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Volumn 13, Issue 5, 2003, Pages 408-415

Expression of mouse agrin in normal, denervated and dystrophic muscle

Author keywords

Congenital muscular dystrophy; dyW; Dystrophin; Laminin; Mouse; 7 integrin

Indexed keywords

AGRIN; POLYCLONAL ANTISERUM;

EID: 0037835964     PISSN: 09608966     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-8966(03)00036-1     Document Type: Article
Times cited : (42)

References (57)
  • 1
    • 0023461553 scopus 로고
    • Identification of agrin, a synaptic organizing protein from Torpedo electric organ
    • Nitkin R.M., Smith M.A., Magill C., et al. Identification of agrin, a synaptic organizing protein from Torpedo electric organ. J Cell Biol. 105:1987;2471-2478.
    • (1987) J Cell Biol , vol.105 , pp. 2471-2478
    • Nitkin, R.M.1    Smith, M.A.2    Magill, C.3
  • 2
    • 0029893117 scopus 로고    scopus 로고
    • Defective neuromuscular synaptogenesis in agrin-deficient mutant mice
    • Gautam M., Noakes P.G., Moscoso L., et al. Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell. 85:1996;525-535.
    • (1996) Cell , vol.85 , pp. 525-535
    • Gautam, M.1    Noakes, P.G.2    Moscoso, L.3
  • 3
    • 0035953645 scopus 로고    scopus 로고
    • Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse
    • Lin W., Burgess R.W., Dominguez B., Pfaff S.L., Sanes J.R., Lee K.F. Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse. Nature. 410:2001;1057-1064.
    • (2001) Nature , vol.410 , pp. 1057-1064
    • Lin, W.1    Burgess, R.W.2    Dominguez, B.3    Pfaff, S.L.4    Sanes, J.R.5    Lee, K.F.6
  • 5
    • 0034597091 scopus 로고    scopus 로고
    • Agrin isoforms with distinct amino termini. Differential expression, localization, and function
    • Burgess R.W., Skarnes W.C., Sanes J.R. Agrin isoforms with distinct amino termini. Differential expression, localization, and function. J Cell Biol. 151:2000;41-52.
    • (2000) J Cell Biol , vol.151 , pp. 41-52
    • Burgess, R.W.1    Skarnes, W.C.2    Sanes, J.R.3
  • 6
    • 0035154191 scopus 로고    scopus 로고
    • An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein
    • Neumann F.R., Bittcher G., Annies M., Schumacher B., Kroger S., Ruegg M.A. An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein. Mol Cell Neurosci. 17:2001;208-225.
    • (2001) Mol Cell Neurosci , vol.17 , pp. 208-225
    • Neumann, F.R.1    Bittcher, G.2    Annies, M.3    Schumacher, B.4    Kroger, S.5    Ruegg, M.A.6
  • 8
    • 0032518822 scopus 로고    scopus 로고
    • Electron microscopic structure of agrin and mapping of its binding site in laminin-1
    • Denzer A.J., Schulthess T., Fauser C., et al. Electron microscopic structure of agrin and mapping of its binding site in laminin-1. EMBO J. 17:1998;335-343.
    • (1998) EMBO J , vol.17 , pp. 335-343
    • Denzer, A.J.1    Schulthess, T.2    Fauser, C.3
  • 9
    • 0033485262 scopus 로고    scopus 로고
    • Interaction of agrin with laminin requires a coiled-coil conformation of the agrin-binding site within the laminin γ1 chain
    • Kammerer R.A., Schulthess T., Landwehr R., et al. Interaction of agrin with laminin requires a coiled-coil conformation of the agrin-binding site within the laminin γ1 chain. EMBO J. 18:1999;6762-6770.
    • (1999) EMBO J , vol.18 , pp. 6762-6770
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3
  • 10
    • 0002791951 scopus 로고    scopus 로고
    • Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction
    • Ruegg M.A., Bixby J.L. Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction. Trends Neurosci. 21:1998;22-27.
    • (1998) Trends Neurosci , vol.21 , pp. 22-27
    • Ruegg, M.A.1    Bixby, J.L.2
  • 11
    • 0027369903 scopus 로고
    • Developmental regulation of highly active alternatively spliced forms of agrin
    • Hoch W., Ferns M., Campanelli J.T., Hall Z.W., Scheller R.H. Developmental regulation of highly active alternatively spliced forms of agrin. Neuron. 11:1993;479-490.
    • (1993) Neuron , vol.11 , pp. 479-490
    • Hoch, W.1    Ferns, M.2    Campanelli, J.T.3    Hall, Z.W.4    Scheller, R.H.5
  • 12
    • 15644366697 scopus 로고    scopus 로고
    • Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane
    • Groffen A.J., Ruegg M.A., Dijkman H., et al. Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane. J Histochem Cytochem. 46:1998;19-27.
    • (1998) J Histochem Cytochem , vol.46 , pp. 19-27
    • Groffen, A.J.1    Ruegg, M.A.2    Dijkman, H.3
  • 13
    • 0033137032 scopus 로고    scopus 로고
    • Alternatively spliced isoforms of nerve- and muscle-derived agrin: Their roles at the neuromuscular junction
    • Burgess R.W., Nguyen Q.T., Son Y.J., Lichtman J.W., Sanes J.R. Alternatively spliced isoforms of nerve- and muscle-derived agrin: their roles at the neuromuscular junction. Neuron. 23:1999;33-44.
    • (1999) Neuron , vol.23 , pp. 33-44
    • Burgess, R.W.1    Nguyen, Q.T.2    Son, Y.J.3    Lichtman, J.W.4    Sanes, J.R.5
  • 14
    • 0031982584 scopus 로고    scopus 로고
    • Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
    • Gesemann M., Brancaccio A., Schumacher B., Ruegg M.A. Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue. J Biol Chem. 273:1998;600-605.
    • (1998) J Biol Chem , vol.273 , pp. 600-605
    • Gesemann, M.1    Brancaccio, A.2    Schumacher, B.3    Ruegg, M.A.4
  • 15
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato H., Yurchenco P.D. Form and function: the laminin family of heterotrimers. Dev Dyn. 218:2000;213-234.
    • (2000) Dev Dyn , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 16
    • 0034279184 scopus 로고    scopus 로고
    • Laminin expression in adult and developing retinae: Evidence of two novel CNS laminins
    • Libby R.T., Champliaud M.F., Claudepierre T., et al. Laminin expression in adult and developing retinae: evidence of two novel CNS laminins. J Neurosci. 20:2000;6517-6528.
    • (2000) J Neurosci , vol.20 , pp. 6517-6528
    • Libby, R.T.1    Champliaud, M.F.2    Claudepierre, T.3
  • 17
    • 0031456144 scopus 로고    scopus 로고
    • Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice
    • Patton B.L., Miner J.H., Chiu A.Y., Sanes J.R. Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice. J Cell Biol. 139:1997;1507-1521.
    • (1997) J Cell Biol , vol.139 , pp. 1507-1521
    • Patton, B.L.1    Miner, J.H.2    Chiu, A.Y.3    Sanes, J.R.4
  • 19
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J.M., Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol. 122:1993;809-823.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 20
    • 0030272647 scopus 로고    scopus 로고
    • Dystroglycan: An extracellular matrix receptor linked to the cytoskeleton
    • Henry M.D., Campbell K.P. Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton. Curr Opin Cell Biol. 8:1996;625-631.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 625-631
    • Henry, M.D.1    Campbell, K.P.2
  • 21
    • 0033758449 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy: Valuable tools for the development of therapies
    • Allamand V., Campbell K.P. Animal models for muscular dystrophy: valuable tools for the development of therapies. Hum Mol Genet. 9:2000;2459-2467.
    • (2000) Hum Mol Genet , vol.9 , pp. 2459-2467
    • Allamand, V.1    Campbell, K.P.2
  • 22
    • 0035212037 scopus 로고    scopus 로고
    • Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan
    • Brockington M., Blake D.J., Prandini P., et al. Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan. Am J Hum Genet. 69:2001;1198-1209.
    • (2001) Am J Hum Genet , vol.69 , pp. 1198-1209
    • Brockington, M.1    Blake, D.J.2    Prandini, P.3
  • 23
    • 0037173670 scopus 로고    scopus 로고
    • Post-translational disruption of dystroglycan ligand interactions in congenital muscular dystrophies
    • Michele D.E., Barresi R., Kanagawa M., et al. Post-translational disruption of dystroglycan ligand interactions in congenital muscular dystrophies. Nature. 418:2002;417-421.
    • (2002) Nature , vol.418 , pp. 417-421
    • Michele, D.E.1    Barresi, R.2    Kanagawa, M.3
  • 24
    • 0026354979 scopus 로고
    • Skeletal myoblasts utilize a novel beta 1-series integrin and not alpha 6 beta 1 for binding to the E8 and T8 fragments of laminin
    • von der Mark H., Durr J., Sonnenberg A., von der Mark K., Deutzmann R., Goodman S.L. Skeletal myoblasts utilize a novel beta 1-series integrin and not alpha 6 beta 1 for binding to the E8 and T8 fragments of laminin. J Biol Chem. 266:1991;23593-23601.
    • (1991) J Biol Chem , vol.266 , pp. 23593-23601
    • Von der Mark, H.1    Durr, J.2    Sonnenberg, A.3    Von der Mark, K.4    Deutzmann, R.5    Goodman, S.L.6
  • 25
    • 0026236965 scopus 로고
    • Laminin-binding integrin alpha 7 beta 1: Functional characterization and expression in normal and malignant melanocytcs
    • Kramer R.H., Vu M.P., Cheng Y.F., Ramos D.M., Timpl R., Waleh N. Laminin-binding integrin alpha 7 beta 1: functional characterization and expression in normal and malignant melanocytcs. Cell Regul. 2:1991;805-817.
    • (1991) Cell Regul , vol.2 , pp. 805-817
    • Kramer, R.H.1    Vu, M.P.2    Cheng, Y.F.3    Ramos, D.M.4    Timpl, R.5    Waleh, N.6
  • 26
    • 0029661978 scopus 로고    scopus 로고
    • Alpha7 integrin mediates cell adhesion and migration on specific laminin isoforms
    • Yao C.C., Ziober B.L., Squillace R.M., Kramer R.H. Alpha7 integrin mediates cell adhesion and migration on specific laminin isoforms. J Biol Chem. 271:1996;25598-25603.
    • (1996) J Biol Chem , vol.271 , pp. 25598-25603
    • Yao, C.C.1    Ziober, B.L.2    Squillace, R.M.3    Kramer, R.H.4
  • 27
    • 0023875632 scopus 로고
    • Laminin alters cell shape and stimulates motility and proliferation of murine skeletal myoblasts
    • Ocalan M., Goodman S.L., Kuhl U., Hauschka S.D., von der Mark K. Laminin alters cell shape and stimulates motility and proliferation of murine skeletal myoblasts. Dev Biol. 125:1988;158-167.
    • (1988) Dev Biol , vol.125 , pp. 158-167
    • Ocalan, M.1    Goodman, S.L.2    Kuhl, U.3    Hauschka, S.D.4    Von der Mark, K.5
  • 28
    • 0024336977 scopus 로고
    • The E8 subfragment of laminin promotes locomotion of myoblasts over extracellular matrix
    • Goodman S.L., Risse G., von der Mark K. The E8 subfragment of laminin promotes locomotion of myoblasts over extracellular matrix. J Cell Biol. 109:1989;799-809.
    • (1989) J Cell Biol , vol.109 , pp. 799-809
    • Goodman, S.L.1    Risse, G.2    Von der Mark, K.3
  • 29
    • 0026591586 scopus 로고
    • H36-alpha 7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis
    • Song W.K., Wang W., Foster R.F., Bielser D.A., Kaufman S.J. H36-alpha 7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis. J Cell Biol. 117:1992;643-657.
    • (1992) J Cell Biol , vol.117 , pp. 643-657
    • Song, W.K.1    Wang, W.2    Foster, R.F.3    Bielser, D.A.4    Kaufman, S.J.5
  • 30
    • 0027433289 scopus 로고
    • Alpha 7 beta 1 integrin is a component of the myotendinous junction on skeletal muscle
    • Bao Z.Z., Lakonishok M., Kaufman S., Horwitz A.F. Alpha 7 beta 1 integrin is a component of the myotendinous junction on skeletal muscle. J Cell Sci. 106:1993;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
  • 31
    • 0029988437 scopus 로고    scopus 로고
    • Synaptic integrins in developing, adult, and mutant muscle: Selective association of α1, α7A, and α7B integrins with the neuromuscular junction
    • Martin P.T., Kaufman S.J., Kramer R.H., Sanes J.R. Synaptic integrins in developing, adult, and mutant muscle: selective association of α1, α7A, and α7B integrins with the neuromuscular junction. Dev Biol. 174:1996;125-139.
    • (1996) Dev Biol , vol.174 , pp. 125-139
    • Martin, P.T.1    Kaufman, S.J.2    Kramer, R.H.3    Sanes, J.R.4
  • 32
    • 0030724952 scopus 로고    scopus 로고
    • Absence of integrin α7 causes a novel form of muscular dystrophy
    • Mayer U., Saher G., Fassler R., et al. Absence of integrin α7 causes a novel form of muscular dystrophy. Nat Genet. 17:1997;318-323.
    • (1997) Nat Genet , vol.17 , pp. 318-323
    • Mayer, U.1    Saher, G.2    Fassler, R.3
  • 33
    • 17344372250 scopus 로고    scopus 로고
    • Mutations in the integrin alpha7 gene cause congenital myopathy
    • Hayashi Y.K., Chou F.L., Engvall E., et al. Mutations in the integrin alpha7 gene cause congenital myopathy. Nat Genet. 19:1998;94-97.
    • (1998) Nat Genet , vol.19 , pp. 94-97
    • Hayashi, Y.K.1    Chou, F.L.2    Engvall, E.3
  • 34
    • 0035911960 scopus 로고    scopus 로고
    • Enhanced expression of the alpha 7 beta 1 integrin reduces muscular dystrophy and restores viability in dystrophic mice
    • Burkin D.J., Wallace G.Q., Nicol K.J., Kaufman D.J., Kaufman S.J. Enhanced expression of the alpha 7 beta 1 integrin reduces muscular dystrophy and restores viability in dystrophic mice. J Cell Biol. 152:2001;1207-1218.
    • (2001) J Cell Biol , vol.152 , pp. 1207-1218
    • Burkin, D.J.1    Wallace, G.Q.2    Nicol, K.J.3    Kaufman, D.J.4    Kaufman, S.J.5
  • 35
    • 0035921981 scopus 로고    scopus 로고
    • An agrin minigene rescues dystrophic symptoms in a mouse model for congenital muscular dystrophy
    • Moll J., Barzaghi P., Lin S., et al. An agrin minigene rescues dystrophic symptoms in a mouse model for congenital muscular dystrophy. Nature. 413:2001;302-307.
    • (2001) Nature , vol.413 , pp. 302-307
    • Moll, J.1    Barzaghi, P.2    Lin, S.3
  • 37
    • 0030804282 scopus 로고    scopus 로고
    • Properties of the extracellular calcium binding module of the proteoglycan testican
    • Kohfeldt E., Maurer P., Vannahme C., Timpl R. Properties of the extracellular calcium binding module of the proteoglycan testican. FEBS Lett. 414:1997;557-561.
    • (1997) FEBS Lett , vol.414 , pp. 557-561
    • Kohfeldt, E.1    Maurer, P.2    Vannahme, C.3    Timpl, R.4
  • 38
    • 0002901790 scopus 로고
    • Production of antibodies
    • J. Coligan, A. Kruisbeek, D. Margulies, E. Shevach, & W. Strober. New York: John Wiley & Sons
    • Cooper H., Paterson Y. Production of antibodies. Coligan J., Kruisbeek A., Margulies D., Shevach E., Strober W. Current protocols in immunology. 1995;241-249 John Wiley & Sons, New York.
    • (1995) Current protocols in immunology , pp. 241-249
    • Cooper, H.1    Paterson, Y.2
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0029591857 scopus 로고
    • An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix
    • Denzer A.J., Gesemann M., Schumacher B., Ruegg M.A. An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix. J Cell Biol. 131:1995;1547-1560.
    • (1995) J Cell Biol , vol.131 , pp. 1547-1560
    • Denzer, A.J.1    Gesemann, M.2    Schumacher, B.3    Ruegg, M.A.4
  • 41
    • 0032528845 scopus 로고    scopus 로고
    • Merosin-deficient congenital muscular dystrophy. Partial genetic correction in two mouse models
    • Kuang W., Xu H., Vachon P.H., et al. Merosin-deficient congenital muscular dystrophy. Partial genetic correction in two mouse models. J Clin Invest. 102:1998;844-852.
    • (1998) J Clin Invest , vol.102 , pp. 844-852
    • Kuang, W.1    Xu, H.2    Vachon, P.H.3
  • 43
    • 0029864658 scopus 로고    scopus 로고
    • A quantitative fluorescence-imaging technique for studying acetylcholine receptor turnover at neuromuscular junctions in living animals
    • Turney S.G., Culican S.M., Lichtman J.W. A quantitative fluorescence-imaging technique for studying acetylcholine receptor turnover at neuromuscular junctions in living animals. J Neurosci Methods. 64:1996;199-208.
    • (1996) J Neurosci Methods , vol.64 , pp. 199-208
    • Turney, S.G.1    Culican, S.M.2    Lichtman, J.W.3
  • 44
    • 0033568506 scopus 로고    scopus 로고
    • Analysis of a YAC with human telomeres and oriP from Epstein-Barr virus in yeast and 293 cells
    • Tolmachova T., Simpson K., Huxley C. Analysis of a YAC with human telomeres and oriP from Epstein-Barr virus in yeast and 293 cells. Nucleic Acids Res. 27:1999;3736-3744.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3736-3744
    • Tolmachova, T.1    Simpson, K.2    Huxley, C.3
  • 45
    • 14444287755 scopus 로고    scopus 로고
    • Differential expression of agrin in renal basement membranes as revealed by domain-specific antibodies
    • Raats C.J., Bakker M.A., Hoch W., et al. Differential expression of agrin in renal basement membranes as revealed by domain-specific antibodies. J Biol Chem. 273:1998;17832-17838.
    • (1998) J Biol Chem , vol.273 , pp. 17832-17838
    • Raats, C.J.1    Bakker, M.A.2    Hoch, W.3
  • 46
    • 0024244794 scopus 로고
    • Basal lamina components are concentrated in premuscle masses and at early acetylcholine receptor clusters in chick embryo hindlimb muscles
    • Godfrey E.W., Siebenlist R.E., Wallskog P.A., Walters L.M., Bolender D.L., Yorde D.E. Basal lamina components are concentrated in premuscle masses and at early acetylcholine receptor clusters in chick embryo hindlimb muscles. Dev Biol. 130:1988;471-486.
    • (1988) Dev Biol , vol.130 , pp. 471-486
    • Godfrey, E.W.1    Siebenlist, R.E.2    Wallskog, P.A.3    Walters, L.M.4    Bolender, D.L.5    Yorde, D.E.6
  • 47
    • 0023200021 scopus 로고
    • Primary, secondary and tertiary myotubes in developing skeletal muscle: A new approach to the analysis of human myogenesis
    • Draeger A., Weeds A.G., Fitzsimons R.B. Primary, secondary and tertiary myotubes in developing skeletal muscle: a new approach to the analysis of human myogenesis. J Neurol Sci. 81:1987;19-43.
    • (1987) J Neurol Sci , vol.81 , pp. 19-43
    • Draeger, A.1    Weeds, A.G.2    Fitzsimons, R.B.3
  • 49
    • 0026328022 scopus 로고
    • Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice
    • Ohlendieck K., Campbell K.P. Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J Cell Biol. 115:1991;1685-1694.
    • (1991) J Cell Biol , vol.115 , pp. 1685-1694
    • Ohlendieck, K.1    Campbell, K.P.2
  • 50
    • 0030728897 scopus 로고    scopus 로고
    • Integrins mediate adhesion to agrin and modulate agrin signaling
    • Martin P.T., Sanes J.R. Integrins mediate adhesion to agrin and modulate agrin signaling. Development. 124:1997;3909-3917.
    • (1997) Development , vol.124 , pp. 3909-3917
    • Martin, P.T.1    Sanes, J.R.2
  • 51
    • 0032538841 scopus 로고    scopus 로고
    • A functional role for specific spliced variants of the alpha7beta1 integrin in acetylcholine receptor clustering
    • Burkin D.J., Gu M., Hodges B.L., Campanelli J.T., Kaufman S.J. A functional role for specific spliced variants of the alpha7beta1 integrin in acetylcholine receptor clustering. J Cell Biol. 143:1998;1067-1075.
    • (1998) J Cell Biol , vol.143 , pp. 1067-1075
    • Burkin, D.J.1    Gu, M.2    Hodges, B.L.3    Campanelli, J.T.4    Kaufman, S.J.5
  • 52
    • 0033824947 scopus 로고    scopus 로고
    • Laminin and alpha7beta1 integrin regulate agrin-induced clustering of acetylcholine receptors
    • Burkin D.J., Kim J.E., Gu M., Kaufinan S.J. Laminin and alpha7beta1 integrin regulate agrin-induced clustering of acetylcholine receptors. J Cell Sci. 113:2000;2877-2886.
    • (2000) J Cell Sci , vol.113 , pp. 2877-2886
    • Burkin, D.J.1    Kim, J.E.2    Gu, M.3    Kaufinan, S.J.4
  • 54
    • 0028935061 scopus 로고
    • Acetylcholine receptor gene expression at the developing neuromuscular junction
    • Duclert A., Changeux J.P. Acetylcholine receptor gene expression at the developing neuromuscular junction. Physiol Rev. 75:1995;339-368.
    • (1995) Physiol Rev , vol.75 , pp. 339-368
    • Duclert, A.1    Changeux, J.P.2
  • 56
    • 0026517609 scopus 로고
    • Muscle-derived agrin in cultured myotubes: Expression in the basal lamina and at induced acetylcholine receptor clusters
    • Lieth E., Cardasis C.A., Fallon J.R. Muscle-derived agrin in cultured myotubes: expression in the basal lamina and at induced acetylcholine receptor clusters. Dev Biol. 149:1992;41-54.
    • (1992) Dev Biol , vol.149 , pp. 41-54
    • Lieth, E.1    Cardasis, C.A.2    Fallon, J.R.3


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