메뉴 건너뛰기




Volumn 105, Issue 1, 2005, Pages 69-84

Modulation of neurotransmitter release by the second messenger-activated protein kinases: Implications for presynaptic plasticity

Author keywords

CaMKII (Ca 2+ calmodulin dependent kinase II); Exocytosis; PKA (cAMP dependent protein kinase A); PKC (protein kinase C); Presynaptic proteins; Synaptic plasticity

Indexed keywords

CALCINEURIN; CALCIUM; CYSTEINE; MITOGEN ACTIVATED PROTEIN KINASE; MUNC18 PROTEIN; NEUROTRANSMITTER; PROTEIN; PROTEIN KINASE C; PROTEIN RAB3; PROTEIN SNAP 25; SNAPIN; SYNAPSIN I; UNCLASSIFIED DRUG;

EID: 11144256944     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2004.10.012     Document Type: Review
Times cited : (145)

References (189)
  • 2
    • 0035900399 scopus 로고    scopus 로고
    • Rapid increase in clusters of presynaptic proteins at onset of long-lasting potentiation
    • I. Antonova, O. Arancio, A.C. Trillat, H.G. Wang, L. Zablow, and H. Udo Rapid increase in clusters of presynaptic proteins at onset of long-lasting potentiation Science 294 2001 1547 1550
    • (2001) Science , vol.294 , pp. 1547-1550
    • Antonova, I.1    Arancio, O.2    Trillat, A.C.3    Wang, H.G.4    Zablow, L.5    Udo, H.6
  • 3
    • 0034679721 scopus 로고    scopus 로고
    • Munc13-1 acts as a priming factor for large dense-core vesicles in bovine chromaffin cells
    • U. Ashery, F. Varoqueaux, T. Voets, A. Betz, P. Thakur, and H. Koch Munc13-1 acts as a priming factor for large dense-core vesicles in bovine chromaffin cells EMBO J 19 2000 3586 3596
    • (2000) EMBO J , vol.19 , pp. 3586-3596
    • Ashery, U.1    Varoqueaux, F.2    Voets, T.3    Betz, A.4    Thakur, P.5    Koch, H.6
  • 4
    • 0033084096 scopus 로고    scopus 로고
    • Differential expression of two novel Munc13 proteins in rat brain
    • I. Augustin, A. Betz, C. Herrmann, T. Jo, and N. Brose Differential expression of two novel Munc13 proteins in rat brain Biochem J 337 1999 363 371
    • (1999) Biochem J , vol.337 , pp. 363-371
    • Augustin, I.1    Betz, A.2    Herrmann, C.3    Jo, T.4    Brose, N.5
  • 5
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • I. Augustin, C. Rosenmund, T.C. Südhof, and N. Brose Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles Nature 400 1999 457 461
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Südhof, T.C.3    Brose, N.4
  • 6
    • 0028950269 scopus 로고
    • The biochemistry of neurotransmitter secretion
    • S.M. Bajjalieh, and R.H. Scheller The biochemistry of neurotransmitter secretion J Biol Chem 270 1995 1971 1974
    • (1995) J Biol Chem , vol.270 , pp. 1971-1974
    • Bajjalieh, S.M.1    Scheller, R.H.2
  • 7
    • 0038532319 scopus 로고    scopus 로고
    • Phosphorylation of Munc18 by protein kinase C regulates the kinetics of exocytosis
    • J.W. Barclay, T.J. Craig, R.J. Fisher, L.F. Ciufo, G.J. Evans, and A. Morgan Phosphorylation of Munc18 by protein kinase C regulates the kinetics of exocytosis J Biol Chem 278 2003 10538 10545
    • (2003) J Biol Chem , vol.278 , pp. 10538-10545
    • Barclay, J.W.1    Craig, T.J.2    Fisher, R.J.3    Ciufo, L.F.4    Evans, G.J.5    Morgan, A.6
  • 8
    • 0024506756 scopus 로고
    • Interactions of synapsin I with small synaptic vesicles: Distinct sites in synapsin I bind to vesicle phospholipids and vesicle proteins
    • F. Benfenati, M. Bahler, R. Jahn, and P. Greengard Interactions of synapsin I with small synaptic vesicles: distinct sites in synapsin I bind to vesicle phospholipids and vesicle proteins J Cell Biol 108 1989 1863 1872
    • (1989) J Cell Biol , vol.108 , pp. 1863-1872
    • Benfenati, F.1    Bahler, M.2    Jahn, R.3    Greengard, P.4
  • 11
    • 0032565873 scopus 로고    scopus 로고
    • Modulation of AMPA receptor unitary conductance by synaptic activity
    • T.A. Benke, A. Luthi, J.T. Isaac, and G.L. Collingridge Modulation of AMPA receptor unitary conductance by synaptic activity Nature 393 1998 793 797
    • (1998) Nature , vol.393 , pp. 793-797
    • Benke, T.A.1    Luthi, A.2    Isaac, J.T.3    Collingridge, G.L.4
  • 12
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • M.K. Bennet, and R.H. Scheller The molecular machinery for secretion is conserved from yeast to neurons Proc Natl Acad Sci U S A 90 1993 2559 2563
    • (1993) Proc Natl Acad Sci U S a , vol.90 , pp. 2559-2563
    • Bennet, M.K.1    Scheller, R.H.2
  • 13
    • 0015460664 scopus 로고
    • The kinetics of transmitter release at the frog neuromuscular junction
    • E.F. Berrett, and C.F. Stevens The kinetics of transmitter release at the frog neuromuscular junction J Physiol (Lond) 227 1972 691 708
    • (1972) J Physiol (Lond) , vol.227 , pp. 691-708
    • Berrett, E.F.1    Stevens, C.F.2
  • 14
    • 0031027591 scopus 로고    scopus 로고
    • Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin
    • A. Betz, M. Okamoto, F. Benseler, and N. Brose Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus 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
  • 15
    • 18544399674 scopus 로고    scopus 로고
    • Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release
    • A. Betz, U. Ashery, M. Rickmann, I. Augustin, E. Neher, and T.C. Sudhof 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    Ashery, U.2    Rickmann, M.3    Augustin, I.4    Neher, E.5    Sudhof, T.C.6
  • 16
    • 0035030935 scopus 로고    scopus 로고
    • Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming
    • A. Betz, P. Thakur, H.J. Junge, U. Ashery, J.S. Rhee, and V. Scheuss Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming Neuron 30 2001 183 196
    • (2001) Neuron , vol.30 , pp. 183-196
    • Betz, A.1    Thakur, P.2    Junge, H.J.3    Ashery, U.4    Rhee, J.S.5    Scheuss, V.6
  • 17
    • 0033991008 scopus 로고    scopus 로고
    • Casein kinase 2 as a potentially important enzyme in the nervous system
    • P.R. Blanquet Casein kinase 2 as a potentially important enzyme in the nervous system Prog Neurobiol 60 2000 211 246
    • (2000) Prog Neurobiol , vol.60 , pp. 211-246
    • Blanquet, P.R.1
  • 18
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • T.V.P. Bliss, and G.L. Collingridge A synaptic model of memory: long-term potentiation in the hippocampus Nature 361 1993 31 39
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.P.1    Collingridge, G.L.2
  • 19
    • 2442540341 scopus 로고    scopus 로고
    • Phosphorylation of syntaphilin by cAMP-dependent protein kinase modulates its interaction with syntaxin-1 and annuls its inhibitory effect on vesicle exocytosis
    • J. Boczan, A.G.M. Leenders, and Z.-H. Sheng Phosphorylation of syntaphilin by cAMP-dependent protein kinase modulates its interaction with syntaxin-1 and annuls its inhibitory effect on vesicle exocytosis J Biol Chem 279 2004 18911 18919
    • (2004) J Biol Chem , vol.279 , pp. 18911-18919
    • Boczan, J.1    Leenders, A.G.M.2    Sheng, Z.-H.3
  • 20
    • 0029133704 scopus 로고
    • Regulation of hippocampal transmitter release during development and long-term potentiation
    • V.Y. Bolshakov, and S.A. Siegelbaum Regulation of hippocampal transmitter release during development and long-term potentiation Science 269 1995 1730 1734
    • (1995) Science , vol.269 , pp. 1730-1734
    • Bolshakov, V.Y.1    Siegelbaum, S.A.2
  • 21
    • 0033460183 scopus 로고    scopus 로고
    • Adenosine suppresses protein kinase A- and C-induced enhancement of glutamate release in the hippocampus
    • A. Bouron Adenosine suppresses protein kinase A- and C-induced enhancement of glutamate release in the hippocampus Eur J Neurosci 11 1999 4446 4450
    • (1999) Eur J Neurosci , vol.11 , pp. 4446-4450
    • Bouron, A.1
  • 22
    • 0033636556 scopus 로고    scopus 로고
    • Increasing numbers of synaptic puncta during late-phase LTP: N-cadherin is synthesized, recruited to synaptic sites, and required for potentiation
    • O. Bozdagi, W. Shan, H. Tanaka, D.L. Benson, and G.W. Huntley Increasing numbers of synaptic puncta during late-phase LTP: N-cadherin is synthesized, recruited to synaptic sites, and required for potentiation Neuron 28 2000 245 259
    • (2000) Neuron , vol.28 , pp. 245-259
    • Bozdagi, O.1    Shan, W.2    Tanaka, H.3    Benson, D.L.4    Huntley, G.W.5
  • 23
    • 0028917370 scopus 로고
    • The multifunctional calcium/calmodulin-dependent protein kinase: From form to function
    • A.P. Braun, and H. Schulman The multifunctional calcium/calmodulin- dependent protein kinase: from form to function Annu Rev Physiol 57 1995 417 445
    • (1995) Annu Rev Physiol , vol.57 , pp. 417-445
    • Braun, A.P.1    Schulman, H.2
  • 24
    • 0141918783 scopus 로고    scopus 로고
    • AMPA receptor trafficking at excitatory synapses
    • D.S. Bredt, and R.A. Nicoll AMPA receptor trafficking at excitatory synapses Neuron 40 2003 361 379
    • (2003) Neuron , vol.40 , pp. 361-379
    • Bredt, D.S.1    Nicoll, R.A.2
  • 25
    • 0036905264 scopus 로고    scopus 로고
    • Move over protein kinase C, you've got company: Alternative cellular effectors of diacylglycerol and phorbol esters
    • N. Brose, and C. Rosenmund Move over protein kinase C, you've got company: alternative cellular effectors of diacylglycerol and phorbol esters J Cell Sci 115 2002 4399 4411
    • (2002) J Cell Sci , vol.115 , pp. 4399-4411
    • Brose, N.1    Rosenmund, C.2
  • 26
    • 0028791349 scopus 로고
    • Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins
    • N. Brose, K. Hofmann, Y. Hata, and T.C. Sudhof 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    Sudhof, T.C.4
  • 27
    • 0034082054 scopus 로고    scopus 로고
    • Regulation of transmitter release by Unc-13 and its homologues
    • N. Brose, C. Rosenmund, and J. Rettig Regulation of transmitter release by Unc-13 and its homologues Curr Opin Neurobiol 10 2000 303 311
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 303-311
    • Brose, N.1    Rosenmund, C.2    Rettig, J.3
  • 28
    • 0036542593 scopus 로고    scopus 로고
    • Splitting the quantum: Regulation of quantal release during vesicle fusion
    • R.D. Burgoyne, and J.W. Barclay Splitting the quantum: regulation of quantal release during vesicle fusion Trends Neurosci 25 2002 176 178
    • (2002) Trends Neurosci , vol.25 , pp. 176-178
    • Burgoyne, R.D.1    Barclay, J.W.2
  • 29
    • 0142138839 scopus 로고    scopus 로고
    • Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells
    • P. Buxton, X.M. Zhang, B. Walsh, A. Sriratana, I. Schenberg, and E. Manickam Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells Biochem J 375 Pt 2 2003 433 440
    • (2003) Biochem J , vol.375 , Issue.2 , pp. 433-440
    • Buxton, P.1    Zhang, X.M.2    Walsh, B.3    Sriratana, A.4    Schenberg, I.5    Manickam, E.6
  • 30
    • 0032545285 scopus 로고    scopus 로고
    • Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study
    • J.M. Cànaves, and M. Montal Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study J Biol Chem 273 1998 34214 34221
    • (1998) J Biol Chem , vol.273 , pp. 34214-34221
    • Cànaves, J.M.1    Montal, M.2
  • 31
    • 0028924892 scopus 로고
    • Presynaptic enhancement of inhibitory synaptic transmission by protein kinases a and C in the rat hippocampus in vitro
    • M. Capogna, B.H. Gähwiler, and S.M. Thompson Presynaptic enhancement of inhibitory synaptic transmission by protein kinases A and C in the rat hippocampus in vitro J Neurosci 15 1995 1249 1260
    • (1995) J Neurosci , vol.15 , pp. 1249-1260
    • Capogna, M.1    Gähwiler, B.H.2    Thompson, S.M.3
  • 34
    • 0036304982 scopus 로고    scopus 로고
    • 2+ sensor that triggers exocytosis?
    • 2+ sensor that triggers exocytosis? Nat Rev Mol Cell Biol 3 2002 498 508
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 498-508
    • Chapman, E.R.1
  • 36
    • 0028054814 scopus 로고
    • Increased transmitter release at excitatory synapses produced by direct activation of adenylate cyclase in rat hippocampal slices
    • L.E. Chavez-Noriega, and C.F. Stevens Increased transmitter release at excitatory synapses produced by direct activation of adenylate cyclase in rat hippocampal slices J Neurosci 14 1994 310 317
    • (1994) J Neurosci , vol.14 , pp. 310-317
    • Chavez-Noriega, L.E.1    Stevens, C.F.2
  • 38
    • 0035071322 scopus 로고    scopus 로고
    • Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex
    • M.G. Chheda, U. Ashery, P. Thakur, J. Rettig, and Z.-H. Sheng Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex Nat Cell Biol 3 2001 331 338
    • (2001) Nat Cell Biol , vol.3 , pp. 331-338
    • Chheda, M.G.1    Ashery, U.2    Thakur, P.3    Rettig, J.4    Sheng, Z.-H.5
  • 39
    • 0035195395 scopus 로고    scopus 로고
    • Synapsin dispersion and reclustering during synaptic activity
    • P. Chi, P. Greengard, and T.A. Ryan Synapsin dispersion and reclustering during synaptic activity Nat Neurosci 4 2001 1187 1193
    • (2001) Nat Neurosci , vol.4 , pp. 1187-1193
    • Chi, P.1    Greengard, P.2    Ryan, T.A.3
  • 40
    • 0345701204 scopus 로고    scopus 로고
    • Synaptic vesicle mobilization is regulated by distinct synapsin I phosphorylation pathways at different frequencies
    • P. Chi, P. Greengard, and T.A. Ryan Synaptic vesicle mobilization is regulated by distinct synapsin I phosphorylation pathways at different frequencies Neuron 38 2003 69 78
    • (2003) Neuron , vol.38 , pp. 69-78
    • Chi, P.1    Greengard, P.2    Ryan, T.A.3
  • 41
    • 0034068876 scopus 로고    scopus 로고
    • Postfusional regulation of cleft glutamate concentration during LTP at 'silent synapses'
    • S. Choi, J. Klingauf, and R.W. Tsien Postfusional regulation of cleft glutamate concentration during LTP at 'silent synapses' Nat Neurosci 3 2000 330 336
    • (2000) Nat Neurosci , vol.3 , pp. 330-336
    • Choi, S.1    Klingauf, J.2    Tsien, R.W.3
  • 42
    • 8544278211 scopus 로고    scopus 로고
    • Regulation of type VI adenylyl cyclase by Snapin, a SNAP25-binding protein
    • J.L. Chou, C.L. Huang, H.L. Lai, A.C. Hung, C.L. Chien, and Y.Y. Kao Regulation of type VI adenylyl cyclase by Snapin, a SNAP25-binding protein J Biol Chem 279 2004 46271 46279
    • (2004) J Biol Chem , vol.279 , pp. 46271-46279
    • Chou, J.L.1    Huang, C.L.2    Lai, H.L.3    Hung, A.C.4    Chien, C.L.5    Kao, Y.Y.6
  • 43
    • 0141543849 scopus 로고    scopus 로고
    • Physiological regulation of Munc18/nSec1 phosphorylation on serine-313
    • T.J. Craig, G.J. Evans, and A. Morgan Physiological regulation of Munc18/nSec1 phosphorylation on serine-313 J Neurochem 86 2003 1450 1457
    • (2003) J Neurochem , vol.86 , pp. 1450-1457
    • Craig, T.J.1    Evans, G.J.2    Morgan, A.3
  • 44
    • 0034663177 scopus 로고    scopus 로고
    • Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis in Drosophila
    • K. Dawson-Scully, P. Bronk, H.L. Atwood, and K.E. Zinsmaier Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis in Drosophila J Neurosci 20 2000 6039 6047
    • (2000) J Neurosci , vol.20 , pp. 6039-6047
    • Dawson-Scully, K.1    Bronk, P.2    Atwood, H.L.3    Zinsmaier, K.E.4
  • 47
    • 0024840154 scopus 로고
    • Adenylate cyclase system is essential for long-term facilitation at the crayfish neuromuscular junction
    • D. Dixon, and H.L. Atwood Adenylate cyclase system is essential for long-term facilitation at the crayfish neuromuscular junction J Neurosci 9 1989 4245 4252
    • (1989) J Neurosci , vol.9 , pp. 4245-4252
    • Dixon, D.1    Atwood, H.L.2
  • 48
    • 0033575749 scopus 로고    scopus 로고
    • A conformational switch in syntaxin during exocytosis: Role of Munc18
    • I. Dulubova, S. Sugita, S. Hill, M. Hosaka, I. Fernandez, and T.C. Südhof A conformational switch in syntaxin during exocytosis: role of Munc18 EMBO J 18 1999 4372 4382
    • (1999) EMBO J , vol.18 , pp. 4372-4382
    • Dulubova, I.1    Sugita, S.2    Hill, S.3    Hosaka, M.4    Fernandez, I.5    Südhof, T.C.6
  • 49
    • 0033529082 scopus 로고    scopus 로고
    • Dendritic spine changes associated with hippocampal long-term synaptic plasticity
    • F. Engert, and T. Bonhoeffer Dendritic spine changes associated with hippocampal long-term synaptic plasticity Nature 399 1999 66 70
    • (1999) Nature , vol.399 , pp. 66-70
    • Engert, F.1    Bonhoeffer, T.2
  • 50
    • 0036606587 scopus 로고    scopus 로고
    • Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I
    • G.J.O. Evans, and A. Morgan Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I Biochem J 364 2002 343 347
    • (2002) Biochem J , vol.364 , pp. 343-347
    • Evans, G.J.O.1    Morgan, A.2
  • 51
    • 0035930540 scopus 로고    scopus 로고
    • Phosphorylation of cysteine string protein by protein kinase A. Implications for the modulation of exocytosis
    • G.J.O. Evans, M.C. Wilkinson, M.E. Graham, K.M. Turner, L.H. Chamberlain, and R.D. Burgoyne Phosphorylation of cysteine string protein by protein kinase A. Implications for the modulation of exocytosis J Biol Chem 276 2001 47877 47885
    • (2001) J Biol Chem , vol.276 , pp. 47877-47885
    • Evans, G.J.O.1    Wilkinson, M.C.2    Graham, M.E.3    Turner, K.M.4    Chamberlain, L.H.5    Burgoyne, R.D.6
  • 52
    • 0141828992 scopus 로고    scopus 로고
    • Tying everything together: The multiple roles of cysteine string protein (CSP) in regulated exocytosis
    • G.J.O. Evans, A. Morgan, and R.D. Burgoyne Tying everything together: the multiple roles of cysteine string protein (CSP) in regulated exocytosis Traffic 4 2003 653 659
    • (2003) Traffic , vol.4 , pp. 653-659
    • Evans, G.J.O.1    Morgan, A.2    Burgoyne, R.D.3
  • 54
    • 0036237621 scopus 로고    scopus 로고
    • The synapsins: Beyond the regulation of neurotransmitter release
    • A. Ferreira, and M. Rapoport The synapsins: beyond the regulation of neurotransmitter release Cell Mol Life Sci 59 2002 589 595
    • (2002) Cell Mol Life Sci , vol.59 , pp. 589-595
    • Ferreira, A.1    Rapoport, M.2
  • 55
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • S. Ferro-Novick, and R. Jahn 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
  • 57
    • 0031050921 scopus 로고    scopus 로고
    • Multiple overlapping processes underlying short-term synaptic enhancement
    • S.A. Fisher, T.M. Fischer, and T.J. Carew Multiple overlapping processes underlying short-term synaptic enhancement Trends Neurosci 20 1997 170 177
    • (1997) Trends Neurosci , vol.20 , pp. 170-177
    • Fisher, S.A.1    Fischer, T.M.2    Carew, T.J.3
  • 58
    • 0029963857 scopus 로고    scopus 로고
    • Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: Its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin
    • Y. Fujita, T. Sasaki, K. Fukui, H. Kontani, T. Kimura, and Y. Hata Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin J Biol Chem 271 1996 7265 7268
    • (1996) J Biol Chem , vol.271 , pp. 7265-7268
    • Fujita, Y.1    Sasaki, T.2    Fukui, K.3    Kontani, H.4    Kimura, T.5    Hata, Y.6
  • 59
    • 0033031477 scopus 로고    scopus 로고
    • Activity-dependent phosphorylation of SNAP-25 in hippocampal organotypic cultures
    • S. Genoud, W. Pralong, B.M. Riederer, L. Eder, S. Catsicas, and D. Muller Activity-dependent phosphorylation of SNAP-25 in hippocampal organotypic cultures J Neurochem 72 1999 1699 1706
    • (1999) J Neurochem , vol.72 , pp. 1699-1706
    • Genoud, S.1    Pralong, W.2    Riederer, B.M.3    Eder, L.4    Catsicas, S.5    Muller, D.6
  • 62
    • 0026800953 scopus 로고
    • Roles of PKA and PKC in facilitation of evoked and spontaneous transmitter release at depressed and nondepressed synapses in Aplysia sensory neurons
    • M. Ghirardi, O. Braha, B. Hochner, P.G. Montarolo, E.R. Kandel, and N. Dale Roles of PKA and PKC in facilitation of evoked and spontaneous transmitter release at depressed and nondepressed synapses in Aplysia sensory neurons Neuron 9 1992 479 489
    • (1992) Neuron , vol.9 , pp. 479-489
    • Ghirardi, M.1    Braha, O.2    Hochner, B.3    Montarolo, P.G.4    Kandel, E.R.5    Dale, N.6
  • 63
    • 0032488659 scopus 로고    scopus 로고
    • Autophosphorylation at Thr286 of the α-calcium-calmodulin kinase II in LTP and learning
    • K.P. Giese, N.B. Fedorov, R.K. Filipkowski, and A.J. Silva Autophosphorylation at Thr286 of the α-calcium-calmodulin kinase II in LTP and learning Science 279 1998 870 873
    • (1998) Science , vol.279 , pp. 870-873
    • Giese, K.P.1    Fedorov, N.B.2    Filipkowski, R.K.3    Silva, A.J.4
  • 64
    • 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
    • K.D. Gillis, R. Mossner, and E. Neher 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    Mossner, R.2    Neher, E.3
  • 65
    • 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
    • M.E. Graham, and R.D. Burgoyne 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 2000 1281 1289
    • (2000) J Neurosci , vol.20 , pp. 1281-1289
    • Graham, M.E.1    Burgoyne, R.D.2
  • 66
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • P. Greengard, F. Valtorta, A.J. Czernik, and F. Benfenati Synaptic vesicle phosphoproteins and regulation of synaptic function Science 259 1993 780 785
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 67
    • 0030021851 scopus 로고    scopus 로고
    • The Sec1 family: A novel family of proteins involved in synaptic transmission and general secretion
    • N. Halachmi, and Z. Lev The Sec1 family: a novel family of proteins involved in synaptic transmission and general secretion J Neurochem 66 1996 889 897
    • (1996) J Neurochem , vol.66 , pp. 889-897
    • Halachmi, N.1    Lev, Z.2
  • 68
    • 0035029611 scopus 로고    scopus 로고
    • Beyond parallel fiber LTD: The diversity of synaptic and non-synaptic plasticity in the cerebellum
    • C. Hansel, D.J. Linden, and E. D'Angelo Beyond parallel fiber LTD: the diversity of synaptic and non-synaptic plasticity in the cerebellum Nat Neurosci 4 2001 467 475
    • (2001) Nat Neurosci , vol.4 , pp. 467-475
    • Hansel, C.1    Linden, D.J.2    D'Angelo, E.3
  • 69
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release-four years of SNARE complexes
    • P.I. Hanson, J.E. Heuser, and R. Jahn Neurotransmitter release-four 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
  • 70
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
    • Y. Hayashi, S.H. Shi, J.A. Esteban, A. Piccini, J.C. Poncer, and R. Malinow Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction Science 287 2000 2262 2267
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1    Shi, S.H.2    Esteban, J.A.3    Piccini, A.4    Poncer, J.C.5    Malinow, R.6
  • 71
    • 0037021418 scopus 로고    scopus 로고
    • Differential phosphorylation of SNAP-25 in vivo by protein kinase C and protein kinase a
    • R. Hepp, J.-P. Cabaniols, and P.A. Roche Differential phosphorylation of SNAP-25 in vivo by protein kinase C and protein kinase A FEBS Lett 532 2002 52 56
    • (2002) FEBS Lett , vol.532 , pp. 52-56
    • Hepp, R.1    Cabaniols, J.-P.2    Roche, P.A.3
  • 72
    • 0033558360 scopus 로고    scopus 로고
    • Regulation of synaptic vesicle fusion by protein kinase C
    • S. Hilfiker, and G.J. Augustine Regulation of synaptic vesicle fusion by protein kinase C J Physiol 515 1999 1
    • (1999) J Physiol , vol.515 , pp. 1
    • Hilfiker, S.1    Augustine, G.J.2
  • 74
    • 0029862503 scopus 로고    scopus 로고
    • Phosphorylation of synaptic vesicle proteins: Modulation of the alpha SNAP interaction with the core complex
    • H. Hirling, and R.H. Scheller Phosphorylation of synaptic vesicle proteins: modulation of the alpha SNAP interaction with the core complex Proc Natl Acad Sci U S A 93 1996 11945 11949
    • (1996) Proc Natl Acad Sci U S a , vol.93 , pp. 11945-11949
    • Hirling, H.1    Scheller, R.H.2
  • 75
    • 0033213603 scopus 로고    scopus 로고
    • A phospho-switch controls the dynamic association of synapsins with synaptic vesicles
    • M. Hosaka, R.E. Hammer, and T.C. Südhof A phospho-switch controls the dynamic association of synapsins with synaptic vesicles Neuron 24 1999 377 387
    • (1999) Neuron , vol.24 , pp. 377-387
    • Hosaka, M.1    Hammer, R.E.2    Südhof, T.C.3
  • 76
    • 1842430915 scopus 로고    scopus 로고
    • The exocyst complex in polarized exocytosis
    • S.C. Hsu, D. TerBush, M. Abraham, and W. Guo The exocyst complex in polarized exocytosis Int Rev Cytol 233 2004 243 265
    • (2004) Int Rev Cytol , vol.233 , pp. 243-265
    • Hsu, S.C.1    Terbush, D.2    Abraham, M.3    Guo, W.4
  • 77
    • 0028170035 scopus 로고
    • CAMP contributes to mossy fiber LTP by initiating both a covalently mediated early phase and macromolecular synthesis-dependent late phase
    • Y.Y. Huang, X.C. Li, and E.R. Kandel cAMP contributes to mossy fiber LTP by initiating both a covalently mediated early phase and macromolecular synthesis-dependent late phase Cell 79 1994 69 79
    • (1994) Cell , vol.79 , pp. 69-79
    • Huang, Y.Y.1    Li, X.C.2    Kandel, E.R.3
  • 78
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • J.M. Ilardi, S. Mochida, and Z.-H. Sheng 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
  • 79
    • 0033809439 scopus 로고    scopus 로고
    • Two distinct mechanisms underline the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells
    • S. Iwasaki, M. Kataoka, M. Sekiguchi, Y. Shimazaki, K. Sato, and M. Takahashi Two distinct mechanisms underline the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells J Biochem 128 2000 407 414
    • (2000) J Biochem , vol.128 , pp. 407-414
    • Iwasaki, S.1    Kataoka, M.2    Sekiguchi, M.3    Shimazaki, Y.4    Sato, K.5    Takahashi, M.6
  • 81
    • 0035798238 scopus 로고    scopus 로고
    • The molecular biology of memory storage: A dialogue between genes and synapses
    • E.R. Kandel The molecular biology of memory storage: a dialogue between genes and synapses Science 294 2001 1030 1038
    • (2001) Science , vol.294 , pp. 1030-1038
    • Kandel, E.R.1
  • 82
    • 2642576793 scopus 로고    scopus 로고
    • Presynaptic mechanism underlying cAMP-dependent synaptic potentiation
    • M. Kaneko, and T. Takahashi Presynaptic mechanism underlying cAMP-dependent synaptic potentiation J Neurosci 24 2004 5202 5208
    • (2004) J Neurosci , vol.24 , pp. 5202-5208
    • Kaneko, M.1    Takahashi, T.2
  • 83
    • 0034089050 scopus 로고    scopus 로고
    • Nerve growth factor-induced phosphorylation of SNAP-25 in PC12 cells: A possible involvement in the regulation of SNAP-25 localization
    • M. Kataoka, R. Kuwahara, S. Iwasaki, Y. Shoji-Kasai, and M. Takahashi Nerve growth factor-induced phosphorylation of SNAP-25 in PC12 cells: a possible involvement in the regulation of SNAP-25 localization J Neurochem 74 2000 2058 2066
    • (2000) J Neurochem , vol.74 , pp. 2058-2066
    • Kataoka, M.1    Kuwahara, R.2    Iwasaki, S.3    Shoji-Kasai, Y.4    Takahashi, M.5
  • 84
    • 0032213268 scopus 로고    scopus 로고
    • CAMP-dependent long-term potentiation of nitric oxide release from cerebellar parallel fibers in rats
    • S. Kimura, S. Uchiyama, H.E. Takahashi, and K. Shibuki cAMP-dependent long-term potentiation of nitric oxide release from cerebellar parallel fibers in rats J Neurosci 18 1998 8551 8558
    • (1998) J Neurosci , vol.18 , pp. 8551-8558
    • Kimura, S.1    Uchiyama, S.2    Takahashi, H.E.3    Shibuki, K.4
  • 85
    • 0026325599 scopus 로고
    • Persistent protein kinase activation in the maintenance phase of long-term potentiation
    • E. Klann, S.J. Chen, and J.D. Sweatt Persistent protein kinase activation in the maintenance phase of long-term potentiation J Biol Chem 266 1991 24253 24256
    • (1991) J Biol Chem , vol.266 , pp. 24253-24256
    • Klann, E.1    Chen, S.J.2    Sweatt, J.D.3
  • 86
    • 0028111675 scopus 로고
    • Synaptic augmentation by 5-HT at rested Aplysia sensorimotor synapses: Independence of action potential prolongation
    • M. Klein Synaptic augmentation by 5-HT at rested Aplysia sensorimotor synapses: independence of action potential prolongation Neuron 13 1994 159 166
    • (1994) Neuron , vol.13 , pp. 159-166
    • Klein, M.1
  • 88
    • 0842281638 scopus 로고    scopus 로고
    • Does the fusion pore contribute to synaptic plasticity?
    • B. Krupa, and G. Liu Does the fusion pore contribute to synaptic plasticity? Trends Neurosci 27 2004 62 66
    • (2004) Trends Neurosci , vol.27 , pp. 62-66
    • Krupa, B.1    Liu, G.2
  • 89
    • 0034073884 scopus 로고    scopus 로고
    • Syntaphilin: A syntaxin-1 clamp that controls SNARE assembly
    • G. Lao, V. Scheuss, C.M. Gerwin, Q. Su, S. Mochida, and J. Rettig Syntaphilin: a syntaxin-1 clamp that controls SNARE assembly Neuron 25 2000 191 201
    • (2000) Neuron , vol.25 , pp. 191-201
    • Lao, G.1    Scheuss, V.2    Gerwin, C.M.3    Su, Q.4    Mochida, S.5    Rettig, J.6
  • 90
    • 0029025641 scopus 로고
    • Synaptic plasticity: Hippocampal LTP
    • A.U. Larkman, and J.J. Jack Synaptic plasticity: hippocampal LTP Curr Opin Neurobiol 5 1995 324 334
    • (1995) Curr Opin Neurobiol , vol.5 , pp. 324-334
    • Larkman, A.U.1    Jack, J.J.2
  • 91
    • 0037672843 scopus 로고    scopus 로고
    • The molecular machinery of synaptic vesicle exocytosis
    • L. Li, and L.S. Chin The molecular machinery of synaptic vesicle exocytosis Cell Mol Life Sci 60 2003 942 960
    • (2003) Cell Mol Life Sci , vol.60 , pp. 942-960
    • Li, L.1    Chin, L.S.2
  • 92
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • R.C. Lin, and R.H. Scheller Structural organization of the synaptic exocytosis core complex Neuron 19 1997 1087 1094
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 93
    • 0033500895 scopus 로고    scopus 로고
    • Activation of presynaptic cAMP-dependent protein kinase is required for induction of cerebellar long-term potentiation
    • D.J. Linden, and S. Ahn Activation of presynaptic cAMP-dependent protein kinase is required for induction of cerebellar long-term potentiation J Neurosci 19 1999 10221 10227
    • (1999) J Neurosci , vol.19 , pp. 10221-10227
    • Linden, D.J.1    Ahn, S.2
  • 94
    • 0024455337 scopus 로고
    • The role of protein kinase C in long-term potentiation: A testable model
    • D.J. Linden, and A. Routtenberg The role of protein kinase C in long-term potentiation: a testable model Brain Res Brain Res Rev 14 1989 279 296
    • (1989) Brain Res Brain Res Rev , vol.14 , pp. 279-296
    • Linden, D.J.1    Routtenberg, A.2
  • 95
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioral memory
    • J. Lisman, H. Schulman, and H. Cline The molecular basis of CaMKII function in synaptic and behavioral memory Nat Rev Neurosci 3 2002 175 190
    • (2002) Nat Rev Neurosci , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 96
    • 0038721600 scopus 로고    scopus 로고
    • Presynaptic control of quantal size: Kinetic mechanisms and implications for synaptic transmission and plasticity
    • G. Liu Presynaptic control of quantal size: kinetic mechanisms and implications for synaptic transmission and plasticity Curr Opin Neurobiol 13 2003 324 331
    • (2003) Curr Opin Neurobiol , vol.13 , pp. 324-331
    • Liu, G.1
  • 97
    • 0031982541 scopus 로고    scopus 로고
    • Region-specific phosphorylation of rabphilin in mossy fiber nerve terminals of the hippocampus
    • G. Lonart, and T.C. Südhof Region-specific phosphorylation of rabphilin in mossy fiber nerve terminals of the hippocampus J Neurosci 18 1998 634 640
    • (1998) J Neurosci , vol.18 , pp. 634-640
    • Lonart, G.1    Südhof, T.C.2
  • 98
    • 0032214487 scopus 로고    scopus 로고
    • Mechanism of action of Rab3A in mossy fiber LTP
    • G. Lonart, R. Janz, K.M. Johnson, and T.C. Südhof Mechanism of action of Rab3A in mossy fiber LTP Neuron 21 1998 1141 1150
    • (1998) Neuron , vol.21 , pp. 1141-1150
    • Lonart, G.1    Janz, R.2    Johnson, K.M.3    Südhof, T.C.4
  • 99
    • 0141987893 scopus 로고    scopus 로고
    • Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses
    • G. Lonart, S. Schoch, P.S. Kaeser, C.J. Larkin, T.C. Südhof, and D.J. Linden Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses Cell 115 2003 49 60
    • (2003) Cell , vol.115 , pp. 49-60
    • Lonart, G.1    Schoch, S.2    Kaeser, P.S.3    Larkin, C.J.4    Südhof, T.C.5    Linden, D.J.6
  • 100
    • 0023633194 scopus 로고
    • Protein kinase C inhibitors eliminate hippocampal long-term potentiation
    • D.M. Lovinger, K.L. Wong, K. Murakami, and A. Routtenberg Protein kinase C inhibitors eliminate hippocampal long-term potentiation Brain Res 436 1987 177 183
    • (1987) Brain Res , vol.436 , pp. 177-183
    • Lovinger, D.M.1    Wong, K.L.2    Murakami, K.3    Routtenberg, A.4
  • 101
    • 0035132869 scopus 로고    scopus 로고
    • Activation of synaptic NMDA receptors induces membrane insertion of new AMPA receptors and LTP in cultured hippocampal neurons
    • W. Lu, H. Man, W. Ju, W.S. Trimble, J.F. MacDonald, and Y.T. Wang Activation of synaptic NMDA receptors induces membrane insertion of new AMPA receptors and LTP in cultured hippocampal neurons Neuron 29 2001 243 254
    • (2001) Neuron , vol.29 , pp. 243-254
    • Lu, W.1    Man, H.2    Ju, W.3    Trimble, W.S.4    MacDonald, J.F.5    Wang, Y.T.6
  • 102
    • 0038285449 scopus 로고    scopus 로고
    • Synaptic plasticity and dynamic modulation of the postsynaptic membrane
    • C. Luscher, R.A. Nicoll, R.C. Malenka, and D. Muller Synaptic plasticity and dynamic modulation of the postsynaptic membrane Nat Neurosci 3 2000 545 550
    • (2000) Nat Neurosci , vol.3 , pp. 545-550
    • Luscher, C.1    Nicoll, R.A.2    Malenka, R.C.3    Muller, D.4
  • 103
    • 0346728801 scopus 로고    scopus 로고
    • Long-term potentiation and memory
    • M.A. Lynch Long-term potentiation and memory Physiol Rev 84 2004 87 136
    • (2004) Physiol Rev , vol.84 , pp. 87-136
    • Lynch, M.A.1
  • 104
    • 0032479813 scopus 로고    scopus 로고
    • Protein kinase C: A physiological mediator of enhanced transmitter output
    • H. Majewski, and L. Iannazzo Protein kinase C: a physiological mediator of enhanced transmitter output Prog Neurobiol 55 1998 463 475
    • (1998) Prog Neurobiol , vol.55 , pp. 463-475
    • Majewski, H.1    Iannazzo, L.2
  • 105
    • 0033578855 scopus 로고    scopus 로고
    • Long-term potentiation-a decade of progress?
    • R.C. Malenka, and R.A. Nicoll Long-term potentiation-a decade of progress? Science 285 1999 1870 1874
    • (1999) Science , vol.285 , pp. 1870-1874
    • Malenka, R.C.1    Nicoll, R.A.2
  • 106
    • 0022446151 scopus 로고
    • Potentiation of synaptic transmission in the hippocampus by phorbol esters
    • R.C. Malenka, D.V. Madison, and R.A. Nicoll Potentiation of synaptic transmission in the hippocampus by phorbol esters Nature 321 1986 175 177
    • (1986) Nature , vol.321 , pp. 175-177
    • Malenka, R.C.1    Madison, D.V.2    Nicoll, R.A.3
  • 107
    • 0024461379 scopus 로고
    • Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP
    • R. Malinow, H. Schulman, and R.W. Tsien Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP Science 245 1989 862 866
    • (1989) Science , vol.245 , pp. 862-866
    • Malinow, R.1    Schulman, H.2    Tsien, R.W.3
  • 108
    • 0035918302 scopus 로고    scopus 로고
    • Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling
    • M. Margittai, D. Fasshauer, S. Pabst, R. Jahn, and R. Langen Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling J Biol Chem 276 2001 13169 13177
    • (2001) J Biol Chem , vol.276 , pp. 13169-13177
    • Margittai, M.1    Fasshauer, D.2    Pabst, S.3    Jahn, R.4    Langen, R.5
  • 110
    • 0029066116 scopus 로고
    • CaMKII regulates the frequency-response function of hippocampal synapses for the production of both LTD and LTP
    • M. Mayford, J. Wang, E.R. Kandel, and T.J. O'Dell CaMKII regulates the frequency-response function of hippocampal synapses for the production of both LTD and LTP Cell 81 1995 891 904
    • (1995) Cell , vol.81 , pp. 891-904
    • Mayford, M.1    Wang, J.2    Kandel, E.R.3    O'Dell, T.J.4
  • 111
    • 0029807527 scopus 로고    scopus 로고
    • Control of memory formation through regulated expression of a CaMKII transgene
    • M. Mayford, M.E. Bach, Y.Y. Huang, L. Wang, R.D. Hawkins, and E.R. Kandel Control of memory formation through regulated expression of a CaMKII transgene Science 274 1996 1678 1683
    • (1996) Science , vol.274 , pp. 1678-1683
    • Mayford, M.1    Bach, M.E.2    Huang, Y.Y.3    Wang, L.4    Hawkins, R.D.5    Kandel, E.R.6
  • 112
    • 0032922388 scopus 로고    scopus 로고
    • Protein kinases: Which one is the memory molecule?
    • J. Micheau, and G. Riedel Protein kinases: which one is the memory molecule? Cell Mol Life Sci 55 1999 534 548
    • (1999) Cell Mol Life Sci , vol.55 , pp. 534-548
    • Micheau, J.1    Riedel, G.2
  • 114
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • K.M. Misura, R.H. Scheller, and W.I. Weis Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex Nature 404 2000 355 362
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 115
    • 2942614748 scopus 로고    scopus 로고
    • Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity
    • C. Morenilla-Palao, R. Planells-Cases, N. Garcia-Sanz, and A. Ferrer-Montiel Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity J Biol Chem 279 2004 25665 25672
    • (2004) J Biol Chem , vol.279 , pp. 25665-25672
    • Morenilla-Palao, C.1    Planells-Cases, R.2    Garcia-Sanz, N.3    Ferrer-Montiel, A.4
  • 116
    • 0042858417 scopus 로고    scopus 로고
    • Cell biology of the presynaptic terminal
    • V.N. Murthy, and P. De Camilli Cell biology of the presynaptic terminal Annu Rev Neurosci 26 2003 701 728
    • (2003) Annu Rev Neurosci , vol.26 , pp. 701-728
    • Murthy, V.N.1    De Camilli, P.2
  • 117
    • 0036848611 scopus 로고    scopus 로고
    • Protein kinase C-dependent phosphorylation of synaptosome-associated protein of 25 kDa at Ser187 potentiates vesicle recruitment
    • G. Nagy, U. Matti, R.B. Nehring, T. Binz, J. Rettig, and E. Neher Protein kinase C-dependent phosphorylation of synaptosome-associated protein of 25 kDa at Ser187 potentiates vesicle recruitment J Neurosci 22 2002 9278 9286
    • (2002) J Neurosci , vol.22 , pp. 9278-9286
    • Nagy, G.1    Matti, U.2    Nehring, R.B.3    Binz, T.4    Rettig, J.5    Neher, E.6
  • 118
    • 1242306711 scopus 로고    scopus 로고
    • Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25
    • G. Nagy, K. Reim, U. Matti, N. Brose, T. Binz, and J. Rettig Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25 Neuron 41 2004 417 429
    • (2004) Neuron , vol.41 , pp. 417-429
    • Nagy, G.1    Reim, K.2    Matti, U.3    Brose, N.4    Binz, T.5    Rettig, J.6
  • 119
    • 0030299803 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II phosphorylation of the presynaptic protein synapsin I is persistently increased during long-term potentiation
    • 2+/calmodulin- dependent protein kinase II phosphorylation of the presynaptic protein synapsin I is persistently increased during long-term potentiation Proc Natl Acad Sci U S A 93 1996 15451 15456
    • (1996) Proc Natl Acad Sci U S a , vol.93 , pp. 15451-15456
    • Nayak, A.S.1    Moore, C.I.2    Browning, M.D.3
  • 120
    • 0029093566 scopus 로고
    • Contrasting properties of two forms of long-term potentiation in the hippocampus
    • R.A. Nicoll, and R.C. Malenka Contrasting properties of two forms of long-term potentiation in the hippocampus Nature 377 1995 115 118
    • (1995) Nature , vol.377 , pp. 115-118
    • Nicoll, R.A.1    Malenka, R.C.2
  • 121
    • 0033492872 scopus 로고    scopus 로고
    • Overexpression of cysteine-string proteins in Drosophila reveals interactions with syntaxin
    • Z. Nie, R. Ranjan, J.J. Wenniger, S.N. Hong, P. Bronk, and K.E. Zinsmaier Overexpression of cysteine-string proteins in Drosophila reveals interactions with syntaxin J Neurosci 19 1999 10270 10279
    • (1999) J Neurosci , vol.19 , pp. 10270-10279
    • Nie, Z.1    Ranjan, R.2    Wenniger, J.J.3    Hong, S.N.4    Bronk, P.5    Zinsmaier, K.E.6
  • 123
    • 1842610004 scopus 로고    scopus 로고
    • Presynaptic CaMKII is necessary for synaptic plasticity in cultured hippocampal neurons
    • I. Ninan, and O. Arancio Presynaptic CaMKII is necessary for synaptic plasticity in cultured hippocampal neurons Neuron 42 2004 129 141
    • (2004) Neuron , vol.42 , pp. 129-141
    • Ninan, I.1    Arancio, O.2
  • 124
    • 0842330769 scopus 로고    scopus 로고
    • Regulation of hippocampal synaptic plasticity by cyclic AMP-dependent protein kinases
    • P.V. Nguyen, and N.H. Woo Regulation of hippocampal synaptic plasticity by cyclic AMP-dependent protein kinases Prog Neurobiol 71 2003 401 437
    • (2003) Prog Neurobiol , vol.71 , pp. 401-437
    • Nguyen, P.V.1    Woo, N.H.2
  • 126
    • 0030857360 scopus 로고    scopus 로고
    • Postsynaptic inhibitors of calcium/calmodulin-dependent protein kinase type II block induction but not maintenance of pairing-induced long-term potentiation
    • N. Otmakhov, L.C. Griffith, and J.E. Lisman Postsynaptic inhibitors of calcium/calmodulin-dependent protein kinase type II block induction but not maintenance of pairing-induced long-term potentiation J Neurosci 17 1997 5357 5365
    • (1997) J Neurosci , vol.17 , pp. 5357-5365
    • Otmakhov, N.1    Griffith, L.C.2    Lisman, J.E.3
  • 128
    • 0027366611 scopus 로고
    • Phorbol esters enhance synaptic transmission by a presynaptic, calcium-dependent mechanism in rat hippocampus
    • K.D. Parfitt, and D.V. Madison Phorbol esters enhance synaptic transmission by a presynaptic, calcium-dependent mechanism in rat hippocampus J Physiol 471 1993 245 268
    • (1993) J Physiol , vol.471 , pp. 245-268
    • Parfitt, K.D.1    Madison, D.V.2
  • 129
    • 0034773788 scopus 로고    scopus 로고
    • Some forms of cAMP-mediated long-lasting potentiation are associated with release of BDNF and nuclear translocation of phospho-MAP Kinase
    • S.L. Patterson, C. Pittenger, A. Morozov, K.C. Martin, H. Scanlin, and C. Drake Some forms of cAMP-mediated long-lasting potentiation are associated with release of BDNF and nuclear translocation of phospho-MAP Kinase Neuron 32 2001 123 140
    • (2001) Neuron , vol.32 , pp. 123-140
    • Patterson, S.L.1    Pittenger, C.2    Morozov, A.3    Martin, K.C.4    Scanlin, H.5    Drake, C.6
  • 130
    • 0033130103 scopus 로고    scopus 로고
    • Transport-vesicle targeting: Tethers before SNAREs
    • S.R. Pfeffer Transport-vesicle targeting: tethers before SNAREs Nat Cell Biol 1 1999 E17 E22
    • (1999) Nat Cell Biol , vol.1
    • Pfeffer, S.R.1
  • 131
    • 0034788303 scopus 로고    scopus 로고
    • Transient synaptic activation of NMDA receptors leads to the insertion of native AMPA receptors at hippocampal neuronal plasma membranes
    • L. Pickard, J. Noel, J.K. Duckworth, S.M. Fitzjohn, J.M. Henley, and G.L. Collingridge Transient synaptic activation of NMDA receptors leads to the insertion of native AMPA receptors at hippocampal neuronal plasma membranes Neuropharmacology 41 2001 700 713
    • (2001) Neuropharmacology , vol.41 , pp. 700-713
    • Pickard, L.1    Noel, J.2    Duckworth, J.K.3    Fitzjohn, S.M.4    Henley, J.M.5    Collingridge, G.L.6
  • 133
    • 0030998361 scopus 로고    scopus 로고
    • Protein kinase C in synaptic plasticity: Changes in the in situ phosphorylation state of identified pre- and postsynaptic substrates
    • G.M. Ramakers, P. Pasinelli, J.J.H. Hens, W.H. Gispen, and P.N.E. De Graan Protein kinase C in synaptic plasticity: changes in the in situ phosphorylation state of identified pre- and postsynaptic substrates Prog Neuropsychopharmacol Biol Psychiatry 21 1997 455 486
    • (1997) Prog Neuropsychopharmacol Biol Psychiatry , vol.21 , pp. 455-486
    • Ramakers, G.M.1    Pasinelli, P.2    Hens, J.J.H.3    Gispen, W.H.4    De Graan, P.N.E.5
  • 134
    • 0031916186 scopus 로고    scopus 로고
    • Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling
    • R. Ranjan, P. Bronk, and K.E. Zinsmaier Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling J Neurosci 18 1998 956 964
    • (1998) J Neurosci , vol.18 , pp. 956-964
    • Ranjan, R.1    Bronk, P.2    Zinsmaier, K.E.3
  • 136
    • 0035102504 scopus 로고    scopus 로고
    • A developmental switch in neurotransmitter flux enhances synaptic efficacy by affecting AMPA receptor activation
    • J.J. Renger, C. Egles, and G. Liu A developmental switch in neurotransmitter flux enhances synaptic efficacy by affecting AMPA receptor activation Neuron 29 2001 469 484
    • (2001) Neuron , vol.29 , pp. 469-484
    • Renger, J.J.1    Egles, C.2    Liu, G.3
  • 137
    • 18244389735 scopus 로고    scopus 로고
    • ß Phorbol ester- and diacylglycerol-induced augmentation of transmitter release is mediated by Munc 13s and not by PKCs
    • J.S. Rhee, A. Betz, S. Pyott, K. Reim, F. Varoqueaux, and I. Augustin ß Phorbol ester- and diacylglycerol-induced augmentation of transmitter release is mediated by Munc 13s and not by PKCs Cell 108 2002 121 133
    • (2002) Cell , vol.108 , pp. 121-133
    • Rhee, J.S.1    Betz, A.2    Pyott, S.3    Reim, K.4    Varoqueaux, F.5    Augustin, I.6
  • 138
    • 0033349884 scopus 로고    scopus 로고
    • Unc-13 is required for synaptic vesicle fusion in C. elegans
    • J.E. Richmond, W.S. David, and E.M. Jorgensen Unc-13 is required for synaptic vesicle fusion in C. elegans Nat Neurosci 2 1999 959 964
    • (1999) Nat Neurosci , vol.2 , pp. 959-964
    • Richmond, J.E.1    David, W.S.2    Jorgensen, E.M.3
  • 139
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • J.E. Richmond, R.M. Welmer, and E.M. Jorgensen An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming Nature 412 2001 338 341
    • (2001) Nature , vol.412 , pp. 338-341
    • Richmond, J.E.1    Welmer, R.M.2    Jorgensen, E.M.3
  • 140
    • 0032926138 scopus 로고    scopus 로고
    • Differential phosphorylation of syntaxin and synaptosome-associated protein of 25 kDa (SNAP-25) isoforms
    • C. Risinger, and M.K. Bennett Differential phosphorylation of syntaxin and synaptosome-associated protein of 25 kDa (SNAP-25) isoforms J Neurochem 72 1999 614 624
    • (1999) J Neurochem , vol.72 , pp. 614-624
    • Risinger, C.1    Bennett, M.K.2
  • 141
    • 0025608979 scopus 로고
    • Strategic location of calcium channels at transmitter release sites of frog neuromuscular synapses
    • R. Robitaille, E.M. Adler, and M.P. Charlton Strategic location of calcium channels at transmitter release sites of frog neuromuscular synapses Neuron 5 1990 773 779
    • (1990) Neuron , vol.5 , pp. 773-779
    • Robitaille, R.1    Adler, E.M.2    Charlton, M.P.3
  • 142
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • J.E. Rothman Mechanisms of intracellular protein transport Nature 372 1994 55 63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 143
    • 0035793039 scopus 로고    scopus 로고
    • Preferential potentiation of fast-releasing synaptic vesicles by cAMP at the calyx of Held
    • T. Sakaba, and E. Neher Preferential potentiation of fast-releasing synaptic vesicles by cAMP at the calyx of Held Proc Natl Acad Sci U S A 98 2001 331 336
    • (2001) Proc Natl Acad Sci U S a , vol.98 , pp. 331-336
    • Sakaba, T.1    Neher, E.2
  • 144
    • 0029961605 scopus 로고    scopus 로고
    • CAMP mediates a presynaptic form of LTP at cerebellar parallel fiber synapses
    • P.A. Salin, R.C. Malenka, and R.A. Nicoll cAMP mediates a presynaptic form of LTP at cerebellar parallel fiber synapses Neuron 16 1996 797 803
    • (1996) Neuron , vol.16 , pp. 797-803
    • Salin, P.A.1    Malenka, R.C.2    Nicoll, R.A.3
  • 145
  • 146
    • 0040576976 scopus 로고    scopus 로고
    • Rabphilin knock-out mice reveal that rabphilin is not required for Rab3 function in regulating neurotransmitter release
    • O.M. Schluter, E. Schnell, M. Verhage, T. Tzonopoulos, R.A. Nicoll, and R. Janz 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
    • Schluter, O.M.1    Schnell, E.2    Verhage, M.3    Tzonopoulos, T.4    Nicoll, R.A.5    Janz, R.6
  • 147
    • 0037122458 scopus 로고    scopus 로고
    • RIM1α forms a protein scaffold for regulating neurotransmitter release at the active zone
    • S. Schoch, P.E. Castillo, T. Jo, K. Mukherjee, M. Geppert, and Y. Wang RIM1α forms a protein scaffold for regulating neurotransmitter release at the active zone Nature 415 2002 321 326
    • (2002) Nature , vol.415 , pp. 321-326
    • Schoch, S.1    Castillo, P.E.2    Jo, T.3    Mukherjee, K.4    Geppert, M.5    Wang, Y.6
  • 148
    • 0037174634 scopus 로고    scopus 로고
    • Postsynaptic signaling and plasticity mechanisms
    • M. Sheng, and M.J. Kim Postsynaptic signaling and plasticity mechanisms Science 298 2002 776 780
    • (2002) Science , vol.298 , pp. 776-780
    • Sheng, M.1    Kim, M.J.2
  • 149
    • 0033546052 scopus 로고    scopus 로고
    • Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation
    • S.H. Shi, Y. Hayashi, R.S. Petralia, S.H. Zaman, R.J. Wenthold, and K. Svoboda Rapid spine delivery and redistribution of AMPA receptors after synaptic NMDA receptor activation Science 284 1999 1811 1816
    • (1999) Science , vol.284 , pp. 1811-1816
    • Shi, S.H.1    Hayashi, Y.2    Petralia, R.S.3    Zaman, S.H.4    Wenthold, R.J.5    Svoboda, K.6
  • 150
    • 0029898850 scopus 로고    scopus 로고
    • Phosphorylation of 25-kDa synaptosome-associated protein. Possible involvement in protein kinase C-mediated regulation of neurotransmitter release
    • Y. Shimazaki, T. Nishiki, A. Omori, M. Sekiguchi, Y. Kamata, and S. Kozaki Phosphorylation of 25-kDa synaptosome-associated protein. Possible involvement in protein kinase C-mediated regulation of neurotransmitter release 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    Sekiguchi, M.4    Kamata, Y.5    Kozaki, S.6
  • 151
    • 0038754049 scopus 로고    scopus 로고
    • Phorbol esters and neurotransmitter release: More than just protein kinase C?
    • E.M. Silinsky, and T.J. Searl Phorbol esters and neurotransmitter release: more than just protein kinase C? Br J Pharmacol 138 2003 1191 1201
    • (2003) Br J Pharmacol , vol.138 , pp. 1191-1201
    • Silinsky, E.M.1    Searl, T.J.2
  • 152
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice
    • A.J. Silva, C.F. Stevens, S. Tonegawa, and Y. Wang Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice Science 257 1992 201 206
    • (1992) Science , vol.257 , pp. 201-206
    • Silva, A.J.1    Stevens, C.F.2    Tonegawa, S.3    Wang, Y.4
  • 153
    • 0026742451 scopus 로고
    • Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice
    • A.J. Silva, R. Paylor, J.M. Wehner, and S. Tonegawa Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice Science 257 1992 206 211
    • (1992) Science , vol.257 , pp. 206-211
    • Silva, A.J.1    Paylor, R.2    Wehner, J.M.3    Tonegawa, S.4
  • 154
    • 0013686246 scopus 로고
    • Translocation of synapsin I in response to depolarization of isolated nerve terminals
    • T.S. Sihra, J.K. Wang, F.S. Gorelick, and P. Greengard Translocation of synapsin I in response to depolarization of isolated nerve terminals Proc Natl Acad Sci U S A 86 1989 8108 8112
    • (1989) Proc Natl Acad Sci U S a , vol.86 , pp. 8108-8112
    • Sihra, T.S.1    Wang, J.K.2    Gorelick, F.S.3    Greengard, P.4
  • 155
    • 0033556325 scopus 로고    scopus 로고
    • 2+ activation of protein kinase C
    • 2+ activation of protein kinase C J Neurosci 19 1999 589 598
    • (1999) J Neurosci , vol.19 , pp. 589-598
    • Smith, C.1
  • 156
    • 0032081255 scopus 로고    scopus 로고
    • 2+ acts by two separate pathways to modulate the supply of release-competent vesicles in chromaffin cells
    • 2+ acts by two separate pathways to modulate the supply of release-competent vesicles in chromaffin cells Neuron 20 1998 1243 1253
    • (1998) Neuron , vol.20 , pp. 1243-1253
    • Smith, C.1    Moser, T.2    Xu, T.3    Neher, E.4
  • 157
    • 0034043203 scopus 로고    scopus 로고
    • CaM-kinases: Modulators of synaptic plasticity
    • T.R. Soderling CaM-kinases: modulators of synaptic plasticity Curr Opin Neurobiol 10 2000 375 380
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 375-380
    • Soderling, T.R.1
  • 160
    • 3142580943 scopus 로고    scopus 로고
    • Identification of Snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)
    • M. Starcevic, and E.C. Dell'Angelica Identification of Snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1) J Biol Chem 279 2004 28393 28401
    • (2004) J Biol Chem , vol.279 , pp. 28393-28401
    • Starcevic, M.1    Dell'Angelica, E.C.2
  • 161
    • 0030729884 scopus 로고    scopus 로고
    • Kinetic analysis of the phosphorylation-dependent interactions of synapsin I with rat brain synaptic vesicles
    • G. Stefani, F. Onofri, F. Valtorta, P. Vaccaro, P. Greengard, and F. Benfenati Kinetic analysis of the phosphorylation-dependent interactions of synapsin I with rat brain synaptic vesicles J Physiol 504 1997 501 515
    • (1997) J Physiol , vol.504 , pp. 501-515
    • Stefani, G.1    Onofri, F.2    Valtorta, F.3    Vaccaro, P.4    Greengard, P.5    Benfenati, F.6
  • 162
    • 0032192448 scopus 로고    scopus 로고
    • Regulation of the readily releasable vesicle pool by protein kinase C
    • C.F. Stevens, and J.M. Sullivan Regulation of the readily releasable vesicle pool by protein kinase C Neuron 21 1998 885 893
    • (1998) Neuron , vol.21 , pp. 885-893
    • Stevens, C.F.1    Sullivan, J.M.2
  • 163
    • 0028020340 scopus 로고
    • Changes in reliability of synaptic function as a mechanism for plasticity
    • C.F. Stevens, and Y. Wang Changes in reliability of synaptic function as a mechanism for plasticity Nature 371 1994 704 707
    • (1994) Nature , vol.371 , pp. 704-707
    • Stevens, C.F.1    Wang, Y.2
  • 164
    • 17644438421 scopus 로고    scopus 로고
    • Impaired cerebellar long-term potentiation in type I adenylyl cyclase mutant mice
    • D.R. Storm, C. Hansel, B. Hacker, A. Parent, and D.J. Linden Impaired cerebellar long-term potentiation in type I adenylyl cyclase mutant mice Neuron 20 1998 1199 1210
    • (1998) Neuron , vol.20 , pp. 1199-1210
    • Storm, D.R.1    Hansel, C.2    Hacker, B.3    Parent, A.4    Linden, D.J.5
  • 165
    • 84860070586 scopus 로고
    • The synaptic cycle: A cascade of protein-protein interactions
    • T.C. Südhof The synaptic cycle: a cascade of protein-protein interactions Nature 362 1995 318 324
    • (1995) Nature , vol.362 , pp. 318-324
    • Südhof, T.C.1
  • 166
    • 0033637985 scopus 로고    scopus 로고
    • The synaptic vesicle cycle revisited
    • T.C. Südhof The synaptic vesicle cycle revisited Neuron 28 2000 317 320
    • (2000) Neuron , vol.28 , pp. 317-320
    • Südhof, T.C.1
  • 167
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • R.B. Sutton, D. Fasshauer, R. Jahn, and A.T. Brunger 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
  • 168
    • 3242747322 scopus 로고    scopus 로고
    • Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons
    • P. Thakur, D.R. Stevens, Z.-H. Sheng, and J. Rettig Effects of PKA-mediated phosphorylation of Snapin on synaptic transmission in cultured hippocampal neurons J Neurosci 24 2004 6476 6481
    • (2004) J Neurosci , vol.24 , pp. 6476-6481
    • Thakur, P.1    Stevens, D.R.2    Sheng, Z.-H.3    Rettig, J.4
  • 169
    • 1342289413 scopus 로고    scopus 로고
    • MAPK cascade signalling and synaptic plasticity
    • G.M. Thomas, and R.L. Huganir MAPK cascade signalling and synaptic plasticity Nat Rev Neurosci 5 2004 173 183
    • (2004) Nat Rev Neurosci , vol.5 , pp. 173-183
    • Thomas, G.M.1    Huganir, R.L.2
  • 170
    • 0027050487 scopus 로고
    • Synapsin I partially dissociates from synaptic vesicles during exocytosis induced by electrical stimulation
    • T.F. Torri, M. Bossi, R. Fesce, P. Greengard, and F. Valtorta Synapsin I partially dissociates from synaptic vesicles during exocytosis induced by electrical stimulation Neuron 9 1992 1143 1153
    • (1992) Neuron , vol.9 , pp. 1143-1153
    • Torri, T.F.1    Bossi, M.2    Fesce, R.3    Greengard, P.4    Valtorta, F.5
  • 171
    • 0030273117 scopus 로고    scopus 로고
    • Direct modulation of the secretory machinery underlies PKA-dependent synaptic facilitation in hippocampal neurons
    • L.E. Trudeau, D.G. Emery, and P.G. Haydon Direct modulation of the secretory machinery underlies PKA-dependent synaptic facilitation in hippocampal neurons Neuron 17 1996 789 797
    • (1996) Neuron , vol.17 , pp. 789-797
    • Trudeau, L.E.1    Emery, D.G.2    Haydon, P.G.3
  • 172
    • 0032499761 scopus 로고    scopus 로고
    • Modulation of an early step in the secretory machinery in hippocampal nerve terminals
    • L.E. Trudeau, Y. Fang, and P.G. Haydon Modulation of an early step in the secretory machinery in hippocampal nerve terminals Proc Natl Acad Sci U S A 95 1998 7163 7168
    • (1998) Proc Natl Acad Sci U S a , vol.95 , pp. 7163-7168
    • Trudeau, L.E.1    Fang, Y.2    Haydon, P.G.3
  • 173
    • 0033215370 scopus 로고    scopus 로고
    • Protein phosphorylation and the regulation of synaptic membrane traffic
    • K.M. Turner, R.D. Burgoyne, and A. Morgan Protein phosphorylation and the regulation of synaptic membrane traffic Trends Neurosci 22 1999 459 464
    • (1999) Trends Neurosci , vol.22 , pp. 459-464
    • Turner, K.M.1    Burgoyne, R.D.2    Morgan, A.3
  • 174
  • 176
    • 2942750191 scopus 로고    scopus 로고
    • Reinvestigation of the role of Snapin in neurotransmitter release
    • O. Vites, J.S. Rhee, M. Schwarz, C. Rosenmund, and R. Jahn Reinvestigation of the role of Snapin in neurotransmitter release J Biol Chem 279 2004 26251 26256
    • (2004) J Biol Chem , vol.279 , pp. 26251-26256
    • Vites, O.1    Rhee, J.S.2    Schwarz, M.3    Rosenmund, C.4    Jahn, R.5
  • 177
    • 0036371005 scopus 로고    scopus 로고
    • Short-term plasticity at the calyx of held
    • H. Von Gersdorff, and J.G.G. Borst Short-term plasticity at the calyx of held Nat Rev Neurosci 3 2002 53 64
    • (2002) Nat Rev Neurosci , vol.3 , pp. 53-64
    • Von Gersdorff, H.1    Borst, J.G.G.2
  • 178
    • 0030877243 scopus 로고    scopus 로고
    • Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion
    • Y. Wang, M. Okamoto, F. Schmitz, K. Hofmann, and T.C. Südhof 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    Hofmann, K.4    Südhof, T.C.5
  • 180
    • 0028051845 scopus 로고
    • Mediation of hippocampal mossy fiber long-term potentiation by cyclic AMP
    • M.G. Weisskopf, P.E. Castillo, R.A. Zalutsky, and R.A. Nicoll Mediation of hippocampal mossy fiber long-term potentiation by cyclic AMP Science 265 1994 1878 1882
    • (1994) Science , vol.265 , pp. 1878-1882
    • Weisskopf, M.G.1    Castillo, P.E.2    Zalutsky, R.A.3    Nicoll, R.A.4
  • 181
    • 2342571477 scopus 로고    scopus 로고
    • An essential role for vesicular glutamate transporter 1 (VGLUT1) in postnatal development and control of quantal size
    • S.M. Wojcik, J.S. Rhee, E. Herzog, A. Sigler, R. Jahn, and S. Takamori An essential role for vesicular glutamate transporter 1 (VGLUT1) in postnatal development and control of quantal size Proc Natl Acad Sci U S A 101 2004 7158 7163
    • (2004) Proc Natl Acad Sci U S a , vol.101 , pp. 7158-7163
    • Wojcik, S.M.1    Rhee, J.S.2    Herzog, E.3    Sigler, A.4    Jahn, R.5    Takamori, S.6
  • 182
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • T. Xu, T. Binz, H. Niemann, and E. Neher Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity Nat Neurosci 1 1998 192 200
    • (1998) Nat Neurosci , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 183
    • 0346728804 scopus 로고    scopus 로고
    • Structural contributions to short-term synaptic plasticity
    • M.A. Xu-Friedman, and W.G. Regehr Structural contributions to short-term synaptic plasticity Physiol Rev 84 2004 69 85
    • (2004) Physiol Rev , vol.84 , pp. 69-85
    • Xu-Friedman, M.A.1    Regehr, W.G.2
  • 185
    • 0037218831 scopus 로고    scopus 로고
    • A developmental switch in the signaling cascades for LTP induction
    • H. Yasuda, A.L. Barth, D. Stellwagen, and R.C. Malenka A developmental switch in the signaling cascades for LTP induction Nat Neurosci 6 2003 15 16
    • (2003) Nat Neurosci , vol.6 , pp. 15-16
    • Yasuda, H.1    Barth, A.L.2    Stellwagen, D.3    Malenka, R.C.4
  • 187
    • 0033598333 scopus 로고    scopus 로고
    • The liprin protein SYD-2 regulates the differentiation of presynaptic termini in C. elegans
    • M. Zhen, and Y. Jin The liprin protein SYD-2 regulates the differentiation of presynaptic termini in C. elegans Nature 401 1999 371 375
    • (1999) Nature , vol.401 , pp. 371-375
    • Zhen, M.1    Jin, Y.2
  • 188
    • 0030476187 scopus 로고    scopus 로고
    • Exocytosis: A molecular and physiological perspective
    • R.S. Zucker Exocytosis: a molecular and physiological perspective Neuron 17 1996 1049 1055
    • (1996) Neuron , vol.17 , pp. 1049-1055
    • Zucker, R.S.1
  • 189
    • 0036201201 scopus 로고    scopus 로고
    • Short-term synaptic plasticity
    • R.S. Zucker, and W.G. Regehr Short-term synaptic plasticity Annu Rev Physiol 64 2002 355 405
    • (2002) Annu Rev Physiol , vol.64 , pp. 355-405
    • Zucker, R.S.1    Regehr, W.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.