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Volumn 16, Issue 9, 1996, Pages 4972-4984

Proteolytic disruption of laminin-integrin complexes on muscle cells during synapse formation

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; INTEGRIN; LAMININ; PROTEOHEPARAN SULFATE; VITRONECTIN;

EID: 9444245909     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.9.4972     Document Type: Article
Times cited : (10)

References (70)
  • 1
    • 0022508407 scopus 로고
    • Nerve-induced remodeling of muscle basal lamina during synaptogenesis
    • Anderson, M. J. 1986. Nerve-induced remodeling of muscle basal lamina during synaptogenesis. J. Cell Biol. 102:863-877.
    • (1986) J. Cell Biol. , vol.102 , pp. 863-877
    • Anderson, M.J.1
  • 2
    • 0025992032 scopus 로고
    • Synaptic differentiation can be evoked by polymer microbeads that mimic localized pericellular proteolysis by removing proteins from adjacent surfaces
    • Anderson, M. J., S. Champaneria, and L. E. Swenarchuk. 1991. Synaptic differentiation can be evoked by polymer microbeads that mimic localized pericellular proteolysis by removing proteins from adjacent surfaces. Dev. Biol. 147:464-479.
    • (1991) Dev. Biol. , vol.147 , pp. 464-479
    • Anderson, M.J.1    Champaneria, S.2    Swenarchuk, L.E.3
  • 3
    • 0017754804 scopus 로고
    • Nerve-induced and spontaneous redistribution of acetylcholine receptors on cultured muscle cells
    • Anderson, M. J., and M. W. Cohen. 1977. Nerve-induced and spontaneous redistribution of acetylcholine receptors on cultured muscle cells. J. Physiol. (London) 268:757-773.
    • (1977) J. Physiol. (London) , vol.268 , pp. 757-773
    • Anderson, M.J.1    Cohen, M.W.2
  • 4
    • 0017640620 scopus 로고
    • Effects of innervation on the distribution of acetylcholine receptors on cultured amphibian muscle cells
    • Anderson, M. J., M. W. Cohen, and E. Zorychta. 1977. Effects of innervation on the distribution of acetylcholine receptors on cultured amphibian muscle cells. J. Physiol. (London) 268:731-756.
    • (1977) J. Physiol. (London) , vol.268 , pp. 731-756
    • Anderson, M.J.1    Cohen, M.W.2    Zorychta, E.3
  • 5
    • 0021085361 scopus 로고
    • Aggregates of acetylcholine receptors are associated with plaques of a basal lamina heparan sulfate proteoglycan on the surface of skeletal muscle fibers
    • Anderson, M. J., and D. M. Fambrough. 1983. Aggregates of acetylcholine receptors are associated with plaques of a basal lamina heparan sulfate proteoglycan on the surface of skeletal muscle fibers. J. Cell Biol. 97:1396-1411.
    • (1983) J. Cell Biol. , vol.97 , pp. 1396-1411
    • Anderson, M.J.1    Fambrough, D.M.2
  • 6
    • 0018376013 scopus 로고
    • Correlation between acetylcholine receptor localization and spontaneous synaptic potentials in cultures of nerve and muscle
    • Anderson, M. J., Y. Kidokoro, and R. Gruener. 1979. Correlation between acetylcholine receptor localization and spontaneous synaptic potentials in cultures of nerve and muscle. Brain Res. 166:185-190.
    • (1979) Brain Res. , vol.166 , pp. 185-190
    • Anderson, M.J.1    Kidokoro, Y.2    Gruener, R.3
  • 7
    • 0021734141 scopus 로고
    • Acetylcholine receptor aggregation parallels the deposition of a basal lamina proteoglycan during development of the neuromuscular junction
    • Anderson, M. J., F. G. Klier, and K. E. Tanguay. 1984. Acetylcholine receptor aggregation parallels the deposition of a basal lamina proteoglycan during development of the neuromuscular junction. J. Cell Biol. 99:1769-1784.
    • (1984) J. Cell Biol. , vol.99 , pp. 1769-1784
    • Anderson, M.J.1    Klier, F.G.2    Tanguay, K.E.3
  • 8
    • 0029146688 scopus 로고
    • Erratic deposition of agrin during the formation of Xenopus neuromuscular junctions in culture
    • Anderson, M. J., Z. Q. Shi, R. Grawel, and S. L. Zackson. 1995. Erratic deposition of agrin during the formation of Xenopus neuromuscular junctions in culture. Dev. Biol. 170:1-20.
    • (1995) Dev. Biol. , vol.170 , pp. 1-20
    • Anderson, M.J.1    Shi, Z.Q.2    Grawel, R.3    Zackson, S.L.4
  • 10
    • 0027433289 scopus 로고
    • Alpha 7 beta 1 integrin is a component of the myotendinous junction on skeletal muscle
    • Bao, Z. Z., M. Lakonishok, S. Kaufman, and A. F. Horwitz. 1993. Alpha 7 beta 1 integrin is a component of the myotendinous junction on skeletal muscle. J. Cell Sci. 106:579-589.
    • (1993) J. Cell Sci. , vol.106 , pp. 579-589
    • Bao, Z.Z.1    Lakonishok, M.2    Kaufman, S.3    Horwitz, A.F.4
  • 11
    • 0021706925 scopus 로고
    • Extracellular matrix organization in developing muscle: Correlation with acetylcholine receptor aggregates
    • Bayne, E. K., M. J. Anderson, and D. M. Fambrough. 1984. Extracellular matrix organization in developing muscle: correlation with acetylcholine receptor aggregates. J. Cell Biol. 99:1486-1581.
    • (1984) J. Cell Biol. , vol.99 , pp. 1486-1581
    • Bayne, E.K.1    Anderson, M.J.2    Fambrough, D.M.3
  • 12
    • 0026688298 scopus 로고
    • Different distributions of dystrophin and related proteins at nerve-muscle junctions
    • Bewick, G. S., L. V. B. Nicholson, C. Young, E. O'Donnel, and C. R. Slater. 1992. Different distributions of dystrophin and related proteins at nerve-muscle junctions. Neuroreport 3:857-860.
    • (1992) Neuroreport , vol.3 , pp. 857-860
    • Bewick, G.S.1    Nicholson, L.V.B.2    Young, C.3    O'Donnel, E.4    Slater, C.R.5
  • 13
    • 0020598429 scopus 로고
    • Cytoskeletal components of the vertebrate neuromuscular junction: Vinculin, alpha-actinin, and filamin
    • Bloch, R. J., and Z. W. Hall. 1983. Cytoskeletal components of the vertebrate neuromuscular junction: vinculin, alpha-actinin, and filamin. J. Cell Biol. 97:217-223.
    • (1983) J. Cell Biol. , vol.97 , pp. 217-223
    • Bloch, R.J.1    Hall, Z.W.2
  • 14
    • 0023880594 scopus 로고
    • Molecular events in synaptogenesis: Nerve-muscle adhesion and postsynaptic differentiation
    • Bloch, R. J., and D. W. Pumplin. 1988. Molecular events in synaptogenesis: nerve-muscle adhesion and postsynaptic differentiation. Am. J. Physiol. 254: C345-C364.
    • (1988) Am. J. Physiol. , vol.254
    • Bloch, R.J.1    Pumplin, D.W.2
  • 16
    • 0023508396 scopus 로고
    • Integrin, a transmembrane glycoprotein complex mediating cell-substratum adhesion
    • Buck, C. A., and A. F. Horwitz. 1987. Integrin, a transmembrane glycoprotein complex mediating cell-substratum adhesion. J. Cell Sci. (Suppl.) 8:231-250.
    • (1987) J. Cell Sci. (Suppl.) , vol.8 , pp. 231-250
    • Buck, C.A.1    Horwitz, A.F.2
  • 17
    • 0018584032 scopus 로고
    • Acetylcholine receptors in regenerating muscle accumulate at original synaptic sites in the absence of the nerve
    • Burden, S., P. B. Sargent, and U. J. McMahan. 1979. Acetylcholine receptors in regenerating muscle accumulate at original synaptic sites in the absence of the nerve. J. Cell Biol. 82:412-425.
    • (1979) J. Cell Biol. , vol.82 , pp. 412-425
    • Burden, S.1    Sargent, P.B.2    McMahan, U.J.3
  • 18
    • 0028358415 scopus 로고
    • Clues for understanding the structure and function of a prototypic human integrin: The platelet glycoprotein IIb/IIIa complex
    • Calvete, J. J. 1994. Clues for understanding the structure and function of a prototypic human integrin: the platelet glycoprotein IIb/IIIa complex. Thromb. Haemostasis 72:1-15.
    • (1994) Thromb. Haemostasis , vol.72 , pp. 1-15
    • Calvete, J.J.1
  • 19
    • 0026556667 scopus 로고
    • Increases in pericellular proteolysis at developing neuromuscular junctions in culture
    • Champaneria, S., L. E. Swenarchuk, and M. J. Anderson. 1992. Increases in pericellular proteolysis at developing neuromuscular junctions in culture. Dev. Biol. 149:261-277.
    • (1992) Dev. Biol. , vol.149 , pp. 261-277
    • Champaneria, S.1    Swenarchuk, L.E.2    Anderson, M.J.3
  • 20
    • 0027972448 scopus 로고
    • N-cadherin expression in developing, adult and denervated chicken neuromuscular system: Accumulations at both the neuromuscular junction and the node of Ranvier
    • Cifuentes-Diaz, C., M. Nicolet, D. Goudou, F. Rieger, and R. M. Mege. 1994. N-cadherin expression in developing, adult and denervated chicken neuromuscular system: accumulations at both the neuromuscular junction and the node of Ranvier. Development 120:1-11.
    • (1994) Development , vol.120 , pp. 1-11
    • Cifuentes-Diaz, C.1    Nicolet, M.2    Goudou, D.3    Rieger, F.4    Mege, R.M.5
  • 21
    • 0027960284 scopus 로고
    • Molecular mechanisms of thrombin signalling
    • Coughlin, S. R. 1994. Molecular mechanisms of thrombin signalling. Semin. Hematol. 31:270-277.
    • (1994) Semin. Hematol. , vol.31 , pp. 270-277
    • Coughlin, S.R.1
  • 23
    • 0021957079 scopus 로고
    • Distribution of cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture
    • Damsky, C. H., K. A. Knudsen, D. Bradley, C. A. Buck, and A. F. Horwitz. 1985. Distribution of cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture. J. Cell Biol. 100:1528-1539.
    • (1985) J. Cell Biol. , vol.100 , pp. 1528-1539
    • Damsky, C.H.1    Knudsen, K.A.2    Bradley, D.3    Buck, C.A.4    Horwitz, A.F.5
  • 24
    • 0027716945 scopus 로고
    • V(+)-fibronectin expression and localization prior to gastrulation in Xenopus laevis embryos
    • Danker, K., H. Hacke, J. Ramos, and D. DeSimone. 1993. V(+)-fibronectin expression and localization prior to gastrulation in Xenopus laevis embryos. Mech. Dev. 44:155-165.
    • (1993) Mech. Dev. , vol.44 , pp. 155-165
    • Danker, K.1    Hacke, H.2    Ramos, J.3    DeSimone, D.4
  • 25
    • 0025856309 scopus 로고
    • Role of lymphocyte adhesion receptors in transient interactions and cell locomotion
    • Dustin, M. L., and T. A. Springer. 1991. Role of lymphocyte adhesion receptors in transient interactions and cell locomotion. Annu. Rev. Immunol. 9:27-66.
    • (1991) Annu. Rev. Immunol. , vol.9 , pp. 27-66
    • Dustin, M.L.1    Springer, T.A.2
  • 26
    • 0028836388 scopus 로고
    • Dynamic regulation of integrins
    • Faull, R. J., and M. H. Ginsberg. 1995. Dynamic regulation of integrins. Stem Cells 13:38-46.
    • (1995) Stem Cells , vol.13 , pp. 38-46
    • Faull, R.J.1    Ginsberg, M.H.2
  • 27
    • 0028283379 scopus 로고
    • Transmembrane signalling across the platelet integrin glycoprotein IIb-IIIa
    • Fox, J. E. 1994. Transmembrane signalling across the platelet integrin glycoprotein IIb-IIIa. Ann. N. Y. Acad. Sci. 714:75-87.
    • (1994) Ann. N. Y. Acad. Sci. , vol.714 , pp. 75-87
    • Fox, J.E.1
  • 28
    • 0026000830 scopus 로고
    • The submembrane machinery for nicotinic acetylcholine receptor clustering
    • Froehner, S. C. 1991. The submembrane machinery for nicotinic acetylcholine receptor clustering. J. Cell Biol. 114:1-7.
    • (1991) J. Cell Biol. , vol.114 , pp. 1-7
    • Froehner, S.C.1
  • 29
    • 0026696956 scopus 로고
    • 1-Integrin is a maternal protein that is inserted into all newly formed plasma membranes during early Xenopus embryogenesis
    • 1-Integrin is a maternal protein that is inserted into all newly formed plasma membranes during early Xenopus embryogenesis. Development 115:595-605.
    • (1992) Development , vol.115 , pp. 595-605
    • Gawantka, V.1    Ellinger-Ziegelbauer, H.2    Hausen, P.3
  • 31
    • 0020055802 scopus 로고
    • Monoclonal antibodies which alter the morphology of cultured chick myogenic cells
    • Greve, J. M., and D. I. Gottlieb. 1982. Monoclonal antibodies which alter the morphology of cultured chick myogenic cells. J. Cell Biochem. 48:221-230.
    • (1982) J. Cell Biochem. , vol.48 , pp. 221-230
    • Greve, J.M.1    Gottlieb, D.I.2
  • 32
    • 0027354449 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall, Z. W., and J. R. Sanes. 1993. Synaptic structure and development: the neuromuscular junction. Cell (Suppl.) 72:99-121.
    • (1993) Cell (Suppl.) , vol.72 , pp. 99-121
    • Hall, Z.W.1    Sanes, J.R.2
  • 33
    • 0027621036 scopus 로고
    • Dynamic aspects of adhesion receptor function: Integrins both twist and shout
    • Humphries, M. J., A. P. Mould, and D. S. Tuckwell. 1993. Dynamic aspects of adhesion receptor function: integrins both twist and shout. Bioessays 15:391-397.
    • (1993) Bioessays , vol.15 , pp. 391-397
    • Humphries, M.J.1    Mould, A.P.2    Tuckwell, D.S.3
  • 34
    • 0019947147 scopus 로고
    • High-affinity monoclonal antibodies to the cardiac glycoside, digoxin
    • Hunter, M. M., M. N. Margolies, A. Ju, and E. Haber. 1982. High-affinity monoclonal antibodies to the cardiac glycoside, digoxin. J. Immunol. 129: 1165-1172.
    • (1982) J. Immunol. , vol.129 , pp. 1165-1172
    • Hunter, M.M.1    Margolies, M.N.2    Ju, A.3    Haber, E.4
  • 35
    • 0024535958 scopus 로고
    • A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction
    • Hunter, D. D., V. Shah, J. P. Merlie, and J. R. Sanes. 1989. A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. Nature (London) 338:229-234.
    • (1989) Nature (London) , vol.338 , pp. 229-234
    • Hunter, D.D.1    Shah, V.2    Merlie, J.P.3    Sanes, J.R.4
  • 36
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signalling in cell adhesion
    • Hynes, R. O. 1992. Integrins: versatility, modulation and signalling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 37
    • 0028088291 scopus 로고
    • Genetic analysis of cell-matrix interactions in development
    • Hynes, R. O. 1994. Genetic analysis of cell-matrix interactions in development. Curr. Opin. Genet. Dev. 4:569-574.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 569-574
    • Hynes, R.O.1
  • 38
    • 0019308325 scopus 로고
    • Changes in synaptic potential properties during acetylcholine receptor accumulation and neurospecific interactions in Xenopus nerve-muscle cell culture
    • Kidokoro, Y., M. J. Anderson, and R. Gruener. 1980. Changes in synaptic potential properties during acetylcholine receptor accumulation and neurospecific interactions in Xenopus nerve-muscle cell culture. Dev. Biol. 78:464-483.
    • (1980) Dev. Biol. , vol.78 , pp. 464-483
    • Kidokoro, Y.1    Anderson, M.J.2    Gruener, R.3
  • 39
    • 0028145301 scopus 로고
    • Association of utrophin and multiple dystrophin short forms with the mammalian Mr 58,000 dystrophin-associated protein (syntrophin)
    • Kramarcy, N. R., A. Vidal, S. C. Froehner, and R. Sealock. 1994. Association of utrophin and multiple dystrophin short forms with the mammalian Mr 58,000 dystrophin-associated protein (syntrophin). J. Biol. Chem. 269:2870-2876.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2870-2876
    • Kramarcy, N.R.1    Vidal, A.2    Froehner, S.C.3    Sealock, R.4
  • 41
    • 0023278851 scopus 로고
    • Expression of Japanese encephalitis virus antigens in Escherichia coli
    • Mason, P. W., P. C. McAda, J. M. Dalrymple, M. J. Fournier, and T. L. Mason. 1987. Expression of Japanese encephalitis virus antigens in Escherichia coli. Virology 158:361-372.
    • (1987) Virology , vol.158 , pp. 361-372
    • Mason, P.W.1    McAda, P.C.2    Dalrymple, J.M.3    Fournier, M.J.4    Mason, T.L.5
  • 42
    • 0027645521 scopus 로고
    • Regulatory mechanisms underlying T cell integrin receptor function
    • Mobley, J. L., P. J. Reynolds, and Y. Shimizu. 1993. Regulatory mechanisms underlying T cell integrin receptor function. Semin. Immunol. 5:227-236.
    • (1993) Semin. Immunol. , vol.5 , pp. 227-236
    • Mobley, J.L.1    Reynolds, P.J.2    Shimizu, Y.3
  • 43
    • 0027209270 scopus 로고
    • The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator
    • Moser, T. L., J. J. Enghild, S. V. Pizzo, and M. S. Stack. 1993. The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator. J. Biol. Chem. 268: 18917-18923.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18917-18923
    • Moser, T.L.1    Enghild, J.J.2    Pizzo, S.V.3    Stack, M.S.4
  • 44
  • 45
    • 0027449283 scopus 로고
    • A review of the role of platelet membrane glycoproteins in the platelet-vessel wall interaction
    • Nurden, A. T., and P. Nurden. 1993. A review of the role of platelet membrane glycoproteins in the platelet-vessel wall interaction. Baillieres Clin. Haematol. 6:653-690.
    • (1993) Baillieres Clin. Haematol. , vol.6 , pp. 653-690
    • Nurden, A.T.1    Nurden, P.2
  • 46
    • 0026094250 scopus 로고
    • Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle
    • Ohlendieck, K., J. M. Ervasti, K. Matsumura, S. D. Dahl, C. J. Leveille, and K. P. Campbell. 1991. Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle. Neuron 7:499-508.
    • (1991) Neuron , vol.7 , pp. 499-508
    • Ohlendieck, K.1    Ervasti, J.M.2    Matsumura, K.3    Dahl, S.D.4    Leveille, C.J.5    Campbell, K.P.6
  • 48
    • 0023191706 scopus 로고
    • Isolation and characterization of a low molecular weight chondroitin sulfate proteoglycan from rabbit skeletal muscle
    • Parthasarathy, N., and M. L. Tanzer. 1987. Isolation and characterization of a low molecular weight chondroitin sulfate proteoglycan from rabbit skeletal muscle. Biochemistry 26:3149-3156.
    • (1987) Biochemistry , vol.26 , pp. 3149-3156
    • Parthasarathy, N.1    Tanzer, M.L.2
  • 49
    • 0026542959 scopus 로고
    • Basement membrane proteins: Structure, assembly, and cellular interactions
    • Paulsson, M. 1992. Basement membrane proteins: structure, assembly, and cellular interactions. Crit. Rev. Biochem. Mol. Biol. 27:93-127.
    • (1992) Crit. Rev. Biochem. Mol. Biol. , vol.27 , pp. 93-127
    • Paulsson, M.1
  • 50
    • 0023581595 scopus 로고
    • Agrin-like molecules at synaptic sites in normal, denervated and damaged skeletal muscles
    • Reist, N. E., C. Magill, and U. J. McMahan. 1987. Agrin-like molecules at synaptic sites in normal, denervated and damaged skeletal muscles. J. Cell Biol. 105:2457-2469.
    • (1987) J. Cell Biol. , vol.105 , pp. 2457-2469
    • Reist, N.E.1    Magill, C.2    McMahan, U.J.3
  • 51
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase?
    • Richardson, A., and J. T. Parsons. 1995. Signal transduction through integrins: a central role for focal adhesion kinase? Bioessays 17:229-236.
    • (1995) Bioessays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 52
    • 0026976953 scopus 로고
    • Signalling between the extracellular matrix and the cytoskeleton: Tyrosine phosphorylation and focal adhesion assembly
    • Romer, L. H., K. Burridge, and C. E. Turner. 1992. Signalling between the extracellular matrix and the cytoskeleton: tyrosine phosphorylation and focal adhesion assembly. Cold Spring Harbor Symp. Quant. Biol. 57:193-202.
    • (1992) Cold Spring Harbor Symp. Quant. Biol. , vol.57 , pp. 193-202
    • Romer, L.H.1    Burridge, K.2    Turner, C.E.3
  • 53
    • 0024146930 scopus 로고
    • Cell-associated plasminogen activation: Regulation and physiological functions
    • Saksela, O., and D. B. Rifkin. 1988. Cell-associated plasminogen activation: regulation and physiological functions. Annu. Rev. Cell Biol. 4:93-126.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 93-126
    • Saksela, O.1    Rifkin, D.B.2
  • 54
    • 0022355907 scopus 로고
    • Plasminogen and tissue-type plasminogen activator bind to immobilized fibronectin
    • Salonen, E. M., O. Saksela, T. Vartio, A. Vaheri, L. S. Nielsen, and J. Zeuthen. 1985. Plasminogen and tissue-type plasminogen activator bind to immobilized fibronectin. J Biol. Chem. 260:12302-12307.
    • (1985) J Biol. Chem. , vol.260 , pp. 12302-12307
    • Salonen, E.M.1    Saksela, O.2    Vartio, T.3    Vaheri, A.4    Nielsen, L.S.5    Zeuthen, J.6
  • 55
    • 0021195598 scopus 로고
    • Laminin interacts with plasminogen and its tissue-type activator
    • Salonen, E. M., A. Zitting, and A. Vaheri. 1984. Laminin interacts with plasminogen and its tissue-type activator. FEBS Lett. 172:29-32.
    • (1984) FEBS Lett. , vol.172 , pp. 29-32
    • Salonen, E.M.1    Zitting, A.2    Vaheri, A.3
  • 56
    • 0002321039 scopus 로고
    • Development and neural control of the neuromuscular junction and of the junctional acetylcholine receptor
    • M. M. Salpeter (ed.), Alan R. Liss, New York
    • Salpeter, M. M. 1987. Development and neural control of the neuromuscular junction and of the junctional acetylcholine receptor, p. 55-115. In M. M. Salpeter (ed.), The vertebrate neuromuscular junction. Alan R. Liss, New York.
    • (1987) The Vertebrate Neuromuscular Junction , pp. 55-115
    • Salpeter, M.M.1
  • 57
    • 0020287269 scopus 로고
    • Laminin, fibronectin, and collagen in synaptic and extrasynaptic portions of muscle fiber basement membrane
    • Sanes, J. R. 1982. Laminin, fibronectin, and collagen in synaptic and extrasynaptic portions of muscle fiber basement membrane. J. Cell Biol. 93:442-451.
    • (1982) J. Cell Biol. , vol.93 , pp. 442-451
    • Sanes, J.R.1
  • 58
    • 0018141960 scopus 로고
    • Reinnervation of muscle fiber basal lamina after removal of myofibers
    • Sanes, J. R., L. M. Marshall, and U. J. McMahan. 1978. Reinnervation of muscle fiber basal lamina after removal of myofibers. J. Cell Biol. 78:176-198.
    • (1978) J. Cell Biol. , vol.78 , pp. 176-198
    • Sanes, J.R.1    Marshall, L.M.2    McMahan, U.J.3
  • 59
    • 0022616860 scopus 로고
    • Expression of several adhesive macromolecules N-CAM, L1, J1, NILE, uvomorulin, laminin, fibronectin, and a heparan sulfate proteoglycan in embryonic, adult, and denervated adult skeletal muscle
    • Sanes, J. R., M. Schachner, and J. Covault. 1986. Expression of several adhesive macromolecules (N-CAM, L1, J1, NILE, uvomorulin, laminin, fibronectin, and a heparan sulfate proteoglycan in embryonic, adult, and denervated adult skeletal muscle. J. Cell Biol. 102:420-431.
    • (1986) J. Cell Biol. , vol.102 , pp. 420-431
    • Sanes, J.R.1    Schachner, M.2    Covault, J.3
  • 60
    • 0022441418 scopus 로고
    • Talin is a post-synaptic component of the rat neuromuscular junction
    • Sealock, R., B. Paschal, M. Beckerle, and K. Burridge. 1986. Talin is a post-synaptic component of the rat neuromuscular junction. Exp. Cell Res. 163:143-150.
    • (1986) Exp. Cell Res. , vol.163 , pp. 143-150
    • Sealock, R.1    Paschal, B.2    Beckerle, M.3    Burridge, K.4
  • 65
    • 0027333411 scopus 로고
    • Tumor cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson, W. G., S. Aznavoorian, and L. A. Liotta. 1993. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol. 9:541-573.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.G.1    Aznavoorian, S.2    Liotta, L.A.3
  • 66
    • 0024727606 scopus 로고
    • Location of integrin complex and extracellular matrix molecules at the chicken myotendinous junction
    • Swadison, S., and R. Mayne. 1989. Location of integrin complex and extracellular matrix molecules at the chicken myotendinous junction. Cell Tissue Res. 257:537-543.
    • (1989) Cell Tissue Res. , vol.257 , pp. 537-543
    • Swadison, S.1    Mayne, R.2
  • 67
    • 0024987666 scopus 로고
    • Induction of a specialized muscle basal lamina at chimaeric synapses in culture
    • Swenarchuk, L. E., S. Champaneria, and M. J. Anderson. 1990. Induction of a specialized muscle basal lamina at chimaeric synapses in culture. Development 110:51-61.
    • (1990) Development , vol.110 , pp. 51-61
    • Swenarchuk, L.E.1    Champaneria, S.2    Anderson, M.J.3
  • 68
    • 0027151901 scopus 로고
    • Proteoglycans of basement membranes
    • Timpl, R. 1993. Proteoglycans of basement membranes. Experientia 49:417-428.
    • (1993) Experientia , vol.49 , pp. 417-428
    • Timpl, R.1
  • 70
    • 0025963549 scopus 로고
    • Localization of paxillin, a focal adhesion protein, to smooth muscle dense plaques and the myotendinous and neuromuscular junctions of skeletal muscle
    • Turner, C. E., N. Kramarcy, R. Sealock, and K. Burridge. 1991. Localization of paxillin, a focal adhesion protein, to smooth muscle dense plaques and the myotendinous and neuromuscular junctions of skeletal muscle. Exp. Cell Res. 192:651-655.
    • (1991) Exp. Cell Res. , vol.192 , pp. 651-655
    • Turner, C.E.1    Kramarcy, N.2    Sealock, R.3    Burridge, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.