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Volumn 3, Issue 7, 2011, Pages 1-19

Fibronectins, their fibrillogenesis, and in vivo functions

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; ISOPROTEIN;

EID: 84863875404     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a005041     Document Type: Review
Times cited : (318)

References (205)
  • 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
    • 0017724384 scopus 로고
    • Effects of cytochalasin B and colchicine on attachment of a major surface protein of fibroblasts
    • Ali IU, Hynes RO. 1977. Effects of cytochalasin B and colchicine on attachment of a major surface protein of fibroblasts. Biochim Biophys Acta 471: 16-24.
    • (1977) Biochim Biophys Acta , vol.471 , pp. 16-24
    • Ali, I.U.1    Hynes, R.O.2
  • 3
    • 0027971378 scopus 로고
    • The short amino acid sequence pro-his-ser-arg-asn in human fibronectin enhances cell adhesive function
    • Aota S, Nomizu M, Yamada K. 1994. The short amino acid sequence pro-his-ser-arg-asn in human fibronectin enhances cell adhesive function. J Biol Chem 269: 24756-24761.
    • (1994) J Biol Chem , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.3
  • 4
    • 67650763823 scopus 로고    scopus 로고
    • Fibronectins in vascular morphogenesis
    • Astrof S, Hynes RO. 2009. Fibronectins in vascular morphogenesis. Angiogenesis 12: 165-175.
    • (2009) Angiogenesis , vol.12 , pp. 165-175
    • Astrof, S.1    Hynes, R.O.2
  • 5
    • 35348890874 scopus 로고    scopus 로고
    • Multiple cardiovascular defects caused by the absence of alternatively spliced segments of fibronectin
    • Astrof S, Crowley D, Hynes RO. 2007. Multiple cardiovascular defects caused by the absence of alternatively spliced segments of fibronectin. Dev Biol 311: 11-24.
    • (2007) Dev Biol , vol.311 , pp. 11-24
    • Astrof, S.1    Crowley, D.2    Hynes, R.O.3
  • 6
    • 4544299823 scopus 로고    scopus 로고
    • Direct test of potential roles of EIIIA and EIIIB alternatively spliced segments of fibronectin in physiological and tumor angiogenesis
    • Astrof S, Crowley D, George EL, Fukuda T, Sekiguchi K, HanahanD, Hynes RO. 2004. Direct test of potential roles of EIIIA and EIIIB alternatively spliced segments of fibronectin in physiological and tumor angiogenesis. Mol Cell Biol 24: 8662-8670.
    • (2004) Mol Cell Biol , vol.24 , pp. 8662-8670
    • Astrof, S.1    Crowley, D.2    George, E.L.3    Fukuda, T.4    Sekiguchi, K.5    Hanahan, D.6    Hynes, R.O.7
  • 7
    • 0035807873 scopus 로고    scopus 로고
    • Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer
    • Baneyx G, Baugh L, Vogel V. 2001. Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer. Proc Natl Acad Sci 98: 14464-14468.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 14464-14468
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 8
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • Baneyx G, Baugh L, Vogel V. 2002. Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc Natl Acad Sci 99: 5139-5143.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 9
    • 0027994367 scopus 로고
    • Interactions between fibronectin and chondroitin sulfate are modulated by molecular context
    • Barkalow FJ, Schwarzbauer JE. 1994. Interactions between fibronectin and chondroitin sulfate are modulated by molecular context. J Biol Chem 269: 3957-3962.
    • (1994) J Biol Chem , vol.269 , pp. 3957-3962
    • Barkalow, F.J.1    Schwarzbauer, J.E.2
  • 10
    • 0026644395 scopus 로고
    • Proposed acquisition of an animal protein domain by bacteria
    • Bork P, Doolittle RF. 1992. Proposed acquisition of an animal protein domain by bacteria. Proc Natl Acad Sci 89: 8990-8994.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 8990-8994
    • Bork, P.1    Doolittle, R.F.2
  • 11
    • 0021062273 scopus 로고
    • Fibronectin in early amphibian embryos. Migrating mesodermal cells contact fibronectin established prior to gastrulation
    • Boucaut JC, Darribere T. 1983a. Fibronectin in early amphibian embryos. Migrating mesodermal cells contact fibronectin established prior to gastrulation. Cell Tissue Res 234: 135-145.
    • (1983) Cell Tissue Res , vol.234 , pp. 135-145
    • Boucaut, J.C.1    Darribere, T.2
  • 12
    • 0020701805 scopus 로고
    • Presence of fibronectin during early embryogenesis in amphibian Pleurodeles waltlii
    • Boucaut JC, Darribere T. 1983b. Presence of fibronectin during early embryogenesis in amphibian Pleurodeles waltlii. Cell Differ 12: 77-83.
    • (1983) Cell Differ , vol.12 , pp. 77-83
    • Boucaut, J.C.1    Darribere, T.2
  • 13
    • 0021720476 scopus 로고
    • Biologically active synthetic peptides as probes of embryonic development: A competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos
    • Boucaut J-C, Darribere T, Poole TJ, Aoyama H, Yamada KM, Thiery JP. 1984a. Biologically active synthetic peptides as probes of embryonic development: A competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos. J Cell Biol 99: 1822-1830.
    • (1984) J Cell Biol , vol.99 , pp. 1822-1830
    • Boucaut, J-C.1    Darribere, T.2    Poole, T.J.3    Aoyama, H.4    Yamada, K.M.5    Thiery, J.P.6
  • 14
    • 0021244335 scopus 로고
    • Prevention of gastrulation but not neurulation by antibodies to fibronectin in amphibian embryos
    • Boucaut JC, Darribère T, Boulekbache H, Thiery JP. 1984b. Prevention of gastrulation but not neurulation by antibodies to fibronectin in amphibian embryos. Nature 307: 364-367.
    • (1984) Nature , vol.307 , pp. 364-367
    • Boucaut, J.C.1    Darribère, T.2    Boulekbache, H.3    Thiery, J.P.4
  • 15
    • 0021720476 scopus 로고
    • Biologically active synthetic peptides as probes of embryonic development: A competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos
    • Boucaut JC, Darribère T, Poole TJ, Aoyama H, Yamada KM, Thiery JP. 1984c. Biologically active synthetic peptides as probes of embryonic development: A competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos. J Cell Biol 99: 1822-1830.
    • (1984) J Cell Biol , vol.99 , pp. 1822-1830
    • Boucaut, J.C.1    Darribère, T.2    Poole, T.J.3    Aoyama, H.4    Yamada, K.M.5    Thiery, J.P.6
  • 17
    • 0034729698 scopus 로고    scopus 로고
    • Regulation of fibronectin matrix assembly by activated Ras in transformed cells
    • Brenner KA, Corbett SA, Schwarzbauer JE. 2000. Regulation of fibronectin matrix assembly by activated Ras in transformed cells. Oncogene 19: 3156-3163.
    • (2000) Oncogene , vol.19 , pp. 3156-3163
    • Brenner, K.A.1    Corbett, S.A.2    Schwarzbauer, J.E.3
  • 18
    • 0028282984 scopus 로고
    • Regulation of Ccadherin function during activin induced morphogenesis of Xenopus animal caps
    • Brieher WM, Gumbiner BM. 1994. Regulation of Ccadherin function during activin induced morphogenesis of Xenopus animal caps. J Cell Biol 126: 519-527.
    • (1994) J Cell Biol , vol.126 , pp. 519-527
    • Brieher, W.M.1    Gumbiner, B.M.2
  • 19
    • 0025906798 scopus 로고
    • Interactions between mesoderm cells and the extracellular matrix following gastrulation in the chick embryo
    • Brown AJ, Sanders EJ. 1991. Interactions between mesoderm cells and the extracellular matrix following gastrulation in the chick embryo. J Cell Sci 99: 431-441.
    • (1991) J Cell Sci , vol.99 , pp. 431-441
    • Brown, A.J.1    Sanders, E.J.2
  • 20
    • 0032579376 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin
    • Bultmann H, Santas AJ, Pesciotta Peters DM. 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    Pesciotta Peters, D.M.3
  • 23
    • 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
  • 24
    • 0025730907 scopus 로고
    • Role of the I-9 and III-1 modules of fibronectin in the formation of an extracellular fibronectin matrix
    • Chernousov MA, Fogerty FJ, Koteliansky VE, Mosher DF. 1991. Role of the I-9 and III-1 modules of fibronectin in the formation of an extracellular fibronectin matrix. J Biol Chem 266: 10851-10858.
    • (1991) J Biol Chem , vol.266 , pp. 10851-10858
    • Chernousov, M.A.1    Fogerty, F.J.2    Koteliansky, V.E.3    Mosher, D.F.4
  • 26
    • 0018583163 scopus 로고
    • Biosynthesis and processing of fibronectin in NIL.8 hamster cells
    • Choi MG, Hynes RO. 1979. Biosynthesis and processing of fibronectin in NIL.8 hamster cells. J Biol Chem 254: 12050-12055.
    • (1979) J Biol Chem , vol.254 , pp. 12050-12055
    • Choi, M.G.1    Hynes, R.O.2
  • 27
    • 0030774882 scopus 로고    scopus 로고
    • Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix
    • Corbett SA, Lee L, Wilson CL, Schwarzbauer JE. 1997. Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix. J Biol Chem 272: 24999-5005.
    • (1997) J Biol Chem , vol.272 , pp. 24999-25005
    • Corbett, S.A.1    Lee, L.2    Wilson, C.L.3    Schwarzbauer, J.E.4
  • 28
    • 78049404922 scopus 로고    scopus 로고
    • Transmembrane signaling proteoglycans
    • Couchman JR. 2010. Transmembrane signaling proteoglycans. Annu Rev Cell Dev Biol 26: 89-114.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 89-114
    • Couchman, J.R.1
  • 29
    • 0018778653 scopus 로고
    • Distribution of fibronectin in the ectoderm of gastrulating chick embryos
    • Critchley DR, England MA, Wakely J, Hynes RO. 1979. Distribution of fibronectin in the ectoderm of gastrulating chick embryos. Nature 280: 498-500.
    • (1979) Nature , vol.280 , pp. 498-500
    • Critchley, D.R.1    England, M.A.2    Wakely, J.3    Hynes, R.O.4
  • 31
    • 0343819799 scopus 로고    scopus 로고
    • Fibronectin matrix composition and organization can regulate cell migration during amphibian development
    • Darribere T, Schwarzbauer JE. 2000. Fibronectin matrix composition and organization can regulate cell migration during amphibian development. Mech Dev 92: 239-250.
    • (2000) Mech Dev , vol.92 , pp. 239-250
    • Darribere, T.1    Schwarzbauer, J.E.2
  • 33
    • 11144297253 scopus 로고    scopus 로고
    • Assembly and remodeling of the fibrillar fibronectin extracellular matrix during gastrulation and neurulation in Xenopus laevis
    • Davidson LA, Keller R, DeSimone DW. 2004. Assembly and remodeling of the fibrillar fibronectin extracellular matrix during gastrulation and neurulation in Xenopus laevis. Dev Dyn 231: 888-895.
    • (2004) Dev Dyn , vol.231 , pp. 888-895
    • Davidson, L.A.1    Keller, R.2    DeSimone, D.W.3
  • 34
    • 54549125813 scopus 로고    scopus 로고
    • Live imaging of cell protrusive activity, and extracellular matrix assembly and remodeling during morphogenesis in the frog, Xenopus laevis
    • Davidson L, Dzamba B, Keller R, Desimone D. 2008. Live imaging of cell protrusive activity, and extracellular matrix assembly and remodeling during morphogenesis in the frog, Xenopus laevis. Dev Dyn 237: 2684-2692.
    • (2008) Dev Dyn , vol.237 , pp. 2684-2692
    • Davidson, L.1    Dzamba, B.2    Keller, R.3    Desimone, D.4
  • 36
    • 33646186048 scopus 로고    scopus 로고
    • 1 and fibronectin regulate polarized cell protrusions required for Xenopus convergence and extension
    • 1 and fibronectin regulate polarized cell protrusions required for Xenopus convergence and extension. Curr Biol 16: 833-844.
    • (2006) Curr Biol , vol.16 , pp. 833-844
    • Davidson, L.A.1    Marsden, M.2    Keller, R.3    DeSimone, D.W.4
  • 37
    • 0026564757 scopus 로고
    • Identification and characterization of alternatively spliced fibronectin mRNAs expressed in early Xenopus embryos
    • DeSimone DW, Norton PA, Hynes RO. 1992. Identification and characterization of alternatively spliced fibronectin mRNAs expressed in early Xenopus embryos. Dev Biol 149: 357-369.
    • (1992) Dev Biol , vol.149 , pp. 357-369
    • DeSimone, D.W.1    Norton, P.A.2    Hynes, R.O.3
  • 38
    • 0020451945 scopus 로고
    • Distribution of fibronectin in the early phase of avian cephalic neural crest cell migration
    • Duband JL, Thiery JP. 1982. Distribution of fibronectin in the early phase of avian cephalic neural crest cell migration. Dev Biol 93: 308-323.
    • (1982) Dev Biol , vol.93 , pp. 308-323
    • Duband, J.L.1    Thiery, J.P.2
  • 40
    • 0025940655 scopus 로고
    • Arrangement of cellular fibronectin in noncollagenous fibrils in human fibroblast cultures
    • Dzamba BJ, Peters DM. 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.2
  • 41
    • 11844275189 scopus 로고    scopus 로고
    • The integrin family of cell adhesion molecules
    • In, (ed. Beckerle MC),. Oxford University Press, Oxford
    • Dzamba BJ, Bolton MA, DeSimone DW. 2001. The integrin family of cell adhesion molecules. In Cell adhesion (ed. Beckerle MC), pp. 100-154. Oxford University Press, Oxford.
    • (2001) Cell adhesion , pp. 100-154
    • Dzamba, B.J.1    Bolton, M.A.2    DeSimone, D.W.3
  • 42
    • 61749097586 scopus 로고    scopus 로고
    • Cadherin adhesion, tissue tension, and noncanonical Wnt signaling regulate fibronectin matrix organization
    • Dzamba BJ, Jakab KR, Marsden M, Schwartz MA, DeSimone DW. 2009. Cadherin adhesion, tissue tension, and noncanonical Wnt signaling regulate fibronectin matrix organization. Dev Cell 16: 421-432.
    • (2009) Dev Cell , vol.16 , pp. 421-432
    • Dzamba, B.J.1    Jakab, K.R.2    Marsden, M.3    Schwartz, M.A.4    DeSimone, D.W.5
  • 43
    • 0017904884 scopus 로고
    • Some early history of cold-insoluble globulin
    • Edsall JT. 1978. Some early history of cold-insoluble globulin. Ann N Y Acad Sci 312: 1-10.
    • (1978) Ann N Y Acad Sci , vol.312 , pp. 1-10
    • Edsall, J.T.1
  • 44
    • 67649922824 scopus 로고    scopus 로고
    • A novel mode of cell detachment from fibrillar fibronectin matrix under shear
    • Engler AJ, Chan M, Boettiger D, Schwarzbauer JE. 2009. A novel mode of cell detachment from fibrillar fibronectin matrix under shear. J Cell Sci 122: 1647-1653.
    • (2009) J Cell Sci , vol.122 , pp. 1647-1653
    • Engler, A.J.1    Chan, M.2    Boettiger, D.3    Schwarzbauer, J.E.4
  • 45
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler AJ, Sen S, Sweeney HL, Discher DE. 2006. Matrix elasticity directs stem cell lineage specification. Cell 126: 677-689.
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 47
    • 0024406027 scopus 로고
    • Alternative splicing of fibronectin is temporally and spatially regulated in the chicken embryo
    • ffrench-Constant C, Hynes RO. 1989. Alternative splicing of fibronectin is temporally and spatially regulated in the chicken embryo. Development 106: 375-388.
    • (1989) Development , vol.106 , pp. 375-388
    • Ffrench-Constant, C.1    Hynes, R.O.2
  • 48
    • 0026316722 scopus 로고
    • Response to fibronectin of mouse primordial germ cells before, during and after migration
    • ffrench-Constant C, Hollingsworth A, Heasman J, Wylie CC. 1991. Response to fibronectin of mouse primordial germ cells before, during and after migration. Development 113: 1365-1373.
    • (1991) Development , vol.113 , pp. 1365-1373
    • Ffrench-Constant, C.1    Hollingsworth, A.2    Heasman, J.3    Wylie, C.C.4
  • 49
    • 0024344620 scopus 로고
    • Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat
    • ffrench-Constant C, Van DeWater L, Dvorak HF, Hynes RO. 1989. Reappearance of an embryonic pattern of fibronectin splicing during wound healing in the adult rat. J Cell Biol 109: 903-914.
    • (1989) J Cell Biol , vol.109 , pp. 903-914
    • Ffrench-Constant, C.1    Van DeWater, L.2    Dvorak, H.F.3    Hynes, R.O.4
  • 50
    • 21644448430 scopus 로고    scopus 로고
    • Cellular fibronectin binds to lysyl oxidase with high affinity and is critical for its proteolytic activation
    • Fogelgren B, Polgár N, Szauter KM, Ujfaludi Z, Laczkó R, Fong KS, Csiszar K. 2005. Cellular fibronectin binds to lysyl oxidase with high affinity and is critical for its proteolytic activation. J Biol Chem 280: 24690-24697.
    • (2005) J Biol Chem , vol.280 , pp. 24690-24697
    • Fogelgren, B.1    Polgár, N.2    Szauter, K.M.3    Ujfaludi, Z.4    Laczkó, R.5    Fong, K.S.6    Csiszar, K.7
  • 52
    • 0036790091 scopus 로고    scopus 로고
    • Mice lacking the EDB segment of fibronectin develop normally but exhibit reduced cell growth and fibronectin matrix assembly in vitro
    • Fukuda T, Yoshida N, Kataoka Y, Manabe R, Mizuno-Horikawa Y, Sato M, Kuriyama K, Yasui N, Sekiguchi K. 2002. Mice lacking the EDB segment of fibronectin develop normally but exhibit reduced cell growth and fibronectin matrix assembly in vitro. Cancer Res 62: 5603-5610.
    • (2002) Cancer Res , vol.62 , pp. 5603-5610
    • Fukuda, T.1    Yoshida, N.2    Kataoka, Y.3    Manabe, R.4    Mizuno-Horikawa, Y.5    Sato, M.6    Kuriyama, K.7    Yasui, N.8    Sekiguchi, K.9
  • 53
    • 36849083029 scopus 로고    scopus 로고
    • Requirements for sulfate transport and the diastrophic dysplasia sulfate transporter in fibronectin matrix assembly
    • Galante LL, Schwarzbauer JE. 2007. Requirements for sulfate transport and the diastrophic dysplasia sulfate transporter in fibronectin matrix assembly. J Cell Biol 179: 999-1009.
    • (2007) J Cell Biol , vol.179 , pp. 999-1009
    • Galante, L.L.1    Schwarzbauer, J.E.2
  • 54
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George EL, Georges-Labouesse EN, Patel-King RS, Rayburn H, Hynes RO. 1993. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development 119: 1079-1091.
    • (1993) Development , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges-Labouesse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 56
    • 3943102141 scopus 로고    scopus 로고
    • Planar cell polarity signalling controls cell division orientation during zebrafish gastrulation
    • Gong Y, Mo C, Fraser SE. 2004. Planar cell polarity signalling controls cell division orientation during zebrafish gastrulation. Nature 430: 689-693.
    • (2004) Nature , vol.430 , pp. 689-693
    • Gong, Y.1    Mo, C.2    Fraser, S.E.3
  • 59
    • 0028926188 scopus 로고
    • Mechanical properties of the extracellular matrix influence fibronectin fibril assembly in vitro
    • Halliday NL, Tomasek JJ. 1995. Mechanical properties of the extracellular matrix influence fibronectin fibril assembly in vitro. Exp Cell Res 217: 109-117.
    • (1995) Exp Cell Res , vol.217 , pp. 109-117
    • Halliday, N.L.1    Tomasek, J.J.2
  • 60
    • 0019800654 scopus 로고
    • Primordial germ cells of Xenopus embryos: The role of fibronectin in their adhesion during migration
    • Heasman J, Hynes RO, Swan AP, Thomas V, Wylie CC. 1981. Primordial germ cells of Xenopus embryos: The role of fibronectin in their adhesion during migration. Cell 27: 437-447.
    • (1981) Cell , vol.27 , pp. 437-447
    • Heasman, J.1    Hynes, R.O.2    Swan, A.P.3    Thomas, V.4    Wylie, C.C.5
  • 62
    • 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
  • 64
    • 0004043397 scopus 로고
    • Springer-Verlag, New York
    • Hynes RO. 1990. Fibronectins. Springer-Verlag, New York.
    • (1990) Fibronectins
    • Hynes, R.O.1
  • 65
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. 2002. Integrins: Bidirectional, allosteric signaling machines. Cell 110: 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 66
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: Not just pretty fibrils
    • Hynes RO. 2009. The extracellular matrix: Not just pretty fibrils. Science 326: 1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 67
    • 0034710157 scopus 로고    scopus 로고
    • The evolution of cell adhesion
    • Hynes RO, Zhao Q. 2000. The evolution of cell adhesion. J Cell Biol 150: F89-96.
    • (2000) J Cell Biol , vol.150 , pp. 89-96
    • Hynes, R.O.1    Zhao, Q.2
  • 69
    • 3142655415 scopus 로고    scopus 로고
    • Localization of a cryptic binding site for tenascin on fibronectin
    • Ingham KC, Brew SA, Erickson HP. 2004. Localization of a cryptic binding site for tenascin on fibronectin. J Biol Chem 279: 28132-28135.
    • (2004) J Biol Chem , vol.279 , pp. 28132-28135
    • Ingham, K.C.1    Brew, S.A.2    Erickson, H.P.3
  • 70
    • 0023906835 scopus 로고
    • Interaction of fibronectin and its gelatin-binding domainswith fluorescent-labeled chains of type I collagen
    • Ingham KC, Brew SA, Isaacs BS. 1988. Interaction of fibronectin and its gelatin-binding domainswith fluorescent-labeled chains of type I collagen. J Biol Chem 263: 4624-4628.
    • (1988) J Biol Chem , vol.263 , pp. 4624-4628
    • Ingham, K.C.1    Brew, S.A.2    Isaacs, B.S.3
  • 71
    • 0033016468 scopus 로고    scopus 로고
    • The compact conformation of fibronectin is determined by intramolecular ionic interactions
    • Johnson KJ, Sage H, Briscoe G, Erickson HP. 1999. The compact conformation of fibronectin is determined by intramolecular ionic interactions. J Biol Chem 274: 15473-15479.
    • (1999) J Biol Chem , vol.274 , pp. 15473-15479
    • Johnson, K.J.1    Sage, H.2    Briscoe, G.3    Erickson, H.P.4
  • 73
    • 20144388729 scopus 로고    scopus 로고
    • Integrinα5 and delta/notch signaling have complementary spatiotemporal requirements during zebrafish somitogenesis
    • Jülich D, Geisler R, Holley SA, Consortium TS. 2005. Integrinα5 and delta/notch signaling have complementary spatiotemporal requirements during zebrafish somitogenesis. Dev Cell 8: 575-586.
    • (2005) Dev Cell , vol.8 , pp. 575-586
    • Jülich, D.1    Geisler, R.2    Holley, S.A.3    Consortium, T.S.4
  • 74
    • 69049095026 scopus 로고    scopus 로고
    • Control of extracellular matrix assembly along tissue boundaries via Integrin and Eph/Ephrin signaling
    • Jülich D, Mould AP, Koper E, Holley SA. 2009. Control of extracellular matrix assembly along tissue boundaries via Integrin and Eph/Ephrin signaling. Development 136: 2913-2921.
    • (2009) Development , vol.136 , pp. 2913-2921
    • Jülich, D.1    Mould, A.P.2    Koper, E.3    Holley, S.A.4
  • 75
    • 0028131531 scopus 로고
    • Distribution of oncofetal fibronectin isoforms in normal, hyperplastic and neoplastic human breast tissues
    • Kaczmarek J, Castellani P, Nicolo G, Spina B, Allemanni G, Zardi L. 1994. Distribution of oncofetal fibronectin isoforms in normal, hyperplastic and neoplastic human breast tissues. Int J Cancer 59: 11-16.
    • (1994) Int J Cancer , vol.59 , pp. 11-16
    • Kaczmarek, J.1    Castellani, P.2    Nicolo, G.3    Spina, B.4    Allemanni, G.5    Zardi, L.6
  • 77
    • 51449116782 scopus 로고    scopus 로고
    • mRNA expression and protein distribution of fibronectin splice variants and high-molecular weight tenascin-C in different phases of human fracture healing
    • Kilian O, Dahse R, Alt V, Zardi L, Hentschel J, Schnettler R, Kosmehl H. 2008. mRNA expression and protein distribution of fibronectin splice variants and high-molecular weight tenascin-C in different phases of human fracture healing. Calcif Tissue Int 83: 101-111.
    • (2008) Calcif Tissue Int , vol.83 , pp. 101-111
    • Kilian, O.1    Dahse, R.2    Alt, V.3    Zardi, L.4    Hentschel, J.5    Schnettler, R.6    Kosmehl, H.7
  • 78
    • 0034003019 scopus 로고    scopus 로고
    • Control of extracellular matrix assembly by syndecan-2 proteoglycan
    • Klass CM, Couchman JR, Woods A. 2000. Control of extracellular matrix assembly by syndecan-2 proteoglycan. J Cell Sci 113: 493-506.
    • (2000) J Cell Sci , vol.113 , pp. 493-506
    • Klass, C.M.1    Couchman, J.R.2    Woods, A.3
  • 79
    • 0027582308 scopus 로고
    • Distribution of tenascin, cellular fibronectins and integrins in the normal, hyperplastic, and neoplastic breast
    • Koukoulis GK, Howeedy MK, Korhen M, Virtanen I, Gould VE. 1993. Distribution of tenascin, cellular fibronectins and integrins in the normal, hyperplastic, and neoplastic breast. J Submicrosc Cytol Pathol 25: 285-295.
    • (1993) J Submicrosc Cytol Pathol , vol.25 , pp. 285-295
    • Koukoulis, G.K.1    Howeedy, M.K.2    Korhen, M.3    Virtanen, I.4    Gould, V.E.5
  • 80
    • 33645086641 scopus 로고    scopus 로고
    • Regulation of somitogenesis by Ena/VASP proteins and FAK during Xenopus development
    • Kragtorp KA, Miller JR. 2006. Regulation of somitogenesis by Ena/VASP proteins and FAK during Xenopus development. Development 133: 685-695.
    • (2006) Development , vol.133 , pp. 685-695
    • Kragtorp, K.A.1    Miller, J.R.2
  • 81
    • 34548816484 scopus 로고    scopus 로고
    • 5 is required for somite rotation and boundary formation in Xenopus
    • 5 is required for somite rotation and boundary formation in Xenopus. Dev Dyn 236: 2713-2720.
    • (2007) Dev Dyn , vol.236 , pp. 2713-2720
    • Kragtorp, K.A.1    Miller, J.R.2
  • 82
    • 0036007121 scopus 로고    scopus 로고
    • Ectodermal syndecan-2 mediates left-right axis formation in migrating mesoderm as a cell-nonautonomous Vg1 cofactor
    • Kramer KL, Yost HJ. 2002. Ectodermal syndecan-2 mediates left-right axis formation in migrating mesoderm as a cell-nonautonomous Vg1 cofactor. Dev Cell 2: 115-124.
    • (2002) Dev Cell , vol.2 , pp. 115-124
    • Kramer, K.L.1    Yost, H.J.2
  • 83
    • 0023009694 scopus 로고
    • Distribution of a putative cell surface receptor for fibronectin and laminin in the avian embryo
    • Krotoski DM, Domingo C, Bronner-Fraser M. 1986. Distribution of a putative cell surface receptor for fibronectin and laminin in the avian embryo. J Cell Biol 103: 1061-1071.
    • (1986) J Cell Biol , vol.103 , pp. 1061-1071
    • Krotoski, D.M.1    Domingo, C.2    Bronner-Fraser, M.3
  • 84
    • 0033014330 scopus 로고    scopus 로고
    • Detection of alternative splicing of fibronectin mRNA in a single cell
    • Kumazaki T, Mitsui Y, Hamada K, Sumida H, Nishiyama M. 1999. Detection of alternative splicing of fibronectin mRNA in a single cell. J Cell Sci 112: 1449-1453.
    • (1999) J Cell Sci , vol.112 , pp. 1449-1453
    • Kumazaki, T.1    Mitsui, Y.2    Hamada, K.3    Sumida, H.4    Nishiyama, M.5
  • 85
    • 0033548441 scopus 로고    scopus 로고
    • Identification of proteindisulfide isomerase activity in fibronectin
    • Langenbach KJ, Sottile J. 1999. Identification of proteindisulfide isomerase activity in fibronectin. J Biol Chem 274: 7032-7038.
    • (1999) J Biol Chem , vol.274 , pp. 7032-7038
    • Langenbach, K.J.1    Sottile, J.2
  • 86
    • 76549121557 scopus 로고    scopus 로고
    • Extracellular matrix assembly and organization during zebrafish gastrulation
    • Latimer A, Jessen JR. 2010. Extracellular matrix assembly and organization during zebrafish gastrulation. Matrix Biol 29: 89-96.
    • (2010) Matrix Biol , vol.29 , pp. 89-96
    • Latimer, A.1    Jessen, J.R.2
  • 87
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Acrystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy DJ, Aukhil I, EricksonHP. 1996. 2.0 Acrystal 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
  • 88
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP. 1992. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258: 987-991.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 89
    • 34547191723 scopus 로고    scopus 로고
    • Cell surface mechanics and the control of cell shape, tissue patterns and morphogenesis
    • Lecuit T, Lenne P-F. 2007. Cell surface mechanics and the control of cell shape, tissue patterns and morphogenesis. Nat Rev Mol Cell Biol 8: 633-644.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 633-644
    • Lecuit, T.1    Lenne, P.-F.2
  • 90
    • 0021247591 scopus 로고
    • Temporal and spatial regulation of fibronectin in early Xenopus development
    • Lee G, Hynes R, Kirschner M. 1984. Temporal and spatial regulation of fibronectin in early Xenopus development. Cell 36: 729-740.
    • (1984) Cell , vol.36 , pp. 729-740
    • Lee, G.1    Hynes, R.2    Kirschner, M.3
  • 92
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
    • Litvinovich SV, BrewSA, Aota S, Akiyama SK, Haudenschild C, InghamKC. 1998. Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J Mol Biol 280: 245-258.
    • (1998) J Mol Biol , vol.280 , pp. 245-258
    • Litvinovich, S.V.1    Brew, S.A.2    Aota, S.3    Akiyama, S.K.4    Haudenschild, C.5    Ingham, K.C.6
  • 93
    • 0029779356 scopus 로고    scopus 로고
    • Fibronectin mRNA splice variant in articular cartilage lacks bases encoding the V, III-15, and I-10 protein segments
    • MacLeod JN, Burton-Wurster N, Gu DN, Lust G. 1996. Fibronectin mRNA splice variant in articular cartilage lacks bases encoding the V, III-15, and I-10 protein segments. J Biol Chem 271: 18954-18960.
    • (1996) J Biol Chem , vol.271 , pp. 18954-18960
    • McLeod, J.N.1    Burton-Wurster, N.2    Gu, D.N.3    Lust, G.4
  • 94
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main AL, Harvey TS, Baron M, Boyd J, Campbell ID. 1992. The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions. Cell 71: 671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 95
    • 0030753274 scopus 로고    scopus 로고
    • Modulation of cell-adhesive activity of fibronectin by the alternatively spliced EDA segment
    • Manabe R, Oh-e N, Maeda T, Fukuda T, Sekiguchi K. 1997. Modulation of cell-adhesive activity of fibronectin by the alternatively spliced EDA segment. J Cell Biol 139: 295-307.
    • (1997) J Cell Biol , vol.139 , pp. 295-307
    • Manabe, R.1    Oh-e, N.2    Maeda, T.3    Fukuda, T.4    Sekiguchi, K.5
  • 96
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • Mao Y, Schwarzbauer JE. 2005. Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol 24: 389-399.
    • (2005) Matrix Biol , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 98
    • 0034796439 scopus 로고    scopus 로고
    • Regulation of cell polarity, radial intercalation and epiboly in Xenopus: Novel roles for integrin and fibronectin
    • Marsden M, DeSimone DW. 2001. Regulation of cell polarity, radial intercalation and epiboly in Xenopus: Novel roles for integrin and fibronectin. Development 128: 3635-3647.
    • (2001) Development , vol.128 , pp. 3635-3647
    • Marsden, M.1    DeSimone, D.W.2
  • 99
    • 0037700454 scopus 로고    scopus 로고
    • Integrin-ECM interactions regulate cadherin-dependent cell adhesion and are required for convergent extension in Xenopus
    • Marsden M, DeSimone DW. 2003. Integrin-ECM interactions regulate cadherin-dependent cell adhesion and are required for convergent extension in Xenopus. Curr Biol 13: 1182-1191.
    • (2003) Curr Biol , vol.13 , pp. 1182-1191
    • Marsden, M.1    DeSimone, D.W.2
  • 100
    • 0023831538 scopus 로고
    • The oncofetal structure of human fibronectin defined by monoclonal antibody FDC-6. Unique structural requirement for the antigenic specificity provided by a glycosylhexapeptide
    • Matsuura H, Takio K, Titani K, Greene T, Levery SB, Salyan ME, Hakomori S. 1988. The oncofetal structure of human fibronectin defined by monoclonal antibody FDC-6. Unique structural requirement for the antigenic specificity provided by a glycosylhexapeptide. J Biol Chem 263: 3314-3322.
    • (1988) J Biol Chem , vol.263 , pp. 3314-3322
    • Matsuura, H.1    Takio, K.2    Titani, K.3    Greene, T.4    Levery, S.B.5    Salyan, M.E.6    Hakomori, S.7
  • 101
    • 1842426730 scopus 로고    scopus 로고
    • Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment
    • McBeath R, Pirone DM, Nelson CM, Bhadriraju K, Chen CS. 2004. Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment. Dev Cell 6: 483-495.
    • (2004) Dev Cell , vol.6 , pp. 483-495
    • McBeath, R.1    Pirone, D.M.2    Nelson, C.M.3    Bhadriraju, K.4    Chen, C.S.5
  • 102
    • 0024150414 scopus 로고
    • Extracellular matrix assembly
    • McDonald JA. 1988. Extracellular matrix assembly. Annu Rev Cell Biol 4: 183-207.
    • (1988) Annu Rev Cell Biol , vol.4 , pp. 183-207
    • McDonald, J.A.1
  • 103
    • 0023178166 scopus 로고
    • Fibronectin's cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix
    • McDonald JA, Quade BJ, Broekelman 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 into 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    Broekelman, T.J.3    LaChance, R.4    Forsman, K.5    Hasegawa, E.6    Akiyama, S.7
  • 104
    • 0020601855 scopus 로고
    • Binding of plasma fibronectin to cell layers of human skin fibroblasts
    • McKeown-Longo PJ, Mosher DF. 1983. Binding of plasma fibronectin to cell layers of human skin fibroblasts. J Cell Biol 97: 466-472.
    • (1983) J Cell Biol , vol.97 , pp. 466-472
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 105
    • 0021926873 scopus 로고
    • Interaction of the 70,000-mol. wt. amino terminal fragment of fibronectin with matrix-assembly receptor of fibroblasts
    • McKeown-Longo PJ, Mosher DF. 1985. Interaction of the 70,000-mol. wt. amino terminal fragment of fibronectin with 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
  • 106
    • 34948854409 scopus 로고    scopus 로고
    • A major fraction of fibronectin present in the extracellular matrix of tissues is plasma-derived
    • Moretti FA, Chauhan AK, Iaconcig A, Porro F, Baralle FE, Muro AF. 2007. A major fraction of fibronectin present in the extracellular matrix of tissues is plasma-derived. J Biol Chem 282: 28057-28062.
    • (2007) J Biol Chem , vol.282 , pp. 28057-28062
    • Moretti, F.A.1    Chauhan, A.K.2    Iaconcig, A.3    Porro, F.4    Baralle, F.E.5    Muro, A.F.6
  • 107
    • 36448970493 scopus 로고    scopus 로고
    • Synergistic control of cell adhesion by integrins and syndecans
    • Morgan MR, Humphries MJ, Bass MD. 2007. Synergistic control of cell adhesion by integrins and syndecans. Nature Rev Mol Cell Biol 8: 957-969.
    • (2007) Nature Rev Mol Cell Biol , vol.8 , pp. 957-969
    • Morgan, M.R.1    Humphries, M.J.2    Bass, M.D.3
  • 108
    • 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
  • 109
    • 0028069348 scopus 로고
    • Superfibronectin is a functionally distinct form of fibronectin
    • Morla A, Zhang Z, Ruoslahtl 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    Ruoslahtl, E.3
  • 110
    • 0016719143 scopus 로고
    • Cross-linking of cold-insoluble globulin by fibrin stabilizing factor
    • Mosher DF. 1975. Cross-linking of cold-insoluble globulin by fibrin stabilizing factor. J Biol Chem 260: 6614-6621.
    • (1975) J Biol Chem , vol.260 , pp. 6614-6621
    • Mosher, D.F.1
  • 111
    • 0004133195 scopus 로고
    • Academic Press, New York
    • Mosher DF, ed. 1989. Fibronectin. Academic Press, New York.
    • (1989) Fibronectin
    • Mosher, D.F.1
  • 112
    • 0035109876 scopus 로고    scopus 로고
    • Identification of a novel heparin-binding site in the alternatively spliced IIICS region of fibronectin: Roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants
    • Mostafavi-Pour Z, Askari JA, Whittard JD, Humphries MJ. 2001. Identification of a novel heparin-binding site in the alternatively spliced IIICS region of fibronectin: Roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants. Matrix Biol 20: 63-73.
    • (2001) Matrix Biol , vol.20 , pp. 63-73
    • Mostafavi-Pour, Z.1    Askari, J.A.2    Whittard, J.D.3    Humphries, M.J.4
  • 114
    • 33744997855 scopus 로고    scopus 로고
    • Syndecan-4 regulates non-canonical Wnt signalling and is essential for convergent and extension movements in Xenopus embryos
    • Muñoz R, Moreno M, Oliva C, Orbenes C, Larraín J. 2006. Syndecan-4 regulates non-canonical Wnt signalling and is essential for convergent and extension movements in Xenopus embryos. Nat Cell Biol 8: 492-500.
    • (2006) Nat Cell Biol , vol.8 , pp. 492-500
    • Muñoz, R.1    Moreno, M.2    Oliva, C.3    Orbenes, C.4    Larraín, J.5
  • 115
    • 0038825157 scopus 로고    scopus 로고
    • Regulated splicing of the fibronectin EDA exon is essential for proper skin wound healing and normal lifespan
    • Muro AF, Chauhan AK, Gajovic S, Iaconcig A, Porro F, Stanta G, Baralle FE. 2003. Regulated splicing of the fibronectin EDA exon is essential for proper skin wound healing and normal lifespan. J Cell Biol 162: 149-160.
    • (2003) J Cell Biol , vol.162 , pp. 149-160
    • Muro, A.F.1    Chauhan, A.K.2    Gajovic, S.3    Iaconcig, A.4    Porro, F.5    Stanta, G.6    Baralle, F.E.7
  • 116
    • 0025948419 scopus 로고
    • Monoclonal antibody characterization of two distant 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 distant 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
  • 117
    • 0032967173 scopus 로고    scopus 로고
    • Establishment of substratum polarity in the blastocoel roof of the Xenopus embryo
    • Nagel M, Winklbauer R. 1999. Establishment of substratum polarity in the blastocoel roof of the Xenopus embryo. Development 126: 1975-1984.
    • (1999) Development , vol.126 , pp. 1975-1984
    • Nagel, M.1    Winklbauer, R.2
  • 118
    • 3042852882 scopus 로고    scopus 로고
    • Guidance of mesoderm cell migration in the Xenopus gastrula requires PDGF signaling
    • Nagel M, Tahinci E, Symes K, Winklbauer R. 2004. Guidance of mesoderm cell migration in the Xenopus gastrula requires PDGF signaling. Development 131: 2727-2736.
    • (2004) Development , vol.131 , pp. 2727-2736
    • Nagel, M.1    Tahinci, E.2    Symes, K.3    Winklbauer, R.4
  • 119
    • 0020647702 scopus 로고
    • Conditioning of a culture substratum by the ectodermal layer promotes attachment and oriented locomotion by amphibian gastrula mesodermal cells
    • Nakatsuji N, Johnson KE. 1983. Conditioning of a culture substratum by the ectodermal layer promotes attachment and oriented locomotion by amphibian gastrula mesodermal cells. J Cell Sci 59: 43-60
    • (1983) J Cell Sci , vol.59 , pp. 43-60
    • Nakatsuji, N.1    Johnson, K.E.2
  • 120
    • 0021234344 scopus 로고
    • Experimental manipulation of a contact guidance system in amphibian gastrulation by mechanical tension
    • Nakatsuji N, Johnson KE. 1984. Experimental manipulation of a contact guidance system in amphibian gastrulation by mechanical tension. Nature 307: 453-5
    • (1984) Nature , vol.307 , pp. 453-455
    • Nakatsuji, N.1    Johnson, K.E.2
  • 121
    • 0020332992 scopus 로고
    • Movement and guidance of migrating mesodermal cells in Ambystoma maculatum gastrulae
    • Nakatsuji N, Gould AC, Johnson KE. 1982. Movement and guidance of migrating mesodermal cells in Ambystoma maculatum gastrulae. J Cell Sci 56: 207-222.
    • (1982) J Cell Sci , vol.56 , pp. 207-222
    • Nakatsuji, N.1    Gould, A.C.2    Johnson, K.E.3
  • 123
    • 0023506887 scopus 로고
    • Alternative splicing of chicken fibronectin in embryos and in normal and transformed cells
    • Norton PA, Hynes RO. 1987. Alternative splicing of chicken fibronectin in embryos and in normal and transformed cells. Mol Cell Biol 7: 4297-4307.
    • (1987) Mol Cell Biol , vol.7 , pp. 4297-4307
    • Norton, P.A.1    Hynes, R.O.2
  • 124
    • 28244461501 scopus 로고    scopus 로고
    • Domain unfolding plays a role in superfibronectin formation
    • Ohashi T, Erickson HP. 2005. Domain unfolding plays a role in superfibronectin formation. J Biol Chem 280: 39143-39151.
    • (2005) J Biol Chem , vol.280 , pp. 39143-39151
    • Ohashi, T.1    Erickson, H.P.2
  • 125
    • 67349229153 scopus 로고    scopus 로고
    • Revisiting themystery of fibronectin multimers: The fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds
    • Ohashi T, EricksonHP. 2009. Revisiting themystery of fibronectin multimers: The fibronectin matrix is composed of fibronectin dimers cross-linked by non-covalent bonds. Matrix Biol 28: 170-175.
    • (2009) Matrix Biol , vol.28 , pp. 170-175
    • Ohashi, T.1    Erickson, H.P.2
  • 126
    • 0033515070 scopus 로고    scopus 로고
    • Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein
    • Ohashi T, Kiehart DP, Erickson HP. 1999. Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein. Proc Natl Acad Sci 96: 2153-2158.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 2153-2158
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 127
    • 0037087773 scopus 로고    scopus 로고
    • Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants
    • Ohashi T, Kiehart DP, Erickson HP. 2002. Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants. J Cell Sci 115: 1221-1229.
    • (2002) J Cell Sci , vol.115 , pp. 1221-1229
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 128
    • 0035412363 scopus 로고    scopus 로고
    • Assembly of a fibronectin matrix by adherent platelets stimulated by lysophosphatidic acid and other agonists
    • Olorundare OE, Peyruchaud O, Albrecht RM, Mosher DF. 2001. Assembly of a fibronectin matrix by adherent platelets stimulated by lysophosphatidic acid and other agonists. Blood 98: 117-124.
    • (2001) Blood , vol.98 , pp. 117-124
    • Olorundare, O.E.1    Peyruchaud, O.2    Albrecht, R.M.3    Mosher, D.F.4
  • 130
    • 0027315769 scopus 로고
    • Coordinate oncodevelopmental modulation of alternative splicing of fibronectin pre-messenger RNA at ED-A, ED-B, and CS1 regions in human liver tumors
    • Oyama F, Hirohashi S, Sakamoto M, Titani K, Sekiguchi K. 1993. Coordinate oncodevelopmental modulation of alternative splicing of fibronectin pre-messenger RNA at ED-A, ED-B, and CS1 regions in human liver tumors. Cancer Res 53: 2005-2011.
    • (1993) Cancer Res , vol.53 , pp. 2005-2011
    • Oyama, F.1    Hirohashi, S.2    Sakamoto, M.3    Titani, K.4    Sekiguchi, K.5
  • 131
    • 0024550609 scopus 로고
    • Patterns of alternative splicing of fibronectin pre-mRNA in human adult and fetal tissues
    • Oyama F, Murata Y, Suganuma N, Kimura T, Titani K, Sekiguchi K. 1989. Patterns of alternative splicing of fibronectin pre-mRNA in human adult and fetal tissues. Biochemistry 28: 1428-1434.
    • (1989) Biochemistry , vol.28 , pp. 1428-1434
    • Oyama, F.1    Murata, Y.2    Suganuma, N.3    Kimura, T.4    Titani, K.5    Sekiguchi, K.6
  • 132
    • 0025718766 scopus 로고
    • Tissue-specific splicing pattern of fibronectin messenger RNA precursor during development and aging in rat
    • Pagani F, Zagato L, Vergani C, Casari G, Sidoli A, Baralle FE. 1991. Tissue-specific splicing pattern of fibronectin messenger RNA precursor during development and aging in rat. J Cell Biol 113: 1223-1229.
    • (1991) J Cell Biol , vol.113 , pp. 1223-1229
    • Pagani, F.1    Zagato, L.2    Vergani, C.3    Casari, G.4    Sidoli, A.5    Baralle, F.E.6
  • 134
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R, Yamada KM. 2002. Fibronectin at a glance. J Cell Sci 115: 3861-3863.
    • (2002) J Cell Sci , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 137
    • 0036665564 scopus 로고    scopus 로고
    • Spatial expression of the alternatively spliced EIIIB and EIIIA segments of fibronectin in the early chicken embryo
    • Peters J, Sechrist J, Luetolf S, Loredo G, Bronner-Fraser M. 2002. Spatial expression of the alternatively spliced EIIIB and EIIIA segments of fibronectin in the early chicken embryo. Cell Commun Adhes 9: 221-238.
    • (2002) Cell Commun Adhes , vol.9 , pp. 221-238
    • Peters, J.1    Sechrist, J.2    Luetolf, S.3    Loredo, G.4    Bronner-Fraser, M.5
  • 139
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher MD, Ruoslahti E. 1984. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309: 30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 140
    • 0027416842 scopus 로고
    • Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin
    • Radek JT, Jeong J-M, Prasanna Murthy SN, Ingham K, Lorand L. 1993. Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin. Proc Natl Acad Sci 90: 3152-3156.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 3152-3156
    • Radek, J.T.1    Jeong, J-M.2    Prasanna Murthy, S.N.3    Ingham, K.4    Lorand, L.5
  • 141
    • 0035894536 scopus 로고    scopus 로고
    • Dorsoventral differences in cell-cell interactions modulate the motile behaviour of cells from the Xenopus gastrula
    • Reintsch WE, Hausen P. 2001. Dorsoventral differences in cell-cell interactions modulate the motile behaviour of cells from the Xenopus gastrula. Dev Biol 240: 387-403.
    • (2001) Dev Biol , vol.240 , pp. 387-403
    • Reintsch, W.E.1    Hausen, P.2
  • 142
    • 0020581958 scopus 로고
    • Neural crest cell migration: Requirements for exogenous fibronectin and high cell density
    • Rovasio RA, Delouvee A, Yamada KM, Timpl R, Thiery JP. 1983. Neural crest cell migration: Requirements for exogenous fibronectin and high cell density. J Cell Biol 96: 462-473.
    • (1983) J Cell Biol , vol.96 , pp. 462-473
    • Rovasio, R.A.1    Delouvee, A.2    Yamada, K.M.3    Timpl, R.4    Thiery, J.P.5
  • 143
    • 77951234989 scopus 로고    scopus 로고
    • The extracellular matrix in development and morphogenesis: A dynamic view
    • Rozario T, DeSimone DW. 2010. The extracellular matrix in development and morphogenesis: A dynamic view. Dev Biol 341: 126-140.
    • (2010) Dev Biol , vol.341 , pp. 126-140
    • Rozario, T.1    DeSimone, D.W.2
  • 144
    • 60549114314 scopus 로고    scopus 로고
    • The physical state of fibronectin matrix differentially regulates morphogenetic movements in vivo
    • Rozario T, Dzamba B, Weber G, Davidson L, Desimone D. 2009. The physical state of fibronectin matrix differentially regulates morphogenetic movements in vivo. Dev Biol 327: 386-398.
    • (2009) Dev Biol , vol.327 , pp. 386-398
    • Rozario, T.1    Dzamba, B.2    Weber, G.3    Davidson, L.4    Desimone, D.5
  • 147
    • 0038141338 scopus 로고    scopus 로고
    • Fibronectin requirement in branching morphogenesis
    • Sakai T, Larsen M, Yamada KM. 2003. Fibronectin requirement in branching morphogenesis. Nature 423: 876-881.
    • (2003) Nature , vol.423 , pp. 876-881
    • Sakai, T.1    Larsen, M.2    Yamada, K.M.3
  • 148
    • 0020335112 scopus 로고
    • Ultrastructural immunocytochemical localization of fibronectin in the early chick embryo
    • Sanders EJ. 1982. Ultrastructural immunocytochemical localization of fibronectin in the early chick embryo. J Embryol Exp Morphol 71: 155-170.
    • (1982) J Embryol Exp Morphol , vol.71 , pp. 155-170
    • Sanders, E.J.1
  • 149
    • 0037134508 scopus 로고    scopus 로고
    • Alternative splicing of the IIICS domain in fibronectin governs the role of the heparin II domain in fibrillogenesis and cell spreading
    • Santas AJ, Peterson JA, Halbleib JL, Craig SE, Humphries MJ, Peters DM. 2002. Alternative splicing of the IIICS domain in fibronectin governs the role of the heparin II domain in fibrillogenesis and cell spreading. J Biol Chem 277: 13650-13658.
    • (2002) J Biol Chem , vol.277 , pp. 13650-13658
    • Santas, A.J.1    Peterson, J.A.2    Halbleib, J.L.3    Craig, S.E.4    Humphries, M.J.5    Peters, D.M.6
  • 150
    • 0023884069 scopus 로고
    • Cell surface proteoglycan binds mouse mammary epithelial cells to fibronectin and behaves as a receptor for interstitial matrix
    • Saunders S, Bernfield M. 1988. Cell surface proteoglycan binds mouse mammary epithelial cells to fibronectin and behaves as a receptor for interstitial matrix. J Cell Biol 106: 423-430.
    • (1988) J Cell Biol , vol.106 , pp. 423-430
    • Saunders, S.1    Bernfield, M.2
  • 151
    • 0032910347 scopus 로고    scopus 로고
    • Identification of fibronectin IIICS variants in human bone marrow stroma
    • Schofield KP, Humphries MJ. 1999. Identification of fibronectin IIICS variants in human bone marrow stroma. Blood 93: 410-411.
    • (1999) Blood , vol.93 , pp. 410-411
    • Schofield, K.P.1    Humphries, M.J.2
  • 152
    • 33748209542 scopus 로고    scopus 로고
    • Fibronectinbinding proteins of gram-positive cocci
    • Schwarz-Linek U, Höök M, Potts JR. 2006. Fibronectinbinding proteins of gram-positive cocci. Microbes Infect 8: 2291-2298.
    • (2006) Microbes Infect , vol.8 , pp. 2291-2298
    • Schwarz-Linek, U.1    Höök, M.2    Potts, J.R.3
  • 153
    • 0025744802 scopus 로고
    • Fibronectin: From gene to protein
    • Schwarzbauer JE. 1991a. Fibronectin: From gene to protein. Curr Opin Cell Biol 3: 786-791.
    • (1991) Curr Opin Cell Biol , vol.3 , pp. 786-791
    • Schwarzbauer, J.E.1
  • 154
    • 0025896188 scopus 로고
    • Identification of the fibronectin sequences required for assembly of a fibrillar matrix
    • Schwarzbauer JE. 1991b. 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
  • 155
    • 0024804591 scopus 로고
    • Selective secretion of alternatively spliced fibronectin variants
    • Schwarzbauer JE, Spencer CS, Wilson CL. 1989. Selective secretion of alternatively spliced fibronectin variants. J Cell Biol 109: 3445-3453.
    • (1989) J Cell Biol , vol.109 , pp. 3445-3453
    • Schwarzbauer, J.E.1    Spencer, C.S.2    Wilson, C.L.3
  • 156
    • 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
  • 157
    • 0021042241 scopus 로고
    • Three different fibronectin mRNAs arise by alternative splicing within the coding region
    • Schwarzbauer JE, Tamkun JW, Lemischka IR, Hynes RO. 1983. Three different fibronectin mRNAs arise by alternative splicing within the coding region. Cell 35: 421-431.
    • (1983) Cell , vol.35 , pp. 421-431
    • Schwarzbauer, J.E.1    Tamkun, J.W.2    Lemischka, I.R.3    Hynes, R.O.4
  • 158
    • 0030659845 scopus 로고    scopus 로고
    • Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly
    • Sechler JL, Corbett SA, Schwarzbauer JE. 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.E.3
  • 160
    • 0035802114 scopus 로고    scopus 로고
    • A novel fibronectin binding site required for fibronectin fibril growth during matrix assembly
    • Sechler JL, Rao H, Cumiskey AM, Vega-Colon I, Smith MS, et al. 2001. A novel fibronectin binding site required for fibronectin fibril growth during matrix assembly. J Cell Biol 154: 1081-1088.
    • (2001) J Cell Biol , vol.154 , pp. 1081-1088
    • Sechler, J.L.1    Rao, H.2    Cumiskey, A.M.3    Vega-Colon, I.4    Smith, M.S.5
  • 161
    • 0030036963 scopus 로고    scopus 로고
    • Altered rate of fibronectin matrix assembly by deletion of the first type III repeats
    • Sechler JL, Takada Y, Schwarzbauer JE. 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.E.3
  • 162
    • 0023234627 scopus 로고
    • Experimental analysis of the extension of the dorsal marginal zone in Pleurodeleswaltl gastrulae
    • Shi DL, Delarue M, Darribere T, Riou JF, Boucaut J-C. 1987. Experimental analysis of the extension of the dorsal marginal zone in Pleurodeleswaltl gastrulae. Development 100: 147-161.
    • (1987) Development , vol.100 , pp. 147-161
    • Shi, D.L.1    Delarue, M.2    Darribere, T.3    Riou, J.F.4    Boucaut, J.-C.5
  • 165
    • 0027364276 scopus 로고
    • Protein kinase C modulation of fibronectin matrix assembly
    • Somers CE, Mosher DF. 1993. Protein kinase C modulation of fibronectin matrix assembly. J Biol Chem 268: 22277-22280.
    • (1993) J Biol Chem , vol.268 , pp. 22277-22280
    • Somers, C.E.1    Mosher, D.F.2
  • 166
    • 0025772946 scopus 로고
    • Five type I modules of fibronectin form a functional unit that binds to fibroblasts and Staphylococcus aureus
    • Sottile J, Schwarzbauer JE, 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.E.2    Selegue, J.3    Mosher, D.F.4
  • 170
    • 3042708208 scopus 로고    scopus 로고
    • Deletion of the alternatively spliced fibronectin EIIIA domain in mice reduces atherosclerosis
    • Tan MH, Sun Z, Opitz SL, Schmidt TE, Peters JH, George EL. 2004. Deletion of the alternatively spliced fibronectin EIIIA domain in mice reduces atherosclerosis. Blood 104: 11-18.
    • (2004) Blood , vol.104 , pp. 11-18
    • Tan, M.H.1    Sun, Z.2    Opitz, S.L.3    Schmidt, T.E.4    Peters, J.H.5    George, E.L.6
  • 171
    • 32044469141 scopus 로고    scopus 로고
    • The monoclonal antibody SM5-1 recognizes a fibronectin variant whcih is widely expressed in melanoma
    • Trefzer U, Chen Y, Herberth G, Hofmann MA, Kiecker F, Guo Y, Sterry W. 2006. The monoclonal antibody SM5-1 recognizes a fibronectin variant whcih is widely expressed in melanoma. BMC Cancer 6: 8.
    • (2006) BMC Cancer , vol.6 , pp. 8
    • Trefzer, U.1    Chen, Y.2    Herberth, G.3    Hofmann, M.A.4    Kiecker, F.5    Guo, Y.6    Sterry, W.7
  • 172
    • 1642318780 scopus 로고    scopus 로고
    • Fibronectin regulates epithelial organization during myocardial migration in zebrafish
    • Trinh LA, Stainier DYR. 2004. Fibronectin regulates epithelial organization during myocardial migration in zebrafish. Dev Cell 6: 371-382.
    • (2004) Dev Cell , vol.6 , pp. 371-382
    • Trinh, L.A.1    Stainier, D.Y.R.2
  • 173
    • 0032063303 scopus 로고    scopus 로고
    • Presence of a fibronectin type III domain in a plant protein
    • Tsyguelnaia I, Doolittle RF. 1998. Presence of a fibronectin type III domain in a plant protein. J Mol Evol 46: 612-614.
    • (1998) J Mol Evol , vol.46 , pp. 612-614
    • Tsyguelnaia, I.1    Doolittle, R.F.2
  • 174
    • 56949084574 scopus 로고    scopus 로고
    • Evidence for the evolution of tenascin and fibronectin early in the chordate lineage
    • Tucker RP, Chiquet-Ehrismann R. 2009. Evidence for the evolution of tenascin and fibronectin early in the chordate lineage. Int J Biochem Cell Biol 41: 424-434.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 424-434
    • Tucker, R.P.1    Chiquet-Ehrismann, R.2
  • 176
    • 34249067404 scopus 로고    scopus 로고
    • Interdomain association in fibronectin: Insight into cryptic sites and fibrillogenesis
    • Vakonakis I, Staunton D, Rooney LM, Campbell ID. 2007. Interdomain association in fibronectin: Insight into cryptic sites and fibrillogenesis. EMBO J 26: 2575-2783.
    • (2007) EMBO J , vol.26 , pp. 2575-2783
    • Vakonakis, I.1    Staunton, D.2    Rooney, L.M.3    Campbell, I.D.4
  • 178
    • 77949344954 scopus 로고    scopus 로고
    • Alternative splicing of the angiogenesis associated extra-domain B of fibronectin regulates the accessibility of the B-C loop of the type III repeat 8
    • Ventura E, Sassi F, Parodi A, Balza E, Borsi L, Castellani P, Carnemolla B, Zardi L. 2010. Alternative splicing of the angiogenesis associated extra-domain B of fibronectin regulates the accessibility of the B-C loop of the type III repeat 8. PLoS One 5: e9145.
    • (2010) PLoS One , vol.5
    • Ventura, E.1    Sassi, F.2    Parodi, A.3    Balza, E.4    Borsi, L.5    Castellani, P.6    Carnemolla, B.7    Zardi, L.8
  • 181
    • 0033956345 scopus 로고    scopus 로고
    • Formation of the avian primitive streak from spatially restricted blastoderm: Evidence for polarized cell division in the elongating streak
    • Wei Y, Mikawa T. 2000. Formation of the avian primitive streak from spatially restricted blastoderm: Evidence for polarized cell division in the elongating streak. Development 127: 87-96.
    • (2000) Development , vol.127 , pp. 87-96
    • Wei, Y.1    Mikawa, T.2
  • 184
    • 0037205416 scopus 로고    scopus 로고
    • Regulatory role for Src and phosphatidylinositol 3-kinase in initiation of fibronectin matrix assembly
    • Wierzbicka-Patynowski I, Schwarzbauer JE. 2002. Regulatory role for Src and phosphatidylinositol 3-kinase in initiation of fibronectin matrix assembly. J Biol Chem 277: 19703-19708.
    • (2002) J Biol Chem , vol.277 , pp. 19703-19708
    • Wierzbicka-Patynowski, I.1    Schwarzbauer, J.E.2
  • 185
    • 0042887252 scopus 로고    scopus 로고
    • The ins and outs of fibronectin matrix assembly
    • Wierzbicka-Patynowski I, Schwarzbauer JE. 2003. The ins and outs of fibronectin matrix assembly. J Cell Sci 116: 3269-3276.
    • (2003) J Cell Sci , vol.116 , pp. 3269-3276
    • Wierzbicka-Patynowski, I.1    Schwarzbauer, J.E.2
  • 186
    • 33846606023 scopus 로고    scopus 로고
    • Continuous requirement for pp60-Src and phosphopaxillin during fibronectin matrix assembly by transformed cells
    • Wierzbicka-Patynowski I, Mao Y, Schwarzbauer JE. 2007. Continuous requirement for pp60-Src and phosphopaxillin during fibronectin matrix assembly by transformed cells. J Cell Physiol 210: 750-756.
    • (2007) J Cell Physiol , vol.210 , pp. 750-756
    • Wierzbicka-Patynowski, I.1    Mao, Y.2    Schwarzbauer, J.E.3
  • 187
    • 0026441355 scopus 로고
    • The alternatively spliced V region contributes to the differential incorporation of plasma and cellular fibronectins into fibrin clots
    • Wilson CL, Schwarzbauer JE. 1992. The alternatively spliced V region contributes to the differential incorporation of plasma and cellular fibronectins into fibrin clots. J Cell Biol 119: 923-933.
    • (1992) J Cell Biol , vol.119 , pp. 923-933
    • Wilson, C.L.1    Schwarzbauer, J.E.2
  • 188
    • 0031782720 scopus 로고    scopus 로고
    • Conditions for fibronectin fibril formation in the early Xenopus embryo
    • Winklbauer R. 1998. Conditions for fibronectin fibril formation in the early Xenopus embryo. Dev Dyn 212: 335-345.
    • (1998) Dev Dyn , vol.212 , pp. 335-345
    • Winklbauer, R.1
  • 189
    • 0030220280 scopus 로고    scopus 로고
    • Fibronectin, mesoderm migration, and gastrulation in Xenopus
    • Winklbauer R, Keller RE. 1996. Fibronectin, mesoderm migration, and gastrulation in Xenopus. Dev Biol 177: 413-426.
    • (1996) Dev Biol , vol.177 , pp. 413-426
    • Winklbauer, R.1    Keller, R.E.2
  • 191
    • 0027178087 scopus 로고
    • Cell interaction and its role in mesoderm cell migration during Xenopus gastrulation
    • Winklbauer R, Selchow A, Nagel M, Angres B. 1992. Cell interaction and its role in mesoderm cell migration during Xenopus gastrulation. Dev Dyn 195: 290-302.
    • (1992) Dev Dyn , vol.195 , pp. 290-302
    • Winklbauer, R.1    Selchow, A.2    Nagel, M.3    Angres, B.4
  • 192
    • 0032080892 scopus 로고    scopus 로고
    • Syndecans: Synergistic activators of cell adhesion
    • Woods A, Couchman JR. 1998. Syndecans: Synergistic activators of cell adhesion. Trends Cell Biol 8: 189-194.
    • (1998) Trends Cell Biol , vol.8 , pp. 189-194
    • Woods, A.1    Couchman, J.R.2
  • 193
    • 0034142030 scopus 로고    scopus 로고
    • Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts
    • Woods A, Longley RL, Tumova S, Couchman JR. 2000. Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. Arch Biochem Biophys 374: 66-72.
    • (2000) Arch Biochem Biophys , vol.374 , pp. 66-72
    • Woods, A.1    Longley, R.L.2    Tumova, S.3    Couchman, J.R.4
  • 194
    • 0027422170 scopus 로고
    • 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly
    • 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
  • 198
    • 23744480002 scopus 로고    scopus 로고
    • The Rho kinases I and II regulate different aspects of myosin II activity
    • Yoneda A, Multhaupt HAB, Couchman JR. 2005. The Rho kinases I and II regulate different aspects of myosin II activity. J Cell Biol 170: 443-453.
    • (2005) J Cell Biol , vol.170 , pp. 443-453
    • Yoneda, A.1    Multhaupt, H.A.B.2    Couchman, J.R.3
  • 199
    • 33846099490 scopus 로고    scopus 로고
    • Fibronectin matrix assembly requires distinct contributions from Rho kinases I and-II
    • Yoneda A, Ushakov D, Multhaupt HA, Couchman JR. 2007. Fibronectin matrix assembly requires distinct contributions from Rho kinases I and-II. Mol Biol Cell 18: 66-75.
    • (2007) Mol Biol Cell , vol.18 , pp. 66-75
    • Yoneda, A.1    Ushakov, D.2    Multhaupt, H.A.3    Couchman, J.R.4
  • 200
    • 33845923423 scopus 로고    scopus 로고
    • Mesodermal cell displacements during avian gastrulation are due to both individual cell-autonomous and convective tissue movements
    • Zamir EA, Czirók A, Cui C, Little CD, Rongish BJ. 2006. Mesodermal cell displacements during avian gastrulation are due to both individual cell-autonomous and convective tissue movements. Proc Natl Acad Sci 103: 19806-19811.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 19806-19811
    • Zamir, E.A.1    Czirók, A.2    Cui, C.3    Little, C.D.4    Rongish, B.J.5
  • 201
    • 0023392493 scopus 로고
    • Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon
    • Zardi L, Carnemolla B, Siri A, Petersen TE, Paolella G, Sebastio G, Baralle FE. 1987. Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon. EMBO J 6: 2337-2342.
    • (1987) EMBO J , vol.6 , pp. 2337-2342
    • Zardi, L.1    Carnemolla, B.2    Siri, A.3    Petersen, T.E.4    Paolella, G.5    Sebastio, G.6    Baralle, F.E.7
  • 202
    • 0028004034 scopus 로고
    • Modulation of cell surface fibronectin assembly sites by lysophosphatidic acid
    • Zhang Q, Checovich WJ, Peters DM, Albrecht RM, Mosher DF. 1994. Modulation of cell surface fibronectin assembly sites by lysophosphatidic acid. J Cell Biol 127: 1447-1459.
    • (1994) J Cell Biol , vol.127 , pp. 1447-1459
    • Zhang, Q.1    Checovich, W.J.2    Peters, D.M.3    Albrecht, R.M.4    Mosher, D.F.5
  • 203
    • 0030928057 scopus 로고    scopus 로고
    • Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction
    • Zhang Q, Magnusson MK, Mosher DF. 1997. Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction. Mol Biol Cell 8: 1415-1425.
    • (1997) Mol Biol Cell , vol.8 , pp. 1415-1425
    • Zhang, Q.1    Magnusson, M.K.2    Mosher, D.F.3
  • 204
    • 0027175838 scopus 로고
    • The avb1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin
    • Zhang Z, Morla AO, Vuori K, Bauer JS, Juliano RL, Ruoslahti E. 1993. The avb1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin. J Cell Biol 122: 235-242.
    • (1993) J Cell Biol , vol.122 , pp. 235-242
    • Zhang, Z.1    Morla, A.O.2    Vuori, K.3    Bauer, J.S.4    Juliano, R.L.5    Ruoslahti, E.6
  • 205
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C, Chrzanowska-Wodnicka M, Brown J, Shaub A, Belkin AM, Burridge K. 1998. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J Cell Biol 141: 539-551.
    • (1998) J Cell Biol , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6


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