메뉴 건너뛰기




Volumn 7, Issue 5, 1997, Pages 624-630

Genetic dissection of synaptic transmission in Drosophila

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; SYNAPTOBREVIN; SYNTAXIN;

EID: 0030729350     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(97)80081-5     Document Type: Article
Times cited : (29)

References (71)
  • 1
    • 0027354448 scopus 로고
    • Storage and release of neurotransmitters
    • Kelly RB: Storage and release of neurotransmitters. Cell/Neuron 1993, 72/10 (suppl):43-53.
    • (1993) Cell/Neuron , vol.72 , Issue.10 SUPPL. , pp. 43-53
    • Kelly, R.B.1
  • 2
    • 0027348039 scopus 로고
    • Synaptic transmission: A bidirectional and self-modifiable form of cell-cell communication
    • Jessell TM, Kandel ER: Synaptic transmission: a bidirectional and self-modifiable form of cell-cell communication. Cell 1993, 72:1-30.
    • (1993) Cell , vol.72 , pp. 1-30
    • Jessell, T.M.1    Kandel, E.R.2
  • 3
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof TC: The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 1995, 375:645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 4
    • 0029118860 scopus 로고
    • Genetic dissection of the molecular mechanisms of transmitter vesicle release during synaptic transmission
    • Broadie KS: Genetic dissection of the molecular mechanisms of transmitter vesicle release during synaptic transmission. J Physiol 1995, 89:59-70.
    • (1995) J Physiol , vol.89 , pp. 59-70
    • Broadie, K.S.1
  • 5
    • 0029420271 scopus 로고
    • Presynaptic proteins involved in exocytosis in Drosophila melanogaster: A genetic analysis
    • Littleton JT, Bellen HJ: Presynaptic proteins involved in exocytosis in Drosophila melanogaster: a genetic analysis. Invertebr Neurosci 1995, 1:3-13.
    • (1995) Invertebr Neurosci , vol.1 , pp. 3-13
    • Littleton, J.T.1    Bellen, H.J.2
  • 7
    • 0029926999 scopus 로고    scopus 로고
    • The Drosophila neuromuscular junction: A model system for studying synaptic development and function
    • Keshishian H, Broadie K, Chiba A, Bate M: The Drosophila neuromuscular junction: a model system for studying synaptic development and function. Annu Rev Neurosci 1996, 19:545-575.
    • (1996) Annu Rev Neurosci , vol.19 , pp. 545-575
    • Keshishian, H.1    Broadie, K.2    Chiba, A.3    Bate, M.4
  • 8
    • 0017089101 scopus 로고
    • Properties of the larval neuromuscular junction in Drosophila melanogaster
    • Jan LY, Jan YN: Properties of the larval neuromuscular junction in Drosophila melanogaster. J Physiol 1976, 262:189-214.
    • (1976) J Physiol , vol.262 , pp. 189-214
    • Jan, L.Y.1    Jan, Y.N.2
  • 9
    • 0027508913 scopus 로고
    • Development of embryonic neuromuscular synapse of Drosophila melanogaster
    • Broadie K, Bate M: Development of embryonic neuromuscular synapse of Drosophila melanogaster. J Neurosci 1993, 13:144-166.
    • (1993) J Neurosci , vol.13 , pp. 144-166
    • Broadie, K.1    Bate, M.2
  • 10
    • 0028221934 scopus 로고
    • Miniature endplate currents at the newly formed neuromuscular junction in Drosophila embryos and larvae
    • Kidokoro Y, Nishikawa K: Miniature endplate currents at the newly formed neuromuscular junction in Drosophila embryos and larvae. Neurosci Res 1994, 19:143-154.
    • (1994) Neurosci Res , vol.19 , pp. 143-154
    • Kidokoro, Y.1    Nishikawa, K.2
  • 12
    • 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 JE, Söllner TH: 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 1997, 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
  • 14
    • 0028862292 scopus 로고
    • Docked granules, the exocytic burst, and the need for ATP hydrolysis in endocrine cells
    • Parsons TD, Coorssen JR, Horstmann H, Almers W: Docked granules, the exocytic burst, and the need for ATP hydrolysis in endocrine cells. Neuron 1995, 15:1085-1096.
    • (1995) Neuron , vol.15 , pp. 1085-1096
    • Parsons, T.D.1    Coorssen, J.R.2    Horstmann, H.3    Almers, W.4
  • 16
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer A, Wickner W, Haas A: Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles. Cell 1996, 85:83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 18
    • 0028817584 scopus 로고
    • Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission
    • Schulze K, Broadie K, Perin M, Bellen HJ: Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission. Cell 1995, 80:311-320.
    • (1995) Cell , vol.80 , pp. 311-320
    • Schulze, K.1    Broadie, K.2    Perin, M.3    Bellen, H.J.4
  • 19
    • 0028815501 scopus 로고
    • Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioural defects
    • Sweeney ST, Broadie K, Keane J, Niemann, O'Kane CJ: Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioural defects. Neuron 1995, 14:341-351.
    • (1995) Neuron , vol.14 , pp. 341-351
    • Sweeney, S.T.1    Broadie, K.2    Keane, J.3    Niemann O'Kane, C.J.4
  • 23
    • 0028233978 scopus 로고
    • Neurally expressed Drosophila genes encoding homologs of the NSF and SNAP secretory proteins
    • Ordway RW, Pallanck L, Ganetzky B: Neurally expressed Drosophila genes encoding homologs of the NSF and SNAP secretory proteins. Proc Natl Acad Sci USA 1994, 91:5715-5719.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5715-5719
    • Ordway, R.W.1    Pallanck, L.2    Ganetzky, B.3
  • 24
    • 0029163609 scopus 로고
    • Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) suggested by the identification of a second Drosophila NSF homolog
    • Pallanck L, Ordway RW, Ramaswami M, Chi WY, Krishnan KS, Ganetzky B: Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) suggested by the identification of a second Drosophila NSF homolog. J Biol Chem 1995, 270:18742-18744.
    • (1995) J Biol Chem , vol.270 , pp. 18742-18744
    • Pallanck, L.1    Ordway, R.W.2    Ramaswami, M.3    Chi, W.Y.4    Krishnan, K.S.5    Ganetzky, B.6
  • 27
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE: Mechanisms of intracellular protein transport Nature 1994, 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 28
    • 0004688543 scopus 로고
    • Neurophysiological defects in temperature-sensitive paralytic mutants of Drosophila melanogaster
    • Siddiqi O, Benzer S: Neurophysiological defects in temperature-sensitive paralytic mutants of Drosophila melanogaster. Proc Natl Acad Sci USA 1976, 73:3253-3257.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 3253-3257
    • Siddiqi, O.1    Benzer, S.2
  • 29
    • 16044369508 scopus 로고    scopus 로고
    • Classic clues to NSF function
    • Morgan A: Classic clues to NSF function. Nature 1996, 382:680.
    • (1996) Nature , vol.382 , pp. 680
    • Morgan, A.1
  • 30
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett MK, Calakos N, Scheller RH: Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 1992, 257:255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 31
    • 0030455864 scopus 로고    scopus 로고
    • Drosophila syntaxin is required for cell viability and may function in membrane formation and stabilization
    • Schulze KL, Bellen HJ: Drosophila syntaxin is required for cell viability and may function in membrane formation and stabilization. Genetics 1996, 144:1713-1724.
    • (1996) Genetics , vol.144 , pp. 1713-1724
    • Schulze, K.L.1    Bellen, H.J.2
  • 32
    • 0028945592 scopus 로고
    • rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin
    • Garcia EP, McPherson PS, Chilcote TJ, Takei K, De Camilli P: rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin. J Cell Biol 1995, 129:105-120.
    • (1995) J Cell Biol , vol.129 , pp. 105-120
    • Garcia, E.P.1    McPherson, P.S.2    Chilcote, T.J.3    Takei, K.4    De Camilli, P.5
  • 33
    • 0029025405 scopus 로고
    • Cellular and subcellular localization of syntaxin-like immunoreactivity in the rat striatum and cortex
    • Sesack SR, Snyder CL: Cellular and subcellular localization of syntaxin-like immunoreactivity in the rat striatum and cortex. Neuroscience 1995, 67:993-1007.
    • (1995) Neuroscience , vol.67 , pp. 993-1007
    • Sesack, S.R.1    Snyder, C.L.2
  • 34
    • 0028878175 scopus 로고
    • Estimates for the pool size of releasable quanta at a single central synapse and for the time required to refill the pool
    • Stevens CF, Tsujimoto T: Estimates for the pool size of releasable quanta at a single central synapse and for the time required to refill the pool. Proc Natl Acad Sci USA 1995, 92:846-849.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 846-849
    • Stevens, C.F.1    Tsujimoto, T.2
  • 35
    • 0030175394 scopus 로고    scopus 로고
    • Definition of the readily releasable pool of vesicles at hippocampal synapses
    • Rosemund C, Stevens CF: Definition of the readily releasable pool of vesicles at hippocampal synapses. Neuron 1996, 16:1197-1207.
    • (1996) Neuron , vol.16 , pp. 1197-1207
    • Rosemund, C.1    Stevens, C.F.2
  • 36
    • 0024659539 scopus 로고
    • A synaptic vesicle membrane protein is conserved from mammals to Drosophila
    • Südhof TC, Baumert M, Perin MS, Jahn R: A synaptic vesicle membrane protein is conserved from mammals to Drosophila. Neuron 1989, 2:1475-1481.
    • (1989) Neuron , vol.2 , pp. 1475-1481
    • Südhof, T.C.1    Baumert, M.2    Perin, M.S.3    Jahn, R.4
  • 37
    • 0027363855 scopus 로고
    • Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding a VAMP (synaptobrevin) that is abundant in non-neuronal cells
    • Chin AC, Burgess RW, Wong BR, Schwarz TL, Scheller RH: Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding a VAMP (synaptobrevin) that is abundant in non-neuronal cells. Gene 1993, 131:175-181.
    • (1993) Gene , vol.131 , pp. 175-181
    • Chin, A.C.1    Burgess, R.W.2    Wong, B.R.3    Schwarz, T.L.4    Scheller, R.H.5
  • 39
    • 0015123666 scopus 로고
    • The effect of type D botulinum toxin on frog neuromuscular junctions
    • Harris AJ, Miledi R: The effect of type D botulinum toxin on frog neuromuscular junctions. J Physiol 1971, 217:497-515.
    • (1971) J Physiol , vol.217 , pp. 497-515
    • Harris, A.J.1    Miledi, R.2
  • 40
    • 0020515818 scopus 로고
    • Different effects of types A and B botulinum toxin on transmitter release at the rat neuromuscular junction
    • Sellin LC, Thesleff S, Dasgupta BR: Different effects of types A and B botulinum toxin on transmitter release at the rat neuromuscular junction. Acta Physiol Scand 1983, 119:127-133.
    • (1983) Acta Physiol Scand , vol.119 , pp. 127-133
    • Sellin, L.C.1    Thesleff, S.2    Dasgupta, B.R.3
  • 42
    • 0024535487 scopus 로고
    • A study of synchronization of quantal transmitter release from mammalian motor endings by the use of botulinal toxins type A and D
    • Molgo J, Siegel LS, Tabti N, Thesleff S: A study of synchronization of quantal transmitter release from mammalian motor endings by the use of botulinal toxins type A and D. J Physiol 1989, 411:195-205.
    • (1989) J Physiol , vol.411 , pp. 195-205
    • Molgo, J.1    Siegel, L.S.2    Tabti, N.3    Thesleff, S.4
  • 43
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • Protopopov V, Govindan B, Novick P, Gerst JE: Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell 1993, 74:855-861.
    • (1993) Cell , vol.74 , pp. 855-861
    • Protopopov, V.1    Govindan, B.2    Novick, P.3    Gerst, J.E.4
  • 44
    • 0027527762 scopus 로고
    • Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport
    • Aalto MK, Ronne H, Keranen S: Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport EMBO J 1993, 12:4095-4104.
    • (1993) EMBO J , vol.12 , pp. 4095-4104
    • Aalto, M.K.1    Ronne, H.2    Keranen, S.3
  • 45
    • 0029985418 scopus 로고    scopus 로고
    • Molecular mechanisms in synaptic vesicle endocytosis and recycling
    • De Camilli P, Takei K: Molecular mechanisms in synaptic vesicle endocytosis and recycling. Neuron 1996, 16:481-486.
    • (1996) Neuron , vol.16 , pp. 481-486
    • De Camilli, P.1    Takei, K.2
  • 46
    • 0029925681 scopus 로고    scopus 로고
    • Neurotransmitter release
    • Matthews G: Neurotransmitter release. Annu Rev Neurosci 1996, 19:219-233.
    • (1996) Annu Rev Neurosci , vol.19 , pp. 219-233
    • Matthews, G.1
  • 47
    • 0015619310 scopus 로고
    • Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction
    • Heuser JE, Reese TS: Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction. J Cell Biol 1973, 57:315-344.
    • (1973) J Cell Biol , vol.57 , pp. 315-344
    • Heuser, J.E.1    Reese, T.S.2
  • 48
    • 0021962833 scopus 로고
    • The subpopulation of brain coated vesicles that carries synaptic vesicle proteins contains two unique polypeptides
    • Pfeffer SR, Kelly RB: The subpopulation of brain coated vesicles that carries synaptic vesicle proteins contains two unique polypeptides. Cell 1985, 40:949-957.
    • (1985) Cell , vol.40 , pp. 949-957
    • Pfeffer, S.R.1    Kelly, R.B.2
  • 49
    • 0026727853 scopus 로고
    • Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling
    • Maycox PR, Link E, Reetz A, Morris SA, Jahn R: Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling. J Cell Biol 1992, 118:1379-1388.
    • (1992) J Cell Biol , vol.118 , pp. 1379-1388
    • Maycox, P.R.1    Link, E.2    Reetz, A.3    Morris, S.A.4    Jahn, R.5
  • 50
    • 0027448777 scopus 로고
    • Clathrin: Its role in receptor-mediated vesicular transport and specialized functions in neurons
    • Pley U, Parham P: Clathrin: its role in receptor-mediated vesicular transport and specialized functions in neurons. Crit Rev Biochem Mol Biol 1993, 28:431-464.
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 431-464
    • Pley, U.1    Parham, P.2
  • 51
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis
    • Robinson MS: The role of clathrin, adaptors and dynamin in endocytosis. Curr Opin Cell Biol 1994, 6:538-544.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 53
    • 0028082406 scopus 로고
    • Dynamics of synaptic vesicle fusion and membrane retrieval in synaptic terminals
    • Von Gersdorff H, Matthews G: Dynamics of synaptic vesicle fusion and membrane retrieval in synaptic terminals. Nature 1994, 367:735-739.
    • (1994) Nature , vol.367 , pp. 735-739
    • Von Gersdorff, H.1    Matthews, G.2
  • 54
    • 0029610859 scopus 로고    scopus 로고
    • Staurosporine blocks evoked release of FM1-43 but not acetylcholine from frog motor nerve terminals
    • Henkel AW, Betz WJ: Staurosporine blocks evoked release of FM1-43 but not acetylcholine from frog motor nerve terminals. J Neurosci 1996, 15:8246-8258.
    • (1996) J Neurosci , vol.15 , pp. 8246-8258
    • Henkel, A.W.1    Betz, W.J.2
  • 56
    • 0343632367 scopus 로고    scopus 로고
    • Role of Drosophila α-adaptin in presynaptic vesicle recycling
    • González-Gaitán M, Jäckle H: Role of Drosophila α-adaptin in presynaptic vesicle recycling. Cell 1997, 88:767-776.
    • (1997) Cell , vol.88 , pp. 767-776
    • González-Gaitán, M.1    Jäckle, H.2
  • 57
    • 0029825051 scopus 로고    scopus 로고
    • Traffic of dynamin within individual Drosophila synaptic boutons relative to compartment-specific markers
    • Estes PS, Roos J, van der Bliek A, Kelly RB, Krishnan KS, Ramaswami M: Traffic of dynamin within individual Drosophila synaptic boutons relative to compartment-specific markers. J Neurosci 1996, 16:5443-5456.
    • (1996) J Neurosci , vol.16 , pp. 5443-5456
    • Estes, P.S.1    Roos, J.2    Van Der Bliek, A.3    Kelly, R.B.4    Krishnan, K.S.5    Ramaswami, M.6
  • 58
    • 0029807825 scopus 로고    scopus 로고
    • Synaptic vesicles have two distinct recycling pathways
    • Koenig JH, Ikeda K: Synaptic vesicles have two distinct recycling pathways. J Cell Biol 1996, 135:797-808.
    • (1996) J Cell Biol , vol.135 , pp. 797-808
    • Koenig, J.H.1    Ikeda, K.2
  • 59
    • 0028986797 scopus 로고
    • The appendage domain of α-adaptin is a high affinity binding site for dynamin
    • Wang L-H, Sudhof TC, Anderson RGW: The appendage domain of α-adaptin is a high affinity binding site for dynamin. J Biol Chem 1995, 270:10079-10083.
    • (1995) J Biol Chem , vol.270 , pp. 10079-10083
    • Wang, L.-H.1    Sudhof, T.C.2    Anderson, R.G.W.3
  • 60
    • 0024368508 scopus 로고
    • Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval
    • Koenig JH, Ikeda K: Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval. J Neurosci 1989, 9:3844-3860.
    • (1989) J Neurosci , vol.9 , pp. 3844-3860
    • Koenig, J.H.1    Ikeda, K.2
  • 61
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
    • Takei K, McPherson PS, Schmid SL, De Camilli P: Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals. Nature 1995, 374:186-189.
    • (1995) Nature , vol.374 , pp. 186-189
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 62
    • 0026536634 scopus 로고
    • Activity-dependent fluorescent staining and destaining of living vertebrate motor nerve terminals
    • Betz WJ, Mao F, Bewick GS: Activity-dependent fluorescent staining and destaining of living vertebrate motor nerve terminals. J Neurosci 1992, 12:363-375.
    • (1992) J Neurosci , vol.12 , pp. 363-375
    • Betz, W.J.1    Mao, F.2    Bewick, G.S.3
  • 63
    • 0019424604 scopus 로고
    • Structural changes after transmitter release at the frog neuromuscular junction
    • Heuser JE, Reese TS: Structural changes after transmitter release at the frog neuromuscular junction. J Cell Biol 1981, 88:564-580.
    • (1981) J Cell Biol , vol.88 , pp. 564-580
    • Heuser, J.E.1    Reese, T.S.2
  • 65
    • 0027180569 scopus 로고
    • Synaptic transmission persists in synaptotagmin mutants of Drosophila
    • DiAntonio A, Parfitt KD, Schwartz TL: Synaptic transmission persists in synaptotagmin mutants of Drosophila. Cell 1993, 73:1281-1290.
    • (1993) Cell , vol.73 , pp. 1281-1290
    • DiAntonio, A.1    Parfitt, K.D.2    Schwartz, T.L.3
  • 67
    • 0028081451 scopus 로고
    • The absence of synaptotagmin disrupts excitation-secretion coupling during synaptic transmission
    • Broadie K, Bellen HJ, DiAntonio A, Littleton JT, Schwarz TL: The absence of synaptotagmin disrupts excitation-secretion coupling during synaptic transmission. Proc Natl Acad Sci USA 1994, 91:10727-10731.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10727-10731
    • Broadie, K.1    Bellen, H.J.2    DiAntonio, A.3    Littleton, J.T.4    Schwarz, T.L.5
  • 68
    • 0027938531 scopus 로고
    • Mutations in the Drosophila rop gene suggest a function in general secretion and synaptic transmission
    • Harrison SD, Broadie K, van de Goor J, Rubin GM: Mutations in the Drosophila rop gene suggest a function in general secretion and synaptic transmission. Neuron 1994, 13:555-566.
    • (1994) Neuron , vol.13 , pp. 555-566
    • Harrison, S.D.1    Broadie, K.2    Van De Goor, J.3    Rubin, G.M.4
  • 69
    • 0028102686 scopus 로고
    • rop, a Drosophila homolog of the vertebrate n-Sec1/Munc-18 and yeast Sec1 proteins, is a negative regulator of neurotransmitter release in vivo
    • Schulze KL, Littleton JT, Salzberg A, Halachmi N, Stern M, Lev Z, Bellen HJ: rop, a Drosophila homolog of the vertebrate n-Sec1/Munc-18 and yeast Sec1 proteins, is a negative regulator of neurotransmitter release in vivo. Neuron 1994, 13:1099-1108.
    • (1994) Neuron , vol.13 , pp. 1099-1108
    • Schulze, K.L.1    Littleton, J.T.2    Salzberg, A.3    Halachmi, N.4    Stern, M.5    Lev, Z.6    Bellen, H.J.7
  • 70
    • 0028281387 scopus 로고
    • Paralysis and early death in cysteine string protein mutants of Drosophila
    • Zinsmaier KE, Eberle KK, Buchner E, Walter N, Benzer S: Paralysis and early death in cysteine string protein mutants of Drosophila. Science 1994, 263:977-980.
    • (1994) Science , vol.263 , pp. 977-980
    • Zinsmaier, K.E.1    Eberle, K.K.2    Buchner, E.3    Walter, N.4    Benzer, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.