메뉴 건너뛰기




Volumn 122, Issue 3, 2003, Pages 659-668

Calcium-dependent maintenance of agrin-induced postsynaptic specializations

Author keywords

Acetylcholine receptor; MuSK; Neuromuscular junction

Indexed keywords

AGRIN; CALCIUM; CHOLINERGIC RECEPTOR; PERVANADATE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE MUSK; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0242569304     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0306-4522(03)00602-X     Document Type: Article
Times cited : (15)

References (64)
  • 2
    • 0033569388 scopus 로고    scopus 로고
    • Rapid and reversible effects of activity on acetylcholine receptor density at the neuromuscular junction in vivo
    • Akaaboune M., Culican S.M., Turney S.G., Lichtman J.W. Rapid and reversible effects of activity on acetylcholine receptor density at the neuromuscular junction in vivo. Science. 286:1999;503-507.
    • (1999) Science , vol.286 , pp. 503-507
    • Akaaboune, M.1    Culican, S.M.2    Turney, S.G.3    Lichtman, J.W.4
  • 3
    • 0030940161 scopus 로고    scopus 로고
    • Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold
    • Apel E.D., Glass D.J., Moscoso L.M., Yancopolous G.D., Sanes J.R. Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold. Neuron. 18:1997;623-635.
    • (1997) Neuron , vol.18 , pp. 623-635
    • Apel, E.D.1    Glass, D.J.2    Moscoso, L.M.3    Yancopolous, G.D.4    Sanes, J.R.5
  • 4
    • 0027462315 scopus 로고
    • In vivo observations of pre- and postsynaptic changes during the transition from multiple to single innervation at developing neuromuscular junctions
    • Balice-Gordon R.J., Lichtman J.W. In vivo observations of pre- and postsynaptic changes during the transition from multiple to single innervation at developing neuromuscular junctions. J Neurosci. 13:1993;834-855.
    • (1993) J Neurosci , vol.13 , pp. 834-855
    • Balice-Gordon, R.J.1    Lichtman, J.W.2
  • 5
    • 0036135033 scopus 로고    scopus 로고
    • Dual role for calcium in agrin signaling and acetylcholine receptor clustering
    • Borges L.S., Lee Y., Ferns M. Dual role for calcium in agrin signaling and acetylcholine receptor clustering. J Neurobiol. 50:2002;69-79.
    • (2002) J Neurobiol , vol.50 , pp. 69-79
    • Borges, L.S.1    Lee, Y.2    Ferns, M.3
  • 6
    • 0028321841 scopus 로고
    • Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: A heteromeric complex related to the dystroglycans
    • Bowe M.A., Deyst K.A., Leszyk J.D., Fallon J.R. Identification and purification of an agrin receptor from Torpedo postsynaptic membranes a heteromeric complex related to the dystroglycans . Neuron. 12:1994;1173-1180.
    • (1994) Neuron , vol.12 , pp. 1173-1180
    • Bowe, M.A.1    Deyst, K.A.2    Leszyk, J.D.3    Fallon, J.R.4
  • 8
    • 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
  • 9
    • 0037320813 scopus 로고    scopus 로고
    • Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein
    • Coleman S.K., Cai C., Mottershead D.G., Haapalahti J.P., Keinanen K. Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein. J Neurosci. 23:2003;798-806.
    • (2003) J Neurosci , vol.23 , pp. 798-806
    • Coleman, S.K.1    Cai, C.2    Mottershead, D.G.3    Haapalahti, J.P.4    Keinanen, K.5
  • 10
    • 0032125483 scopus 로고    scopus 로고
    • Axon withdrawal during synapse elimination at the neuromuscular junction is accompanied by disassembly of the postsynaptic specialization and withdrawal of Schwann cell processes
    • Culican S.M., Nelson C.C., Lichtman J.W. Axon withdrawal during synapse elimination at the neuromuscular junction is accompanied by disassembly of the postsynaptic specialization and withdrawal of Schwann cell processes. J Neurosci. 18:1998;4953-4965.
    • (1998) J Neurosci , vol.18 , pp. 4953-4965
    • Culican, S.M.1    Nelson, C.C.2    Lichtman, J.W.3
  • 11
    • 0032578035 scopus 로고    scopus 로고
    • A role of tyrosine phosphatase in acetylcholine receptor cluster dispersal and formation
    • Dai Z., Peng H.B. A role of tyrosine phosphatase in acetylcholine receptor cluster dispersal and formation. J Cell Biol. 141:1998;1613-1624.
    • (1998) J Cell Biol , vol.141 , pp. 1613-1624
    • Dai, Z.1    Peng, H.B.2
  • 13
    • 0030059338 scopus 로고    scopus 로고
    • Signaling from synapse to nucleus: Postsynaptic CREB phosphorylation during multiple forms of hippocampal synaptic plasticity
    • Deisseroth K., Bito H., Tsien R.W. Signaling from synapse to nucleus postsynaptic CREB phosphorylation during multiple forms of hippocampal synaptic plasticity . Neuron. 16:1996;89-101.
    • (1996) Neuron , vol.16 , pp. 89-101
    • Deisseroth, K.1    Bito, H.2    Tsien, R.W.3
  • 14
    • 0030789733 scopus 로고    scopus 로고
    • Association of muscle-specific kinase MuSK with the acetylcholine receptor in mammalian muscle
    • Fuhrer C., Sugiyama J.E., Taylor R.G., Hall Z.W. Association of muscle-specific kinase MuSK with the acetylcholine receptor in mammalian muscle. EMBO J. 16:1997;4951-4960.
    • (1997) EMBO J , vol.16 , pp. 4951-4960
    • Fuhrer, C.1    Sugiyama, J.E.2    Taylor, R.G.3    Hall, Z.W.4
  • 16
    • 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., Merlie J.P. 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    Merlie, J.P.7
  • 18
    • 0033231419 scopus 로고    scopus 로고
    • Disruption of Trkb-mediated signaling induces disassembly of postsynaptic receptor clusters at neuromuscular junctions
    • Gonzalez M., Ruggiero F.P., Chang Q., Shi Y.J., Rich M.M., Kraner S., Balice-Gordon R.J. Disruption of Trkb-mediated signaling induces disassembly of postsynaptic receptor clusters at neuromuscular junctions. Neuron. 24:1999;567-583.
    • (1999) Neuron , vol.24 , pp. 567-583
    • Gonzalez, M.1    Ruggiero, F.P.2    Chang, Q.3    Shi, Y.J.4    Rich, M.M.5    Kraner, S.6    Balice-Gordon, R.J.7
  • 19
    • 0035992379 scopus 로고    scopus 로고
    • Development of glutamatergic synapses in the rat retina: The postnatal expression of ionotropic glutamate receptor subunits
    • Hack I., Koulen P., Peichl L., Brandstatter J.H. Development of glutamatergic synapses in the rat retina the postnatal expression of ionotropic glutamate receptor subunits . Vis Neurosci. 19:2002;1-13.
    • (2002) Vis Neurosci , vol.19 , pp. 1-13
    • Hack, I.1    Koulen, P.2    Peichl, L.3    Brandstatter, J.H.4
  • 20
    • 0030048631 scopus 로고    scopus 로고
    • Stabilizing neuromuscular contacts increases motoneuron survival after neonatal nerve injury in rats
    • Harding D.I., Greensmith L., Connold A.L., Vrbova G. Stabilizing neuromuscular contacts increases motoneuron survival after neonatal nerve injury in rats. Neuroscience. 70:1996;799-805.
    • (1996) Neuroscience , vol.70 , pp. 799-805
    • Harding, D.I.1    Greensmith, L.2    Connold, A.L.3    Vrbova, G.4
  • 21
    • 0034669148 scopus 로고    scopus 로고
    • Dystroglycan overexpression in vivo alters acetylcholine receptor aggregation at the neuromuscular junction
    • Heathcote R.D., Ekman J.M., Campbell K.P., Godfrey E.W. Dystroglycan overexpression in vivo alters acetylcholine receptor aggregation at the neuromuscular junction. Dev Biol. 227:2000;595-605.
    • (2000) Dev Biol , vol.227 , pp. 595-605
    • Heathcote, R.D.1    Ekman, J.M.2    Campbell, K.P.3    Godfrey, E.W.4
  • 22
    • 0036315343 scopus 로고    scopus 로고
    • Subcellular localization of GABA receptors in the central nervous system using post-embedding immunohistochemistry
    • Heck W.L., Slusarczyk A., Basaraba A.M., Schweitzer L. Subcellular localization of GABA receptors in the central nervous system using post-embedding immunohistochemistry. Brain Res Brain Res Protoc. 9:2002;173-180.
    • (2002) Brain Res Brain Res Protoc , vol.9 , pp. 173-180
    • Heck, W.L.1    Slusarczyk, A.2    Basaraba, A.M.3    Schweitzer, L.4
  • 23
    • 0036930663 scopus 로고    scopus 로고
    • Restoration of synapse formation in MuSK mutant mice expressing a MuSK/Trk chimeric receptor
    • Herbst R., Avetisova E., 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
  • 24
    • 0034602844 scopus 로고    scopus 로고
    • The juxtamembrane region of MuSK has a critical role in agrin-mediated signaling
    • Herbst R., 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
  • 25
    • 0032513058 scopus 로고    scopus 로고
    • Dimerization of the muscle-specific kinase induces tyrosine phosphorylation of acetylcholine peceptors and their aggregation on the surface of myotubes
    • Hopf C., Hoch W. Dimerization of the muscle-specific kinase induces tyrosine phosphorylation of acetylcholine peceptors and their aggregation on the surface of myotubes. J Biol Chem. 273:1998;6467-6473.
    • (1998) J Biol Chem , vol.273 , pp. 6467-6473
    • Hopf, C.1    Hoch, W.2
  • 26
    • 0032522775 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the muscle-specific kinase is exclusively induced by acetylcholine receptor-aggregating agrin fragments
    • Hopf C., Hoch W. Tyrosine phosphorylation of the muscle-specific kinase is exclusively induced by acetylcholine receptor-aggregating agrin fragments. Eur J Biochem. 253:1998;382-389.
    • (1998) Eur J Biochem , vol.253 , pp. 382-389
    • Hopf, C.1    Hoch, W.2
  • 27
    • 0032529544 scopus 로고    scopus 로고
    • Alpha-Dystroglycan functions in acetylcholine receptor aggregation but is not a coreceptor for agrin-MuSK signaling
    • Jacobson C., Montanaro F., Lindenbaum M., Carbonetto S., Ferns M. alpha-Dystroglycan functions in acetylcholine receptor aggregation but is not a coreceptor for agrin-MuSK signaling. J Neurosci. 18:1998;6340-6348.
    • (1998) J Neurosci , vol.18 , pp. 6340-6348
    • Jacobson, C.1    Montanaro, F.2    Lindenbaum, M.3    Carbonetto, S.4    Ferns, M.5
  • 28
    • 0034530293 scopus 로고    scopus 로고
    • Nitric oxide is a downstream mediator of agrin-induced acetylcholine receptor aggregation
    • Jones M.A., Werle M.J. Nitric oxide is a downstream mediator of agrin-induced acetylcholine receptor aggregation. Mol Cell Neurosci. 16:2000;649-660.
    • (2000) Mol Cell Neurosci , vol.16 , pp. 649-660
    • Jones, M.A.1    Werle, M.J.2
  • 29
    • 0035866068 scopus 로고    scopus 로고
    • Pertussis toxin-sensitive G-protein and protein kinase C activity are involved in normal synapse elimination in the neonatal rat muscle
    • Lanuza M.A., Garcia N., Santafe M., Nelson P.G., Fenoll-Brunet M.R., Tomas J. Pertussis toxin-sensitive G-protein and protein kinase C activity are involved in normal synapse elimination in the neonatal rat muscle. J Neurosci Res. 63:2001;330-340.
    • (2001) J Neurosci Res , vol.63 , pp. 330-340
    • Lanuza, M.A.1    Garcia, N.2    Santafe, M.3    Nelson, P.G.4    Fenoll-Brunet, M.R.5    Tomas, J.6
  • 30
    • 0033764559 scopus 로고    scopus 로고
    • Synapse elimination and indelible memory
    • Lichtman J.W., Colman H. Synapse elimination and indelible memory. Neuron. 25:2000;269-278.
    • (2000) Neuron , vol.25 , pp. 269-278
    • Lichtman, J.W.1    Colman, H.2
  • 31
    • 0027233511 scopus 로고
    • Muscle agrin: Neural regulation and localization at nerve-induced acetylcholine receptor clusters
    • Lieth E., Fallon J.R. Muscle agrin neural regulation and localization at nerve-induced acetylcholine receptor clusters . J Neurosci. 13:1993;2509-2514.
    • (1993) J Neurosci , vol.13 , pp. 2509-2514
    • Lieth, E.1    Fallon, J.R.2
  • 34
    • 0024389582 scopus 로고
    • Molecules in basal lamina that direct the formation of synaptic specializations at neuromuscular junctions
    • McMahan U.J., Wallace B.G. Molecules in basal lamina that direct the formation of synaptic specializations at neuromuscular junctions. Dev Neurosci. 11:1989;227-247.
    • (1989) Dev Neurosci , vol.11 , pp. 227-247
    • Mcmahan, U.J.1    Wallace, B.G.2
  • 35
    • 0031972621 scopus 로고    scopus 로고
    • Intracellular calcium regulates agrin-induced acetylcholine receptor clustering
    • Megeath L.J., Fallon J.R. Intracellular calcium regulates agrin-induced acetylcholine receptor clustering. J Neurosci. 18:1998;672-678.
    • (1998) J Neurosci , vol.18 , pp. 672-678
    • Megeath, L.J.1    Fallon, J.R.2
  • 36
    • 0025996816 scopus 로고
    • Purification and characterization of a protein tyrosine phosphatase which dephosphorylates the nicotinic acetylcholine receptor
    • Mei L., Huganir R.L. Purification and characterization of a protein tyrosine phosphatase which dephosphorylates the nicotinic acetylcholine receptor. J Biol Chem. 266:1991;16063-16072.
    • (1991) J Biol Chem , vol.266 , pp. 16063-16072
    • Mei, L.1    Huganir, R.L.2
  • 37
    • 0031865212 scopus 로고    scopus 로고
    • Recruitment of a nicotinic acetylcholine receptor mutant lacking cytoplasmic tyrosine residues in its beta subunit into agrin-induced aggregates
    • Meyer G., Wallace B.G. Recruitment of a nicotinic acetylcholine receptor mutant lacking cytoplasmic tyrosine residues in its beta subunit into agrin-induced aggregates. Mol Cell Neurosci. 11:1998;324-333.
    • (1998) Mol Cell Neurosci , vol.11 , pp. 324-333
    • Meyer, G.1    Wallace, B.G.2
  • 38
    • 0035957950 scopus 로고    scopus 로고
    • Agrin-induced activation of acetylcholine receptor-bound Src family kinases requires Rapsyn and correlates with acetylcholine receptor clustering
    • Mittaud P., Marangi P.A., Erb-Vogtli S., Fuhrer C. Agrin-induced activation of acetylcholine receptor-bound Src family kinases requires Rapsyn and correlates with acetylcholine receptor clustering. J Biol Chem. 276:2001;14505-14513.
    • (2001) J Biol Chem , vol.276 , pp. 14505-14513
    • Mittaud, P.1    Marangi, P.A.2    Erb-Vogtli, S.3    Fuhrer, C.4
  • 39
    • 0035370294 scopus 로고    scopus 로고
    • Src-class kinases act within the agrin/MuSK pathway to regulate acetylcholine receptor phosphorylation, cytoskeletal anchoring, and clustering
    • Mohamed A.S., Rivas-Plata K.A., Kraas J.R., Saleh S.M., Swope S.L. Src-class kinases act within the agrin/MuSK pathway to regulate acetylcholine receptor phosphorylation, cytoskeletal anchoring, and clustering. J Neurosci. 21:2001;3806-3818.
    • (2001) J Neurosci , vol.21 , pp. 3806-3818
    • Mohamed, A.S.1    Rivas-Plata, K.A.2    Kraas, J.R.3    Saleh, S.M.4    Swope, S.L.5
  • 41
    • 0242397552 scopus 로고
    • Agrin binding to neurons of the embryonic chick spinal cord
    • Nastuk M.A., Fallon J.R. Agrin binding to neurons of the embryonic chick spinal cord. Soc Neurosci Abstr. 17:1991;219.
    • (1991) Soc Neurosci Abstr , vol.17 , pp. 219
    • Nastuk, M.A.1    Fallon, J.R.2
  • 42
    • 0026041581 scopus 로고
    • The putative agrin receptor binds ligand in a calcium-dependent manner and aggregates during agrin-induced acetylcholine receptor clustering
    • Nastuk M.A., Lieth E., Ma J., Cardasis C.A., Moynihan E.B., McKechnie B.A., Fallon J.R. The putative agrin receptor binds ligand in a calcium-dependent manner and aggregates during agrin-induced acetylcholine receptor clustering. Neuron. 7:1991;807-818.
    • (1991) Neuron , vol.7 , pp. 807-818
    • Nastuk, M.A.1    Lieth, E.2    Ma, J.3    Cardasis, C.A.4    Moynihan, E.B.5    Mckechnie, B.A.6    Fallon, J.R.7
  • 43
    • 0029886442 scopus 로고    scopus 로고
    • Mechanism of synapse disassembly at the developing neuromuscular junction
    • Nguyen Q.T., Lichtman J.W. Mechanism of synapse disassembly at the developing neuromuscular junction. Curr Opin Neurobiol. 6:1996;104-112.
    • (1996) Curr Opin Neurobiol , vol.6 , pp. 104-112
    • Nguyen, Q.T.1    Lichtman, J.W.2
  • 44
    • 0025026367 scopus 로고
    • Agrin-induced reorganization of extracellular matrix components on cultured myotubes: Relationship to AChR-aggregation
    • Nitkin R.M., Rothschild T.C. Agrin-induced reorganization of extracellular matrix components on cultured myotubes relationship to AChR-aggregation . J Cell Biol. 111:1990;1161-1170.
    • (1990) J Cell Biol , vol.111 , pp. 1161-1170
    • Nitkin, R.M.1    Rothschild, T.C.2
  • 45
    • 0033153155 scopus 로고    scopus 로고
    • Synaptic clustering of AMPA receptors by the extracellular immediate-early gene product Narp
    • O'Brien R.J., Xu D., Petralia R.S., Steward O., Huganir R.L., Worley P. Synaptic clustering of AMPA receptors by the extracellular immediate-early gene product Narp. Neuron. 23:1999;309-323.
    • (1999) Neuron , vol.23 , pp. 309-323
    • O'brien, R.J.1    Xu, D.2    Petralia, R.S.3    Steward, O.4    Huganir, R.L.5    Worley, P.6
  • 46
  • 47
    • 0035813230 scopus 로고    scopus 로고
    • Identification of tyrosine phosphorylation sites on 3-phosphoinositide- dependent protein kinase-1 and their role in regulating kinase activity
    • Park J., Hill M.M., Hess D., Brazil D.P., Hofsteenge J., Hemmings B.A. Identification of tyrosine phosphorylation sites on 3-phosphoinositide- dependent protein kinase-1 and their role in regulating kinase activity. J Biol Chem. 276:2001;37459-37471.
    • (2001) J Biol Chem , vol.276 , pp. 37459-37471
    • Park, J.1    Hill, M.M.2    Hess, D.3    Brazil, D.P.4    Hofsteenge, J.5    Hemmings, B.A.6
  • 48
    • 0024307890 scopus 로고
    • In vivo visualization of pre- and postsynaptic changes during synapse elimination in reinnervated mouse muscle
    • Rich M.M., Lichtman J.W. In vivo visualization of pre- and postsynaptic changes during synapse elimination in reinnervated mouse muscle. J Neurosci. 9:1989;1781-1805.
    • (1989) J Neurosci , vol.9 , pp. 1781-1805
    • Rich, M.M.1    Lichtman, J.W.2
  • 49
    • 0027212083 scopus 로고
    • Spatial calcium buffering in saccular hair cells
    • Roberts W.M. Spatial calcium buffering in saccular hair cells. Nature. 363:1993;74-76.
    • (1993) Nature , vol.363 , pp. 74-76
    • Roberts, W.M.1
  • 50
    • 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
  • 51
    • 0032936983 scopus 로고    scopus 로고
    • Development of the vertebrate neuromuscular junction
    • Sanes J.R., Lichtman J.W. Development of the vertebrate neuromuscular junction. Annu Rev Neurosci. 22:1999;389-442.
    • (1999) Annu Rev Neurosci , vol.22 , pp. 389-442
    • Sanes, J.R.1    Lichtman, J.W.2
  • 52
    • 0035511932 scopus 로고    scopus 로고
    • Induction, assembly, maturation and maintenance of a postsynaptic apparatus
    • Sanes J.R., Lichtman J.W. Induction, assembly, maturation and maintenance of a postsynaptic apparatus. Nat Rev Neurosci. 2:2001;791-805.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 791-805
    • Sanes, J.R.1    Lichtman, J.W.2
  • 53
    • 0035341457 scopus 로고    scopus 로고
    • Src, Fyn, and Yes are not required for neuromuscular synapse formation but are necessary for stabilization of agrin-induced clusters of acetylcholine receptors
    • Smith C.L., Mittaud P., Prescott E.D., Fuhrer C., Burden S.J. Src, Fyn, and Yes are not required for neuromuscular synapse formation but are necessary for stabilization of agrin-induced clusters of acetylcholine receptors. J Neurosci. 21:2001;3151-3160.
    • (2001) J Neurosci , vol.21 , pp. 3151-3160
    • Smith, C.L.1    Mittaud, P.2    Prescott, E.D.3    Fuhrer, C.4    Burden, S.J.5
  • 55
    • 0026504464 scopus 로고
    • Buffering of calcium in the vicinity of a channel pore
    • Stern M.D. Buffering of calcium in the vicinity of a channel pore. Cell Calcium. 13:1992;183-192.
    • (1992) Cell Calcium , vol.13 , pp. 183-192
    • Stern, M.D.1
  • 56
    • 0030879133 scopus 로고    scopus 로고
    • Laminin-induced acetylcholine receptor clustering: An alternative pathway
    • Sugiyama J.E., Glass D.J., Yancopoulos G.D., 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
  • 57
    • 0019333905 scopus 로고
    • New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures
    • Tsien R.Y. New calcium indicators and buffers with high selectivity against magnesium and protons design, synthesis, and properties of prototype structures . Biochemistry. 19:1980;2396-2404.
    • (1980) Biochemistry , vol.19 , pp. 2396-2404
    • Tsien, R.Y.1
  • 58
    • 0023729036 scopus 로고
    • ++ and phorbol ester
    • ++ and phorbol ester. J Cell Biol. 107:1988;267-278.
    • (1988) J Cell Biol , vol.107 , pp. 267-278
    • Wallace, B.G.1
  • 59
    • 0028956758 scopus 로고
    • Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase
    • Wallace B.G. Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase. J Cell Biol. 128:1995;1121-1129.
    • (1995) J Cell Biol , vol.128 , pp. 1121-1129
    • Wallace, B.G.1
  • 60
    • 0025779156 scopus 로고
    • Agrin induces phosphorylation of the nicotinic acetylcholine receptor
    • Wallace B.G., Qu Z., Huganir R.L. Agrin induces phosphorylation of the nicotinic acetylcholine receptor. Neuron. 6:1991;869-878.
    • (1991) Neuron , vol.6 , pp. 869-878
    • Wallace, B.G.1    Qu, Z.2    Huganir, R.L.3
  • 61
    • 0033531225 scopus 로고    scopus 로고
    • GABA(A)-receptor-associated protein links GABA(A) receptors and the cytoskeleton
    • Wang H., Bedford F.K., Brandon N.J., Moss S.J., Olsen R.W. GABA(A)-receptor-associated protein links GABA(A) receptors and the cytoskeleton. Nature. 397:1999;69-72.
    • (1999) Nature , vol.397 , pp. 69-72
    • Wang, H.1    Bedford, F.K.2    Brandon, N.J.3    Moss, S.J.4    Olsen, R.W.5
  • 63
    • 0034631836 scopus 로고    scopus 로고
    • Agrin-induced acetylcholine receptor clustering is mediated by the small guanosine triphosphatases Rac and Cdc42
    • Weston C., Yee B., Hod E., Prives J. Agrin-induced acetylcholine receptor clustering is mediated by the small guanosine triphosphatases Rac and Cdc42. J Cell Biol. 150:2000;205-212.
    • (2000) J Cell Biol , vol.150 , pp. 205-212
    • Weston, C.1    Yee, B.2    Hod, E.3    Prives, J.4
  • 64
    • 0033152452 scopus 로고    scopus 로고
    • Variability in the time course of single photon responses from toad rods: Termination of rhodopsin's activity
    • Whitlock G.G., Lamb T.D. Variability in the time course of single photon responses from toad rods termination of rhodopsin's activity . Neuron. 23:1999;337-351.
    • (1999) Neuron , vol.23 , pp. 337-351
    • Whitlock, G.G.1    Lamb, T.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.