메뉴 건너뛰기




Volumn 19, Issue 5, 2009, Pages 366-378

Aberrant development of neuromuscular junctions in glycosylation-defective Largemyd mice

Author keywords

Dystroglycan; Glycosylation; Neuromuscular junction; Skeletal muscle

Indexed keywords

AGRIN; ALPHA BUNGAROTOXIN; CHOLINERGIC RECEPTOR;

EID: 67349118126     PISSN: 09608966     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nmd.2009.02.011     Document Type: Article
Times cited : (17)

References (70)
  • 1
    • 0028935085 scopus 로고
    • Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors
    • Martin P.T., and Sanes J.R. Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors. Neuron 14 (1995) 743-754
    • (1995) Neuron , vol.14 , pp. 743-754
    • Martin, P.T.1    Sanes, J.R.2
  • 2
    • 0032951240 scopus 로고    scopus 로고
    • Distinct structures and functions of related pre- and postsynaptic carbohydrates at the mammalian neuromuscular junction
    • Martin P.T., Scott L.J., Porter B.E., and Sanes J.R. Distinct structures and functions of related pre- and postsynaptic carbohydrates at the mammalian neuromuscular junction. Mol Cell Neurosci 13 (1999) 105-118
    • (1999) Mol Cell Neurosci , vol.13 , pp. 105-118
    • Martin, P.T.1    Scott, L.J.2    Porter, B.E.3    Sanes, J.R.4
  • 3
    • 0036118161 scopus 로고    scopus 로고
    • Glycobiology of the synapse
    • Martin P.T. Glycobiology of the synapse. Glycobiology 12 (2002) 1R-7R
    • (2002) Glycobiology , vol.12
    • Martin, P.T.1
  • 4
    • 0031149753 scopus 로고    scopus 로고
    • N-glycosylation at the conserved sites ensures the expression of properly folded functional ACh receptors
    • Gehle V.M., Walcott E.C., Nishizaki T., and Sumikawa K. N-glycosylation at the conserved sites ensures the expression of properly folded functional ACh receptors. Brain Res Mol Brain Res 45 (1997) 219-229
    • (1997) Brain Res Mol Brain Res , vol.45 , pp. 219-229
    • Gehle, V.M.1    Walcott, E.C.2    Nishizaki, T.3    Sumikawa, K.4
  • 5
    • 0025605063 scopus 로고
    • Mutational analysis of muscle nicotinic acetylcholine receptor subunit assembly
    • Blount P., and Merlie J.P. Mutational analysis of muscle nicotinic acetylcholine receptor subunit assembly. J Cell Biol 111 (1990) 2613-2622
    • (1990) J Cell Biol , vol.111 , pp. 2613-2622
    • Blount, P.1    Merlie, J.P.2
  • 6
    • 0020027832 scopus 로고
    • Inhibition of glycosylation with tunicamycin blocks assembly of newly synthesized acetylcholine receptor subunits in muscle cells
    • Merlie J.P., Sebbane R., Tzartos S., and Lindstrom J. Inhibition of glycosylation with tunicamycin blocks assembly of newly synthesized acetylcholine receptor subunits in muscle cells. J Biol Chem 257 (1982) 2694-2701
    • (1982) J Biol Chem , vol.257 , pp. 2694-2701
    • Merlie, J.P.1    Sebbane, R.2    Tzartos, S.3    Lindstrom, J.4
  • 7
    • 0020614157 scopus 로고
    • Effect of tunicamycin, an inhibitor of protein glycosylation, on the biological properties of acetylcholine receptor in cultured muscle cells
    • Prives J., and Bar-Sagi D. Effect of tunicamycin, an inhibitor of protein glycosylation, on the biological properties of acetylcholine receptor in cultured muscle cells. J Biol Chem 258 (1983) 1775-1780
    • (1983) J Biol Chem , vol.258 , pp. 1775-1780
    • Prives, J.1    Bar-Sagi, D.2
  • 8
    • 0028813382 scopus 로고
    • Agrin is a heparan sulfate proteoglycan
    • Tsen G., Halfter W., Kroger S., and Cole G.J. Agrin is a heparan sulfate proteoglycan. J Biol Chem 270 (1995) 3392-3399
    • (1995) J Biol Chem , vol.270 , pp. 3392-3399
    • Tsen, G.1    Halfter, W.2    Kroger, S.3    Cole, G.J.4
  • 9
    • 0041529510 scopus 로고    scopus 로고
    • Agrin is a chimeric proteoglycan with the attachment sites for heparan sulfate/chondroitin sulfate located in two multiple serine-glycine clusters
    • Winzen U., Cole G.J., and Halfter W. Agrin is a chimeric proteoglycan with the attachment sites for heparan sulfate/chondroitin sulfate located in two multiple serine-glycine clusters. J Biol Chem 278 (2003) 30106-30114
    • (2003) J Biol Chem , vol.278 , pp. 30106-30114
    • Winzen, U.1    Cole, G.J.2    Halfter, W.3
  • 10
    • 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., and 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
  • 11
    • 0037184974 scopus 로고    scopus 로고
    • MuSK glycosylation restrains MuSK activation and acetylcholine receptor clustering
    • Watty A., and Burden S.J. MuSK glycosylation restrains MuSK activation and acetylcholine receptor clustering. J Biol Chem 277 (2002) 50457-50462
    • (2002) J Biol Chem , vol.277 , pp. 50457-50462
    • Watty, A.1    Burden, S.J.2
  • 12
    • 0033814140 scopus 로고    scopus 로고
    • Molecular basis of muscular dystrophies
    • Cohn R.D., and Campbell K.P. Molecular basis of muscular dystrophies. Muscle Nerve 23 (2000) 1456-1471
    • (2000) Muscle Nerve , vol.23 , pp. 1456-1471
    • Cohn, R.D.1    Campbell, K.P.2
  • 13
    • 9244239201 scopus 로고    scopus 로고
    • Structural abnormalities at neuromuscular synapses lacking multiple syntrophin isoforms
    • Adams M.E., Kramarcy N., Fukuda T., Engel A.G., Sealock R., and Froehner S.C. Structural abnormalities at neuromuscular synapses lacking multiple syntrophin isoforms. J Neurosci 24 (2004) 10302-10309
    • (2004) J Neurosci , vol.24 , pp. 10302-10309
    • Adams, M.E.1    Kramarcy, N.2    Fukuda, T.3    Engel, A.G.4    Sealock, R.5    Froehner, S.C.6
  • 14
    • 8044260252 scopus 로고    scopus 로고
    • Postsynaptic abnormalities at the neuromuscular junctions of utrophin-deficient mice
    • Deconinck A.E., Potter A.C., Tinsley J.M., Wood S.J., Vater R., Young C., et al. Postsynaptic abnormalities at the neuromuscular junctions of utrophin-deficient mice. J Cell Biol 136 (1997) 883-894
    • (1997) J Cell Biol , vol.136 , pp. 883-894
    • Deconinck, A.E.1    Potter, A.C.2    Tinsley, J.M.3    Wood, S.J.4    Vater, R.5    Young, C.6
  • 15
    • 0034981528 scopus 로고    scopus 로고
    • Properly formed but improperly localized synaptic specializations in the absence of laminin α4
    • Patton B.L., Cunningham J.M., Thyboll J., Kortesmaa J., Westerblad H., Edstrom L., et al. Properly formed but improperly localized synaptic specializations in the absence of laminin α4. Nat Neurosci 4 (2001) 597-604
    • (2001) Nat Neurosci , vol.4 , pp. 597-604
    • Patton, B.L.1    Cunningham, J.M.2    Thyboll, J.3    Kortesmaa, J.4    Westerblad, H.5    Edstrom, L.6
  • 16
    • 0030927063 scopus 로고    scopus 로고
    • Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice
    • Williamson R.A., Henry M.D., Daniels K.J., Hrstka R.F., Lee J.C., Sunada Y., et al. Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice. Hum Mol Genet 6 (1997) 831-841
    • (1997) Hum Mol Genet , vol.6 , pp. 831-841
    • Williamson, R.A.1    Henry, M.D.2    Daniels, K.J.3    Hrstka, R.F.4    Lee, J.C.5    Sunada, Y.6
  • 17
    • 0041710928 scopus 로고    scopus 로고
    • Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses
    • Cote P.D., Moukhles H., Lindenbaum M., and Carbonetto S. Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses. Nat Genet 23 (1999) 338-342
    • (1999) Nat Genet , vol.23 , pp. 338-342
    • Cote, P.D.1    Moukhles, H.2    Lindenbaum, M.3    Carbonetto, S.4
  • 18
    • 0035809195 scopus 로고    scopus 로고
    • The dystroglycan complex is necessary for stabilization of acetylcholine receptor clusters at neuromuscular junctions and formation of the synaptic basement membrane
    • Jacobson C., Cote P.D., Rossi S.G., Rotundo R.L., and Carbonetto S. The dystroglycan complex is necessary for stabilization of acetylcholine receptor clusters at neuromuscular junctions and formation of the synaptic basement membrane. J Cell Biol 152 (2001) 435-450
    • (2001) J Cell Biol , vol.152 , pp. 435-450
    • Jacobson, C.1    Cote, P.D.2    Rossi, S.G.3    Rotundo, R.L.4    Carbonetto, S.5
  • 19
    • 0034975777 scopus 로고    scopus 로고
    • Mutant glycosyltransferase and altered glycosylation of α-dystroglycan in the myodystrophy mouse
    • Grewal P.K., Holzfeind P.J., Bittner R.E., and Hewitt J.E. Mutant glycosyltransferase and altered glycosylation of α-dystroglycan in the myodystrophy mouse. Nat Genet 28 (2001) 151-154
    • (2001) Nat Genet , vol.28 , pp. 151-154
    • Grewal, P.K.1    Holzfeind, P.J.2    Bittner, R.E.3    Hewitt, J.E.4
  • 20
    • 0036799939 scopus 로고    scopus 로고
    • Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle-eye-brain disorders
    • Holzfeind P.J., Grewal P.K., Reitsamer H.A., Kechvar J., Lassmann H., Hoeger H., et al. Skeletal, cardiac and tongue muscle pathology, defective retinal transmission, and neuronal migration defects in the Large(myd) mouse defines a natural model for glycosylation-deficient muscle-eye-brain disorders. Hum Mol Genet 11 (2002) 2673-2687
    • (2002) Hum Mol Genet , vol.11 , pp. 2673-2687
    • Holzfeind, P.J.1    Grewal, P.K.2    Reitsamer, H.A.3    Kechvar, J.4    Lassmann, H.5    Hoeger, H.6
  • 21
    • 0037173670 scopus 로고    scopus 로고
    • Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies
    • Michele D.E., Barresi R., Kanagawa M., Saito F., Cohn R.D., Satz J.S., et al. Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. Nature 418 (2002) 417-422
    • (2002) Nature , vol.418 , pp. 417-422
    • Michele, D.E.1    Barresi, R.2    Kanagawa, M.3    Saito, F.4    Cohn, R.D.5    Satz, J.S.6
  • 23
    • 0141925704 scopus 로고    scopus 로고
    • Glycosylation defects: a new mechanism for muscular dystrophy?
    • Grewal P.K., and Hewitt J.E. Glycosylation defects: a new mechanism for muscular dystrophy?. Hum Mol Genet 12 Spec No. 2 (2003) R259-R264
    • (2003) Hum Mol Genet , vol.12 , Issue.Spec 2
    • Grewal, P.K.1    Hewitt, J.E.2
  • 24
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: from biosynthesis to pathogenesis of human disease
    • Barresi R., and Campbell K.P. Dystroglycan: from biosynthesis to pathogenesis of human disease. J Cell Sci 119 (2006) 199-207
    • (2006) J Cell Sci , vol.119 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 25
    • 0037173629 scopus 로고    scopus 로고
    • Deletion of brain dystroglycan recapitulates aspects of congenital muscular dystrophy
    • Moore S.A., Saito F., Chen J., Michele D.E., Henry M.D., Messing A., et al. Deletion of brain dystroglycan recapitulates aspects of congenital muscular dystrophy. Nature 418 (2002) 422-425
    • (2002) Nature , vol.418 , pp. 422-425
    • Moore, S.A.1    Saito, F.2    Chen, J.3    Michele, D.E.4    Henry, M.D.5    Messing, A.6
  • 26
    • 0036930663 scopus 로고    scopus 로고
    • Restoration of synapse formation in Musk mutant mice expressing a Musk/Trk chimeric receptor
    • Herbst R., Avetisova E., and Burden S.J. Restoration of synapse formation in Musk mutant mice expressing a Musk/Trk chimeric receptor. Development 129 (2002) 5449-5460
    • (2002) Development , vol.129 , pp. 5449-5460
    • Herbst, R.1    Avetisova, E.2    Burden, S.J.3
  • 27
    • 0034602844 scopus 로고    scopus 로고
    • The juxtamembrane region of MuSK has a critical role in agrin-mediated signaling
    • Herbst R., and Burden S.J. The juxtamembrane region of MuSK has a critical role in agrin-mediated signaling. Embo J 19 (2000) 67-77
    • (2000) Embo J , vol.19 , pp. 67-77
    • Herbst, R.1    Burden, S.J.2
  • 28
    • 0028971642 scopus 로고
    • Neuregulin receptors, erbB3 and erbB4, are localized at neuromuscular synapses
    • Zhu X., Lai C., Thomas S., and Burden S.J. Neuregulin receptors, erbB3 and erbB4, are localized at neuromuscular synapses. Embo J 14 (1995) 5842-5848
    • (1995) Embo J , vol.14 , pp. 5842-5848
    • Zhu, X.1    Lai, C.2    Thomas, S.3    Burden, S.J.4
  • 29
    • 78651012385 scopus 로고
    • A biochemical method for localizing cholinesterase activity
    • Koelle G.B., and Friedenwald J.S. A biochemical method for localizing cholinesterase activity. Proc Soc Ex Biol Methods 70 (1949) 617-622
    • (1949) Proc Soc Ex Biol Methods , vol.70 , pp. 617-622
    • Koelle, G.B.1    Friedenwald, J.S.2
  • 31
    • 0030848338 scopus 로고    scopus 로고
    • Skeletal and cardiac myopathies in mice lacking utrophin and dystrophin: a model for Duchenne muscular dystrophy
    • Grady R.M., Teng H., Nichol M.C., Cunningham J.C., Wilkinson R.S., and Sanes J.R. Skeletal and cardiac myopathies in mice lacking utrophin and dystrophin: a model for Duchenne muscular dystrophy. Cell 90 (1997) 729-738
    • (1997) Cell , vol.90 , pp. 729-738
    • Grady, R.M.1    Teng, H.2    Nichol, M.C.3    Cunningham, J.C.4    Wilkinson, R.S.5    Sanes, J.R.6
  • 32
    • 15844417385 scopus 로고    scopus 로고
    • The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo
    • DeChiara T.M., Bowen D.C., Valenzuela D.M., Simmons M.V., Poueymirou W.T., Thomas S., et al. The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo. Cell 85 (1996) 501-512
    • (1996) Cell , vol.85 , pp. 501-512
    • DeChiara, T.M.1    Bowen, D.C.2    Valenzuela, D.M.3    Simmons, M.V.4    Poueymirou, W.T.5    Thomas, S.6
  • 33
    • 0029050847 scopus 로고
    • Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyn-deficient mice
    • Gautam M., Noakes P.G., Mudd J., Nichol M., Chu G.C., Sanes J.R., et al. Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyn-deficient mice. Nature 377 (1995) 232-236
    • (1995) Nature , vol.377 , pp. 232-236
    • Gautam, M.1    Noakes, P.G.2    Mudd, J.3    Nichol, M.4    Chu, G.C.5    Sanes, J.R.6
  • 34
    • 0029893117 scopus 로고    scopus 로고
    • Defective neuromuscular synaptogenesis in agrin-deficient mutant mice
    • Gautam M., Noakes P.G., Moscoso L., Rupp F., Scheller R.H., Merlie J.P., 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    Rupp, F.4    Scheller, R.H.5    Merlie, J.P.6
  • 35
    • 0027935193 scopus 로고
    • β2-Syntrophin: localization at the neuromuscular junction in skeletal muscle
    • Peters M.F., Kramarcy N.R., Sealock R., and Froehner S.C. β2-Syntrophin: localization at the neuromuscular junction in skeletal muscle. Neuroreport 5 (1994) 1577-1580
    • (1994) Neuroreport , vol.5 , pp. 1577-1580
    • Peters, M.F.1    Kramarcy, N.R.2    Sealock, R.3    Froehner, S.C.4
  • 36
    • 0019904425 scopus 로고
    • Primary structure of α-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence
    • Noda M., Takahashi H., Tanabe T., Toyosato M., Furutani Y., Hirose T., et al. Primary structure of α-subunit precursor of Torpedo californica acetylcholine receptor deduced from cDNA sequence. Nature 299 (1982) 793-797
    • (1982) Nature , vol.299 , pp. 793-797
    • Noda, M.1    Takahashi, H.2    Tanabe, T.3    Toyosato, M.4    Furutani, Y.5    Hirose, T.6
  • 37
    • 0021132711 scopus 로고
    • Identification of the α-subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site
    • Kao P.N., Dwork A.J., Kaldany R.R., Silver M.L., Wideman J., Stein S., et al. Identification of the α-subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site. J Biol Chem 259 (1984) 11662-11665
    • (1984) J Biol Chem , vol.259 , pp. 11662-11665
    • Kao, P.N.1    Dwork, A.J.2    Kaldany, R.R.3    Silver, M.L.4    Wideman, J.5    Stein, S.6
  • 38
    • 3042585525 scopus 로고    scopus 로고
    • Glycobiology of the neuromuscular junction
    • Martin P.T. Glycobiology of the neuromuscular junction. J Neurocytol 32 (2003) 915-929
    • (2003) J Neurocytol , vol.32 , pp. 915-929
    • Martin, P.T.1
  • 39
    • 0022405847 scopus 로고
    • Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes
    • Blanchard D., Capon C., Leroy Y., Cartron J.P., and Fournet B. Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes. Biochem J 232 (1985) 813-818
    • (1985) Biochem J , vol.232 , pp. 813-818
    • Blanchard, D.1    Capon, C.2    Leroy, Y.3    Cartron, J.P.4    Fournet, B.5
  • 40
    • 0020643574 scopus 로고
    • A blood group Sda-active pentasaccharide isolated from Tamm-Horsfall urinary glycoprotein
    • Donald A.S., Yates A.D., Soh C.P., Morgan W.T., and Watkins W.M. A blood group Sda-active pentasaccharide isolated from Tamm-Horsfall urinary glycoprotein. Biochem Biophys Res Commun 115 (1983) 625-631
    • (1983) Biochem Biophys Res Commun , vol.115 , pp. 625-631
    • Donald, A.S.1    Yates, A.D.2    Soh, C.P.3    Morgan, W.T.4    Watkins, W.M.5
  • 41
    • 0025367755 scopus 로고
    • Comparison of the carbohydrate-binding specificities of seven N-acetyl-d-galactosamine-recognizing lectins
    • Piller V., Piller F., and Cartron J.P. Comparison of the carbohydrate-binding specificities of seven N-acetyl-d-galactosamine-recognizing lectins. Eur J Biochem 191 (1990) 461-466
    • (1990) Eur J Biochem , vol.191 , pp. 461-466
    • Piller, V.1    Piller, F.2    Cartron, J.P.3
  • 42
    • 24944532170 scopus 로고    scopus 로고
    • Ocular abnormalities in Large(myd) and Large(vls) mice, spontaneous models for muscle, eye, and brain diseases
    • Lee Y., Kameya S., Cox G.A., Hsu J., Hicks W., Maddatu T.P., et al. Ocular abnormalities in Large(myd) and Large(vls) mice, spontaneous models for muscle, eye, and brain diseases. Mol Cell Neurosci 30 (2005) 160-172
    • (2005) Mol Cell Neurosci , vol.30 , pp. 160-172
    • Lee, Y.1    Kameya, S.2    Cox, G.A.3    Hsu, J.4    Hicks, W.5    Maddatu, T.P.6
  • 43
    • 15244348873 scopus 로고    scopus 로고
    • Disruption of the mouse Large gene in the enr and myd mutants results in nerve, muscle, and neuromuscular junction defects
    • Levedakou E.N., Chen X.J., Soliven B., and Popko B. Disruption of the mouse Large gene in the enr and myd mutants results in nerve, muscle, and neuromuscular junction defects. Mol Cell Neurosci 28 (2005) 757-769
    • (2005) Mol Cell Neurosci , vol.28 , pp. 757-769
    • Levedakou, E.N.1    Chen, X.J.2    Soliven, B.3    Popko, B.4
  • 44
    • 33645806539 scopus 로고    scopus 로고
    • Aberrant neuromuscular junctions and delayed terminal muscle fiber maturation in α-dystroglycanopathies
    • Taniguchi M., Kurahashi H., Noguchi S., Fukudome T., Okinaga T., Tsukahara T., et al. Aberrant neuromuscular junctions and delayed terminal muscle fiber maturation in α-dystroglycanopathies. Hum Mol Genet 15 (2006) 1279-1289
    • (2006) Hum Mol Genet , vol.15 , pp. 1279-1289
    • Taniguchi, M.1    Kurahashi, H.2    Noguchi, S.3    Fukudome, T.4    Okinaga, T.5    Tsukahara, T.6
  • 46
    • 0034279193 scopus 로고    scopus 로고
    • Structural and functional alterations of neuromuscular junctions in NCAM-deficient mice
    • Rafuse V.F., Polo-Parada L., and Landmesser L.T. Structural and functional alterations of neuromuscular junctions in NCAM-deficient mice. J Neurosci 20 (2000) 6529-6539
    • (2000) J Neurosci , vol.20 , pp. 6529-6539
    • Rafuse, V.F.1    Polo-Parada, L.2    Landmesser, L.T.3
  • 47
    • 45249085301 scopus 로고    scopus 로고
    • Structural factors influencing the efficacy of neuromuscular transmission
    • Slater C.R. Structural factors influencing the efficacy of neuromuscular transmission. Ann NY Acad Sci 1132 (2008) 1-12
    • (2008) Ann NY Acad Sci , vol.1132 , pp. 1-12
    • Slater, C.R.1
  • 48
    • 1842613541 scopus 로고    scopus 로고
    • Nerve-independent formation of a topologically complex postsynaptic apparatus
    • Kummer T.T., Misgeld T., Lichtman J.W., and Sanes J.R. Nerve-independent formation of a topologically complex postsynaptic apparatus. J Cell Biol 164 (2004) 1077-1087
    • (2004) J Cell Biol , vol.164 , pp. 1077-1087
    • Kummer, T.T.1    Misgeld, T.2    Lichtman, J.W.3    Sanes, J.R.4
  • 49
    • 0030879133 scopus 로고    scopus 로고
    • Laminin-induced acetylcholine receptor clustering: an alternative pathway
    • Sugiyama J.E., Glass D.J., Yancopoulos G.D., and Hall Z.W. Laminin-induced acetylcholine receptor clustering: an alternative pathway. J Cell Biol 139 (1997) 181-191
    • (1997) J Cell Biol , vol.139 , pp. 181-191
    • Sugiyama, J.E.1    Glass, D.J.2    Yancopoulos, G.D.3    Hall, Z.W.4
  • 50
    • 20444362083 scopus 로고    scopus 로고
    • Neurotransmitter acetylcholine negatively regulates neuromuscular synapse formation by a Cdk5-dependent mechanism
    • Lin W., Dominguez B., Yang J., Aryal P., Brandon E.P., Gage F.H., et al. Neurotransmitter acetylcholine negatively regulates neuromuscular synapse formation by a Cdk5-dependent mechanism. Neuron 46 (2005) 569-579
    • (2005) Neuron , vol.46 , pp. 569-579
    • Lin, W.1    Dominguez, B.2    Yang, J.3    Aryal, P.4    Brandon, E.P.5    Gage, F.H.6
  • 51
    • 23344453327 scopus 로고    scopus 로고
    • Agrin promotes synaptic differentiation by counteracting an inhibitory effect of neurotransmitter
    • Misgeld T., Kummer T.T., Lichtman J.W., and Sanes J.R. Agrin promotes synaptic differentiation by counteracting an inhibitory effect of neurotransmitter. Proc Natl Acad Sci USA 102 (2005) 11088-11093
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11088-11093
    • Misgeld, T.1    Kummer, T.T.2    Lichtman, J.W.3    Sanes, J.R.4
  • 52
    • 0037709890 scopus 로고    scopus 로고
    • Unique role of dystroglycan in peripheral nerve myelination, nodal structure, and sodium channel stabilization
    • Saito F., Moore S.A., Barresi R., Henry M.D., Messing A., Ross-Barta S.E., et al. Unique role of dystroglycan in peripheral nerve myelination, nodal structure, and sodium channel stabilization. Neuron 38 (2003) 747-758
    • (2003) Neuron , vol.38 , pp. 747-758
    • Saito, F.1    Moore, S.A.2    Barresi, R.3    Henry, M.D.4    Messing, A.5    Ross-Barta, S.E.6
  • 53
    • 0345119040 scopus 로고    scopus 로고
    • Glial cells maintain synaptic structure and function and promote development of the neuromuscular junction in vivo
    • Reddy L.V., Koirala S., Sugiura Y., Herrera A.A., and Ko C.P. Glial cells maintain synaptic structure and function and promote development of the neuromuscular junction in vivo. Neuron 40 (2003) 563-580
    • (2003) Neuron , vol.40 , pp. 563-580
    • Reddy, L.V.1    Koirala, S.2    Sugiura, Y.3    Herrera, A.A.4    Ko, C.P.5
  • 54
    • 0034073858 scopus 로고    scopus 로고
    • Cysteine-rich domain isoforms of the neuregulin-1 gene are required for maintenance of peripheral synapses
    • Wolpowitz D., Mason T.B., Dietrich P., Mendelsohn M., Talmage D.A., and Role L.W. Cysteine-rich domain isoforms of the neuregulin-1 gene are required for maintenance of peripheral synapses. Neuron 25 (2000) 79-91
    • (2000) Neuron , vol.25 , pp. 79-91
    • Wolpowitz, D.1    Mason, T.B.2    Dietrich, P.3    Mendelsohn, M.4    Talmage, D.A.5    Role, L.W.6
  • 55
    • 0022454719 scopus 로고
    • Molecular distinction between fetal and adult forms of muscle acetylcholine receptor
    • Mishina M., Takai T., Imoto K., Noda M., Takahashi T., Numa S., et al. Molecular distinction between fetal and adult forms of muscle acetylcholine receptor. Nature 321 (1986) 406-411
    • (1986) Nature , vol.321 , pp. 406-411
    • Mishina, M.1    Takai, T.2    Imoto, K.3    Noda, M.4    Takahashi, T.5    Numa, S.6
  • 56
    • 0030813536 scopus 로고    scopus 로고
    • Identification of equivalent residues in the gamma, delta, and epsilon subunits of the nicotinic receptor that contribute to α-bungarotoxin binding
    • Sine S.M. Identification of equivalent residues in the gamma, delta, and epsilon subunits of the nicotinic receptor that contribute to α-bungarotoxin binding. J Biol Chem 272 (1997) 23521-23527
    • (1997) J Biol Chem , vol.272 , pp. 23521-23527
    • Sine, S.M.1
  • 57
    • 0037997772 scopus 로고
    • Structure, oligosaccharide structures, and posttranslationally modified sites of the nicotinic acetylcholine receptor
    • Poulter L., Earnest J.P., Stroud R.M., and Burlingame A.L. Structure, oligosaccharide structures, and posttranslationally modified sites of the nicotinic acetylcholine receptor. Proc Natl Acad Sci USA 86 (1989) 6645-6649
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6645-6649
    • Poulter, L.1    Earnest, J.P.2    Stroud, R.M.3    Burlingame, A.L.4
  • 58
    • 0026653556 scopus 로고
    • Detailed structural analysis of asparagine-linked oligosaccharides of the nicotinic acetylcholine receptor from Torpedo californica
    • Shoji H., Takahashi N., Nomoto H., Ishikawa M., Shimada I., Arata Y., et al. Detailed structural analysis of asparagine-linked oligosaccharides of the nicotinic acetylcholine receptor from Torpedo californica. Eur J Biochem 207 (1992) 631-641
    • (1992) Eur J Biochem , vol.207 , pp. 631-641
    • Shoji, H.1    Takahashi, N.2    Nomoto, H.3    Ishikawa, M.4    Shimada, I.5    Arata, Y.6
  • 60
    • 0026709052 scopus 로고
    • Assembly of mutant subunits of the nicotinic acetylcholine receptor lacking the conserved disulfide loop structure
    • Sumikawa K., and Gehle V.M. Assembly of mutant subunits of the nicotinic acetylcholine receptor lacking the conserved disulfide loop structure. J Biol Chem 267 (1992) 6286-6290
    • (1992) J Biol Chem , vol.267 , pp. 6286-6290
    • Sumikawa, K.1    Gehle, V.M.2
  • 61
    • 0025887334 scopus 로고
    • Site-directed mutagenesis of the conserved N-glycosylation site on the nicotinic acetylcholine receptor subunits
    • Gehle V.M., and Sumikawa K. Site-directed mutagenesis of the conserved N-glycosylation site on the nicotinic acetylcholine receptor subunits. Brain Res Mol Brain Res 11 (1991) 17-25
    • (1991) Brain Res Mol Brain Res , vol.11 , pp. 17-25
    • Gehle, V.M.1    Sumikawa, K.2
  • 62
    • 3142731311 scopus 로고    scopus 로고
    • LARGE can functionally bypass α-dystroglycan glycosylation defects in distinct congenital muscular dystrophies
    • Barresi R., Michele D.E., Kanagawa M., Harper H.A., Dovico S.A., Satz J.S., et al. LARGE can functionally bypass α-dystroglycan glycosylation defects in distinct congenital muscular dystrophies. Nat Med 10 (2004) 696-703
    • (2004) Nat Med , vol.10 , pp. 696-703
    • Barresi, R.1    Michele, D.E.2    Kanagawa, M.3    Harper, H.A.4    Dovico, S.A.5    Satz, J.S.6
  • 63
    • 0021111873 scopus 로고
    • The B4 lectin from Vicia villosa seeds interacts with N-acetylgalactosamine residues α-linked to serine or threonine residues in cell surface glycoproteins
    • Tollefsen S.E., and Kornfeld R. The B4 lectin from Vicia villosa seeds interacts with N-acetylgalactosamine residues α-linked to serine or threonine residues in cell surface glycoproteins. J Biol Chem 258 (1983) 5172-5176
    • (1983) J Biol Chem , vol.258 , pp. 5172-5176
    • Tollefsen, S.E.1    Kornfeld, R.2
  • 64
    • 0021111871 scopus 로고
    • Isolation and characterization of lectins from Vicia villosa. Two distinct carbohydrate-binding activities are present in seed extracts
    • Tollefsen S.E., and Kornfeld R. Isolation and characterization of lectins from Vicia villosa. Two distinct carbohydrate-binding activities are present in seed extracts. J Biol Chem 258 (1983) 5165-5171
    • (1983) J Biol Chem , vol.258 , pp. 5165-5171
    • Tollefsen, S.E.1    Kornfeld, R.2
  • 65
    • 0026481151 scopus 로고
    • Carbohydrate-binding specificity of the Tn-antigen binding lectin from Vicia villosa seeds (VVLB4)
    • Puri K.D., Gopalakrishnan B., and Surolia A. Carbohydrate-binding specificity of the Tn-antigen binding lectin from Vicia villosa seeds (VVLB4). FEBS Lett 312 (1992) 208-212
    • (1992) FEBS Lett , vol.312 , pp. 208-212
    • Puri, K.D.1    Gopalakrishnan, B.2    Surolia, A.3
  • 66
    • 0037203241 scopus 로고    scopus 로고
    • Definition of pre- and postsynaptic forms of the CT carbohydrate antigen at the neuromuscular junction: ubiquitous expression of the CT antigens and the CT GalNAc transferase in mouse tissues
    • Hoyte K., Kang C., and Martin P.T. Definition of pre- and postsynaptic forms of the CT carbohydrate antigen at the neuromuscular junction: ubiquitous expression of the CT antigens and the CT GalNAc transferase in mouse tissues. Brain Res Mol Brain Res 109 (2002) 146-160
    • (2002) Brain Res Mol Brain Res , vol.109 , pp. 146-160
    • Hoyte, K.1    Kang, C.2    Martin, P.T.3
  • 67
    • 0020458870 scopus 로고
    • Lectin binding reveals a synapse-specific carbohydrate in skeletal muscle
    • Sanes J.R., and Cheney J.M. Lectin binding reveals a synapse-specific carbohydrate in skeletal muscle. Nature 300 (1982) 646-647
    • (1982) Nature , vol.300 , pp. 646-647
    • Sanes, J.R.1    Cheney, J.M.2
  • 68
    • 0036468066 scopus 로고    scopus 로고
    • Overexpression of the CT GalNAc transferase in skeletal muscle alters myofiber growth, neuromuscular structure, and laminin expression
    • Xia B., Hoyte K., Kammesheidt A., Deerinck T., Ellisman M., and Martin P.T. Overexpression of the CT GalNAc transferase in skeletal muscle alters myofiber growth, neuromuscular structure, and laminin expression. Dev Biol 242 (2002) 58-73
    • (2002) Dev Biol , vol.242 , pp. 58-73
    • Xia, B.1    Hoyte, K.2    Kammesheidt, A.3    Deerinck, T.4    Ellisman, M.5    Martin, P.T.6
  • 69
    • 0032712593 scopus 로고    scopus 로고
    • O-mannosyl glycans in mammals
    • Endo T. O-mannosyl glycans in mammals. Biochim Biophys Acta 1473 (1999) 237-246
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 237-246
    • Endo, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.