메뉴 건너뛰기




Volumn 27, Issue , 2004, Pages 509-547

The synaptic vesicle cycle

Author keywords

Active zone; Calcium channel; Neurotransmitter release; RIM; Synaptic plasticity; Synaptotagmin

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; CALCIUM SENSITIZER; MONOCLONAL ANTIBODY; RAB PROTEIN; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; SYNTAXIN;

EID: 2942556680     PISSN: 0147006X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.neuro.26.041002.131412     Document Type: Review
Times cited : (1992)

References (209)
  • 2
    • 0027274981 scopus 로고
    • The Caenorhabditis elegans unc-17 gene: A putative vesicular acetylcholine transporter
    • Alfonso A, Grundahl K, Duerr JS, Man HP, Rand JB. 1993. The Caenorhabditis elegans unc-17 gene: a putative vesicular acetylcholine transporter. Science 261:617-19
    • (1993) Science , vol.261 , pp. 617-619
    • Alfonso, A.1    Grundahl, K.2    Duerr, J.S.3    Man, H.P.4    Rand, J.B.5
  • 3
    • 0034255152 scopus 로고    scopus 로고
    • The SNARE Vtila-beta is localized to small synaptic vesicles and participates in a novel SNARE complex
    • Antonin W, Riedel D, von Mollard GF. 2000. The SNARE Vtila-beta is localized to small synaptic vesicles and participates in a novel SNARE complex. J. Neurosci. 20:5724-32
    • (2000) J. Neurosci. , vol.20 , pp. 5724-5732
    • Antonin, W.1    Riedel, D.2    Von Mollard, G.F.3
  • 4
    • 0025308495 scopus 로고
    • Regulation of reversible binding of smg p25A to synaptic plasma membranes and vesicles by GDP dissociation inhibitor
    • Araki S, Kikuchi A, Hata Y, Isomura M, Takai Y. 1990. Regulation of reversible binding of smg p25A to synaptic plasma membranes and vesicles by GDP dissociation inhibitor. J. Biol. Chem. 265:13007-15
    • (1990) J. Biol. Chem. , vol.265 , pp. 13007-13015
    • Araki, S.1    Kikuchi, A.2    Hata, Y.3    Isomura, M.4    Takai, Y.5
  • 6
    • 0037166310 scopus 로고    scopus 로고
    • Complexin regulates the closure of the fusion pore during regulated vesicle exocytosis
    • Archer DA, Graham ME, Burgoyne RD. 2002. Complexin regulates the closure of the fusion pore during regulated vesicle exocytosis. J. Biol. Chem. 277:18249-52
    • (2002) J. Biol. Chem. , vol.277 , pp. 18249-18252
    • Archer, D.A.1    Graham, M.E.2    Burgoyne, R.D.3
  • 7
    • 0032531948 scopus 로고    scopus 로고
    • Delayed release of neurotransmitter from cerebellar granule cells
    • Atluri PP, Regehr WG. 1998. Delayed release of neurotransmitter from cerebellar granule cells. J. Neurosci. 18:8214-27
    • (1998) J. Neurosci. , vol.18 , pp. 8214-8227
    • Atluri, P.P.1    Regehr, W.G.2
  • 8
    • 0015441751 scopus 로고
    • Choline metabolism in the cerebral cortex of guinea pigs. Stable-bound acetylcholine
    • Barker LA, Dowdall MJ, Whittaker VP. 1972. Choline metabolism in the cerebral cortex of guinea pigs. Stable-bound acetylcholine. Biochem. J. 130:1063-75
    • (1972) Biochem. J. , vol.130 , pp. 1063-1075
    • Barker, L.A.1    Dowdall, M.J.2    Whittaker, V.P.3
  • 9
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • Augustin I, Rosenmund C, Südhof TC, Brose N. 1999. Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature 400:457-61
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Südhof, T.C.3    Brose, N.4
  • 10
    • 0035449939 scopus 로고    scopus 로고
    • Chronic blockade of glutamate receptors enhances presynaptic release and downregulates the interaction between synaptophysin-synaptobrevin 2
    • Bacci A, Coco S, Pravettoni E, Schenk U, Armano S, et al. 2001. Chronic blockade of glutamate receptors enhances presynaptic release and downregulates the interaction between synaptophysin-synaptobrevin 2. J. Neurosci. 21:6588-96
    • (2001) J. Neurosci. , vol.21 , pp. 6588-6596
    • Bacci, A.1    Coco, S.2    Pravettoni, E.3    Schenk, U.4    Armano, S.5
  • 12
    • 0015460664 scopus 로고
    • The kinetics of transmitter release at the frog neuromuscular junction
    • Barrett EF, Stevens CF. 1972. The kinetics of transmitter release at the frog neuromuscular junction. J. Physiol. 227:691-708
    • (1972) J. Physiol. , vol.227 , pp. 691-708
    • Barrett, E.F.1    Stevens, C.F.2
  • 14
    • 0025150653 scopus 로고
    • Origin of variability in quantal size in cultured hippocampal neurons and hippocampal slices
    • Bekkers JM, Richerson GB, Stevens CF. 1990. Origin of variability in quantal size in cultured hippocampal neurons and hippocampal slices. Proc. Natl. Acad. Sci. USA 87:5359-62
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5359-5362
    • Bekkers, J.M.1    Richerson, G.B.2    Stevens, C.F.3
  • 15
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett MK, Calakos N, Scheller RH. 1992. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257:255-59
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 16
    • 0024506755 scopus 로고
    • Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers
    • Benfenati F, Greengard P, Brunner J, Bahler M. 1989. Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers. J. Cell Biol. 108:1851-62
    • (1989) J. Cell Biol. , vol.108 , pp. 1851-1862
    • Benfenati, F.1    Greengard, P.2    Brunner, J.3    Bahler, M.4
  • 17
    • 0031027591 scopus 로고    scopus 로고
    • Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin
    • Betz A, Okamoto M, Benseler F, Brose N. 1997. Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin. J. Biol. Chem. 272:2520-26
    • (1997) J. Biol. Chem. , vol.272 , pp. 2520-2526
    • Betz, A.1    Okamoto, M.2    Benseler, F.3    Brose, N.4
  • 18
    • 0035030935 scopus 로고    scopus 로고
    • Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming
    • Betz A, Thakur P, Junge HJ, Ashery U, Rhee JS, et al. 2001. Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming. Neuron 30:183-96
    • (2001) Neuron , vol.30 , pp. 183-196
    • Betz, A.1    Thakur, P.2    Junge, H.J.3    Ashery, U.4    Rhee, J.S.5
  • 19
    • 0034637149 scopus 로고    scopus 로고
    • Calcium sensitivity of glutamate release in a calyx-type terminal
    • Bollmann JH, Sakmann B, Gerard J, Borst G. 2000. Calcium sensitivity of glutamate release in a calyx-type terminal. Science 289:953-57
    • (2000) Science , vol.289 , pp. 953-957
    • Bollmann, J.H.1    Sakmann, B.2    Gerard, J.3    Borst, G.4
  • 20
    • 0029738891 scopus 로고    scopus 로고
    • Calcium influx, and transmitter release in a fast CNS synapse
    • Borst JG, Sakmann B. 1996. Calcium influx, and transmitter release in a fast CNS synapse. Nature 383:431-34
    • (1996) Nature , vol.383 , pp. 431-434
    • Borst, J.G.1    Sakmann, B.2
  • 21
    • 0029616349 scopus 로고
    • Pre-and postsynaptic whole-cell recordings in the medial nucleus of the trapezoid body of the rat
    • Borst JGG, Helmchen F, Sakmann B. 1995. Pre-and postsynaptic whole-cell recordings in the medial nucleus of the trapezoid body of the rat. J. Physiol. 489:825-40
    • (1995) J. Physiol. , vol.489 , pp. 825-840
    • Borst, J.G.G.1    Helmchen, F.2    Sakmann, B.3
  • 22
    • 0023238873 scopus 로고
    • Currents through the fusion pore that forms during exocytosis of a secretory vesicle
    • Breckenridge LJ, Almers W. 1987. Currents through the fusion pore that forms during exocytosis of a secretory vesicle. Nature 328:814-17
    • (1987) Nature , vol.328 , pp. 814-817
    • Breckenridge, L.J.1    Almers, W.2
  • 23
    • 0342748583 scopus 로고    scopus 로고
    • Sequential steps in clathrin-mediated synaptic vesicle endocytosis
    • Brodin L, Low P, Shupliakov O. 2000. Sequential steps in clathrin-mediated synaptic vesicle endocytosis. Curr. Opin. Neurobiol. 10:312-20
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 312-320
    • Brodin, L.1    Low, P.2    Shupliakov, O.3
  • 24
    • 0028791349 scopus 로고
    • Mammalian homologues of C. elegans unc-13 gene define novel family of C2-domain proteins
    • Brose N, Hofmann K, Hata Y, Südhof TC. 1995 Mammalian homologues of C. elegans unc-13 gene define novel family of C2-domain proteins. J. Biol. Chem. 270:25273-80
    • (1995) J. Biol. Chem. , vol.270 , pp. 25273-25280
    • Brose, N.1    Hofmann, K.2    Hata, Y.3    Südhof, T.C.4
  • 26
    • 0021922503 scopus 로고
    • Identification of a transmembrane glycoprotein specific for secretory vesicles of neural and endocrine cells
    • Buckley K, Kelly RB. 1985. Identification of a transmembrane glycoprotein specific for secretory vesicles of neural and endocrine cells. J. Cell Biol. 100:1284-94
    • (1985) J. Cell Biol. , vol.100 , pp. 1284-1294
    • Buckley, K.1    Kelly, R.B.2
  • 27
    • 0027971368 scopus 로고
    • Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle
    • Calakos N, Scheller R. 1994. Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle. J. Biol. Chem. 269:24534-37
    • (1994) J. Biol. Chem. , vol.269 , pp. 24534-24537
    • Calakos, N.1    Scheller, R.2
  • 31
    • 0033570341 scopus 로고    scopus 로고
    • Presynaptic long-term potentiation in corticothalamic synapses
    • Castro-Alamancos MA, Calcagnotto ME. 1999. Presynaptic long-term potentiation in corticothalamic synapses. J. Neurosci. 19: 9090-97
    • (1999) J. Neurosci. , vol.19 , pp. 9090-9097
    • Castro-Alamancos, M.A.1    Calcagnotto, M.E.2
  • 32
    • 0015618402 scopus 로고
    • Turnover of transmitter and synaptic vesicles at the frog neuromuscular junction
    • Ceccarelli B, Hurlbut WP, Mauro A. 1973. Turnover of transmitter and synaptic vesicles at the frog neuromuscular junction. J. Cell Biol. 57:499-524
    • (1973) J. Cell Biol. , vol.57 , pp. 499-524
    • Ceccarelli, B.1    Hurlbut, W.P.2    Mauro, A.3
  • 35
    • 0037204076 scopus 로고    scopus 로고
    • Three-dimensional structure of the complexin/SNARE complex
    • Chen X, Tomchick DR, Kovrigin E, Arac D, Machius M, et al. 2002a. Three-dimensional structure of the complexin/SNARE complex. Neuron 33:397-409
    • (2002) Neuron , vol.33 , pp. 397-409
    • Chen, X.1    Tomchick, D.R.2    Kovrigin, E.3    Arac, D.4    Machius, M.5
  • 39
    • 0034044580 scopus 로고    scopus 로고
    • Multiple aspects of Rab protein action in the secretory pathway: Focus on Rab3 and Rab6
    • Darchen F, Goud B. 2000. Multiple aspects of Rab protein action in the secretory pathway: focus on Rab3 and Rab6. Biochimie 82:375-84
    • (2000) Biochimie , vol.82 , pp. 375-384
    • Darchen, F.1    Goud, B.2
  • 42
    • 0033575749 scopus 로고    scopus 로고
    • A conformational switch in syntaxin during exocytosis
    • Dulubova I, Sugita S, Hill S, Hosaka M, Fernandez I, et al. 1999. A conformational switch in syntaxin during exocytosis. EMBO J. 18:4372-82
    • (1999) EMBO J. , vol.18 , pp. 4372-4382
    • Dulubova, I.1    Sugita, S.2    Hill, S.3    Hosaka, M.4    Fernandez, I.5
  • 44
    • 0034663146 scopus 로고    scopus 로고
    • F-actin is concentrated in nonrelease domains at frog neuromuscular junctions
    • Dunaevsky A, Connor EA. 2000. F-actin is concentrated in nonrelease domains at frog neuromuscular junctions. J. Neurosci. 20:6007-12
    • (2000) J. Neurosci. , vol.20 , pp. 6007-6012
    • Dunaevsky, A.1    Connor, E.A.2
  • 45
    • 0028819440 scopus 로고
    • Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine
    • Edelmann L, Hanson PI, Chapman ER, Jahn R. 1995. Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. EMBO J. 14:224-31
    • (1995) EMBO J. , vol.14 , pp. 224-231
    • Edelmann, L.1    Hanson, P.I.2    Chapman, E.R.3    Jahn, R.4
  • 46
    • 0026458380 scopus 로고
    • Expression cloning of a reserpine-sensitive vesicular monoamine transporter
    • Erickson JD, Eiden LE, Hoffman BJ. 1992. Expression cloning of a reserpine-sensitive vesicular monoamine transporter. Proc. Natl. Acad. Sci. USA 89:10993-97
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10993-10997
    • Erickson, J.D.1    Eiden, L.E.2    Hoffman, B.J.3
  • 51
    • 0035924571 scopus 로고    scopus 로고
    • Three-dimensional structure of the synaptotagmin 1 C2B-domain: Synaptotagmin 1 as a phospholipid binding machine
    • Fernandez I, Arac D, Ubach J, Gerber SH, Shin O, et al. 2001. Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine. Neuron 32:1057-69
    • (2001) Neuron , vol.32 , pp. 1057-1069
    • Fernandez, I.1    Arac, D.2    Ubach, J.3    Gerber, S.H.4    Shin, O.5
  • 53
    • 0026067472 scopus 로고
    • A small GTP-binding protein (rab3A) dissociates from synaptic vesicles during exocytosis
    • Fischer von Mollard G, Südhof TC, Jahn R. 1991. A small GTP-binding protein (rab3A) dissociates from synaptic vesicles during exocytosis. Nature 349:79-81
    • (1991) Nature , vol.349 , pp. 79-81
    • Fischer Von Mollard, G.1    Südhof, T.C.2    Jahn, R.3
  • 54
    • 0028558754 scopus 로고
    • Localization of rab5 to synaptic vesicles identifies endosomal intermediate in synaptic vesicle recycling pathway
    • Fischer von Mollard G, Stahl B, Walch-Solimena C, Takei K, Daniels L, et al. 1994. Localization of rab5 to synaptic vesicles identifies endosomal intermediate in synaptic vesicle recycling pathway. Eur. J. Cell Biol. 65:319-26
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 319-326
    • Fischer Von Mollard, G.1    Stahl, B.2    Walch-Solimena, C.3    Takei, K.4    Daniels, L.5
  • 55
    • 0035793377 scopus 로고    scopus 로고
    • Control of fusion pore dynamics during exocytosis by Munc18
    • Fisher RJ, Pevsner J, Burgoyne RD. 2001. Control of fusion pore dynamics during exocytosis by Munc18. Science 291:875-78
    • (2001) Science , vol.291 , pp. 875-878
    • Fisher, R.J.1    Pevsner, J.2    Burgoyne, R.D.3
  • 56
    • 0037401513 scopus 로고    scopus 로고
    • + channel revealed by co-immunoprecipitation and pull-down assays: Implications for identification of protein-protein interactions
    • + channel revealed by co-immunoprecipitation and pull-down assays: implications for identification of protein-protein interactions. Neuropharmacology 44:817-27
    • (2003) Neuropharmacology , vol.44 , pp. 817-827
    • Fletcher, S.1    Bowden, S.E.2    Marrion, N.V.3
  • 57
    • 0037195086 scopus 로고    scopus 로고
    • The identification of vesicular glutamate transporter 3 suggests novel modes of signaling by glutamate
    • Fremeau RT Jr, Burman J, Qureshi T, Tran CH, Proctor J, et al. 2002. The identification of vesicular glutamate transporter 3 suggests novel modes of signaling by glutamate. Proc. Natl. Acad. Sci. USA 99:14488-93
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14488-14493
    • Fremeau Jr., R.T.1    Burman, J.2    Qureshi, T.3    Tran, C.H.4    Proctor, J.5
  • 58
    • 17344376286 scopus 로고    scopus 로고
    • Tomosyn: A syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process
    • Fujita Y, Shirataki H, Sakisaka T, Asakura T, Ohya T, et al. 1998. Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process. Neuron 20:905-15
    • (1998) Neuron , vol.20 , pp. 905-915
    • Fujita, Y.1    Shirataki, H.2    Sakisaka, T.3    Asakura, T.4    Ohya, T.5
  • 59
    • 0029801022 scopus 로고    scopus 로고
    • Amino acid neurotransmission: Dynamics of vesicular uptake
    • Fykse EM, Fonnum F. 1996. Amino acid neurotransmission: dynamics of vesicular uptake. Neurochem. Res. 21:1053-60
    • (1996) Neurochem. Res. , vol.21 , pp. 1053-1060
    • Fykse, E.M.1    Fonnum, F.2
  • 60
    • 4243795793 scopus 로고    scopus 로고
    • Cycling of synaptic vesicles: How far? How fast!
    • Galli T, Haucke V. 2001. Cycling of synaptic vesicles: How far? How fast! Sci. STKE 88:RE1
    • (2001) Sci. STKE , vol.88
    • Galli, T.1    Haucke, V.2
  • 61
    • 0038172566 scopus 로고    scopus 로고
    • Three modes of synaptic vesicular recycling revealed by single-vesicle imaging
    • Gandhi SP, Stevens CF. 2003. Three modes of synaptic vesicular recycling revealed by single-vesicle imaging. Nature 423:607-13
    • (2003) Nature , vol.423 , pp. 607-613
    • Gandhi, S.P.1    Stevens, C.F.2
  • 62
    • 0025879767 scopus 로고
    • Synaptotagmin II: A novel differentially distributed form of synaptotagmin
    • Geppert M, Archer BT III, Südhof TC. 1991. Synaptotagmin II: a novel differentially distributed form of synaptotagmin. J. Biol. Chem. 266:13548-52
    • (1991) J. Biol. Chem. , vol.266 , pp. 13548-13552
    • Geppert, M.1    Archer III, B.T.2    Südhof, T.C.3
  • 65
    • 0028145024 scopus 로고
    • Synaptic targeting domains of synapsin I revealed by transgenic expression in photoreceptor cells
    • Geppert M, Ullrich B, Green DG, Takei K, Daniels L, et al. 1994c. Synaptic targeting domains of synapsin I revealed by transgenic expression in photoreceptor cells. EMBO J. 13:3720-27
    • (1994) EMBO J. , vol.13 , pp. 3720-3727
    • Geppert, M.1    Ullrich, B.2    Green, D.G.3    Takei, K.4    Daniels, L.5
  • 66
    • 0030980279 scopus 로고    scopus 로고
    • The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion
    • Geppert M, Goda Y, Stevens CF, Südhof TC. 1997. The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion. Nature 387:810-14
    • (1997) Nature , vol.387 , pp. 810-814
    • Geppert, M.1    Goda, Y.2    Stevens, C.F.3    Südhof, T.C.4
  • 67
    • 0343307123 scopus 로고    scopus 로고
    • Calcium regulation of neurotransmitter release: Reliably unreliable
    • Goda Y, Südhof TC. 1997. Calcium regulation of neurotransmitter release: reliably unreliable. Curr. Opin. Cell Biol. 9:513-18
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 513-518
    • Goda, Y.1    Südhof, T.C.2
  • 68
    • 0028587383 scopus 로고
    • Two components of transmitter release at a central synapse
    • Goda Y, Stevens CF. 1994. Two components of transmitter release at a central synapse. Proc. Natl. Acad. Sci. USA 91:12942-46
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12942-12946
    • Goda, Y.1    Stevens, C.F.2
  • 69
    • 0034652087 scopus 로고    scopus 로고
    • Comparison of cysteine string protein (Csp) and mutant alpha-SNAP overexpression reveals a role for Csp in late steps of membrane fusion in dense-core granule exocytosis in adrenal chromaffin cells
    • Graham ME, Burgoyne RD. 2000. Comparison of cysteine string protein (Csp) and mutant alpha-SNAP overexpression reveals a role for Csp in late steps of membrane fusion in dense-core granule exocytosis in adrenal chromaffin cells. J. Neurosci. 20:1281-89
    • (2000) J. Neurosci. , vol.20 , pp. 1281-1289
    • Graham, M.E.1    Burgoyne, R.D.2
  • 70
    • 0036662899 scopus 로고    scopus 로고
    • A third vesicular glutamate transporter expressed by cholinergic and serotoninergic neurons
    • Gras C, Herzog E, Bellenchi GC, Bernard V, Ravassard P, et al. 2002. A third vesicular glutamate transporter expressed by cholinergic and serotoninergic neurons. J. Neurosci. 22:5442-51
    • (2002) J. Neurosci. , vol.22 , pp. 5442-5451
    • Gras, C.1    Herzog, E.2    Bellenchi, G.C.3    Bernard, V.4    Ravassard, P.5
  • 71
    • 0028708598 scopus 로고
    • Synapsin I, an actin-binding protein regulating synaptic vesicle traffic in the nerve terminal. Adv second messenger
    • Greengard P, Benfenati F, Valtorta F. 1994. Synapsin I, an actin-binding protein regulating synaptic vesicle traffic in the nerve terminal. Adv second messenger. Phosphoprotein Res. 29:31-45
    • (1994) Phosphoprotein Res. , vol.29 , pp. 31-45
    • Greengard, P.1    Benfenati, F.2    Valtorta, F.3
  • 72
    • 0035007574 scopus 로고    scopus 로고
    • Properties of synchronous and asynchronous release during pulse train depression in cultured hippocampal neurons
    • Hagler DJ, Goda Y. 2001. Properties of synchronous and asynchronous release during pulse train depression in cultured hippocampal neurons. J. Neurophysiol. 85:2324-34
    • (2001) J. Neurophysiol. , vol.85 , pp. 2324-2334
    • Hagler, D.J.1    Goda, Y.2
  • 73
    • 0035029611 scopus 로고    scopus 로고
    • Beyond parallel fiber LTD: The diversity of synaptic and non-synaptic plasticity in the cerebellum
    • Hansel C, Linden DJ, D'Angelo E. 2001. Beyond parallel fiber LTD: the diversity of synaptic and non-synaptic plasticity in the cerebellum. Nat. Neurosci. 4:467-75
    • (2001) Nat. Neurosci. , vol.4 , pp. 467-475
    • Hansel, C.1    Linden, D.J.2    D'Angelo, E.3
  • 74
    • 0035945556 scopus 로고    scopus 로고
    • The architecture of active zone material at the frog's neuromuscular junction
    • Harlow LH, Ress D, Stoschek A, Marshall RM, McMahan UJ. 2001. The architecture of active zone material at the frog's neuromuscular junction. Nature 409:479-84
    • (2001) Nature , vol.409 , pp. 479-484
    • Harlow, L.H.1    Ress, D.2    Stoschek, A.3    Marshall, R.M.4    McMahan, U.J.5
  • 75
    • 0026734317 scopus 로고
    • Three-dimensional structure of dendritic spines and synapses in rat hippocampus (CA1) at postnatal day 15 and adult ages: Implications for the maturation of synaptic physiology and long-term potentiation
    • Harris KM, Jensen FE, Tsao B. 1992. Three-dimensional structure of dendritic spines and synapses in rat hippocampus (CA1) at postnatal day 15 and adult ages: implications for the maturation of synaptic physiology and long-term potentiation. J. Neurosci. 12:2685-705
    • (1992) J. Neurosci. , vol.12 , pp. 2685-2705
    • Harris, K.M.1    Jensen, F.E.2    Tsao, B.3
  • 76
    • 0031056522 scopus 로고    scopus 로고
    • Calcium dynamics associated with a single action potential in a CNS presynaptic terminal
    • Helmchen F, Borst JGG, Sakmann B. 1997. Calcium dynamics associated with a single action potential in a CNS presynaptic terminal. Biophys. J. 72:1458-71
    • (1997) Biophys. J. , vol.72 , pp. 1458-1471
    • Helmchen, F.1    Borst, J.G.G.2    Sakmann, B.3
  • 77
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains une-18 homologue bound to syntaxin
    • Hata Y, Slaughter CA, Südhof TC. 1993. Synaptic vesicle fusion complex contains une-18 homologue bound to syntaxin. Nature 366:347-51
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Südhof, T.C.3
  • 78
    • 0042733066 scopus 로고    scopus 로고
    • The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis
    • Hatsuzawa K, Lang T, Fasshauer D, Bruns D, Jahn R. 2003. The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis. J. Biol. Chem. 278:31159-66
    • (2003) J. Biol. Chem. , vol.278 , pp. 31159-31166
    • Hatsuzawa, K.1    Lang, T.2    Fasshauer, D.3    Bruns, D.4    Jahn, R.5
  • 79
    • 0015619310 scopus 로고
    • Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction
    • Heuser JE, Reese TS. 1973. Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction. J. Cell Biol. 57:315-44
    • (1973) J. Cell Biol. , vol.57 , pp. 315-344
    • Heuser, J.E.1    Reese, T.S.2
  • 84
    • 0040964284 scopus 로고    scopus 로고
    • Homo- and heterodimerization of synapsins
    • Hosaka M, Südhof TC. 1999. Homo- and heterodimerization of synapsins. J. Biol. Chem. 274:16747-53
    • (1999) J. Biol. Chem. , vol.274 , pp. 16747-16753
    • Hosaka, M.1    Südhof, T.C.2
  • 85
    • 0033213603 scopus 로고    scopus 로고
    • A phospho-switch controls the dynamic association of synapsins with synaptic vesicles
    • Hosaka M, Hammer RE, Südhof TC. 1999. A phospho-switch controls the dynamic association of synapsins with synaptic vesicles. Neuron 24:377-87
    • (1999) Neuron , vol.24 , pp. 377-387
    • Hosaka, M.1    Hammer, R.E.2    Südhof, T.C.3
  • 86
    • 0028170035 scopus 로고
    • AMP contributes to mossy fiber LTP by initiating both a covalently mediated early phase and macromolecular synthesis-dependent late phase
    • Huang YY, Li XC, Kandel ER. 1994. cAMP contributes to mossy fiber LTP by initiating both a covalently mediated early phase and macromolecular synthesis-dependent late phase. Cell 79:69-79
    • (1994) Cell , vol.79 , pp. 69-79
    • Huang, Y.Y.1    Li, X.C.2    Kandel, E.R.3
  • 89
    • 0032533935 scopus 로고    scopus 로고
    • SVOP, an evolutionarily conserved synaptic vesicle protein, suggests novel transport functions of synaptic vesicles
    • Janz R, Hofmann K, Südhof TC. 1998. SVOP, an evolutionarily conserved synaptic vesicle protein, suggests novel transport functions of synaptic vesicles. J. Neurosci. 18:9269-81
    • (1998) J. Neurosci. , vol.18 , pp. 9269-9281
    • Janz, R.1    Hofmann, K.2    Südhof, T.C.3
  • 90
    • 0344761960 scopus 로고    scopus 로고
    • SV2C is a synaptic vesicle protein with an unusually restricted localization: Anatomy of a synaptic vesicle protein family
    • Janz R, Südhof TC. 1999. SV2C is a synaptic vesicle protein with an unusually restricted localization: anatomy of a synaptic vesicle protein family. Neuroscience 94:1279-90
    • (1999) Neuroscience , vol.94 , pp. 1279-1290
    • Janz, R.1    Südhof, T.C.2
  • 92
    • 0028356773 scopus 로고
    • The GTPase Rab3a negatively controls calcium-dependent exocytosis in neuroendocrine cells
    • Johannes L, Lledo PM, Roa M, Vincent JD, Henry JP, Darchen F. 1994. The GTPase Rab3a negatively controls calcium-dependent exocytosis in neuroendocrine cells. EMBO J. 13:2029-37
    • (1994) EMBO J. , vol.13 , pp. 2029-2037
    • Johannes, L.1    Lledo, P.M.2    Roa, M.3    Vincent, J.D.4    Henry, J.P.5    Darchen, F.6
  • 93
    • 0025784181 scopus 로고
    • Rab3A attachment to the synaptic vesicle membrane mediated by a conserved polyisoprenylated carboxy-terminal sequence
    • Johnston PA, Archer BT III, Robinson K, Mignery GA, Jahn R, Südhof TC. 1991. Rab3A attachment to the synaptic vesicle membrane mediated by a conserved polyisoprenylated carboxy-terminal sequence. Neuron 7:101-9
    • (1991) Neuron , vol.7 , pp. 101-109
    • Johnston, P.A.1    Archer III, B.T.2    Robinson, K.3    Mignery, G.A.4    Jahn, R.5    Südhof, T.C.6
  • 94
    • 0025374891 scopus 로고
    • The multisubunit structure of synaptophysin. Relationship between disulfide bonding and homooligomerization
    • Johnston PA, Südhof TC. 1990. The multisubunit structure of synaptophysin. Relationship between disulfide bonding and homooligomerization. J. Biol. Chem. 265:8869-73
    • (1990) J. Biol. Chem. , vol.265 , pp. 8869-8873
    • Johnston, P.A.1    Südhof, T.C.2
  • 95
    • 0037114029 scopus 로고    scopus 로고
    • 2+ entry is unchanged during hippocampal mossy fiber long-term potentiation
    • 2+ entry is unchanged during hippocampal mossy fiber long-term potentiation. J. Neurosci. 22:10524-28
    • (2002) J. Neurosci. , vol.22 , pp. 10524-10528
    • Kamiya, H.1    Umeda, K.2    Ozawa, S.3    Manabe, T.4
  • 99
    • 0142242179 scopus 로고    scopus 로고
    • Interaction of the ERC family of RIM-binding proteins with the liprin-α family of multidomain proteins
    • Ko J, Na M, Kim S, Lee JR, Kim E. 2003. Interaction of the ERC family of RIM-binding proteins with the liprin-α family of multidomain proteins. J. Biol. Chem. 278:42377-85
    • (2003) J. Biol. Chem. , vol.278 , pp. 42377-42385
    • Ko, J.1    Na, M.2    Kim, S.3    Lee, J.R.4    Kim, E.5
  • 100
    • 0029807825 scopus 로고    scopus 로고
    • Synaptic vesicles have two distinct recycling pathways
    • Koenig JH, Ikeda K. 1996. Synaptic vesicles have two distinct recycling pathways. J. Cell Biol. 135:797-808
    • (1996) J. Cell Biol. , vol.135 , pp. 797-808
    • Koenig, J.H.1    Ikeda, K.2
  • 101
    • 0034671201 scopus 로고    scopus 로고
    • Calcium dynamics associated with action potentials in single nerve terminals of pyramidal cells in layer 2/3 of the young rat neocortex
    • Koester H, Sakmann B. 2000. Calcium dynamics associated with action potentials in single nerve terminals of pyramidal cells in layer 2/3 of the young rat neocortex. J. Physiol. 529:625-46
    • (2000) J. Physiol. , vol.529 , pp. 625-646
    • Koester, H.1    Sakmann, B.2
  • 102
    • 0030661912 scopus 로고    scopus 로고
    • Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane domain
    • Laage R, Langosch D. 1997. Dimerization of the synaptic vesicle protein synaptobrevin (vesicle-associated membrane protein) II depends on specific residues within the transmembrane domain. Eur. J. Biochem. 249:540-46
    • (1997) Eur. J. Biochem. , vol.249 , pp. 540-546
    • Laage, R.1    Langosch, D.2
  • 105
    • 0029059605 scopus 로고
    • Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice
    • Li L, Chin LS, Shupliakov O, Brodin L, Sihra TS, et al. 1995b. Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice. Proc. Natl. Acad. Sci. USA 92:9235-39
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9235-9239
    • Li, L.1    Chin, L.S.2    Shupliakov, O.3    Brodin, L.4    Sihra, T.S.5
  • 106
    • 0030906740 scopus 로고    scopus 로고
    • Long-term potentiation of glial synaptic currents in cerebellar culture
    • Linden DJ. 1997. Long-term potentiation of glial synaptic currents in cerebellar culture. Neuron 18:983-94
    • (1997) Neuron , vol.18 , pp. 983-994
    • Linden, D.J.1
  • 108
    • 0141987893 scopus 로고    scopus 로고
    • Phosphorylation of RIM1α by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses
    • Lonart G, Schoch S, Käser PS, Larkin CJ, Südhof TC, Linden DJ. 2003. Phosphorylation of RIM1α by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses. Cell 115:49-60
    • (2003) Cell , vol.115 , pp. 49-60
    • Lonart, G.1    Schoch, S.2    Käser, P.S.3    Larkin, C.J.4    Südhof, T.C.5    Linden, D.J.6
  • 109
    • 0036642290 scopus 로고    scopus 로고
    • RIM1: An edge for presynaptic plasticity
    • Lonart G. 2002. RIM1: an edge for presynaptic plasticity. Trends Neurosci. 25:329-32
    • (2002) Trends Neurosci. , vol.25 , pp. 329-332
    • Lonart, G.1
  • 110
    • 0023715532 scopus 로고
    • Glutamate uptake by brain synaptic vesicles. Energy dependence of transport and functional reconstitution in proteoliposomes
    • Maycox PR, Deckwerth T, Hell JW, Jahn R. 1988. Glutamate uptake by brain synaptic vesicles. Energy dependence of transport and functional reconstitution in proteoliposomes. J. Biol. Chem. 263:15423-28
    • (1988) J. Biol. Chem. , vol.263 , pp. 15423-15428
    • Maycox, P.R.1    Deckwerth, T.2    Hell, J.W.3    Jahn, R.4
  • 112
    • 0028880456 scopus 로고
    • Complexins: Cytosolic proteins that regulate SNAP receptor function
    • McMahon HT, Missler M, Li C, Südhof TC. 1995. Complexins: cytosolic proteins that regulate SNAP receptor function. Cell 83:111-19
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Südhof, T.C.4
  • 113
    • 0036523041 scopus 로고    scopus 로고
    • Calcium secretion coupling at calyx of Held governed by non-uniform channel-vesicle topography
    • Meinrenken CJ, Borst JGG, Sakmann B. 2002. Calcium secretion coupling at calyx of Held governed by non-uniform channel-vesicle topography. J. Neurosci. 22:1648-67
    • (2002) J. Neurosci. , vol.22 , pp. 1648-1667
    • Meinrenken, C.J.1    Borst, J.G.G.2    Sakmann, B.3
  • 114
    • 0037444568 scopus 로고    scopus 로고
    • 2+ signal for phasic transmitter release at the rat calyx of Held
    • 2+ signal for phasic transmitter release at the rat calyx of Held. J. Physiol. 547:665-89
    • (2003) J. Physiol. , vol.547 , pp. 665-689
    • Meinrenken, C.J.1    Borst, J.G.2    Sakmann, B.3
  • 115
    • 0033681170 scopus 로고    scopus 로고
    • Actin-dependent regulation of neurotransmitter release at central synapses
    • Morales M, Colicos MA, Goda Y. 2000. Actin-dependent regulation of neurotransmitter release at central synapses. Neuron 27:539-50
    • (2000) Neuron , vol.27 , pp. 539-550
    • Morales, M.1    Colicos, M.A.2    Goda, Y.3
  • 116
    • 0033361973 scopus 로고    scopus 로고
    • Reversal of synaptic vesicle docking at central synapses
    • Murthy VN, Stevens CF. 1999. Reversal of synaptic vesicle docking at central synapses. Nat. Neurosci. 2:503-7
    • (1999) Nat. Neurosci. , vol.2 , pp. 503-507
    • Murthy, V.N.1    Stevens, C.F.2
  • 117
    • 0029093566 scopus 로고
    • Contrasting properties of two forms of long-term potentiation in the hippocampus
    • Nicoll RA, Malenka RC. 1995. Contrasting properties of two forms of long-term potentiation in the hippocampus. Nature 377:115-18
    • (1995) Nature , vol.377 , pp. 115-118
    • Nicoll, R.A.1    Malenka, R.C.2
  • 118
    • 0034735512 scopus 로고    scopus 로고
    • Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain
    • Nielsen E, Christoforidis S, Uttenweiler-Joseph S, Miaczynska M, Dewitte F, et al. 2000. Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain. J. Cell Biol. 151:601-12
    • (2000) J. Cell Biol. , vol.151 , pp. 601-612
    • Nielsen, E.1    Christoforidis, S.2    Uttenweiler-Joseph, S.3    Miaczynska, M.4    Dewitte, F.5
  • 120
    • 0036329841 scopus 로고    scopus 로고
    • Cast, a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1
    • Ohtsuka T, Takao-Rikitsu E, Inoue E, Inoue M, Takeuchi M, et al. 2002. Cast, a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1. J. Cell Biol. 158:577-90
    • (2002) J. Cell Biol. , vol.158 , pp. 577-590
    • Ohtsuka, T.1    Takao-Rikitsu, E.2    Inoue, E.3    Inoue, M.4    Takeuchi, M.5
  • 121
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin MS, Fried VA, Mignery GA, Jahn R, Südhof TC. 1990. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 345:260-63
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Südhof, T.C.5
  • 122
    • 0025907484 scopus 로고
    • Structure of the 11.6 kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump
    • Perin MS, Fried VA, Stone DK, Xie X-S, Südhof TC. 1991a. Structure of the 11.6 kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump. J. Biol. Chem. 266:3877-81
    • (1991) J. Biol. Chem. , vol.266 , pp. 3877-3881
    • Perin, M.S.1    Fried, V.A.2    Stone, D.K.3    Xie, X.-S.4    Südhof, T.C.5
  • 125
    • 0029004514 scopus 로고
    • Stimulation of inositol 1,4,5-trisphosphate production by peptides corresponding to the effector domain of different Rab3 isoforms and cross-linking of an effector domain peptide target
    • Piiper A, Stryjek-Kaminska D, Jahn R, Zeuzem S. 1995. Stimulation of inositol 1,4,5-trisphosphate production by peptides corresponding to the effector domain of different Rab3 isoforms and cross-linking of an effector domain peptide target. Biochem. J. 309:621-27
    • (1995) Biochem. J. , vol.309 , pp. 621-627
    • Piiper, A.1    Stryjek-Kaminska, D.2    Jahn, R.3    Zeuzem, S.4
  • 127
    • 0033635239 scopus 로고    scopus 로고
    • Rapid reuse of readily releasable pool vesicles at hippocampal synapses
    • Pyle JL, Kavalali E, Piedras-Renteria ES, Tsien RW. 2000. Rapid reuse of readily releasable pool vesicles at hippocampal synapses. Neuron 28:221-31
    • (2000) Neuron , vol.28 , pp. 221-231
    • Pyle, J.L.1    Kavalali, E.2    Piedras-Renteria, E.S.3    Tsien, R.W.4
  • 128
    • 0033050930 scopus 로고    scopus 로고
    • Modulation of transmitter release by action potential duration at the hippocampal CA3-CA1 synapse
    • Qian J, Saggau P. 1999. Modulation of transmitter release by action potential duration at the hippocampal CA3-CA1 synapse. J. Neurophysiol. 81:288-98
    • (1999) J. Neurophysiol. , vol.81 , pp. 288-298
    • Qian, J.1    Saggau, P.2
  • 129
    • 0025998783 scopus 로고
    • The maintenance of LTP at hippocampal mossy fiber synapses is independent of sustained presynaptic calcium
    • Regehr WG, Tank DW. 1991. The maintenance of LTP at hippocampal mossy fiber synapses is independent of sustained presynaptic calcium. Neuron 7:451-59
    • (1991) Neuron , vol.7 , pp. 451-459
    • Regehr, W.G.1    Tank, D.W.2
  • 131
    • 0033695839 scopus 로고    scopus 로고
    • Two endocytic recycling routes selectively fill two vesicle pools in frog motor nerve terminals
    • Richards DA, Guatimosim C, Betz WJ. 2000. Two endocytic recycling routes selectively fill two vesicle pools in frog motor nerve terminals. Neuron 27:551-59
    • (2000) Neuron , vol.27 , pp. 551-559
    • Richards, D.A.1    Guatimosim, C.2    Betz, W.J.3
  • 132
    • 0043198288 scopus 로고    scopus 로고
    • Synaptic vesicle pools at the frog neuromuscular junction
    • Richards DA, Guatimosim C, Rizzoli SO, Betz WJ. 2003. Synaptic vesicle pools at the frog neuromuscular junction. Neuron 39:529-41
    • (2003) Neuron , vol.39 , pp. 529-541
    • Richards, D.A.1    Guatimosim, C.2    Rizzoli, S.O.3    Betz, W.J.4
  • 133
    • 0036801359 scopus 로고    scopus 로고
    • The synaptic vesicle cycle: Exocytosis and endocytosis in Drosophila and C. elegans
    • Richmond JE, Broadie KS. 2002. The synaptic vesicle cycle: exocytosis and endocytosis in Drosophila and C. elegans. Curr. Opin. Neurobiol. 12:499-507
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 499-507
    • Richmond, J.E.1    Broadie, K.S.2
  • 134
    • 0037115043 scopus 로고    scopus 로고
    • Effects of 2-(4-morpholinyl)-8-phenyl-4H-1benzopyran-4-one on synaptic vesicle cycling at the frog neuromuscular junction
    • Rizzoli SO, Betz WJ. 2002. Effects of 2-(4-morpholinyl)-8-phenyl-4H- 1benzopyran-4-one on synaptic vesicle cycling at the frog neuromuscular junction. J. Neurosci. 22:10680-89
    • (2002) J. Neurosci. , vol.22 , pp. 10680-10689
    • Rizzoli, S.O.1    Betz, W.J.2
  • 136
    • 0029024135 scopus 로고
    • Essential functions of synapsins I and II in synaptic vesicle regulation
    • Rosahl TW, Spillane D, Missler M, Herz J, Selig DK, et al. 1995. Essential functions of synapsins I and II in synaptic vesicle regulation. Nature 375:488-93
    • (1995) Nature , vol.375 , pp. 488-493
    • Rosahl, T.W.1    Spillane, D.2    Missler, M.3    Herz, J.4    Selig, D.K.5
  • 137
    • 0027482675 scopus 로고
    • Short term synaptic plasticity is altered in mice lacking synapsin I
    • Rosahl TW, Geppert M, Spillane D, Herz J, Hammer RE, et al. 1993. Short term synaptic plasticity is altered in mice lacking synapsin I. Cell 75:661-70
    • (1993) Cell , vol.75 , pp. 661-670
    • Rosahl, T.W.1    Geppert, M.2    Spillane, D.3    Herz, J.4    Hammer, R.E.5
  • 138
    • 0030175394 scopus 로고    scopus 로고
    • Definition of the readily releasable pool of vesicles at hippocampal synapses
    • Rosenmund C, Stevens CF. 1996. Definition of the readily releasable pool of vesicles at hippocampal synapses. Neuron 16:1197-201
    • (1996) Neuron , vol.16 , pp. 1197-1201
    • Rosenmund, C.1    Stevens, C.F.2
  • 139
    • 0029990813 scopus 로고    scopus 로고
    • Timing of neurotransmission at fast synapses in the mammalian brain
    • Sabatini BL, Regehr WG. 1996. Timing of neurotransmission at fast synapses in the mammalian brain. Nature 384:170-72
    • (1996) Nature , vol.384 , pp. 170-172
    • Sabatini, B.L.1    Regehr, W.G.2
  • 140
    • 0030840107 scopus 로고    scopus 로고
    • Cloning of a functional vesicular GABA and glycine transporter by screening of genome databases
    • Sagne C, El Mestikawy S, Isambert MF, Hamon M, Henry JP, et al. 1997. Cloning of a functional vesicular GABA and glycine transporter by screening of genome databases. FEBS Lett. 417:177-83
    • (1997) FEBS Lett. , vol.417 , pp. 177-183
    • Sagne, C.1    El Mestikawy, S.2    Isambert, M.F.3    Hamon, M.4    Henry, J.P.5
  • 141
    • 0035863051 scopus 로고    scopus 로고
    • Quantitative relationship between transmitter release and calcium current at the calyx of held synapse
    • Sakaba T, Neher E. 2001. Quantitative relationship between transmitter release and calcium current at the calyx of held synapse. J. Neurosci. 21:462-76
    • (2001) J. Neurosci. , vol.21 , pp. 462-476
    • Sakaba, T.1    Neher, E.2
  • 142
    • 0029961605 scopus 로고    scopus 로고
    • Cyclic AMP mediates a presynaptic form of LTP at cerebellar parallel fiber synapses
    • Salin PA, Malenka RC, Nicoll RA. 1996. Cyclic AMP mediates a presynaptic form of LTP at cerebellar parallel fiber synapses. Neuron 16:797-803
    • (1996) Neuron , vol.16 , pp. 797-803
    • Salin, P.A.1    Malenka, R.C.2    Nicoll, R.A.3
  • 143
    • 0037115113 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of a calyx of Held and its postsynaptic principal neuron in the medial nucleus of the trapezoid body
    • Sätzler K, Söhl LF, Bollmann JH, Borst JGG, Frotscher M, et al. 2002. Three-dimensional reconstruction of a calyx of Held and its postsynaptic principal neuron in the medial nucleus of the trapezoid body. J. Neurosci. 22:10567-79
    • (2002) J. Neurosci. , vol.22 , pp. 10567-10579
    • Sätzler, K.1    Söhl, L.F.2    Bollmann, J.H.3    Borst, J.G.G.4    Frotscher, M.5
  • 144
    • 0037008753 scopus 로고    scopus 로고
    • Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly
    • Scales SJ, Hesser BA, Masuda ES, Scheller RH. 2002. Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly. J. Biol. Chem. 277:28271-79
    • (2002) J. Biol. Chem. , vol.277 , pp. 28271-28279
    • Scales, S.J.1    Hesser, B.A.2    Masuda, E.S.3    Scheller, R.H.4
  • 145
    • 0038139324 scopus 로고    scopus 로고
    • Molecular cloning and functional identification of mouse vesicular glutamate transporter 3 and its expression in subsets of novel excitatory neurons
    • Schafer MK, Varoqui H, Defamie N, Weihe E, Erickson JD. 2002. Molecular cloning and functional identification of mouse vesicular glutamate transporter 3 and its expression in subsets of novel excitatory neurons. J. Biol. Chem. 277:50734-48
    • (2002) J. Biol. Chem. , vol.277 , pp. 50734-50748
    • Schafer, M.K.1    Varoqui, H.2    Defamie, N.3    Weihe, E.4    Erickson, J.D.5
  • 146
    • 0035095914 scopus 로고    scopus 로고
    • Morphological correlates of functionally defined synaptic vesicle populations
    • Schikorski T, Stevens CF. 2001. Morphological correlates of functionally defined synaptic vesicle populations. Nat. Neurosci. 4:391-95
    • (2001) Nat. Neurosci. , vol.4 , pp. 391-395
    • Schikorski, T.1    Stevens, C.F.2
  • 147
    • 0029861418 scopus 로고    scopus 로고
    • Isoform-specific, calcium-regulated interaction of the synaptic vesicle proteins SV2 and synaptotagmin
    • Schivell AE, Batchelor RH, Bajjalieh SM. 1996. Isoform-specific, calcium-regulated interaction of the synaptic vesicle proteins SV2 and synaptotagmin. J. Biol. Chem. 271:27770-75
    • (1996) J. Biol. Chem. , vol.271 , pp. 27770-27775
    • Schivell, A.E.1    Batchelor, R.H.2    Bajjalieh, S.M.3
  • 148
    • 0040576976 scopus 로고    scopus 로고
    • Rabphilin knock-out mice reveal rat rabphilin is not required for rab3 function in regulating neurotransmitter release
    • Schlüter OM, Schnell E, Verhage M, Tzonopoulos T, Nicoll RA, et al. 1999. Rabphilin knock-out mice reveal rat rabphilin is not required for rab3 function in regulating neurotransmitter release. J. Neurosci. 19:5834-46
    • (1999) J. Neurosci. , vol.19 , pp. 5834-5846
    • Schlüter, O.M.1    Schnell, E.2    Verhage, M.3    Tzonopoulos, T.4    Nicoll, R.A.5
  • 149
    • 0037175049 scopus 로고    scopus 로고
    • Localization versus function of Rab3 proteins: Evidence for a common regulatory role in controlling fusion
    • Schlüter OM, Khvotchev M, Jahn R, Südhof TC. 2002. Localization versus function of Rab3 proteins: evidence for a common regulatory role in controlling fusion. J. Biol. Chem. 277:40919-29
    • (2002) J. Biol. Chem. , vol.277 , pp. 40919-40929
    • Schlüter, O.M.1    Khvotchev, M.2    Jahn, R.3    Südhof, T.C.4
  • 150
    • 0034710645 scopus 로고    scopus 로고
    • Intracellular calcium dependence of transmitter release rates at a fast central synapse
    • Schneggenburger R, Neher E. 2000. Intracellular calcium dependence of transmitter release rates at a fast central synapse. Nature 406:889-93
    • (2000) Nature , vol.406 , pp. 889-893
    • Schneggenburger, R.1    Neher, E.2
  • 151
    • 0036542627 scopus 로고    scopus 로고
    • Vesicle pools and short-term synaptic depression: Lessons from a large synapse
    • Schneggenburger R, Sakaba T, Neher E. 2002. Vesicle pools and short-term synaptic depression: lessons from a large synapse. Trends Neurosci. 25:206-12
    • (2002) Trends Neurosci. , vol.25 , pp. 206-212
    • Schneggenburger, R.1    Sakaba, T.2    Neher, E.3
  • 152
    • 0035798088 scopus 로고    scopus 로고
    • SNARE function analyzed in synaptobrevin/VAMP knockout mice
    • Schoch S, Deak F, Konigstorfer A, Mozhayeva M, Sara Y, et al. 2001. SNARE function analyzed in synaptobrevin/VAMP knockout mice. Science 294:1117-22
    • (2001) Science , vol.294 , pp. 1117-1122
    • Schoch, S.1    Deak, F.2    Konigstorfer, A.3    Mozhayeva, M.4    Sara, Y.5
  • 153
    • 0037122458 scopus 로고    scopus 로고
    • RIM1α forms a protein scaffold for regulating neurotransmitter release at the active zone
    • Schoch S, Castillo PE, Jo T, Mukherjee K, Geppert M, et al. 2002. RIM1α forms a protein scaffold for regulating neurotransmitter release at the active zone. Nature 415:321-26
    • (2002) Nature , vol.415 , pp. 321-326
    • Schoch, S.1    Castillo, P.E.2    Jo, T.3    Mukherjee, K.4    Geppert, M.5
  • 154
    • 0027278599 scopus 로고
    • The SV2 protein of synaptic vesicles is a keratan sulfate proteoglycan
    • Scranton TW, Iwata M, Carlson SS. 1993. The SV2 protein of synaptic vesicles is a keratan sulfate proteoglycan. J. Neurochem. 61:29-44
    • (1993) J. Neurochem. , vol.61 , pp. 29-44
    • Scranton, T.W.1    Iwata, M.2    Carlson, S.S.3
  • 155
    • 0032546658 scopus 로고    scopus 로고
    • Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins
    • Serra-Pages C, Medley QG, Tang M, Hart A, Streuli M. 1998. Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins. J. Biol. Chem. 273:15611-20
    • (1998) J. Biol. Chem. , vol.273 , pp. 15611-15620
    • Serra-Pages, C.1    Medley, Q.G.2    Tang, M.3    Hart, A.4    Streuli, M.5
  • 156
    • 0037427025 scopus 로고    scopus 로고
    • 2+ binding site of the synaptotagmin l C2B domain triggers fast exocytosis without stimulating SNARE interactions
    • 2+ binding site of the synaptotagmin l C2B domain triggers fast exocytosis without stimulating SNARE interactions. Neuron 37:99-108
    • (2003) Neuron , vol.37 , pp. 99-108
    • Shin, O.H.1    Rhee, J.S.2    Tang, J.3    Sugita, S.4    Rosenmund, C.5    Südhof, T.C.6
  • 158
    • 0027461829 scopus 로고
    • Rabphilin-3A, a putative target protein for smg p25A/rab3A small GTP-binding protein related to synaptotagmin
    • Shirataki H, Kaibuchi K, Sakoda T, Kishida S, Yamaguchi T, et al. 1993. Rabphilin-3A, a putative target protein for smg p25A/rab3A small GTP-binding protein related to synaptotagmin. Mol. Cell Biol. 13:2061-68
    • (1993) Mol. Cell Biol. , vol.13 , pp. 2061-2068
    • Shirataki, H.1    Kaibuchi, K.2    Sakoda, T.3    Kishida, S.4    Yamaguchi, T.5
  • 159
    • 0034573212 scopus 로고    scopus 로고
    • Accessory factors in clathrin-dependent synaptic vesicle endocytosis
    • Slepnev VI, De Camilli P. 2000. Accessory factors in clathrin-dependent synaptic vesicle endocytosis. Nat. Rev. Neurosci. 1:161-72
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 161-172
    • Slepnev, V.I.1    De Camilli, P.2
  • 162
    • 0037199678 scopus 로고    scopus 로고
    • Activation of cyclic AMP-dependent protein kinase is required for long-term enhancement at corticostriatal synapses in rats
    • Spencer JP, Murphy KP. 2002. Activation of cyclic AMP-dependent protein kinase is required for long-term enhancement at corticostriatal synapses in rats. Neurosci. Lett. 329:217-21
    • (2002) Neurosci. Lett. , vol.329 , pp. 217-221
    • Spencer, J.P.1    Murphy, K.P.2
  • 163
    • 0021767871 scopus 로고
    • Synaptic vesicles contain an ATP-dependent proton pump and show 'knob-like' protrusions on their surface
    • Stadler H, Tsukita S. 1984. Synaptic vesicles contain an ATP-dependent proton pump and show 'knob-like' protrusions on their surface. EMBO J. 3:3333-37
    • (1984) EMBO J. , vol.3 , pp. 3333-3337
    • Stadler, H.1    Tsukita, S.2
  • 164
    • 0021116675 scopus 로고
    • Evidence for a divalent cation dependent catecholamine storage complex in chromaffin granules
    • Südhof TC. 1983. Evidence for a divalent cation dependent catecholamine storage complex in chromaffin granules. Biochem. Biophys. Res. Comm. 116:663-68
    • (1983) Biochem. Biophys. Res. Comm. , vol.116 , pp. 663-668
    • Südhof, T.C.1
  • 165
    • 0024461324 scopus 로고
    • Synapsins: Mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins
    • Südhof TC, Czernik AJ, Kao H, Takei K, Johnston PA, et al. 1989. Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins. Science 245:1474-80
    • (1989) Science , vol.245 , pp. 1474-1480
    • Südhof, T.C.1    Czernik, A.J.2    Kao, H.3    Takei, K.4    Johnston, P.A.5
  • 166
    • 0033637985 scopus 로고    scopus 로고
    • The synaptic vesicle cycle revisited
    • Südhof TC. 2000. The synaptic vesicle cycle revisited. Neuron 28:317-20
    • (2000) Neuron , vol.28 , pp. 317-320
    • Südhof, T.C.1
  • 167
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof TC. 1995. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375:645-53
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 168
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: Why so many?
    • Südhof TC. 2002. Synaptotagmins: Why so many? J. Biol. Chem. 277:7629-32
    • (2002) J. Biol. Chem. , vol.277 , pp. 7629-7632
    • Südhof, T.C.1
  • 172
    • 0035033931 scopus 로고    scopus 로고
    • Fast kinetics of exocytosis revealed by simultaneous measurements of presynaptic capacitance and postsynaptic currents at a central synapse
    • Sun JY, Wu LG. 2001. Fast kinetics of exocytosis revealed by simultaneous measurements of presynaptic capacitance and postsynaptic currents at a central synapse. Neuron 30:171-82
    • (2001) Neuron , vol.30 , pp. 171-182
    • Sun, J.Y.1    Wu, L.G.2
  • 173
    • 0037198628 scopus 로고    scopus 로고
    • Single and multiple vesicle fusion induce different rates of endocytosis at a central synapse
    • Sun JY, Wu XS, Wu LG. 2002. Single and multiple vesicle fusion induce different rates of endocytosis at a central synapse. Nature 417:555-59
    • (2002) Nature , vol.417 , pp. 555-559
    • Sun, J.Y.1    Wu, X.S.2    Wu, L.G.3
  • 174
    • 0034648770 scopus 로고    scopus 로고
    • Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons
    • Takamori S, Rhee JS, Rosenmund C, Jahn R. 2000. Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons. Nature 407:189-94
    • (2000) Nature , vol.407 , pp. 189-194
    • Takamori, S.1    Rhee, J.S.2    Rosenmund, C.3    Jahn, R.4
  • 175
    • 0036668641 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of human vesicular glutamate transporter 3
    • Takamori S, Malherbe P, Broger C, Jahn R. 2002. Molecular cloning and functional characterization of human vesicular glutamate transporter 3. EMBO Rep. 3:798-803
    • (2002) EMBO Rep. , vol.3 , pp. 798-803
    • Takamori, S.1    Malherbe, P.2    Broger, C.3    Jahn, R.4
  • 176
  • 177
    • 0023685654 scopus 로고
    • Identification of synaptophysin as a hexameric channel protein of the synaptic vesicle membrane
    • Thomas L, Hartung K, Langosch D, Rehm H, Bamberg E, et al. 1988. Identification of synaptophysin as a hexameric channel protein of the synaptic vesicle membrane. Science 242:1050-53
    • (1988) Science , vol.242 , pp. 1050-1053
    • Thomas, L.1    Hartung, K.2    Langosch, D.3    Rehm, H.4    Bamberg, E.5
  • 178
    • 14444271321 scopus 로고    scopus 로고
    • Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals
    • tom Dieck S, Sanmarti-Vila L, Langnaese K, Richter K, Kindler S, et al. 1998. Bassoon, a novel zinc-finger CAG/glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals. J. Cell Biol. 142:499-509
    • (1998) J. Cell Biol. , vol.142 , pp. 499-509
    • Tom Dieck, S.1    Sanmarti-Vila, L.2    Langnaese, K.3    Richter, K.4    Kindler, S.5
  • 179
    • 0025098982 scopus 로고
    • Redistribution of synaptophysin and synapsin I during α-latrotoxin-induced release of neurotransmitter at the neuromuscular junction
    • Torri-Tarelli F, Villa A, Valtorta F, De Camilli P, Greengard P, Ceccarelli B. 1990. Redistribution of synaptophysin and synapsin I during α-latrotoxin-induced release of neurotransmitter at the neuromuscular junction. J. Cell Biol. 110:449-59
    • (1990) J. Cell Biol. , vol.110 , pp. 449-459
    • Torri-Tarelli, F.1    Villa, A.2    Valtorta, F.3    De Camilli, P.4    Greengard, P.5    Ceccarelli, B.6
  • 180
    • 0037340258 scopus 로고    scopus 로고
    • Heterogeneous presynaptic release probabilities: Functional relevance for short-term plasticity
    • Trommershäuser J, Schneggenberger R, Zippelius A, Neher E. 2003. Heterogeneous presynaptic release probabilities: functional relevance for short-term plasticity. Biophys. J. 84:1563-79
    • (2003) Biophys. J. , vol.84 , pp. 1563-1579
    • Trommershäuser, J.1    Schneggenberger, R.2    Zippelius, A.3    Neher, E.4
  • 181
    • 0028579515 scopus 로고
    • Functional properties of multiple synaptotagmins in brain
    • Ullrich B, Li C, Zhang JZ, McMahon H, Anderson RGW, et al. 1994. Functional properties of multiple synaptotagmins in brain. Neuron 13:1281-91
    • (1994) Neuron , vol.13 , pp. 1281-1291
    • Ullrich, B.1    Li, C.2    Zhang, J.Z.3    McMahon, H.4    Anderson, R.G.W.5
  • 184
    • 0026008186 scopus 로고
    • The regulation of quantal size
    • van der Kloot W. 1991. The regulation of quantal size. Prog. Neurobiol. 36:93-130
    • (1991) Prog. Neurobiol. , vol.36 , pp. 93-130
    • Van Der Kloot, W.1
  • 185
    • 0028195078 scopus 로고
    • Cloning and expression of the vesamicol binding protein from the marine ray Torpedo. Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans
    • Varoqui H, Diebler MF, Meunier FM, Rand JB, Usdin TB, et al. 1994. Cloning and expression of the vesamicol binding protein from the marine ray Torpedo. Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans. FEBS Lett. 342:97-102
    • (1994) FEBS Lett. , vol.342 , pp. 97-102
    • Varoqui, H.1    Diebler, M.F.2    Meunier, F.M.3    Rand, J.B.4    Usdin, T.B.5
  • 186
    • 0034603030 scopus 로고    scopus 로고
    • Synaptic assembly of the brain in the absence of neurotransmitter secretion
    • Verhage M, Maia AS, Plomp JJ, Brussaard AB, Heeroma JH, et al. 2000. Synaptic assembly of the brain in the absence of neurotransmitter secretion. Science 287:864-69
    • (2000) Science , vol.287 , pp. 864-869
    • Verhage, M.1    Maia, A.S.2    Plomp, J.J.3    Brussaard, A.B.4    Heeroma, J.H.5
  • 187
  • 189
    • 0034733706 scopus 로고    scopus 로고
    • 2 domain proteins. Interactions with Rab3 and a new class of Src homology 3 domain proteins
    • 2 domain proteins. Interactions with Rab3 and a new class of Src homology 3 domain proteins. J. Biol. Chem. 275:20033-44
    • (2000) J. Biol. Chem. , vol.275 , pp. 20033-20044
    • Wang, Y.1    Sugita, S.2    Südhof, T.C.3
  • 190
    • 0035798162 scopus 로고    scopus 로고
    • Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles
    • Wang CT, Grishanin R, Earles CA, Chang PY, Martin TF, et al. 2001 a. Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles. Science 294:1111-15
    • (2001) Science , vol.294 , pp. 1111-1115
    • Wang, C.T.1    Grishanin, R.2    Earles, C.A.3    Chang, P.Y.4    Martin, T.F.5
  • 191
    • 0035980002 scopus 로고    scopus 로고
    • Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially related through N-terminal α-helix motifs
    • Wang X, Hu B, Zimmermann B, Kilimann MW. 2001b. Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially related through N-terminal α-helix motifs. J. Biol. Chem. 276:32480-88
    • (2001) J. Biol. Chem. , vol.276 , pp. 32480-32488
    • Wang, X.1    Hu, B.2    Zimmermann, B.3    Kilimann, M.W.4
  • 192
    • 0041858035 scopus 로고    scopus 로고
    • Different domains of synaptotagmin control the choice between kiss-and-run and full fusion
    • Wang CT, Lu JC, Bai J, Chang PY, Martin TF, et al. 2003. Different domains of synaptotagmin control the choice between kiss-and-run and full fusion. Nature 424:943-47
    • (2003) Nature , vol.424 , pp. 943-947
    • Wang, C.T.1    Lu, J.C.2    Bai, J.3    Chang, P.Y.4    Martin, T.F.5
  • 193
    • 0037195108 scopus 로고    scopus 로고
    • A family of RTM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones
    • Wang Y, Liu X, Biederer T, Südhof TC. 2002. A family of RTM-binding proteins regulated by alternative splicing: implications for the genesis of synaptic active zones. Proc. Natl. Acad. Sci. USA 99:14464-69
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14464-14469
    • Wang, Y.1    Liu, X.2    Biederer, T.3    Südhof, T.C.4
  • 194
    • 0030877243 scopus 로고    scopus 로고
    • RIM: A putative Rab3-effector in regulating synaptic vesicle fusion
    • Wang Y, Okamoto M, Schmitz F, Hofman K, Südhof TC. 1997a. RIM: a putative Rab3-effector in regulating synaptic vesicle fusion. Nature 388:593-98
    • (1997) Nature , vol.388 , pp. 593-598
    • Wang, Y.1    Okamoto, M.2    Schmitz, F.3    Hofman, K.4    Südhof, T.C.5
  • 195
    • 0031458923 scopus 로고    scopus 로고
    • Knockout of the vesicular monoamine transporter 2 gene results in neonatal death and supersensitivity to cocaine and amphetamine
    • Wang YM, Gainetdinov RR, Fumagalli F, Xu F, Jones SR, et al. 1997b. Knockout of the vesicular monoamine transporter 2 gene results in neonatal death and supersensitivity to cocaine and amphetamine. Neuron 19:1285-96
    • (1997) Neuron , vol.19 , pp. 1285-1296
    • Wang, Y.M.1    Gainetdinov, R.R.2    Fumagalli, F.3    Xu, F.4    Jones, S.R.5
  • 196
    • 0037295116 scopus 로고    scopus 로고
    • Genomic definition of RIM proteins: Evolutionary amplification of a family of synaptic regulatory proteins
    • Wang Y, Südhof TC. 2003. Genomic definition of RIM proteins: evolutionary amplification of a family of synaptic regulatory proteins. Genomics 81:126-37
    • (2003) Genomics , vol.81 , pp. 126-137
    • Wang, Y.1    Südhof, T.C.2
  • 197
    • 0028942065 scopus 로고
    • Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin
    • Washbourne P, Schiavo G, Montecucco C. 1995. Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin. Biochem. J. 305:721-24
    • (1995) Biochem. J. , vol.305 , pp. 721-724
    • Washbourne, P.1    Schiavo, G.2    Montecucco, C.3
  • 198
    • 0036138744 scopus 로고    scopus 로고
    • Genetic ablation of the t-SNARE SNAP-25 distinguishes mechanisms of neuroexocytosis
    • Washbourne P, Thompson PM, Carta M, Costa ET, Mathews JR, et al. 2002. Genetic ablation of the t-SNARE SNAP-25 distinguishes mechanisms of neuroexocytosis. Nat. Neurosci. 5:19-26
    • (2002) Nat. Neurosci. , vol.5 , pp. 19-26
    • Washbourne, P.1    Thompson, P.M.2    Carta, M.3    Costa, E.T.4    Mathews, J.R.5
  • 199
    • 0028051845 scopus 로고
    • Mediation of hippocampal mossy fiber long-term potentiation by cyclic AMP
    • Weisskopf MG, Castillo PE, Zalutsky RA, Nicoll RA. 1994. Mediation of hippocampal mossy fiber long-term potentiation by cyclic AMP. Science 265:1878-82
    • (1994) Science , vol.265 , pp. 1878-1882
    • Weisskopf, M.G.1    Castillo, P.E.2    Zalutsky, R.A.3    Nicoll, R.A.4
  • 200
    • 0035899302 scopus 로고    scopus 로고
    • Presynaptic specificity of endocannabinoid signaling in the hippocampus
    • Wilson RI, Kunos G, Nicoll RA. 2001. Presynaptic specificity of endocannabinoid signaling in the hippocampus. Neuron 31:453-62
    • (2001) Neuron , vol.31 , pp. 453-462
    • Wilson, R.I.1    Kunos, G.2    Nicoll, R.A.3
  • 201
    • 0041573299 scopus 로고    scopus 로고
    • 2+ sensitivity of vesicle pool depletion at a fast CNS synapse
    • 2+ sensitivity of vesicle pool depletion at a fast CNS synapse. J. Neurosci. 23:7059-68
    • (2003) J. Neurosci. , vol.23 , pp. 7059-7068
    • Wölfel, M.1    Schneggenburger, R.2
  • 202
    • 0037598589 scopus 로고    scopus 로고
    • Role of Drosophila Rab5 during endosomal trafficking at the synapse and evoked neurotransmitter release
    • Wucherpfennig T, Wilsch-Brauninger M, Gonzalez-Gaitan M. 2003. Role of Drosophila Rab5 during endosomal trafficking at the synapse and evoked neurotransmitter release. J Cell Biol. 161:609-24
    • (2003) J. Cell Biol. , vol.161 , pp. 609-624
    • Wucherpfennig, T.1    Wilsch-Brauninger, M.2    Gonzalez-Gaitan, M.3
  • 203
    • 0035448875 scopus 로고    scopus 로고
    • Three-dimensional comparison of ultrastructural characteristics at depressing and facilitating synapses onto cerebellar Purkinje cells
    • Xu-Friedman MA, Harris KM, Regehr WG. 2001. Three-dimensional comparison of ultrastructural characteristics at depressing and facilitating synapses onto cerebellar Purkinje cells. J. Neurosci. 21:6666-72
    • (2001) J. Neurosci. , vol.21 , pp. 6666-6672
    • Xu-Friedman, M.A.1    Harris, K.M.2    Regehr, W.G.3
  • 204
    • 0034908225 scopus 로고    scopus 로고
    • SV2 modulates the size of the readily releasable pool of secretory vesicles
    • Xu T, Bajjalieh SM. 2001. SV2 modulates the size of the readily releasable pool of secretory vesicles. Nat. Cell Biol. 3:691-98
    • (2001) Nat. Cell Biol. , vol.3 , pp. 691-698
    • Xu, T.1    Bajjalieh, S.M.2
  • 206
    • 0038206589 scopus 로고    scopus 로고
    • Developmental increase in vesicular glutamate content does not cause saturation of AMPA receptors at the calyx of held synapse
    • Yamashita T, Ishikawa T, Takahashi T. 2003. Developmental increase in vesicular glutamate content does not cause saturation of AMPA receptors at the calyx of held synapse. J. Neurosci. 23:3633-38
    • (2003) J. Neurosci. , vol.23 , pp. 3633-3638
    • Yamashita, T.1    Ishikawa, T.2    Takahashi, T.3
  • 207
    • 0035879063 scopus 로고    scopus 로고
    • Stages of synapse development defined by dependence on F-actin
    • Zhang W, Benson DL. 2001. Stages of synapse development defined by dependence on F-actin. J. Neurosci. 21:5169-81
    • (2001) J. Neurosci. , vol.21 , pp. 5169-5181
    • Zhang, W.1    Benson, D.L.2
  • 208
    • 0005521375 scopus 로고
    • Simultaneous electrical and optical measurements show that membrane fusion precedes secretory granule swelling during exocytosis of beige mouse mast cells
    • Zimmerberg J, Curran M, Cohen FS, Brodwick M. 1987. Simultaneous electrical and optical measurements show that membrane fusion precedes secretory granule swelling during exocytosis of beige mouse mast cells. Proc. Natl. Acad. Sci. USA 84:1585-89
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1585-1589
    • Zimmerberg, J.1    Curran, M.2    Cohen, F.S.3    Brodwick, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.