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Volumn 147, Issue 6, 1999, Pages 1249-1260

Botulinum neurotoxin a blocks synaptic vesicle exocytosis but not endocytosis at the nerve terminal

Author keywords

Botulinum toxin type A; Endocytosis; Exocytosis; Presynaptic terminals; Synaptic vesicles

Indexed keywords

BOTULINUM TOXIN A; CALCIUM ION; CLOSTRIDIUM TOXIN; MEMBRANE PROTEIN; NEUROTOXIN; POTASSIUM ION; TETANUS TOXIN;

EID: 0033552583     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.6.1249     Document Type: Article
Times cited : (78)

References (68)
  • 5
    • 0023134919 scopus 로고
    • Differential effects of tetanus toxin on inhibitory and excitatory synaptic transmission in mammalian spinal cord neurons in culture: A presynaptic locus of action for tetanus toxin
    • Bergey, G.K., H. Bigalke, and P.G. Nelson. 1987. Differential effects of tetanus toxin on inhibitory and excitatory synaptic transmission in mammalian spinal cord neurons in culture: a presynaptic locus of action for tetanus toxin. J. Neurophysiol. 57:121-131.
    • (1987) J. Neurophysiol. , vol.57 , pp. 121-131
    • Bergey, G.K.1    Bigalke, H.2    Nelson, P.G.3
  • 6
    • 0026584039 scopus 로고
    • Optical analysis of synaptic vesicle recycling at the frog neuromuscular junction
    • Betz, W.J., and G.S. Bewick. 1992. Optical analysis of synaptic vesicle recycling at the frog neuromuscular junction. Science. 255:200-203.
    • (1992) Science , vol.255 , pp. 200-203
    • Betz, W.J.1    Bewick, G.S.2
  • 7
    • 0022397774 scopus 로고
    • Botulinum A neurotoxin inhibits non-cholinergic synaptic transmission in mouse spinal cord neurons in culture
    • Bigalke, H., F. Dreyer, and G. Bergey. 1985. Botulinum A neurotoxin inhibits non-cholinergic synaptic transmission in mouse spinal cord neurons in culture. Brain Res. 360:318-324.
    • (1985) Brain Res. , vol.360 , pp. 318-324
    • Bigalke, H.1    Dreyer, F.2    Bergey, G.3
  • 8
    • 0029093329 scopus 로고
    • Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila
    • Broadie, K., A. Prokop, H.J. Bellen, C.J. O'Kane, K.L. Schulze, and S.T. Sweeney. 1995. Syntaxin and synaptobrevin function downstream of vesicle docking in Drosophila. Neuron. 15:663-673.
    • (1995) Neuron , vol.15 , pp. 663-673
    • Broadie, K.1    Prokop, A.2    Bellen, H.J.3    O'Kane, C.J.4    Schulze, K.L.5    Sweeney, S.T.6
  • 9
    • 0030612655 scopus 로고    scopus 로고
    • 2+ partially rescues synaptic transmission in hippocampal cultures treated with botulinum toxin A and C, but not tetanus toxin
    • 2+ partially rescues synaptic transmission in hippocampal cultures treated with botulinum toxin A and C, but not tetanus toxin. J. Neurosci. 17:7190-7202.
    • (1997) J. Neurosci. , vol.17 , pp. 7190-7202
    • Capogna, M.1    McKinney, R.A.2    O'Connor, V.3    Gähwiler, B.H.4    Thompson, S.M.5
  • 10
    • 0019069857 scopus 로고
    • 2+-dependent recycling of synaptic vesicles at the frog neuromuscular junction
    • 2+-dependent recycling of synaptic vesicles at the frog neuromuscular junction. J. Cell Biol. 87:297-303.
    • (1980) J. Cell Biol. , vol.87 , pp. 297-303
    • Ceccarelli, B.1    Hurlbut, W.P.2
  • 11
    • 0015618402 scopus 로고
    • Turnover of transmitter and synaptic vesicles at the frog neuromuscular junction
    • Ceccarelli, B., W.P. Hurlbut, and A. Mauro. 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
  • 12
    • 0018843364 scopus 로고
    • Reversible effects of low doses of tetanus toxin on synaptic inhibition in the substantia nigra and turning behaviour in the rat
    • Collingridge, G.L., and J. Davies. 1980. Reversible effects of low doses of tetanus toxin on synaptic inhibition in the substantia nigra and turning behaviour in the rat. Brain Res. 185:455-459.
    • (1980) Brain Res. , vol.185 , pp. 455-459
    • Collingridge, G.L.1    Davies, J.2
  • 13
    • 0029985418 scopus 로고    scopus 로고
    • Molecular mechanisms in synaptic vesicle endocytosis and recycling
    • De Camilli, P., and K. Takei. 1996. Molecular mechanisms in synaptic vesicle endocytosis and recycling. Neuron. 16:481-486.
    • (1996) Neuron , vol.16 , pp. 481-486
    • De Camilli, P.1    Takei, K.2
  • 14
    • 0023101807 scopus 로고
    • Differential effects of various secretagogues on quantal transmitter release from mouse motor nerve terminals treated with botulinum A and tetanus toxin
    • Dreyer, F., F. Rosenberg, C. Becker, H. Bigalke, and R. Penner. 1987. Differential effects of various secretagogues on quantal transmitter release from mouse motor nerve terminals treated with botulinum A and tetanus toxin. Naunyn Schmiedebergs Arch. Pharmacol. 335:1-7.
    • (1987) Naunyn Schmiedebergs Arch. Pharmacol. , vol.335 , pp. 1-7
    • Dreyer, F.1    Rosenberg, F.2    Becker, C.3    Bigalke, H.4    Penner, R.5
  • 16
    • 0002231080 scopus 로고
    • Dissociated spinal cord-dorsal root ganglion cultures on plastic tissue culture dishes and glass coverslips and wells
    • A. Shahar, J. deVellis, A. Vernadakis, and B. Haber. editors. Alan R. Liss, Inc., New York
    • Fitzgerald, S.C. 1489. Dissociated spinal cord-dorsal root ganglion cultures on plastic tissue culture dishes and glass coverslips and wells. In A Dissection and Tissue Culture Manual of the Nervous System. A. Shahar, J. deVellis, A. Vernadakis, and B. Haber. editors. Alan R. Liss, Inc., New York. 219-222.
    • (1489) A Dissection and Tissue Culture Manual of the Nervous System , pp. 219-222
    • Fitzgerald, S.C.1
  • 17
    • 0032148395 scopus 로고    scopus 로고
    • 2+-triggered synaptic vesicle exocytosis and clathrin-mediated endocytosis at a central synapse
    • 2+-triggered synaptic vesicle exocytosis and clathrin-mediated endocytosis at a central synapse. Neuron. 21:607-616.
    • (1998) Neuron , vol.21 , pp. 607-616
    • Gad, H.1    Low, P.2    Zotova, E.3    Brodin, L.4    Shupliakov, O.5
  • 18
    • 0019191156 scopus 로고
    • The effects of botulinum toxin on the synthesis, storage and release of acetylcholine
    • Gundersen, C.B. 1980. The effects of botulinum toxin on the synthesis, storage and release of acetylcholine. Prog. Neurobiol. 14:99-119.
    • (1980) Prog. Neurobiol. , vol.14 , pp. 99-119
    • Gundersen, C.B.1
  • 19
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., R. Roth, H. Morisaki, R. Jahn, and J.E. Heuser. 1997. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell. 90:523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 20
    • 0029610859 scopus 로고
    • Staurosporine blocks evoked release of FM1-43 but not acetylcholine from frog motor nerve terminals
    • Henkel, A.W., and W.J. Betz. 1995. Staurosporine blocks evoked release of FM1-43 but not acetylcholine from frog motor nerve terminals. J. Neurosci. 15:8246-8258.
    • (1995) J. Neurosci. , vol.15 , pp. 8246-8258
    • Henkel, A.W.1    Betz, W.J.2
  • 21
    • 0015619310 scopus 로고
    • Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction
    • Heuser, J.E., and T.S. Reese. 1973. Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction. J. Cell Biol. 57:315-344.
    • (1973) J. Cell Biol. , vol.57 , pp. 315-344
    • Heuser, J.E.1    Reese, T.S.2
  • 22
    • 0029798593 scopus 로고    scopus 로고
    • Rapid exocytosis and endocytosis in nerve terminals of the rat posterior pituitary
    • 494.2
    • Hsu, S.-F., and M.B. Jackson. 1996. Rapid exocytosis and endocytosis in nerve terminals of the rat posterior pituitary. J. Physiol. 494.2:539-553.
    • (1996) J. Physiol. , pp. 539-553
    • Hsu, S.-F.1    Jackson, M.B.2
  • 25
    • 0014541501 scopus 로고
    • The "vesicle in a basket."
    • Kanaseki, T., and K. Kadota. 1969. The "vesicle in a basket." J. Cell Biol. 42: 202-220.
    • (1969) J. Cell Biol. , vol.42 , pp. 202-220
    • Kanaseki, T.1    Kadota, K.2
  • 26
    • 0032535040 scopus 로고    scopus 로고
    • Synaptic physiology and ultrastructure in comatose mutants define an in vivo role for NSF in neurotransmitter release
    • Kawasaki, F., A.M. Mattiuz, and R.W. Ordway. 1998. Synaptic physiology and ultrastructure in comatose mutants define an in vivo role for NSF in neurotransmitter release. J. Neurosci. 18:10241-10249.
    • (1998) J. Neurosci. , vol.18 , pp. 10241-10249
    • Kawasaki, F.1    Mattiuz, A.M.2    Ordway, R.W.3
  • 27
    • 0032490945 scopus 로고    scopus 로고
    • Kinetics and regulation of fast endocytosis at hippocampal synapses
    • Klingauf, J., E.T. Kavalali, and R.W. Tsien. 1998. Kinetics and regulation of fast endocytosis at hippocampal synapses. Nature. 394:581-585.
    • (1998) Nature , vol.394 , pp. 581-585
    • Klingauf, J.1    Kavalali, E.T.2    Tsien, R.W.3
  • 28
    • 0029031896 scopus 로고
    • Synaptic vesicle dynamics in living cultured hippocampal neurons visualized with Cy3-conjugated antibodies directed against the lumenal domain of synaptotagmin
    • Kraszewski, K., O. Mundigl, L. Daniell, C. Verderio, M. Matteoli, and P. De Camilli. 1995. Synaptic vesicle dynamics in living cultured hippocampal neurons visualized with Cy3-conjugated antibodies directed against the lumenal domain of synaptotagmin. J. Neurosci. 15:4328-4342.
    • (1995) J. Neurosci. , vol.15 , pp. 4328-4342
    • Kraszewski, K.1    Mundigl, O.2    Daniell, L.3    Verderio, C.4    Matteoli, M.5    De Camilli, P.6
  • 29
    • 0030900523 scopus 로고    scopus 로고
    • Importance of two adjacent C-terminal sequences of SNAP-25 in exocytosis from intact and permeabilized chromaffin cells revealed by inhibition with botulinum neurotoxins A and E
    • Lawrence, G.W., P. Foran, N. Mohammed, B.R. DasGupta, and J.O. Dolly. 1997. Importance of two adjacent C-terminal sequences of SNAP-25 in exocytosis from intact and permeabilized chromaffin cells revealed by inhibition with botulinum neurotoxins A and E. Biochemistry. 36:3061-3067.
    • (1997) Biochemistry , vol.36 , pp. 3061-3067
    • Lawrence, G.W.1    Foran, P.2    Mohammed, N.3    DasGupta, B.R.4    Dolly, J.O.5
  • 30
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin, R.C., and R.H. Scheller. 1997. Structural organization of the synaptic exocytosis core complex. Neuron. 19:1087-1094.
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 31
    • 0031963851 scopus 로고    scopus 로고
    • The relation of exocytosis and rapid endocytosis to calcium entry evoked by short repetitive depolarizing pulses in rat melanotropic cells
    • Mansvelder, H.D., and K.S. Kits. 1998. The relation of exocytosis and rapid endocytosis to calcium entry evoked by short repetitive depolarizing pulses in rat melanotropic cells. J. Neurosci. 18:81-92.
    • (1998) J. Neurosci. , vol.18 , pp. 81-92
    • Mansvelder, H.D.1    Kits, K.S.2
  • 32
    • 0032543766 scopus 로고    scopus 로고
    • Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals
    • Marks, B., and H.T. McMahon. 1998. Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals. Curr. Biol. 8:740-749.
    • (1998) Curr. Biol. , vol.8 , pp. 740-749
    • Marks, B.1    McMahon, H.T.2
  • 33
    • 0026719481 scopus 로고
    • Exoendocytotic recycling of synaptic vesicles in developing processes of cultured hippocampal neurons
    • Matteoli, M., K. Takei, M.S. Perin, T.C. Sudhof, and P. De Camilli. 1992. Exoendocytotic recycling of synaptic vesicles in developing processes of cultured hippocampal neurons. J. Cell Biol. 117:849-861.
    • (1992) J. Cell Biol. , vol.117 , pp. 849-861
    • Matteoli, M.1    Takei, K.2    Perin, M.S.3    Sudhof, T.C.4    De Camilli, P.5
  • 34
    • 0027265710 scopus 로고
    • Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein
    • McMahon, H.T., Y.A. Ushkaryov, L. Edelmann, E. Link, T. Binz, H. Niemann, R. Jahn, and T.C. Südhof. 1993. Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature. 364:346-349.
    • (1993) Nature , vol.364 , pp. 346-349
    • McMahon, H.T.1    Ushkaryov, Y.A.2    Edelmann, L.3    Link, E.4    Binz, T.5    Niemann, H.6    Jahn, R.7    Südhof, T.C.8
  • 35
    • 0023919946 scopus 로고
    • The effect of lanthanum on nerve terminals in goldfish muscle after paralysis with tetanus toxin
    • Mellanby, J., M.A. Beaumont, and P.A. Thompson. 1988. The effect of lanthanum on nerve terminals in goldfish muscle after paralysis with tetanus toxin. Neuroscience. 25:1095-1106.
    • (1988) Neuroscience , vol.25 , pp. 1095-1106
    • Mellanby, J.1    Beaumont, M.A.2    Thompson, P.A.3
  • 36
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Montecucco, C., and G. Schiavo. 1995. Structure and function of tetanus and botulinum neurotoxins. Quart. Rev. Biophys. 28:423-472.
    • (1995) Quart. Rev. Biophys. , vol.28 , pp. 423-472
    • Montecucco, C.1    Schiavo, G.2
  • 38
    • 0032473998 scopus 로고    scopus 로고
    • Synaptic vesicles retain their identity through the endocytic cycle
    • Murthy, V.N., and C.F. Stevens. 1998. Synaptic vesicles retain their identity through the endocytic cycle. Nature. 392:497-501.
    • (1998) Nature , vol.392 , pp. 497-501
    • Murthy, V.N.1    Stevens, C.F.2
  • 39
    • 0017881790 scopus 로고
    • Intracellular horseradish peroxidase injection for correlation of light and electron microscopic anatomy with synaptic physiology of cultured mouse spinal cord neurons
    • Neale, E.A., R.L. Macdonald, and P.G. Nelson. 1978. Intracellular horseradish peroxidase injection for correlation of light and electron microscopic anatomy with synaptic physiology of cultured mouse spinal cord neurons. Brain Res. 152:265-282.
    • (1978) Brain Res. , vol.152 , pp. 265-282
    • Neale, E.A.1    Macdonald, R.L.2    Nelson, P.G.3
  • 40
    • 0342871818 scopus 로고
    • Applications of tetanus toxin for structure-function studies in neuronal cell cultures
    • (Leningrad). G. Nisticò, B. Bizzini, B. Bytchenko, and R. Triau, editors. Pythagora Press, Rome-Milan
    • Neale, E.A., W.H. Habig, B.K. Schrier, G.K. Bergey, L.M. Bowers, and J. Koh. 1989. Applications of tetanus toxin for structure-function studies in neuronal cell cultures. In Eighth International Conference on Tetanus (Leningrad). G. Nisticò, B. Bizzini, B. Bytchenko, and R. Triau, editors. Pythagora Press, Rome-Milan. 58-65.
    • (1989) Eighth International Conference on Tetanus , pp. 58-65
    • Neale, E.A.1    Habig, W.H.2    Schrier, B.K.3    Bergey, G.K.4    Bowers, L.M.5    Koh, J.6
  • 41
    • 85013509071 scopus 로고
    • Multicompartment cell cultures for studies of neuronal interactions
    • P.M. Conn, editor. Academic Press Inc., San Diego
    • Neale, E.A., S.C. Fitzgerald, L.M. Bowers, C. Yu, R.D. Fields, and P.G. Nelson. 1991. Multicompartment cell cultures for studies of neuronal interactions. In Methods in Neurosciences. Vol. 4. P.M. Conn, editor. Academic Press Inc., San Diego, 312-349.
    • (1991) Methods in Neurosciences , vol.4 , pp. 312-349
    • Neale, E.A.1    Fitzgerald, S.C.2    Bowers, L.M.3    Yu, C.4    Fields, R.D.5    Nelson, P.G.6
  • 42
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • Protopopov, V., B. Govindan, P. Novick, and J.E. Gerst. 1993. Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell. 74:855-861.
    • (1993) Cell , vol.74 , pp. 855-861
    • Protopopov, V.1    Govindan, B.2    Novick, P.3    Gerst, J.E.4
  • 43
    • 0028017289 scopus 로고
    • Intermediates in synaptic vesicle recycling revealed by optical imaging of Drosophila neuromuscular junctions
    • Ramaswami, M., K.S. Krishnan, and R.B. Kelly. 1994. Intermediates in synaptic vesicle recycling revealed by optical imaging of Drosophila neuromuscular junctions. Neuron. 13:363-375.
    • (1994) Neuron , vol.13 , pp. 363-375
    • Ramaswami, M.1    Krishnan, K.S.2    Kelly, R.B.3
  • 44
    • 0017669602 scopus 로고
    • Mouse spinal cord in cell culture. I. Morphology and intrinsic neuronal electrophysiologic properties
    • Ransom, B.R., E.A. Neale, M. Henkart, P.N. Bullock, and P.G. Nelson. 1977. Mouse spinal cord in cell culture. I. Morphology and intrinsic neuronal electrophysiologic properties. J. Neurophysiol. 40:1132-1150.
    • (1977) J. Neurophysiol. , vol.40 , pp. 1132-1150
    • Ransom, B.R.1    Neale, E.A.2    Henkart, M.3    Bullock, P.N.4    Nelson, P.G.5
  • 45
    • 0030023904 scopus 로고    scopus 로고
    • VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues
    • Rossetto, O., L. Gorza, G. Schiavo, N. Schiavo, R.H. Scheller, and C. Montecucco. 1996. VAMP/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues. J. Cell Biol. 132:167-179.
    • (1996) J. Cell Biol. , vol.132 , pp. 167-179
    • Rossetto, O.1    Gorza, L.2    Schiavo, G.3    Schiavo, N.4    Scheller, R.H.5    Montecucco, C.6
  • 46
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman, J.E., and G. Warren. 1994. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr. Biol. 4:220-233.
    • (1994) Curr. Biol. , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 47
    • 0030480825 scopus 로고    scopus 로고
    • Endocytosis at nerve terminals: Timing is everything
    • Ryan, T.A. 1996. Endocytosis at nerve terminals: timing is everything. Neuron. 17:1035-1037.
    • (1996) Neuron , vol.17 , pp. 1035-1037
    • Ryan, T.A.1
  • 48
    • 0030856448 scopus 로고    scopus 로고
    • Optical detection of a quantal presynaptic membrane turnover
    • Ryan, T.A., H. Reuter, and S.J. Smith. 1997. Optical detection of a quantal presynaptic membrane turnover. Nature. 388:478-482.
    • (1997) Nature , vol.388 , pp. 478-482
    • Ryan, T.A.1    Reuter, H.2    Smith, S.J.3
  • 49
    • 0027487057 scopus 로고
    • The kinetics of synaptic vesicle recycling measured at single presynaplic boutons
    • Ryan, T.A., H. Reuter, B. Wendland, F.E. Schweizer, R.W. Tsien, and S.J. Smith. 1993. The kinetics of synaptic vesicle recycling measured at single presynaplic boutons. Neuron. 11:713-724.
    • (1993) Neuron , vol.11 , pp. 713-724
    • Ryan, T.A.1    Reuter, H.2    Wendland, B.3    Schweizer, F.E.4    Tsien, R.W.5    Smith, S.J.6
  • 50
    • 0032198135 scopus 로고    scopus 로고
    • A v-SNARE participates in synaptic vesicle formation mediated by the AP3 adaptor complex
    • Salem, N., V. Faúndez, J.-T. Horng, and R.B. Kelly. 1998. A v-SNARE participates in synaptic vesicle formation mediated by the AP3 adaptor complex. Nat. Neurosci. 1:551-556.
    • (1998) Nat. Neurosci. , vol.1 , pp. 551-556
    • Salem, N.1    Faúndez, V.2    Horng, J.-T.3    Kelly, R.B.4
  • 52
    • 0031019926 scopus 로고    scopus 로고
    • Binding of the synaptic vesicle v-SNARE. synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses
    • Schiavo, G., G. Stenbeck, J.E. Rothman, and T.H. Söllner. 1997. Binding of the synaptic vesicle v-SNARE. synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses. Proc. Natl. Acad. Sci. USA. 94:997-1001.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Söllner, T.H.4
  • 55
    • 0030718608 scopus 로고    scopus 로고
    • Multiple forms of endocytosis in bovine adrenal chromaffin cells
    • Smith, C., and E. Neher. 1997. Multiple forms of endocytosis in bovine adrenal chromaffin cells. J. Cell Biol. 139:885-894.
    • (1997) J. Cell Biol. , vol.139 , pp. 885-894
    • Smith, C.1    Neher, E.2
  • 57
    • 0029894198 scopus 로고    scopus 로고
    • The synaptic vesicle cycle: A single vesicle budding step involving clathrin and dynamin
    • Takei, K., O. Mundigl, L. Daniell, and P. De Camilli. 1996. The synaptic vesicle cycle: a single vesicle budding step involving clathrin and dynamin. J. Cell Biol. 133:1237-1250.
    • (1996) J. Cell Biol. , vol.133 , pp. 1237-1250
    • Takei, K.1    Mundigl, O.2    Daniell, L.3    De Camilli, P.4
  • 59
    • 0025194244 scopus 로고
    • 2+. Exocytosis, and endocytosis in single melanotrophs of the rat pituitary
    • 2+. exocytosis, and endocytosis in single melanotrophs of the rat pituitary. Neuron. 5:723-733.
    • (1990) Neuron , vol.5 , pp. 723-733
    • Thomas, P.1    Suprenant, A.2    Almers, W.3
  • 60
    • 0025098982 scopus 로고
    • Redistribution of synaptophysin and synapsin 1 during alphalatrotoxin-induced release of neurotransmitter at the neuromuscular junction
    • Torri-Tarelli, F., A. Villa, F. Valtorta, P. De Camilli, P. Greengard, and B. Ceccarelli. 1990. Redistribution of synaptophysin and synapsin 1 during alphalatrotoxin-induced release of neurotransmitter at the neuromuscular junction. J. Cell Biol. 110:449-159.
    • (1990) J. Cell Biol. , vol.110 , pp. 449-1159
    • Torri-Tarelli, F.1    Villa, A.2    Valtorta, F.3    De Camilli, P.4    Greengard, P.5    Ceccarelli, B.6
  • 61
    • 0032499761 scopus 로고    scopus 로고
    • Modulation of an early step in the secretory machinery in hippocampal nerve terminals
    • Trudeau, L.-E., Y. Fang, and P.G. Haydon. 1998. Modulation of an early step in the secretory machinery in hippocampal nerve terminals. Proc. Natl. Acad. Sci. USA. 95:7163-7168.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7163-7168
    • Trudeau, L.-E.1    Fang, Y.2    Haydon, P.G.3
  • 62
    • 0024232977 scopus 로고
    • Synaptophysin (p38) at the frog neuromuscular junction: Its incorporation into the axolemma and recycling after intense quantal secretion
    • Valtorta, F., R. Jahn, R. Fesce, P. Greengard, and B. Ceccarelli. 1988. Synaptophysin (p38) at the frog neuromuscular junction: its incorporation into the axolemma and recycling after intense quantal secretion. J. Cell Biol. 107: 2717-2727.
    • (1988) J. Cell Biol. , vol.107 , pp. 2717-2727
    • Valtorta, F.1    Jahn, R.2    Fesce, R.3    Greengard, P.4    Ceccarelli, B.5
  • 63
    • 0019519742 scopus 로고
    • Transfer of synaptic vesicle antigens to the presynaplic plasma membrane during exocytosis
    • von Wedel, R.J., S.S. Carlson, and R.B. Kelly. 1981. Transfer of synaptic vesicle antigens to the presynaplic plasma membrane during exocytosis. Proc. Natl. Acad. Sci. USA. 78:1014-1018.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1014-1018
    • Von Wedel, R.J.1    Carlson, S.S.2    Kelly, R.B.3
  • 64
    • 0005939686 scopus 로고
    • The development of spontaneous electrical activity in spinal cord cultures
    • F. Caciagli, E. Giacobini, and R. Paoletti, editors. Elsevier Science Publishing Co. Inc., New York
    • Westbrook, G.L., and D.E. Brenneman. 1984. The development of spontaneous electrical activity in spinal cord cultures. In Developmental Neuroscience: Physiological, Pharmacological and Clinical Aspects. F. Caciagli, E. Giacobini, and R. Paoletti, editors. Elsevier Science Publishing Co. Inc., New York. 11-17.
    • (1984) Developmental Neuroscience: Physiological, Pharmacological and Clinical Aspects , pp. 11-17
    • Westbrook, G.L.1    Brenneman, D.E.2
  • 65
    • 0026526207 scopus 로고
    • Differential effects of tetanus toxin on inhibitory and excitatory neurotransmitter release from mammalian spinal cord cells in culture
    • Williamson, L.C., S.C. Fitzgerald, and E.A. Neale. 1992. Differential effects of tetanus toxin on inhibitory and excitatory neurotransmitter release from mammalian spinal cord cells in culture. J. Neurochem. 59:2148-2157.
    • (1992) J. Neurochem. , vol.59 , pp. 2148-2157
    • Williamson, L.C.1    Fitzgerald, S.C.2    Neale, E.A.3
  • 66
    • 0029980484 scopus 로고    scopus 로고
    • Clostridial neurotoxins and substrate proteolysis in intact neurons. Botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa
    • Williamson, L.C., J.L. Halpern, C. Montecucco, J.E. Brown, and E.A. Neale. 1996. Clostridial neurotoxins and substrate proteolysis in intact neurons. Botulinum neurotoxin C acts on synaptosomal-associated protein of 25 kDa. J. Biol. Chem. 271:7694-7699.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7694-7699
    • Williamson, L.C.1    Halpern, J.L.2    Montecucco, C.3    Brown, J.E.4    Neale, E.A.5
  • 67
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu, T., T. Binz, H. Niemann, and E. Neher. 1998. Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nat. Neurosci. 1:192-200.
    • (1998) Nat. Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 68
    • 0030476187 scopus 로고    scopus 로고
    • Exocytosis: A molecular and physiological perspective
    • Zucker, R.S. 1996. Exocytosis: a molecular and physiological perspective. Neuron. 17:1049-1055.
    • (1996) Neuron , vol.17 , pp. 1049-1055
    • Zucker, R.S.1


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