메뉴 건너뛰기




Volumn 36, Issue 3, 2000, Pages 175-182

Protein-protein interactions in neurotransmitter release

Author keywords

Ca2+ channels; Exocytosis; Neurotransmitter release; Snare proteins; Synaptic terminal proteins; Synaptic vesicle

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25;

EID: 0033981878     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-0102(99)00128-5     Document Type: Article
Times cited : (59)

References (79)
  • 3
    • 0030786774 scopus 로고    scopus 로고
    • Better late than never: A role for rabs late in exocytosis
    • Bean A.J., Scheller R.H. Better late than never: a role for rabs late in exocytosis. Neuron. 19:1997;751-754.
    • (1997) Neuron , vol.19 , pp. 751-754
    • Bean, A.J.1    Scheller, R.H.2
  • 4
    • 0033363646 scopus 로고    scopus 로고
    • The septin CDCrel-1 binds syntaxin and inhibits exocytosis
    • Beites C.L., Xie H., Bowser R., Trimble W.S. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat. Neurosci. 2:1999;434-439.
    • (1999) Nat. Neurosci. , vol.2 , pp. 434-439
    • Beites, C.L.1    Xie, H.2    Bowser, R.3    Trimble, W.S.4
  • 5
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett M.K., Scheller R.H. The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl. Acad. Sci. USA. 90:1993;2559-2563.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 6
    • 0031027591 scopus 로고    scopus 로고
    • Direct interaction of the rat unc-13 homologue Munc13-1 with the N-terminal of syntaxin
    • Betz A., Okamoto M., Benseler F., Brose N. Direct interaction of the rat unc-13 homologue Munc13-1 with the N-terminal of syntaxin. J. Biol. Chem. 272:1997;2520-2526.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2520-2526
    • Betz, A.1    Okamoto, M.2    Benseler, F.3    Brose, N.4
  • 7
    • 18544399674 scopus 로고    scopus 로고
    • Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release
    • Betz A., Ashley U., Rickmann M. et al. Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release. Neuron. 21:1998;123-136.
    • (1998) Neuron , vol.21 , pp. 123-136
    • Betz, A.1    Ashley, U.2    Rickmann, M.3
  • 8
    • 0028783997 scopus 로고
    • Functional impact of syntaxin on gating of N-type and Q-type calcium channels
    • Bezprozvanny I., Scheller R.H., Tsien R.W. Functional impact of syntaxin on gating of N-type and Q-type calcium channels. Nature. 378:1995;623-626.
    • (1995) Nature , vol.378 , pp. 623-626
    • Bezprozvanny, I.1    Scheller, R.H.2    Tsien, R.W.3
  • 9
    • 0027269605 scopus 로고
    • Inhibition of neurotransmitter release by C2-domain peptides implicates synaptotagmin in exocytosis
    • Bommert K., Charton M.P., DeBello W.M. et al. Inhibition of neurotransmitter release by C2-domain peptides implicates synaptotagmin in exocytosis. Nature. 363:1993;163-165.
    • (1993) Nature , vol.363 , pp. 163-165
    • Bommert, K.1    Charton, M.P.2    Debello, W.M.3
  • 10
    • 0029093329 scopus 로고
    • Syntaxin and VAMP function downstream of vesicle docking in Drosophila
    • Broadie K., Prokop A., Bellen H.J. et al. Syntaxin and VAMP function downstream of vesicle docking in Drosophila. Neuron. 15:1995;663-673.
    • (1995) Neuron , vol.15 , pp. 663-673
    • Broadie, K.1    Prokop, A.2    Bellen, H.J.3
  • 11
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose N., Petrenko A.G., Südhof T.C., Jahn R. Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science. 256:1992;1021-1025.
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Südhof, T.C.3    Jahn, R.4
  • 12
    • 0028791349 scopus 로고
    • Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins
    • Brose N., Hofmann K., Hata Y., Südhof T.C. Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins. J. Biol. Chem. 270:1995;25273-25280.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25273-25280
    • Brose, N.1    Hofmann, K.2    Hata, Y.3    Südhof, T.C.4
  • 13
    • 0031915887 scopus 로고    scopus 로고
    • Rabphilin-3A: A multifunctional regulator of synaptic vesicle traffic
    • Burns E.M., Sasaki T., Takai Y., Augustine G.J. Rabphilin-3A: a multifunctional regulator of synaptic vesicle traffic. J. Gen. Physiol. 111:1998;243-255.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 243-255
    • Burns, E.M.1    Sasaki, T.2    Takai, Y.3    Augustine, G.J.4
  • 14
    • 0030791511 scopus 로고    scopus 로고
    • Rab3A is essential for mossy fibre long-term potentiation in the hippocampus
    • Castillo P.E., Janz R., Südhof T.C. et al. Rab3A is essential for mossy fibre long-term potentiation in the hippocampus. Nature. 388:1997;590-593.
    • (1997) Nature , vol.388 , pp. 590-593
    • Castillo, P.E.1    Janz, R.2    Südhof, T.C.3
  • 15
    • 0027973132 scopus 로고
    • SNAP-25, a t-SNARE which binds to both syntaxin and VAMP via domains that may form cioled coils
    • Chapman E.R., An S., Barton N., Jahn R. SNAP-25, a t-SNARE which binds to both syntaxin and VAMP via domains that may form cioled coils. J. Biol. Chem. 269:1995a;27427-27432.
    • (1995) J. Biol. Chem. , vol.269 , pp. 27427-27432
    • Chapman, E.R.1    An, S.2    Barton, N.3    Jahn, R.4
  • 16
    • 0028970788 scopus 로고
    • 2+ regulates the interaction between synaptotagmin and syntaxin 1
    • 2+ regulates the interaction between synaptotagmin and syntaxin 1. J. Biol. Chem. 270:1995b;23667-23671.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23667-23671
    • Chapman, E.R.1    Hanson, P.I.2    An, S.3    Jahn, R.4
  • 18
    • 0033213302 scopus 로고    scopus 로고
    • 2+ and assembly with core snare complex onto membranes
    • 2+ and assembly with core snare complex onto membranes. Neuron. 24:1999;363-376.
    • (1999) Neuron , vol.24 , pp. 363-376
    • Davis, A.F.1    Bai, J.2    Fasshauer, D.3
  • 19
    • 0028985213 scopus 로고
    • SNAP-mediated protein-protein interactions essential for neurotransmitter release
    • DeBello W.M., O'Conner V., Dresbach T. et al. SNAP-mediated protein-protein interactions essential for neurotransmitter release. Nature. 373:1995;626-630.
    • (1995) Nature , vol.373 , pp. 626-630
    • Debello, W.M.1    O'Conner, V.2    Dresbach, T.3
  • 20
    • 0032521343 scopus 로고    scopus 로고
    • Distinct requirements for evoked and spontaneous release of neurotransmitter are revealed by mutations in the Drosophila gene neuronal-VAMP
    • Deitcher D.L., Ueda A., Stewart B.A. et al. Distinct requirements for evoked and spontaneous release of neurotransmitter are revealed by mutations in the Drosophila gene neuronal-VAMP. J. Neurosci. 18:1998;2028-2039.
    • (1998) J. Neurosci. , vol.18 , pp. 2028-2039
    • Deitcher, D.L.1    Ueda, A.2    Stewart, B.A.3
  • 21
    • 0032523028 scopus 로고    scopus 로고
    • A neuronal Sec1 homolog regulates neurotransmitter release at the squid giant synapse
    • Dresbach T., Burns M.E., O'Conner V. et al. A neuronal Sec1 homolog regulates neurotransmitter release at the squid giant synapse. J. Neurosci. 18:1998;2923-2932.
    • (1998) J. Neurosci. , vol.18 , pp. 2923-2932
    • Dresbach, T.1    Burns, M.E.2    O'Conner, V.3
  • 22
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick S., Jahn R. Vesicle fusion from yeast to man. Nature. 370:1994;191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 23
    • 0033548070 scopus 로고    scopus 로고
    • Regulation of exocytosis by cyclin-dependent kinase 5 via phosphorylatoin of munc-18
    • Fletcher A.I., Shuang R., Giovannucci D.R. et al. Regulation of exocytosis by cyclin-dependent kinase 5 via phosphorylatoin of munc-18. J. Biol. Chem. 274:1999;4027-4035.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4027-4035
    • Fletcher, A.I.1    Shuang, R.2    Giovannucci, D.R.3
  • 24
    • 17344376286 scopus 로고    scopus 로고
    • Tomosyn: A syntaxin-1-binding protein that forms a novel complex in the neurotransmitter process
    • Fujita Y., Shirataki H., Sakisaka T. et al. Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter process. Neuron. 20:1998a;905-915.
    • (1998) Neuron , vol.20 , pp. 905-915
    • Fujita, Y.1    Shirataki, H.2    Sakisaka, T.3
  • 25
    • 0029963857 scopus 로고    scopus 로고
    • Phosphorylation of munc-18/n-Sec1/rbSec1 by protein kinase C
    • Fujita Y., Sasaki T., Fukui K. et al. Phosphorylation of munc-18/n-Sec1/rbSec1 by protein kinase C. J. Biol. Chem. 271:1998b;7265-7268.
    • (1998) J. Biol. Chem. , vol.271 , pp. 7265-7268
    • Fujita, Y.1    Sasaki, T.2    Fukui, K.3
  • 26
    • 0028343430 scopus 로고
    • Role of the rab3A in neurotransmitter release
    • Geppert M., Bolshakov V.Y., Siegelbaum S.A. et al. Role of the rab3A in neurotransmitter release. Nature. 369:1994;493-497.
    • (1994) Nature , vol.369 , pp. 493-497
    • Geppert, M.1    Bolshakov, V.Y.2    Siegelbaum, S.A.3
  • 27
    • 0028061861 scopus 로고
    • 2+ sensor for transmitter release at a central synapse
    • 2+ sensor for transmitter release at a central synapse. Cell. 79:1994;717-727.
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1    Goda, Y.2    Hammer, R.E.3
  • 28
    • 0030980279 scopus 로고    scopus 로고
    • The small GTP-binding protein rab3A regulates a late step in synaptic vesicle fusion
    • Geppert M., Goda Y., Stevens C.F., Südhof T.C. The small GTP-binding protein rab3A regulates a late step in synaptic vesicle fusion. Nature. 387:1997;810-814.
    • (1997) Nature , vol.387 , pp. 810-814
    • Geppert, M.1    Goda, Y.2    Stevens, C.F.3    Südhof, T.C.4
  • 29
    • 0030176052 scopus 로고    scopus 로고
    • Protein kinase C enhances exocytosis from chromaffin cells by increasing the size of the readily releasable pool of secretory granules
    • Gillis K.D., Möbner R., Neher E. Protein kinase C enhances exocytosis from chromaffin cells by increasing the size of the readily releasable pool of secretory granules. Neuron. 16:1996;1209-1220.
    • (1996) Neuron , vol.16 , pp. 1209-1220
    • Gillis, K.D.1    Möbner, R.2    Neher, E.3
  • 30
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release - 4 years of SNARE complexes
    • Hanson P.I., Heuser J.E., Jahn R. Neurotransmitter release - 4 years of SNARE complexes. Curr. Opin. Neurobiol. 7:1997;310-315.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 310-315
    • Hanson, P.I.1    Heuser, J.E.2    Jahn, R.3
  • 31
    • 0029004741 scopus 로고
    • Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro
    • Hayashi T., Yamasaki S., Nauenburg S., Binz T., Niemann H. Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J. 14:1995;2317-2325.
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayashi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Niemann, H.5
  • 32
    • 0029862503 scopus 로고    scopus 로고
    • Phosphorylation of synaptic vesicle proteins: Modulation of the αsNAP interaction with the core complex
    • Hirling H., Scheller R.H. Phosphorylation of synaptic vesicle proteins: modulation of the αSNAP interaction with the core complex. Proc. Natl. Acad. Sci. USA. 93:1996;11945-11949.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11945-11949
    • Hirling, H.1    Scheller, R.H.2
  • 33
    • 0028263696 scopus 로고
    • A post-docking role for VAMP in synaptic vesicle fusion
    • Hunt J.M., Bommert K., Charlton M.P. et al. A post-docking role for VAMP in synaptic vesicle fusion. Neuron. 12:1994;1269-1279.
    • (1994) Neuron , vol.12 , pp. 1269-1279
    • Hunt, J.M.1    Bommert, K.2    Charlton, M.P.3
  • 34
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • Ilardi J.M., Mochida S., Sheng Z.-H. Snapin: a SNARE-associated protein implicated in synaptic transmission. Nat. Neurosci. 2:1999;119-124.
    • (1999) Nat. Neurosci. , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.-H.3
  • 38
    • 0032142949 scopus 로고    scopus 로고
    • Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly
    • Littleton J.T., Chapman E.R., Kreber R. et al. Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly. Neuron. 21:1998;401-413.
    • (1998) Neuron , vol.21 , pp. 401-413
    • Littleton, J.T.1    Chapman, E.R.2    Kreber, R.3
  • 39
    • 0033584339 scopus 로고    scopus 로고
    • Synaptic function modulated by changes in the ratio of synaptotagmin I and IV
    • Littleton J.T., Serano T.L., Rubin G.M., Ganetzky B., Chapman E.R. Synaptic function modulated by changes in the ratio of synaptotagmin I and IV. Nature. 400:1999;757-760.
    • (1999) Nature , vol.400 , pp. 757-760
    • Littleton, J.T.1    Serano, T.L.2    Rubin, G.M.3    Ganetzky, B.4    Chapman, E.R.5
  • 40
    • 0031001794 scopus 로고    scopus 로고
    • T-SNARE activation through transient interaction with rab-like guanosine triphosphate
    • Lupashin V.V., Waters M.G. t-SNARE activation through transient interaction with rab-like guanosine triphosphate. Science. 276:1997;1255-1258.
    • (1997) Science , vol.276 , pp. 1255-1258
    • Lupashin, V.V.1    Waters, M.G.2
  • 41
    • 0026053020 scopus 로고
    • A phorbol ester/diacylglycerol-binding protein encoded by the unc-13 gene of Caenorhabditis elegans
    • Maruyama I.N., Brenner S. A phorbol ester/diacylglycerol-binding protein encoded by the unc-13 gene of Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA. 88:1991;5729-5733.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5729-5733
    • Maruyama, I.N.1    Brenner, S.2
  • 42
    • 0023770753 scopus 로고
    • Nucleotide and deduced amino acid sequences of a GTP-binding protein family with molecular weights of 25000 from bovine brain
    • Matsui Y., Kikuchi A., Kondo J. et al. Nucleotide and deduced amino acid sequences of a GTP-binding protein family with molecular weights of 25000 from bovine brain. J. Biol. Chem. 263:1988;11071-11074.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11071-11074
    • Matsui, Y.1    Kikuchi, A.2    Kondo, J.3
  • 43
    • 0028880456 scopus 로고
    • Complexins: Cytosolic proteins that regulate SNAP receptor function
    • McMahon H.T., Missler M., Li C., Südhof T.C. Complexins: cytosolic proteins that regulate SNAP receptor function. Cell. 83:1995;111-119.
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Südhof, T.C.4
  • 44
    • 0030175826 scopus 로고    scopus 로고
    • Nitric oxide modulates synaptic vesicle docking/fusion reactions
    • Meffert M.K., Calakos N.C., Scheller R.H., Schulman H. Nitric oxide modulates synaptic vesicle docking/fusion reactions. Neuron. 16:1996;1229-1236.
    • (1996) Neuron , vol.16 , pp. 1229-1236
    • Meffert, M.K.1    Calakos, N.C.2    Scheller, R.H.3    Schulman, H.4
  • 45
    • 0028799119 scopus 로고
    • Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse terminal
    • Mikoshiba K., Fukuda M., Moreira J.E. et al. Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse terminal. Proc. Natl. Acad. Sci. USA. 92:1995;10703-10707.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10703-10707
    • Mikoshiba, K.1    Fukuda, M.2    Moreira, J.E.3
  • 47
    • 0030888066 scopus 로고    scopus 로고
    • Role of synaptotagmin C2 domains in neurotransmitter secretion and inositol high-polyphosphate binding at mammalian cholinergic synapses
    • Mochida S., Fukuda M., Niinobe M., Kobayashi H., Mikoshiba K. Role of synaptotagmin C2 domains in neurotransmitter secretion and inositol high-polyphosphate binding at mammalian cholinergic synapses. Neuroscience. 77:1997;937-943.
    • (1997) Neuroscience , vol.77 , pp. 937-943
    • Mochida, S.1    Fukuda, M.2    Niinobe, M.3    Kobayashi, H.4    Mikoshiba, K.5
  • 48
    • 0032530085 scopus 로고    scopus 로고
    • Role of the Doc2a-Munc-13-1 interaction in the neurotransmitter release process
    • Mochida S., Orita S., Sakaguchi G., Sasaki T., Takai Y. Role of the Doc2a-Munc-13-1 interaction in the neurotransmitter release process. Proc. Natl. Acad. Sci. USA. 95:1998a;11418-11422.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11418-11422
    • Mochida, S.1    Orita, S.2    Sakaguchi, G.3    Sasaki, T.4    Takai, Y.5
  • 50
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • Monteccuco C., Schiavo G. Structure and function of tetanus and botulinum neurotoxins. Quart. Rev. Biophys. 28:1995;423-472.
    • (1995) Quart. Rev. Biophys. , vol.28 , pp. 423-472
    • Monteccuco, C.1    Schiavo, G.2
  • 51
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann H., Blasi J., Jahn R. Clostridial neurotoxins: new tools for dissecting exocytosis. Trens. Cell. Biol. 4:1994;179-185.
    • (1994) Trens. Cell. Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 52
    • 18544407805 scopus 로고    scopus 로고
    • Regulatory roles of complexins in neurotransmitter release from mature presynaptic nerve terminals
    • Ono S., Baux G., Sekiguchi M. et al. Regulatory roles of complexins in neurotransmitter release from mature presynaptic nerve terminals. Eur. J. Neurosci. 10:1998;2143-2152.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 2143-2152
    • Ono, S.1    Baux, G.2    Sekiguchi, M.3
  • 53
    • 0028897324 scopus 로고
    • Molecular cloning of an isoform of Doc2 having two C2-like domains
    • Orita S., Sasaki T., Komura R. et al. Molecular cloning of an isoform of Doc2 having two C2-like domains. Biochem. Biophys. Res. Commun. 206:1995;439-448.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 439-448
    • Orita, S.1    Sasaki, T.2    Komura, R.3
  • 55
    • 0027932454 scopus 로고
    • Specificity and regulation of a synaptic vesicle docking complex
    • Pevsner J., Hsu S.-C., Braun J.E.A. et al. Specificity and regulation of a synaptic vesicle docking complex. Neuron. 13:1994;353-361.
    • (1994) Neuron , vol.13 , pp. 353-361
    • Pevsner, J.1    Hsu, S.-C.2    Braun, J.E.A.3
  • 58
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J.E. Mechanisms of intracellular protein transport. Nature. 372:1994;55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 59
    • 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., Stenbeck G., Rothman J.E., Söllner T.H. 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. 94:1997;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
  • 60
    • 0040576976 scopus 로고    scopus 로고
    • Rabphilin knock out mice reveal that rabphilin is not required for rab3 function in regulating neurotransmitter release
    • Schülter O.M., Schnell E., Verhage M. et al. Rabphilin knock out mice reveal that rabphilin is not required for rab3 function in regulating neurotransmitter release. J. Neurosci. 19:1999;5834-5846.
    • (1999) J. Neurosci. , vol.19 , pp. 5834-5846
    • Schülter, O.M.1    Schnell, E.2    Verhage, M.3
  • 61
    • 0028817584 scopus 로고
    • Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission
    • Schulze K.L., Broadie K., Perin M.S., Bellen H.J. Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission. Cell. 80:1995;311-320.
    • (1995) Cell , vol.80 , pp. 311-320
    • Schulze, K.L.1    Broadie, K.2    Perin, M.S.3    Bellen, H.J.4
  • 62
    • 0031019191 scopus 로고    scopus 로고
    • 2+-dependent electrostatic switch
    • 2+-dependent electrostatic switch. Neuron. 18:1997;133-142.
    • (1997) Neuron , vol.18 , pp. 133-142
    • Shao, X.1    Li, C.2    Fernandez, I.3
  • 63
    • 0028595727 scopus 로고
    • Identification of a syntaxin-binding site on N-type calcium channels
    • Sheng Z.-H., Rettig J., Takahashi M., Catterall W.A. Identification of a syntaxin-binding site on N-type calcium channels. Neuron. 13:1994;1303-1313.
    • (1994) Neuron , vol.13 , pp. 1303-1313
    • Sheng, Z.-H.1    Rettig, J.2    Takahashi, M.3    Catterall, W.A.4
  • 64
    • 0030048838 scopus 로고
    • Calcium-dependent interaction of N-type calcium channels with the synaptic core-complex
    • Sheng Z.-H., Rettig J., Cook T., Catterall W.A. Calcium-dependent interaction of N-type calcium channels with the synaptic core-complex. Nature. 379:1994;451-454.
    • (1994) Nature , vol.379 , pp. 451-454
    • Sheng, Z.-H.1    Rettig, J.2    Cook, T.3    Catterall, W.A.4
  • 65
    • 0029898850 scopus 로고    scopus 로고
    • Phosphorylation of 25-kDa synaptosome-associated protein
    • Shimazaki Y., Nishiki T., Omori A. et al. Phosphorylation of 25-kDa synaptosome-associated protein. J. Biol. Chem. 271:1996;14548-14553.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14548-14553
    • Shimazaki, Y.1    Nishiki, T.2    Omori, A.3
  • 66
    • 0027461829 scopus 로고
    • Rabphilin-3A, a putative target protein for smg p25/rab3A p25 small GTP-binding protein related to synaptotagmin
    • Shirataki H., Kaibuchi K., Sakoda T. et al. Rabphilin-3A, a putative target protein for smg p25/rab3A p25 small GTP-binding protein related to synaptotagmin. Mol. Cell. Biol. 13:1993;2061-2068.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2061-2068
    • Shirataki, H.1    Kaibuchi, K.2    Sakoda, T.3
  • 67
    • 0028168008 scopus 로고
    • A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Søgaard M., Tani K., Ye R.R. et al. A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell. 78:1994;937-948.
    • (1994) Cell , vol.78 , pp. 937-948
    • Søgaard, M.1    Tani, K.2    Ye, R.R.3
  • 68
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • Söllner T., Whiteheat S.W., Brunner M. et al. SNAP receptors implicated in vesicle targeting and fusion. Nature. 362:1993a;318-324.
    • (1993) Nature , vol.362 , pp. 318-324
    • Söllner, T.1    Whiteheat, S.W.2    Brunner, M.3
  • 69
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation and fusion
    • Söllner T., Bennett M.K., Whiteheat S.W., Scheller R.H., Rothman J.E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation and fusion. Cell. 75:1993b;409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheat, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 70
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof T.C. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:1995;645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 71
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton R.B., Fasshauer D., Jahn R., Brunger A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature. 395:1998;347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 72
    • 0028815501 scopus 로고
    • Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects
    • Sweeney S.T., Broadie K., Keane J., Niemann H., O'Kane C.J. Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects. Neuron. 14:1995;341-351.
    • (1995) Neuron , vol.14 , pp. 341-351
    • Sweeney, S.T.1    Broadie, K.2    Keane, J.3    Niemann, H.4    O'Kane, C.J.5
  • 73
    • 0032968998 scopus 로고    scopus 로고
    • Reduced hippocampal LTP in mice lacking a presynaptic protein: Complexin II
    • Takahashi S., Ujihara H., Huang G.-Z. et al. Reduced hippocampal LTP in mice lacking a presynaptic protein: complexin II. Eur. J. Neurosci. 11:1999;2359-2366.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 2359-2366
    • Takahashi, S.1    Ujihara, H.2    Huang, G.-Z.3
  • 74
    • 0023478620 scopus 로고
    • Four additional members of the ras gene superfamily isolated by an oligonucleotide strategy: Molecular cloning of YPT-related cDNAs from a rat brain library
    • Touchot N., Chardin P., Tavitian A. Four additional members of the ras gene superfamily isolated by an oligonucleotide strategy: molecular cloning of YPT-related cDNAs from a rat brain library. Proc. Natl. Acad. Sci. USA. 84:1987;8210-8214.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8210-8214
    • Touchot, N.1    Chardin, P.2    Tavitian, A.3
  • 75
    • 0030877243 scopus 로고    scopus 로고
    • Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion
    • Wang Y., Okamoto M., Schmitz F., Hoffmann K., Südhof T.C. Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion. Nature. 388:1997;593-598.
    • (1997) Nature , vol.388 , pp. 593-598
    • Wang, Y.1    Okamoto, M.2    Schmitz, F.3    Hoffmann, K.4    Südhof, T.C.5
  • 76
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber T., Zemelman B.V., McNew J.A. et al. SNAREpins: minimal machinery for membrane fusion. Cell. 92:1998;759-772.
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    McNew, J.A.3
  • 78
    • 0000040564 scopus 로고    scopus 로고
    • Syntaxin 1A interacts with multiple exocytic proteins to regulate neurotransmitter release in vivo
    • Wu M.N., Fergestad T., Lloyed T.E. et al. Syntaxin 1A interacts with multiple exocytic proteins to regulate neurotransmitter release in vivo. Neuron. 23:1999;593-605.
    • (1999) Neuron , vol.23 , pp. 593-605
    • Wu, M.N.1    Fergestad, T.2    Lloyed, T.E.3
  • 79
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu T., Binz T., Niemann H., Neher E. Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Natu. Neurosci. 1:1998;192-200.
    • (1998) Natu. Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.