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Volumn 4, Issue 4, 1998, Pages 385-396

Conformation of fibronectin fibrils varies: Discrete globular domains of type III repeats detected

Author keywords

Atomic projectiles; Cluster projectiles; Cryo scanning electron microscopy; Emission yield; Extracellular matrix; Fibrils; Fibronectin; Molecular dynamics simulations

Indexed keywords


EID: 0032271293     PISSN: 14319276     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1431927698980369     Document Type: Article
Times cited : (26)

References (56)
  • 1
    • 0028043949 scopus 로고
    • Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule
    • Aguirre KM, McCormick RJ, Schwarzbauer JE (1994) Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule. J Biol Chem 269: 27863-27868
    • (1994) J Biol Chem , vol.269 , pp. 27863-27868
    • Aguirre, K.M.1    McCormick, R.J.2    Schwarzbauer, J.E.3
  • 2
    • 0032579376 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin
    • Bultmann H, Santas AJ, Peters DMP (1998) Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin. J Biol Chem 273:2601-2609
    • (1998) J Biol Chem , vol.273 , pp. 2601-2609
    • Bultmann, H.1    Santas, A.J.2    Peters, D.M.P.3
  • 3
    • 0023650942 scopus 로고
    • Localization of the cellular-fibronectin-specific epitope recognized by the monoclonal antibody IST-9, using fusion proteins expressed in E. coli
    • Carnemolla B, Borsi L, Zardi L, Owens RJ, Baralle FE (1987) Localization of the cellular-fibronectin-specific epitope recognized by the monoclonal antibody IST-9, using fusion proteins expressed in E. coli. FEBS Lett 2:269-273
    • (1987) FEBS Lett , vol.2 , pp. 269-273
    • Carnemolla, B.1    Borsi, L.2    Zardi, L.3    Owens, R.J.4    Baralle, F.E.5
  • 4
    • 0026476010 scopus 로고
    • The inclusion of the type III repeat ED-B in the fibronectin molecule generates conformational modifications that unmask a cryptic sequence
    • Carnemolla B, Leprini A, Allemanni G, Saginati M, Zardi L (1992) The inclusion of the type III repeat ED-B in the fibronectin molecule generates conformational modifications that unmask a cryptic sequence. J Biol Chem 267:24689-24692
    • (1992) J Biol Chem , vol.267 , pp. 24689-24692
    • Carnemolla, B.1    Leprini, A.2    Allemanni, G.3    Saginati, M.4    Zardi, L.5
  • 5
    • 0023021573 scopus 로고
    • Transformed human cells release different fibronectin variants than do normal cells
    • Castellani P, Siri A, Rosellini C, Infusini E, Borsi L, Zardi L (1986) Transformed human cells release different fibronectin variants than do normal cells. J Cell Biol 103:1671-1677
    • (1986) J Cell Biol , vol.103 , pp. 1671-1677
    • Castellani, P.1    Siri, A.2    Rosellini, C.3    Infusini, E.4    Borsi, L.5    Zardi, L.6
  • 6
    • 0029882793 scopus 로고    scopus 로고
    • Formation of sodium dodecyl sulfate-stable fibronectin multimers
    • Chen H, Mosher DF (1996) Formation of sodium dodecyl sulfate-stable fibronectin multimers. J Biol Chem 271:9084-9089
    • (1996) J Biol Chem , vol.271 , pp. 9084-9089
    • Chen, H.1    Mosher, D.F.2
  • 7
    • 0029134694 scopus 로고
    • Imaging of cytoskeletal elements by low temperature high resolution scanning electron microscopy
    • Chen Y, Centonze V, Verkhovsky A, Borisy G (1995) Imaging of cytoskeletal elements by low temperature high resolution scanning electron microscopy. J Microsc 179:67-76
    • (1995) J Microsc , vol.179 , pp. 67-76
    • Chen, Y.1    Centonze, V.2    Verkhovsky, A.3    Borisy, G.4
  • 8
    • 0031200818 scopus 로고    scopus 로고
    • High resolution cryo-scanning electron microscopy (cryo-HRSEM) study of the macromolecular structure of fibronectin fibrils
    • Chen Y, Zardi L, Peters DMP (1997) High resolution cryo-scanning electron microscopy (cryo-HRSEM) study of the macromolecular structure of fibronectin fibrils. Scan Microsc 19:349-355
    • (1997) Scan Microsc , vol.19 , pp. 349-355
    • Chen, Y.1    Zardi, L.2    Peters, D.M.P.3
  • 9
    • 0025730907 scopus 로고
    • Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular matrix
    • Chernousov MA, Fogerty F, Koteliansky VE, Mosher DF (1991) Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular matrix. J Biol Chem 266:10851-10858
    • (1991) J Biol Chem , vol.266 , pp. 10851-10858
    • Chernousov, M.A.1    Fogerty, F.2    Koteliansky, V.E.3    Mosher, D.F.4
  • 10
    • 0030943367 scopus 로고    scopus 로고
    • Localization of fibronectin matrix assembly sites of fibroblasts and endothelial cells
    • Christopher RA, Kowalczyk AP, McKeown-Longo PJ (1997) Localization of fibronectin matrix assembly sites of fibroblasts and endothelial cells. J Cell Sci 110:569-581
    • (1997) J Cell Sci , vol.110 , pp. 569-581
    • Christopher, R.A.1    Kowalczyk, A.P.2    McKeown-Longo, P.J.3
  • 12
    • 0025940655 scopus 로고
    • Arrangement of cellular fibronectin in noncollagenous fibrils in human fibroblast cultures
    • Dzamba BJ, Peters DMP (1991) Arrangement of cellular fibronectin in noncollagenous fibrils in human fibroblast cultures. J Cell Sci 100:605-612
    • (1991) J Cell Sci , vol.100 , pp. 605-612
    • Dzamba, B.J.1    Peters, D.M.P.2
  • 13
    • 0027308871 scopus 로고
    • Fibronectin binding site in type I collagen regulates fibronectin fibril formation
    • Dzamba BJ, Wu H, Jaenisch R, Peters DM (1993) Fibronectin binding site in type I collagen regulates fibronectin fibril formation. J Cell Biol 121:1165-1172
    • (1993) J Cell Biol , vol.121 , pp. 1165-1172
    • Dzamba, B.J.1    Wu, H.2    Jaenisch, R.3    Peters, D.M.4
  • 14
    • 0028106117 scopus 로고
    • Substrate-specific binding of the amino terminus of fibronectin to an integrin complex in focal adhesions
    • Dzamba BJ, Bultmann H, Akiyama SK, Peters DM (1994) Substrate-specific binding of the amino terminus of fibronectin to an integrin complex in focal adhesions. J Biol Chem 269:19646-19652
    • (1994) J Biol Chem , vol.269 , pp. 19646-19652
    • Dzamba, B.J.1    Bultmann, H.2    Akiyama, S.K.3    Peters, D.M.4
  • 15
    • 0023587128 scopus 로고
    • Electron microscopy and other physical methods for the characterization of extracellular matrix components: Laminin, fibronectin, collagen IV, collagen VI, and proteoglycans
    • Engel J, Furthmayr H (1987) Electron microscopy and other physical methods for the characterization of extracellular matrix components: laminin, fibronectin, collagen IV, collagen VI, and proteoglycans. Methods Enzymol 145:3-78
    • (1987) Methods Enzymol , vol.145 , pp. 3-78
    • Engel, J.1    Furthmayr, H.2
  • 16
    • 0019888221 scopus 로고
    • Shapes, domain organizations and flexibility of laminin and fibronectin. Two multifunctional proteins of the extracellular matrix
    • Engel J, Odermatt E, Engel A, Madri JA, Furthmayr H, Rohde H, Timpl R (1981) Shapes, domain organizations and flexibility of laminin and fibronectin. Two multifunctional proteins of the extracellular matrix. J Mol Biol 150:97-120.
    • (1981) J Mol Biol , vol.150 , pp. 97-120
    • Engel, J.1    Odermatt, E.2    Engel, A.3    Madri, J.A.4    Furthmayr, H.5    Rohde, H.6    Timpl, R.7
  • 17
    • 0028028999 scopus 로고
    • Reversible unfolding of fibronectin type III and immunoglobin domains provides the structural basis for stretch and elasticity of titin
    • Erickson HP (1994) Reversible unfolding of fibronectin type III and immunoglobin domains provides the structural basis for stretch and elasticity of titin. Proc Natl Acad Sci USA 91:10114-10118
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10114-10118
    • Erickson, H.P.1
  • 18
    • 0019846214 scopus 로고
    • Fibronectin molecule visualized in electron microscopy: A long, thin, flexible strand
    • Erickson HP, Carrel N, McDonagh J (1981) Fibronectin molecule visualized in electron microscopy: a long, thin, flexible strand. J Cell Biol 91:673-678
    • (1981) J Cell Biol , vol.91 , pp. 673-678
    • Erickson, H.P.1    Carrel, N.2    McDonagh, J.3
  • 19
    • 0025362679 scopus 로고
    • Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (α5β1) antibodies
    • Fogerty FJ, Akiyama SK, Yamada SK, Yamada KM, Mosher DF (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, S.K.3    Yamada, K.M.4    Mosher, D.F.5
  • 20
    • 0025214421 scopus 로고
    • Elevated levels of the α5β1 fibronectin suppress the transformed phenotype of Chinese hamster ovary cells
    • Giancotti F, Ruoslahti E (1990) Elevated levels of the α5β1 fibronectin suppress the transformed phenotype of Chinese hamster ovary cells. Cell 60:849-859
    • (1990) Cell , vol.60 , pp. 849-859
    • Giancotti, F.1    Ruoslahti, E.2
  • 21
    • 0019302993 scopus 로고
    • Fibroblast receptor for cell-substratum adhesive: Studies on the interaction of baby hamster kidney cells with latex beads coated by cold insoluble globulin (plasma fibronectin)
    • Grinnell F (1980) Fibroblast receptor for cell-substratum adhesive: studies on the interaction of baby hamster kidney cells with latex beads coated by cold insoluble globulin (plasma fibronectin). J Cell Biol 86:104-112
    • (1980) J Cell Biol , vol.86 , pp. 104-112
    • Grinnell, F.1
  • 22
    • 0028364087 scopus 로고
    • Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin
    • Hocking DC, Sottile J, McKeown-Longo PJ (1994) Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin. J Biol Chem 269:19183-19191
    • (1994) J Biol Chem , vol.269 , pp. 19183-19191
    • Hocking, D.C.1    Sottile, J.2    McKeown-Longo, P.J.3
  • 23
    • 0029897753 scopus 로고    scopus 로고
    • A novel role for the integrin-binding III-10 module in fibronectin matrix assembly
    • Hocking DC, Smith RK, McKeown-Longo PJ (1996) A novel role for the integrin-binding III-10 module in fibronectin matrix assembly. J Cell Biol 133:431-444
    • (1996) J Cell Biol , vol.133 , pp. 431-444
    • Hocking, D.C.1    Smith, R.K.2    McKeown-Longo, P.J.3
  • 24
    • 0022252997 scopus 로고
    • Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth
    • Homandberg GA, Williams JE, Grant D, Schumacher B, Eisenstein R (1985) Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth. Am J Pathol 120:327-332
    • (1985) Am J Pathol , vol.120 , pp. 327-332
    • Homandberg, G.A.1    Williams, J.E.2    Grant, D.3    Schumacher, B.4    Eisenstein, R.5
  • 25
    • 0031036225 scopus 로고    scopus 로고
    • Cryptic self-association sites in type III modules of fibronectin
    • Ingham KC, Brew SA, Huff S, Litvinovich SV (1997) Cryptic self-association sites in type III modules of fibronectin. J Biol Chem 272:1718-1724
    • (1997) J Biol Chem , vol.272 , pp. 1718-1724
    • Ingham, K.C.1    Brew, S.A.2    Huff, S.3    Litvinovich, S.V.4
  • 26
    • 0021954281 scopus 로고
    • Demonstration of high affinity fibronectin receptors on rat hepatocytes in suspension
    • Johansson S (1985) Demonstration of high affinity fibronectin receptors on rat hepatocytes in suspension. J Biol Chem 260:1557-1561
    • (1985) J Biol Chem , vol.260 , pp. 1557-1561
    • Johansson, S.1
  • 27
    • 0030050396 scopus 로고    scopus 로고
    • 2.0Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy DJ, Aukhil I, Erickson HP (1996) 2.0Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84:155-164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 28
    • 0023178166 scopus 로고
    • Fibronectin's cell adhesive domain and an amino-terminal matrix assembly domain participate in its assembly in fibroblast pericellular matrix
    • McDonald JA, Quade BJ, Broekelmann TJ, LaChance R, Forsman K, Hasegawa E, Akiyama S (1987) Fibronectin's cell adhesive domain and an amino-terminal matrix assembly domain participate in its assembly in fibroblast pericellular matrix. J Biol Chem 262;2957-2967
    • (1987) J Biol Chem , vol.262 , pp. 2957-2967
    • McDonald, J.A.1    Quade, B.J.2    Broekelmann, T.J.3    LaChance, R.4    Forsman, K.5    Hasegawa, E.6    Akiyama, S.7
  • 29
    • 0021926873 scopus 로고
    • Interaction of the 70,000 molecular weight amino terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts
    • McKeown-Longo PJ, Mosher DF (1985) Interaction of the 70,000 molecular weight amino terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts. J Cell Biol 100:364-374
    • (1985) J Cell Biol , vol.100 , pp. 364-374
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 30
    • 0026652898 scopus 로고
    • A fibronectin self-assembly site involved in fibronectin matrix assembly: Reconstruction in a synthetic peptide
    • Morla A, Ruoslahti E (1992) A fibronectin self-assembly site involved in fibronectin matrix assembly: reconstruction in a synthetic peptide. J Cell Biol 118:421-429
    • (1992) J Cell Biol , vol.118 , pp. 421-429
    • Morla, A.1    Ruoslahti, E.2
  • 31
    • 0028069348 scopus 로고
    • Superfibronectin is a functionally distinct form of fibronectin
    • Morla A, Zhang Z, Ruoslahti E (1994) Superfibronectin is a functionally distinct form of fibronectin. Nature 367:193-196
    • (1994) Nature , vol.367 , pp. 193-196
    • Morla, A.1    Zhang, Z.2    Ruoslahti, E.3
  • 32
    • 0027483402 scopus 로고
    • Assembly of fibronectin into extracellular matrix
    • Mosher DF (1993) Assembly of fibronectin into extracellular matrix. Curr Opin Struct Biol 3:214-222
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 214-222
    • Mosher, D.F.1
  • 33
    • 0021111985 scopus 로고
    • In vitro formation of disulfide-bonded fibronectin multimers
    • Mosher DF, Johnson RB (1983) In vitro formation of disulfide-bonded fibronectin multimers. J Biol Chem 258:6595-6601
    • (1983) J Biol Chem , vol.258 , pp. 6595-6601
    • Mosher, D.F.1    Johnson, R.B.2
  • 34
    • 0025948419 scopus 로고
    • Monoclonal antibody characterization of two distinct sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly
    • Nagai T, Yamakawa N, Aota S, Yamada SS, Akiyama SK, Olden K, Yamada KM (1991) Monoclonal antibody characterization of two distinct sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly. J Cell Biol 114:1295-1305
    • (1991) J Cell Biol , vol.114 , pp. 1295-1305
    • Nagai, T.1    Yamakawa, N.2    Aota, S.3    Yamada, S.S.4    Akiyama, S.K.5    Olden, K.6    Yamada, K.M.7
  • 35
    • 0018098477 scopus 로고
    • Substrate activation of cell adheson factor as a prerequisite for cell adhesion
    • Pearlstein E (1978) Substrate activation of cell adheson factor as a prerequisite for cell adhesion. Int J Cancer 22:32-35
    • (1978) Int J Cancer , vol.22 , pp. 32-35
    • Pearlstein, E.1
  • 36
    • 0001652757 scopus 로고
    • Formation of Fibronectin Extracellular Matrix
    • Yurchenco PD, Birk DE, Mecham RP. New York: Academic Press
    • Peters DM, Mosher DF (1994) Formation of Fibronectin Extracellular Matrix. In: Extracellular Matrix Assembly and Structure, Yurchenco PD, Birk DE, Mecham RP. New York: Academic Press, pp 315-352
    • (1994) Extracellular Matrix Assembly and Structure , pp. 315-352
    • Peters, D.M.1    Mosher, D.F.2
  • 37
    • 0023119196 scopus 로고
    • Localization of cell surface sites involved in fibronectin fibrillogenesis
    • Peters DMP, Mosher DF (1987a) Localization of cell surface sites involved in fibronectin fibrillogenesis. J Cell Biol 104:121-130
    • (1987) J Cell Biol , vol.104 , pp. 121-130
    • Peters, D.M.P.1    Mosher, D.F.2
  • 38
    • 0023352980 scopus 로고
    • Assembly and alignment of fibronectin-coated beads into fibrils by human skin fibroblasts
    • Peters DMP, Mosher DF (1987b) Assembly and alignment of fibronectin-coated beads into fibrils by human skin fibroblasts. Scan Microsc 1:757-763
    • (1987) Scan Microsc , vol.1 , pp. 757-763
    • Peters, D.M.P.1    Mosher, D.F.2
  • 39
    • 0025372344 scopus 로고
    • Coassembly of plasma and cellular fibronectins into fibrils in human fibroblast cultures
    • Peters DMP, Portz LM, Fullenwider J, Mosher DF (1990) Coassembly of plasma and cellular fibronectins into fibrils in human fibroblast cultures. J Cell Biol 111:249-256
    • (1990) J Cell Biol , vol.111 , pp. 249-256
    • Peters, D.M.P.1    Portz, L.M.2    Fullenwider, J.3    Mosher, D.F.4
  • 40
  • 41
    • 0024273065 scopus 로고
    • Fibronectin's amino terminal matrix assembly site is located within the 29-kDa amino terminal domain containing five type I repeats
    • Quade BJ, McDonald JA (1988) Fibronectin's amino terminal matrix assembly site is located within the 29-kDa amino terminal domain containing five type I repeats. J Biol Chem 263:19602-19609
    • (1988) J Biol Chem , vol.263 , pp. 19602-19609
    • Quade, B.J.1    McDonald, J.A.2
  • 43
    • 0024328167 scopus 로고
    • The fibronectin receptor is organized by extracellular matrix fibronectin: Implications for oncogenic transformation and for cell recognition of fibronectin matrices
    • Roman JJ, LaChance RM, Broekelmann TJ, Kennedy CJ, Wayner EA, Carter WG, McDonald JA (1989) The fibronectin receptor is organized by extracellular matrix fibronectin: implications for oncogenic transformation and for cell recognition of fibronectin matrices. J Cell Biol 108:2529-2543
    • (1989) J Cell Biol , vol.108 , pp. 2529-2543
    • Roman, J.J.1    LaChance, R.M.2    Broekelmann, T.J.3    Kennedy, C.J.4    Wayner, E.A.5    Carter, W.G.6    McDonald, J.A.7
  • 44
    • 0025896188 scopus 로고
    • Identification of the fibronectin sequences required for assembly of a fibrillar matrix
    • Schwarzbauer JE (1991) Identification of the fibronectin sequences required for assembly of a fibrillar matrix. J Cell Biol 113:1463-1473
    • (1991) J Cell Biol , vol.113 , pp. 1463-1473
    • Schwarzbauer, J.E.1
  • 45
    • 0023409308 scopus 로고
    • Multiple sites of alternative splicing of the rat fibronectin gene transcript
    • Schwarzbauer JE, Patel RS, Fonda D, Hynes RO (1987) Multiple sites of alternative splicing of the rat fibronectin gene transcript. EMBO J 6:2573-2580
    • (1987) EMBO J , vol.6 , pp. 2573-2580
    • Schwarzbauer, J.E.1    Patel, R.S.2    Fonda, D.3    Hynes, R.O.4
  • 46
    • 0030659845 scopus 로고    scopus 로고
    • Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly
    • Sechler JL, Corbett SA, Schwarzbauer J (1997) Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly. Mol Biol Cell 8:2563-2573
    • (1997) Mol Biol Cell , vol.8 , pp. 2563-2573
    • Sechler, J.L.1    Corbett, S.A.2    Schwarzbauer, J.3
  • 47
    • 0030036963 scopus 로고    scopus 로고
    • Altered rate of fibronectin matrix assembly by deletion of the first type III repeats
    • Sechler JL, Takada Y, Schwarzbauer J (1996) Altered rate of fibronectin matrix assembly by deletion of the first type III repeats. J Cell Biol 134:573-583
    • (1996) J Cell Biol , vol.134 , pp. 573-583
    • Sechler, J.L.1    Takada, Y.2    Schwarzbauer, J.3
  • 49
    • 0025772946 scopus 로고
    • Five type I modules of fibronectin form a functional unit that binds to fibroblasts and Staphylococcus aureus
    • Sottile J, Schwarzbauer J, Selegue J, Mosher DF (1991) Five type I modules of fibronectin form a functional unit that binds to fibroblasts and Staphylococcus aureus. J Biol Chem 266:12840-12843
    • (1991) J Biol Chem , vol.266 , pp. 12840-12843
    • Sottile, J.1    Schwarzbauer, J.2    Selegue, J.3    Mosher, D.F.4
  • 50
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 53
    • 0028935604 scopus 로고
    • Fibronectin Fibril growth on the extracellular matrix of the Xenopus embryo
    • Winklbauer R, Stoltz C (1995) Fibronectin Fibril growth on the extracellular matrix of the Xenopus embryo. J Cell Sci 108:1575-1586
    • (1995) J Cell Sci , vol.108 , pp. 1575-1586
    • Winklbauer, R.1    Stoltz, C.2
  • 54
    • 0027422170 scopus 로고
    • The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain functions in an early and essential step in fibronectin matrix assembly
    • Wu C, Bauer JS, Juliano RL, McDonald JA (1993) The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain functions in an early and essential step in fibronectin matrix assembly. J Biol Chem 268:21883-21888
    • (1993) J Biol Chem , vol.268 , pp. 21883-21888
    • Wu, C.1    Bauer, J.S.2    Juliano, R.L.3    McDonald, J.A.4
  • 56
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeleton interaction are essential for the assembly of a fibronectin matrix
    • Wu C, Keivens VM, O'Toole TE, McDonald JA, Ginsberg MH (1995b) Integrin activation and cytoskeleton interaction are essential for the assembly of a fibronectin matrix. Cell 83:715-724
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5


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