032473476 scopus 로고    scopus 로고
    • Tenascin-C matrix assembly in oral squamous cell carcinoma
    • Ramos, D. M., Chen, B. L., Regezi, J., Zardi, L., and Pytela, R. (1998). Tenascin-C matrix assembly in oral squamous cell carcinoma. Int. J. Cancer 75, 680-687.
    • (1998) Int. J. Cancer , vol.75 , pp. 680-687
    • Ramos, D.M.1    Chen, B.L.2    Regezi, J.3    Zardi, L.4    Pytela, R.5
  • 41
    • 0030768281 scopus 로고    scopus 로고
    • Tenascin-C tissue concentration in inflammatory and neoplastic diseases of the colon mucosa
    • Riedl, S., Kadmon, M., Tandara, A., Hinz, U., Moller, P., and Faissner, A. (1997). Tenascin-C tissue concentration in inflammatory and neoplastic diseases of the colon mucosa. Anti-cancer Res. 17, 3165-3166.
    • (1997) Anti-cancer Res , vol.17 , pp. 3165-3166
    • Riedl, S.1    Kadmon, M.2    Tandara, A.3    Hinz, U.4    Moller, P.5    Faissner, A.6
  • 42
    • 0028688488 scopus 로고
    • Can tenascin be redundant in cancer development?
    • Sakakura, T., and Kusakabe, M. (1994). Can tenascin be redundant in cancer development? Perspect. Dev. Neurobiol. 2, 111-116.
    • (1994) Perspect. Dev. Neurobiol , vol.2 , pp. 111-116
    • Sakakura, T.1    Kusakabe, M.2
  • 44
    • 0028981367 scopus 로고
    • The human integrin α8β1 functions as a receptor for tenascin, fibronectin, and vitronectin
    • Schnapp, L. M., Hatch, N., Ramos, D. M., Klimanskaya, I. V., Sheppard, D., and Pytela, R. (1995). The human integrin α8β1 functions as a receptor for tenascin, fibronectin, and vitronectin. J. Biol. Chem. 270, 23196-23202.
    • (1995) J. Biol. Chem , vol.270 , pp. 23196-23202
    • Schnapp, L.M.1    Hatch, N.2    Ramos, D.M.3    Klimanskaya, I.V.4    Sheppard, D.5    Pytela, R.6
  • 45
    • 0031008836 scopus 로고    scopus 로고
    • Extracellular matrices expression in invasion area of adenoid cystic carcinoma of salivary glands
    • Shintani, S, Alcalde, R. E., Matsumura, T., and Terakado, N. (1997). Extracellular matrices expression in invasion area of adenoid cystic carcinoma of salivary glands. Cancer Lett. 116, 9-14.
    • (1997) Cancer Lett , vol.116 , pp. 9-14
    • Shintani, S.1    Alcalde, R.E.2    Matsumura, T.3    Terakado, N.4
  • 46
    • 0027363935 scopus 로고
    • Tenascin staining positivity and the survival of patients with invasive breast carcinoma
    • Shoji, T., Kamiya, T., Tsubura, A., Hamada, Y., Hatano, T., Hioki, K., and Morii, S. (1993). Tenascin staining positivity and the survival of patients with invasive breast carcinoma. J. Surg. Res. 55, 295-297.
    • (1993) J. Surg. Res , vol.55 , pp. 295-297
    • Shoji, T.1    Kamiya, T.2    Tsubura, A.3    Hamada, Y.4    Hatano, T.5    Hioki, K.6    Morii, S.7
  • 47
    • 0028908403 scopus 로고
    • Different susceptibility of small and large human tenascin-C isoforms to degradation by matrix metalloproteinases
    • Siri, A., Knauper, V., Veirana, N., Caocci, F., Murphy, G., and Zardi, L. (1995). Different susceptibility of small and large human tenascin-C isoforms to degradation by matrix metalloproteinases. J. Biol. Chem. 270, 8650-8654.
    • (1995) J. Biol. Chem , vol.270 , pp. 8650-8654
    • Siri, A.1    Knauper, V.2    Veirana, N.3    Caocci, F.4    Murphy, G.5    Zardi, L.6
  • 49
    • 0030069164 scopus 로고    scopus 로고
    • Combined analysis of expression of cerbB-2, Ki-67 antigen, and tenascin provides a better prognostic indicator of carcinoma of the papilla of Vater
    • Vaidya, P., Yosida, T., Sakakura, T., Yatani, R., Noguchi, T., and Kawarada, Y. (1996). Combined analysis of expression of cerbB-2, Ki-67 antigen, and tenascin provides a better prognostic indicator of carcinoma of the papilla of Vater. Pancreas 12, 196-201.
    • (1996) Pancreas , vol.12 , pp. 196-201
    • Vaidya, P.1    Yosida, T.2    Sakakura, T.3    Yatani, R.4    Noguchi, T.5    Kawarada, Y.6
  • 54
    • 0031864089 scopus 로고    scopus 로고
    • Expression of periglandular tenascin-C and basement membrane laminin in normal prostate, benign prostatic hyperplasia and prostate carcinoma
    • Xue, Y., Smedts, F., Latijnhouwers, M. A., Ruijter, E., Aalders, T. W., Rosette, J., Ebruyne, F. M. J., and Schalken, J. A. (1998). Expression of periglandular tenascin-C and basement membrane laminin in normal prostate, benign prostatic hyperplasia and prostate carcinoma. Br. J. Urol. 81, 844-851.
    • (1998) Br. J. Urol , vol.81 , pp. 844-851
    • Xue, Y.1    Smedts, F.2    Latijnhouwers, M.A.3    Ruijter, E.4    Aalders, T.W.5    Rosette, J.6    Ebruyne, F.M.J.7    Schalken, J.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.