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Volumn 78, Issue 2, 1997, Pages 1135-1143

N-methyl-D-aspartate evokes rapid net depolymerization of filamentous actin in cultured rat cerebellar granule cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CYTOCHALASIN; N METHYL DEXTRO ASPARTIC ACID; PHALLOTOXIN;

EID: 0030857117     PISSN: 00223077     EISSN: None     Source Type: Journal    
DOI: 10.1152/jn.1997.78.2.1135     Document Type: Article
Times cited : (19)

References (62)
  • 1
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • AGNEW, B. J., MINAMIDE, L. S., AND HAMBURG, J. R. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. biol. Chem. 270: 17582-17587, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Hamburg, J.R.3
  • 2
    • 0028603483 scopus 로고
    • Gelsolin displaces phalloidin from actin filaments
    • ALLEN, P. G. AND JANMEY, P. A. Gelsolin displaces phalloidin from actin filaments. J. Biol. Chem. 269: 32916-32923, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32916-32923
    • Allen, P.G.1    Janmey, P.A.2
  • 3
    • 0027183089 scopus 로고
    • Cytochalasin modulation of nicotinic cholinergic receptor expression and muscarinic receptor function in human TE671/RD cells: A possible functional role of the cytoskeleton
    • BENCHERIF, M. AND LUKAS, R. J. Cytochalasin modulation of nicotinic cholinergic receptor expression and muscarinic receptor function in human TE671/RD cells: a possible functional role of the cytoskeleton. J. Neurochem. 61: 852-864, 1993.
    • (1993) J. Neurochem. , vol.61 , pp. 852-864
    • Bencherif, M.1    Lukas, R.J.2
  • 4
    • 0024708109 scopus 로고
    • Cycling of actin assembly in synaptosomes and neurotransmitter release
    • BERNSTEIN, B. W. AND BAMBURG, J. R. Cycling of actin assembly in synaptosomes and neurotransmitter release. Neuron 3: 257-265, 1989.
    • (1989) Neuron , vol.3 , pp. 257-265
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 6
    • 0025219721 scopus 로고
    • Chemoattractant-stimulated polymorphonuclear leukocytes contain two populations of actin filaments that differ in their spatial distributions and relative stabilities
    • CASSIMERIS, L., MCNEILL, H., AND ZIGMOND, S. H. Chemoattractant-stimulated polymorphonuclear leukocytes contain two populations of actin filaments that differ in their spatial distributions and relative stabilities. J. Cell Biol. 110: 1067-1075, 1990.
    • (1990) J. Cell Biol. , vol.110 , pp. 1067-1075
    • Cassimeris, L.1    Mcneill, H.2    Zigmond, S.H.3
  • 7
    • 0003075812 scopus 로고
    • Cytoskeleton in secretion and neurotransmitter release
    • edited by R. D. Burgoyne. New York: Wiley-Liss
    • CHEEK, T. R. AND BURGOYNE, R. D. Cytoskeleton in secretion and neurotransmitter release. In: The Neuronal Cytoskeleton, edited by R. D. Burgoyne. New York: Wiley-Liss, 1991, p. 309-325..
    • (1991) The Neuronal Cytoskeleton , pp. 309-325
    • Cheek, T.R.1    Burgoyne, R.D.2
  • 8
    • 0023427610 scopus 로고
    • Effects of cytochalasins and phalloidin on actin
    • COOPER, J. A. Effects of cytochalasins and phalloidin on actin. J. Cell Biol. 105: 1473-1478, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 9
    • 0029998871 scopus 로고    scopus 로고
    • The dynamics of dendritic structure in developing hippocampal slices
    • DAILEY, M. E. AND SMITH, S. J. The dynamics of dendritic structure in developing hippocampal slices. J. Neurosci. 16: 2983-2994, 1996.
    • (1996) J. Neurosci. , vol.16 , pp. 2983-2994
    • Dailey, M.E.1    Smith, S.J.2
  • 10
    • 0029129811 scopus 로고
    • Characterization of excitoprotective actions of N-methyl-D-aspartate in cultured cerebellar granule neurons
    • DAMSCHRADER-WILLIAMS, P., IRWIN, R. P., LIN, S.-Z., AND PAUL, S. M. Characterization of excitoprotective actions of N-methyl-D-aspartate in cultured cerebellar granule neurons. J. Neurochem. 65: 1069-1076, 1995.
    • (1995) J. Neurochem. , vol.65 , pp. 1069-1076
    • Damschrader-Williams, P.1    Irwin, R.P.2    Lin, S.-Z.3    Paul, S.M.4
  • 11
    • 0029257299 scopus 로고
    • Induction of cytoskeleton rearrangements and loss of volume regulation in epithelial cells by
    • DE FILIPPO, A. B., ELLEN, R. P., AND MCCULLOCH, A. G. Induction of cytoskeleton rearrangements and loss of volume regulation in epithelial cells by Treponema denticola. Arch. Oral Biol. 40: 199-207, 1995.
    • (1995) Treponema Denticola. Arch. Oral Biol. , vol.40 , pp. 199-207
    • De Filippo, A.B.1    Ellen, R.P.2    Mcculloch, A.G.3
  • 12
    • 0026069186 scopus 로고
    • Parathyroid hormone promotes disassembly of cytoskeletal actin and myosin in cultured osteoblastic cells: Mediation by cyclic AMP
    • EGAN, J. J., GRONOWICZ, G., AND RODAN, G. A. Parathyroid hormone promotes disassembly of cytoskeletal actin and myosin in cultured osteoblastic cells: mediation by cyclic AMP. J. Cell. Biochem. 45: 101-111, 1991.
    • (1991) J. Cell. Biochem. , vol.45 , pp. 101-111
    • Egan, J.J.1    Gronowicz, G.2    Rodan, G.A.3
  • 13
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit
    • EHLERS, M. D., ZHANG, S., BERNHARDT, J. P., AND HUGANIR, R. L. Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell 84: 745-755, 1996.
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhardt, J.P.3    Huganir, R.L.4
  • 14
    • 0022971647 scopus 로고
    • Excitatory amino acids and intracellular pH in motoneurons of the isolated frog spinal cord
    • ENDRES, W., BALLANYI, K., SERVE, G., AND GRAFE. P. Excitatory amino acids and intracellular pH in motoneurons of the isolated frog spinal cord. Neurosci. Lett. 72: 54-58, 1986.
    • (1986) Neurosci. Lett. , vol.72 , pp. 54-58
    • Endres, W.1    Ballanyi, K.2    Serve, G.3    Grafe, P.4
  • 15
    • 0027192866 scopus 로고
    • The organisation of F-actin and microtubules in growth cones exposed to brain-derived collapsing factor
    • FAN, J., MANSFIELD, S. G., REDMOND, T., GORDON-WEEKS, P. R., AND RAPER, J. A. The organisation of F-actin and microtubules in growth cones exposed to brain-derived collapsing factor. J. Cell Biol. 121: 867-878, 1993.
    • (1993) J. Cell Biol. , vol.121 , pp. 867-878
    • Fan, J.1    Mansfield, S.G.2    Redmond, T.3    Gordon-Weeks, P.R.4    Raper, J.A.5
  • 16
    • 0027489905 scopus 로고
    • Focusing on unpolymerized actin
    • FECHHEIMER, M. AND ZIGMOND, S. H. Focusing on unpolymerized actin. J. Cell Biol. 123: 1-5, 1993.
    • (1993) J. Cell Biol. , vol.123 , pp. 1-5
    • Fechheimer, M.1    Zigmond, S.H.2
  • 17
    • 0024095187 scopus 로고
    • Actions of cytochalasins on the organisation of actin filaments and microtubules in a neuronal growth cone
    • FORSCHER, P. AND SMITH, S. Actions of cytochalasins on the organisation of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol. 107: 1505-1516, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.2
  • 18
    • 0027184957 scopus 로고
    • Cotranslational assembly of some cytoskeletal proteins: Implications and prospects
    • FULTON, A. B. AND L'ECUYER, T. Cotranslational assembly of some cytoskeletal proteins: implications and prospects. J. Cell Sci. 105: 867-871, 1993.
    • (1993) J. Cell Sci. , vol.105 , pp. 867-871
    • Fulton, A.B.1    L'Ecuyer, T.2
  • 19
    • 0029165076 scopus 로고
    • Cytochalasins protect hippocampal neurons against amyloid beta petide toxicity: Evidence that actin depolymerization suppresses calcium influx
    • FURUKAWA, K. AND MATTSON, M. P. Cytochalasins protect hippocampal neurons against amyloid beta petide toxicity: evidence that actin depolymerization suppresses calcium influx. J. Neurochem. 65: 1061-1068, 1995.
    • (1995) J. Neurochem. , vol.65 , pp. 1061-1068
    • Furukawa, K.1    Mattson, M.P.2
  • 21
    • 0025039456 scopus 로고
    • Activation of NMDA receptors induces rapid dephosphorylation of the cytoskeletal protein MAP2
    • HALPAIN, S. AND GREENGARD, P. Activation of NMDA receptors induces rapid dephosphorylation of the cytoskeletal protein MAP2. Neuron 5: 237-246, 1990.
    • (1990) Neuron , vol.5 , pp. 237-246
    • Halpain, S.1    Greengard, P.2
  • 22
    • 0026784141 scopus 로고
    • Mechanisms of actin rearrangements mediating platelet activation
    • HARTWIG, J. H. Mechanisms of actin rearrangements mediating platelet activation. J. Cell Biol. 118: 1421-1442, 1992.
    • (1992) J. Cell Biol. , vol.118 , pp. 1421-1442
    • Hartwig, J.H.1
  • 25
    • 0030048284 scopus 로고    scopus 로고
    • The role of cellular hydration in the regulation of cell function
    • HÄUSSINGER, D. The role of cellular hydration in the regulation of cell function. Biochem. J. 313: 697-710, 1996.
    • (1996) Biochem. J. , vol.313 , pp. 697-710
    • Häussinger, D.1
  • 26
    • 0022181812 scopus 로고
    • The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils
    • HOWARD, T. H. AND ORESAJO, C. O. The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils. J. Cell Biol. 101: 1078-1085, 1985a.
    • (1985) J. Cell Biol. , vol.101 , pp. 1078-1085
    • Howard, T.H.1    Oresajo, C.O.2
  • 27
    • 0022293456 scopus 로고
    • A method for quantifying f-actin in chemotactic peptide induced change in chemotactic peptide activated neutrophils: Study of the effect of fBOC peptide
    • HOWARD, T. H. AND ORESAJO, C. O. A method for quantifying f-actin in chemotactic peptide induced change in chemotactic peptide activated neutrophils: study of the effect of fBOC peptide. Cell Motil. 5: 545-557, 1985b.
    • (1985) Cell Motil. , vol.5 , pp. 545-557
    • Howard, T.H.1    Oresajo, C.O.2
  • 28
    • 0026593496 scopus 로고
    • Phallotoxin and actin binding assay by fluorescence enhancement
    • HUANG, Z., You, W., AND HAUGHLAND, R. P. Phallotoxin and actin binding assay by fluorescence enhancement (Abstract). Anal. Biochem. 200: 1992, 1992.
    • (1992) Anal. Biochem. , vol.200 , pp. 1992
    • Huang, Z.1    You, W.2    Haughland, R.P.3
  • 30
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • JANMEY, P. A. AND STOSSEL, T. P. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 325: 362-364, 1987.
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 32
    • 0020123666 scopus 로고
    • Actin polymerization and its regulation by proteins from nonmuscle cells
    • KORN, E. D. Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol. Rev. 62: 672-737, 1982.
    • (1982) Physiol. Rev. , vol.62 , pp. 672-737
    • Korn, E.D.1
  • 34
    • 0024415408 scopus 로고
    • Evidence that calcium may control neurite outgrowth by regulating the stability of actin filaments
    • LANKFORD, K. L. AND LETOURNEAU, P. C. Evidence that calcium may control neurite outgrowth by regulating the stability of actin filaments. J. Cell Biol. 109: 1229-1243, 1989.
    • (1989) J. Cell Biol. , vol.109 , pp. 1229-1243
    • Lankford, K.L.1    Letourneau, P.C.2
  • 35
    • 0028953495 scopus 로고
    • Growth cone advance is inversely proportional to retrograde F-actin flow
    • LIN, C.-H. AND FORSCHER, P. Growth cone advance is inversely proportional to retrograde F-actin flow. Neuron 14: 763-771, 1995.
    • (1995) Neuron , vol.14 , pp. 763-771
    • Lin, C.-H.1    Forscher, P.2
  • 36
    • 0018076070 scopus 로고
    • Characterisation of ionomycin as a calcium ionophore
    • LIU, C. AND HERMANN, T. E. Characterisation of ionomycin as a calcium ionophore. J. Biol. Chem. 253: 5892-5894, 1978.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5892-5894
    • Liu, C.1    Hermann, T.E.2
  • 38
    • 0023433171 scopus 로고
    • Agonist- And voltage-gated calcium entry in cultured mouse spinal cord neurons under voltage clamp measured using Arsenazo III
    • MAYER, M. L., MACDERMOTT, A. B., WESTBROOK, G. L., SMITH, S. J., AND BARKER, J. L. Agonist-and voltage-gated calcium entry in cultured mouse spinal cord neurons under voltage clamp measured using Arsenazo III. J. Neurosci. 7: 3230-3244, 1987.
    • (1987) J. Neurosci. , vol.7 , pp. 3230-3244
    • Mayer, M.L.1    MacDermott, A.B.2    Westbrook, G.L.3    Smith, S.J.4    Barker, J.L.5
  • 39
    • 0027162747 scopus 로고
    • N-methyl-D-aspartate stimulates the dephosphorylation of the microtubule-associated protein 2 and potentiates excitatory synaptic pathways in the rat hippocampus
    • MONTORO, R. J., DIAZ-NIDO, J., AVILA, J., AND LOPES-BARNEO, J. N-methyl-D-aspartate stimulates the dephosphorylation of the microtubule-associated protein 2 and potentiates excitatory synaptic pathways in the rat hippocampus. Neuroscience 54: 859-871, 1993.
    • (1993) Neuroscience , vol.54 , pp. 859-871
    • Montoro, R.J.1    Diaz-Nido, J.2    Avila, J.3    Lopes-Barneo, J.4
  • 40
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • MORRIS, R. L. AND HOLLENBECK, P. J. Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J. Cell Biol. 131: 1315-1326, 1995.
    • (1995) J. Cell Biol. , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 41
    • 0028889137 scopus 로고
    • Actin filament disassembly is a sufficient final trigger for exocytosis in non-excitable cells
    • MUALLEM, S., KWIATKOWSKA, K., XU, X., AND YIN, H. Actin filament disassembly is a sufficient final trigger for exocytosis in non-excitable cells. J. Cell biol. 128: 589-598, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 589-598
    • Muallem, S.1    Kwiatkowska, K.2    Xu, X.3    Yin, H.4
  • 42
    • 0028035005 scopus 로고
    • Disruption of microfilaments in growth cones following depolarization and calcium influx
    • NEELY, M. D. AND GESEMANN, M. Disruption of microfilaments in growth cones following depolarization and calcium influx. J. Neurosci. 14: 7511-7520, 1994.
    • (1994) J. Neurosci. , vol.14 , pp. 7511-7520
    • Neely, M.D.1    Gesemann, M.2
  • 43
    • 0024953749 scopus 로고
    • Calcium-activated neutral proteinases as regulators of cellular function. Implications for Alzheimer's disease pathogenesis
    • NIXON, R. A. Calcium-activated neutral proteinases as regulators of cellular function. Implications for Alzheimer's disease pathogenesis. Ann. NY Acad. Sci. 568: 198-208, 1989.
    • (1989) Ann. NY Acad. Sci. , vol.568 , pp. 198-208
    • Nixon, R.A.1
  • 44
    • 0021260967 scopus 로고
    • Magnesium gates glutamate-activated channels in mouse central neurones
    • NOWAK, L., BREGESTOVSKI, P. ASCHER, P., HERBET, A., AND PROCHIANTZ, A. Magnesium gates glutamate-activated channels in mouse central neurones. Nature Lond. 307: 462-465, 1984.
    • (1984) Nature Lond. , vol.307 , pp. 462-465
    • Nowak, L.1    Bregestovski, P.2    Ascher, P.3    Herbet, A.4    Prochiantz, A.5
  • 45
    • 0027992341 scopus 로고
    • Mechanosensitivity of NMDA receptors in cultured mouse central neurons
    • PAOLETTI, P. AND ASCHER, P. Mechanosensitivity of NMDA receptors in cultured mouse central neurons. Neuron 13: 645-655, 1994.
    • (1994) Neuron , vol.13 , pp. 645-655
    • Paoletti, P.1    Ascher, P.2
  • 46
    • 0028987148 scopus 로고
    • Characterisation of calcium channel currents in cultured rat cerebellar granule neurones
    • PEARSON, H. A., SUTTON, K. G., SCOTT, R. H., AND DOLPHIN, A. C. Characterisation of calcium channel currents in cultured rat cerebellar granule neurones. J. Physiol. (Lond.) 482: 493-509, 1995.
    • (1995) J. Physiol. (Lond.) , vol.482 , pp. 493-509
    • Pearson, H.A.1    Sutton, K.G.2    Scott, R.H.3    Dolphin, A.C.4
  • 47
    • 0026515691 scopus 로고
    • 2+-mediated secretion in parotid acinar cells is associated with reversible changes in the organisation of the cytoskeleton
    • 2+-mediated secretion in parotid acinar cells is associated with reversible changes in the organisation of the cytoskeleton. J. Cell biol. 116: 127-134, 1992.
    • (1992) J. Cell Biol. , vol.116 , pp. 127-134
    • Perrin, D.1    Moller, K.2    Hanke, K.3    Soling, H.D.4
  • 48
    • 0020646521 scopus 로고
    • Isolation of a calcium-dependent actin-fragmenting protein from brain, spinal cord, and cultured neurones
    • PETRUCCI, T. C., THOMAS, C., AND BRAY, D. Isolation of a calcium-dependent actin-fragmenting protein from brain, spinal cord, and cultured neurones. J. Neurochem. 40: 1507-1516, 1983.
    • (1983) J. Neurochem. , vol.40 , pp. 1507-1516
    • Petrucci, T.C.1    Thomas, C.2    Bray, D.3
  • 50
    • 0028800660 scopus 로고
    • The role of receptor/channel activity in neuronal cell migration
    • RAKIC, P. AND KOMURO, H. The role of receptor/channel activity in neuronal cell migration. J. Neurobiol. 26: 299-315, 1995.
    • (1995) J. Neurobiol. , vol.26 , pp. 299-315
    • Rakic, P.1    Komuro, H.2
  • 51
    • 0028944942 scopus 로고
    • Motility and cytoskeletal organisation of migrating cerebellar granule neurons
    • RIVAS, R. J. AND HATTEN, M. E. Motility and cytoskeletal organisation of migrating cerebellar granule neurons. J. Neurosci. 15: 981-989, 1995.
    • (1995) J. Neurosci. , vol.15 , pp. 981-989
    • Rivas, R.J.1    Hatten, M.E.2
  • 52
    • 0027258451 scopus 로고
    • Calcium-induced actin de-polymerization reduces NMDA channel activity
    • ROSENMUND, C. AND WESTBROOK, G. L. Calcium-induced actin de-polymerization reduces NMDA channel activity. Neuron 10: 805-814, 1993.
    • (1993) Neuron , vol.10 , pp. 805-814
    • Rosenmund, C.1    Westbrook, G.L.2
  • 53
  • 54
    • 0029928159 scopus 로고    scopus 로고
    • NMDA receptor activation-responsive phosphoproteins in the developing optic tectum
    • SCHEETZ, A. J. AND CONSTANTINE-PATON, M. NMDA receptor activation-responsive phosphoproteins in the developing optic tectum. J. Neurosci. 16: 1460-1469, 1996.
    • (1996) J. Neurosci. , vol.16 , pp. 1460-1469
    • Scheetz, A.J.1    Constantine-Paton, M.2
  • 55
    • 0023766340 scopus 로고
    • Stimulation of NMDA receptors induces proteolysis of spectrin in hippocampus
    • SEUBERT, P., LARSON, J., OLIVER, M., JUNG, M. W., BAUDRY, M., AND LYNCH, G. Stimulation of NMDA receptors induces proteolysis of spectrin in hippocampus. Brain Res. 460: 189-194, 1988.
    • (1988) Brain Res. , vol.460 , pp. 189-194
    • Seubert, P.1    Larson, J.2    Oliver, M.3    Jung, M.W.4    Baudry, M.5    Lynch, G.6
  • 56
    • 0029000811 scopus 로고
    • Actin filament organisation in the fish keratocyte lamellipodium
    • SMALL, J. V., HERZOG, M., AND ANDERSON, K. Actin filament organisation in the fish keratocyte lamellipodium. J. Cell Biol. 129: 1275-1286, 1995.
    • (1995) J. Cell Biol. , vol.129 , pp. 1275-1286
    • Small, J.V.1    Herzog, M.2    Anderson, K.3
  • 57
    • 0025785552 scopus 로고
    • Control of actin polymerization in live and permeabilized fibroblasts
    • SYMONS, M. H. AND MITCHISON, T. J. Control of actin polymerization in live and permeabilized fibroblasts. J. Cell Biol 114: 503-513, 1991.
    • (1991) J. Cell Biol , vol.114 , pp. 503-513
    • Symons, M.H.1    Mitchison, T.J.2
  • 58
    • 0028863477 scopus 로고
    • Making the connection: Cytoskeletal rearrangements during growth cone guidance
    • TANAKA, E. AND SABRY, J. Making the connection: cytoskeletal rearrangements during growth cone guidance. Cell 83: 171-176, 1995.
    • (1995) Cell , vol.83 , pp. 171-176
    • Tanaka, E.1    Sabry, J.2
  • 59
    • 0025840196 scopus 로고
    • Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin
    • VITALE, M. L., DEL CASTILLO, R., TCHAKAROV, L., AND TRIFARÓ, J.-M. Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin. J. Cell Biol. 113: 1057-1067, 1991.
    • (1991) J. Cell Biol. , vol.113 , pp. 1057-1067
    • Vitale, M.L.1    Del Castillo, R.2    Tchakarov, L.3    Trifaró, J.-M.4
  • 60
    • 0030042310 scopus 로고    scopus 로고
    • Effects of cytochalasin treatment on short term synaptic plasticity at developing neuromuscular junctions in frogs
    • WANG, X., ZHENG, J. Q., AND POO, M. Effects of cytochalasin treatment on short term synaptic plasticity at developing neuromuscular junctions in frogs. J. Physiol. (Lond.) 491: 187-195, 1996.
    • (1996) J. Physiol. (Lond.) , vol.491 , pp. 187-195
    • Wang, X.1    Zheng, J.Q.2    Poo, M.3
  • 61
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of α-actinin and calmodulin to the NMDA receptor
    • WYSZYNSKI, M., LIN, J., RAO, A., NIGH, E., BEGGS, A. H., CRAIG, A. M., AND SHENG, M. Competitive binding of α-actinin and calmodulin to the NMDA receptor. Nature 385: 439-442, 1997.
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 62
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • YIN, H. L. AND STOSSEL, T. P. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature 281: 583-586, 1979.
    • (1979) Nature , vol.281 , pp. 583-586
    • Yin, H.L.1    Stossel, T.P.2


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