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Volumn 32, Issue 4, 2013, Pages 545-558

The phenomenon of synaptic vesicle clustering as the prefusion state in the model system of exocytosis

Author keywords

Antiepileptic drugs; Cell free system; Cholesterol; Membrane fusion; Synaptic vesicle aggregation

Indexed keywords

CALCIUM ION; CHOLESTEROL; CYTOPLASM PROTEIN; ETHOSUXIMIDE; SPIDER VENOM; VALPROIC ACID;

EID: 84893665087     PISSN: 02315882     EISSN: 13384325     Source Type: Journal    
DOI: 10.4149/gpb_2013037     Document Type: Article
Times cited : (5)

References (69)
  • 1
    • 25844468999 scopus 로고    scopus 로고
    • Cholesterol content regulates acrosomal exocytosis by enhancing Rab3A plasma membrane association
    • Belmonte S. A., Lopez C. I., Roggero C. M., De Blas G. A., Tomes C. N., Mayorga L. S. (2005): Cholesterol content regulates acrosomal exocytosis by enhancing Rab3A plasma membrane association. Dev. Biol. 285, 393-408 http://dx.doi.org/10.1016/j.ydbio.2005.07.001
    • (2005) Dev. Biol. , vol.285 , pp. 393-408
    • Belmonte, S.A.1    Lopez, C.I.2    Roggero, C.M.3    De Blas, G.A.4    Tomes, C.N.5    Mayorga, L.S.6
  • 2
    • 0024506755 scopus 로고
    • Electrostatic and hydrophobic interactions of synapsin i and synapsin i fragments with phospholipid bilayers
    • Benfenati F., Greengard P., Brunner J., Bahler M. (1989): Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers. J. Cell Biol. 108, 1851-1862 http://dx.doi.org/10.1083/ jcb.108.5.1851
    • (1989) J. Cell Biol. , vol.108 , pp. 1851-1862
    • Benfenati, F.1    Greengard, P.2    Brunner, J.3    Bahler, M.4
  • 3
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E. G., Dyer W. J. (1959): A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37, 911-917 http://dx.doi.org/10. 1139/o59-099
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 4
    • 77049110746 scopus 로고    scopus 로고
    • Cholesterol depletion attenuates tonic release but increases the ambient level of glutamate in rat brain synaptosomes
    • Borisova T., Krisanova N., Sivko R., Borysov A. (2010a): Cholesterol depletion attenuates tonic release but increases the ambient level of glutamate in rat brain synaptosomes. Neurochem. Int. 56, 466-478 http://dx.doi.org/10. 1016/j.neuint.2009.12.006
    • (2010) Neurochem. Int. , vol.56 , pp. 466-478
    • Borisova, T.1    Krisanova, N.2    Sivko, R.3    Borysov, A.4
  • 5
    • 77957720789 scopus 로고    scopus 로고
    • Diverse presynaptic mechanisms underlying methyl-beta-cyclodextrin - Mediated changes in glutamate transport
    • Borisova T., Sivko R., Borysov A., Krisanova N. (2010b): Diverse presynaptic mechanisms underlying methyl-beta-cyclodextrin - mediated changes in glutamate transport. Cell. Mol. Neurobiol. 30, 1013-1023 http://dx.doi.org/10. 1007/s10571-010-9532-x
    • (2010) Cell. Mol. Neurobiol. , vol.30 , pp. 1013-1023
    • Borisova, T.1    Sivko, R.2    Borysov, A.3    Krisanova, N.4
  • 6
    • 80255138169 scopus 로고    scopus 로고
    • The proton gradient of secretory granules and glutamate transport in blood platelets during cholesterol depletion of the plasma membrane by methyl-β-cyclodextrin
    • Borisova T., Kasatkina L., Ostapchenko L. (2011): The proton gradient of secretory granules and glutamate transport in blood platelets during cholesterol depletion of the plasma membrane by methyl-β-cyclodextrin. Neurochem. Int. 59, 965-975 http://dx.doi.org/10.1016/j.neuint.2011.07.007
    • (2011) Neurochem. Int. , vol.59 , pp. 965-975
    • Borisova, T.1    Kasatkina, L.2    Ostapchenko, L.3
  • 7
    • 38849201796 scopus 로고    scopus 로고
    • Cholesterol in islet dysfunction and type 2 diabetes
    • Brunham L. R., Kruit J. K., Verchere C. B., Hayden M. R. (2008): Cholesterol in islet dysfunction and type 2 diabetes. J. Clin. Invest. 118, 403-408 http://dx.doi.org/10.1172/JCI33296
    • (2008) J. Clin. Invest. , vol.118 , pp. 403-408
    • Brunham, L.R.1    Kruit, J.K.2    Verchere, C.B.3    Hayden, M.R.4
  • 9
    • 34548433783 scopus 로고    scopus 로고
    • Neuronal fusion pore assembly requires membrane cholesterol
    • Cho W. J., Jeremic A., Jin H., Ren G., Jena B. P. (2007): Neuronal fusion pore assembly requires membrane cholesterol. Cell. Biol. Int. 31, 1301-1308 http://dx.doi.org/10.1016/j.cellbi.2007.06.011
    • (2007) Cell. Biol. Int. , vol.31 , pp. 1301-1308
    • Cho, W.J.1    Jeremic, A.2    Jin, H.3    Ren, G.4    Jena, B.P.5
  • 10
    • 0030695849 scopus 로고    scopus 로고
    • Use of cyclodextrins for manipulating cellular cholesterol content
    • Christian A. E., Haynes M. P., Phillips M. C., Rothblat G. H. (1997): Use of cyclodextrins for manipulating cellular cholesterol content. J. Lipid. Res. 38, 2264-2272
    • (1997) J. Lipid. Res. , vol.38 , pp. 2264-2272
    • Christian, A.E.1    Haynes, M.P.2    Phillips, M.C.3    Rothblat, G.H.4
  • 11
    • 27844526588 scopus 로고    scopus 로고
    • Cholesterol facilitates the native mechanism of Ca2+-triggered membrane fusion
    • Churchward M. A., Rogasevskaia T., Hofgen J., Bau J., Coorssen J. R. (2005): Cholesterol facilitates the native mechanism of Ca2+-triggered membrane fusion. J. Cell. Sci. 118, 4833-4848 http://dx.doi.org/10.1242/jcs.02601
    • (2005) J. Cell. Sci. , vol.118 , pp. 4833-4848
    • Churchward, M.A.1    Rogasevskaia, T.2    Hofgen, J.3    Bau, J.4    Coorssen, J.R.5
  • 12
    • 12844274908 scopus 로고    scopus 로고
    • Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions
    • Ciufo L. F., Barclay J. W., Burgoyne R. D., Morgan A. (2005): Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions. Mol. Biol. Cell. 16, 470-482 http://dx.doi.org/10.1091/mbc.E04-08- 0685
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 470-482
    • Ciufo, L.F.1    Barclay, J.W.2    Burgoyne, R.D.3    Morgan, A.4
  • 13
    • 0017813945 scopus 로고
    • Calcium dependent neurotransmitter release and protein phosphorylation in synaptic vesicles
    • de Lorenzo R. J., Freedman S. D. (1978): Calcium dependent neurotransmitter release and protein phosphorylation in synaptic vesicles. Biochem. Biophys. Res. Commun. 80, 183-192 http://dx.doi.org/10.1016/0006- 291X(78)91121-X
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 183-192
    • De Lorenzo, R.J.1    Freedman, S.D.2
  • 14
    • 0014057051 scopus 로고
    • Ultrastructural and enzymic studies of cholinergic and noncholinergic synaptic membranes isolated from brain cortex
    • de Lores Arnaiz G. R., Alverci M., de Robertis E. (1967): Ultrastructural and enzymic studies of cholinergic and noncholinergic synaptic membranes isolated from brain cortex. J. Neurochem. 14, 215-225 http://dx.doi.org/10.1111/ j.1471-4159.1967.tb05897.x
    • (1967) J. Neurochem. , vol.14 , pp. 215-225
    • De Lores-Arnaiz, G.R.1    Alverci, M.2    De Robertis, E.3
  • 15
    • 54949110127 scopus 로고    scopus 로고
    • Docking of secretory vesicles is syntaxin dependent
    • de Wit H., Cornelisse L. N., Toonen R. F., Verhage M. (2006): Docking of secretory vesicles is syntaxin dependent. PLoS One 27, e126 http://dx.doi.org/ 10.1371/journal.pone.0000126
    • (2006) PLoS One , vol.27
    • De Wit, H.1    Cornelisse, L.N.2    Toonen, R.F.3    Verhage, M.4
  • 16
    • 69449108209 scopus 로고    scopus 로고
    • Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes
    • de Wit H., Walter A. M., Milosevic I., Gulyas-Kovacs A., Riedel D., Sorensen J. B., Verhage M. (2009): Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes. Cell 138, 935-946 http://dx.doi.org/10. 1016/j.cell.2009.07.027
    • (2009) Cell , vol.138 , pp. 935-946
    • De Wit, H.1    Walter, A.M.2    Milosevic, I.3    Gulyas-Kovacs, A.4    Riedel, D.5    Sorensen, J.B.6    Verhage, M.7
  • 17
    • 80054722414 scopus 로고    scopus 로고
    • The reserve pool of synaptic vesicles acts as a buffer for proteins involved in synaptic vesicle recycling
    • Denker A., Krohnert K., Buckers J., Neher E., Rizzoli S. O. (2011): The reserve pool of synaptic vesicles acts as a buffer for proteins involved in synaptic vesicle recycling. PNAS 108, 17183-17188 http://dx.doi.org/10.1073/ pnas.1112690108
    • (2011) PNAS , vol.108 , pp. 17183-17188
    • Denker, A.1    Krohnert, K.2    Buckers, J.3    Neher, E.4    Rizzoli, S.O.5
  • 18
    • 77951729758 scopus 로고    scopus 로고
    • Singlevesicle fusion assay reveals munc18-1 binding to the snare core is sufficient for stimulating membrane fusion
    • Diao J., Su Z., Lu X., Yoon T. Y., Shin Y. K., Ha T. (2010): Singlevesicle fusion assay reveals munc18-1 binding to the snare core is sufficient for stimulating membrane fusion. ACS Chem. Neurosci. 1, 168-174 http://dx.doi.org/10.1021/cn900034p
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 168-174
    • Diao, J.1    Su, Z.2    Lu, X.3    Yoon, T.Y.4    Shin, Y.K.5    Ha, T.6
  • 20
    • 33847326814 scopus 로고    scopus 로고
    • Munc18-1 binds directly to the neuronal SNARE complex
    • Dulubova I., Khvotchev M., Liu S., Huryeva I., Sudhof T. C., Rizo J. (2007): Munc18-1 binds directly to the neuronal SNARE complex. PNAS 104, 2697-2702 http://dx.doi.org/10.1073/pnas.0611318104
    • (2007) PNAS , vol.104 , pp. 2697-2702
    • Dulubova, I.1    Khvotchev, M.2    Liu, S.3    Huryeva, I.4    Sudhof, T.C.5    Rizo, J.6
  • 21
    • 7444250811 scopus 로고    scopus 로고
    • Evidence that fast exocytosis can be predominantly mediated by vesicles not docked at active zones in frog saccular hair cells
    • Edmonds B. W, Gregory F. D., Schweizer F. E. (2004): Evidence that fast exocytosis can be predominantly mediated by vesicles not docked at active zones in frog saccular hair cells. J. Physiol. (Lond) 560, 439-450 http://dx.doi.org/10.1113/jphysiol.2004.066035
    • (2004) J. Physiol. (Lond) , vol.560 , pp. 439-450
    • Edmonds, B.W.1    Gregory, F.D.2    Schweizer, F.E.3
  • 22
    • 33744512299 scopus 로고    scopus 로고
    • Cholesterol and the interaction of proteins with membrane domains
    • Epand R. M. (2006): Cholesterol and the interaction of proteins with membrane domains. Prog. Lipid Res. 45, 279-294 http://dx.doi.org/10.1016/j. plipres.2006.02.001
    • (2006) Prog. Lipid Res. , vol.45 , pp. 279-294
    • Epand, R.M.1
  • 23
    • 75749090069 scopus 로고    scopus 로고
    • Quantitative analysis of the native presynaptic cytomatrix by cryoelectron tomography
    • Fernandez-Busnadiego R., Zuber B., Maurer U. E., Cyrklaff M., Baumeister W., Lucic V. (2010): Quantitative analysis of the native presynaptic cytomatrix by cryoelectron tomography. J. Cell. Biol. 188, 145-156 http://dx.doi.org/10. 1083/jcb.200908082
    • (2010) J. Cell. Biol. , vol.188 , pp. 145-156
    • Fernandez-Busnadiego, R.1    Zuber, B.2    Maurer, U.E.3    Cyrklaff, M.4    Baumeister, W.5    Lucic, V.6
  • 24
    • 0036159084 scopus 로고    scopus 로고
    • Transmitter release at the hair cell ribbon synapse
    • Glowatzki E., Fuchs P. A. (2002): Transmitter release at the hair cell ribbon synapse. Nat. Neurosci. 5, 147-154 http://dx.doi.org/10.1038/nn796
    • (2002) Nat. Neurosci. , vol.5 , pp. 147-154
    • Glowatzki, E.1    Fuchs, P.A.2
  • 25
    • 79960313181 scopus 로고    scopus 로고
    • Effects of antiepileptic agents on homotypic fusion of synaptic vesicles
    • Gumenyuk V. P., Volinets G. P., Kuchmerovskaya T. M., Trikash I. O. (2009): Effects of antiepileptic agents on homotypic fusion of synaptic vesicles. Neurophysiology 41, 395-403 http://dx.doi.org/10.1007/s11062-010-9118- 8
    • (2009) Neurophysiology , vol.41 , pp. 395-403
    • Gumenyuk, V.P.1    Volinets, G.P.2    Kuchmerovskaya, T.M.3    Trikash, I.O.4
  • 26
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson P. I., Roth R., Morisaki H., Jahn R., Heuser J. E. (1997): Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535 http://dx.doi.org/10.1016/S0092-8674(00)80512-7
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 27
    • 0028023444 scopus 로고
    • Calcium dependence of the rate of exocytosis in a synaptic terminal
    • Heidelberger R., Heinemann C., Neher E., Matthews G. (1994): Calcium dependence of the rate of exocytosis in a synaptic terminal. Nature. 371, 513-515 http://dx.doi.org/10.1038/371513a0
    • (1994) Nature. , vol.371 , pp. 513-515
    • Heidelberger, R.1    Heinemann, C.2    Neher, E.3    Matthews, G.4
  • 28
    • 0021673527 scopus 로고
    • Fluorescence method for measuring the kinetics of fusion between biological membranes
    • Hoekstra D., de Boer T., Klappe K., Wilschut J. (1984): Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry 23, 5675-5681 http://dx.doi.org/10.1021/bi00319a002
    • (1984) Biochemistry , vol.23 , pp. 5675-5681
    • Hoekstra, D.1    De Boer, T.2    Klappe, K.3    Wilschut, J.4
  • 29
    • 79959461200 scopus 로고    scopus 로고
    • Exocytotic steps in cell-free system after cholesterol deprivation in synaptosomal plasma membranes and synaptic vesicles
    • Humeniuk V. P., Trykash I.O. (2011): Exocytotic steps in cell-free system after cholesterol deprivation in synaptosomal plasma membranes and synaptic vesicles. Ukr. Biokhim. Zh. 83, 53-64
    • (2011) Ukr. Biokhim. Zh. , vol.83 , pp. 53-64
    • Humeniuk, V.P.1    Trykash, I.O.2
  • 30
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R., Südhof T. C. (1999): Membrane fusion and exocytosis. Annu. Rev Biochem. 68, 863-911 http://dx.doi.org/10.1146/annurev.biochem.68.1.863
    • (1999) Annu. Rev Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 31
    • 0017642339 scopus 로고
    • A fluorescence enhancement assay of cell fusion
    • Keller P. M., Person S., Snipes W. (1977): A fluorescence enhancement assay of cell fusion. J. Cell. Sci. 28, 167-177
    • (1977) J. Cell. Sci. , vol.28 , pp. 167-177
    • Keller, P.M.1    Person, S.2    Snipes, W.3
  • 32
    • 0029059605 scopus 로고
    • Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice
    • Li L., Chin L. S., Shupliakov O., Brodin L., Sihra T. S., Hvalby O., Jensen V., Zheng D., McNamara J. O., Greengard P. (1995): Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice. PNAS 92, 9235-9239 http://dx.doi.org/10.1073/pnas.92.20.9235
    • (1995) PNAS , vol.92 , pp. 9235-9239
    • Li, L.1    Chin, L.S.2    Shupliakov, O.3    Brodin, L.4    Sihra, T.S.5    Hvalby, O.6    Jensen, V.7    Zheng, D.8    McNamara, J.O.9    Greengard, P.10
  • 33
    • 0030807735 scopus 로고    scopus 로고
    • Structural organization of the synaptic exocytosis core complex
    • Lin R. C., Scheller R. H. (1997): Structural organization of the synaptic exocytosis core complex. Neuron 19, 1087-1094 http://dx.doi.org/10.1016/S0896- 6273(00)80399-2
    • (1997) Neuron , vol.19 , pp. 1087-1094
    • Lin, R.C.1    Scheller, R.H.2
  • 34
    • 0033681141 scopus 로고    scopus 로고
    • Presynaptic calcium stores underlie large-amplitude miniature IPSCs and spontaneous calcium transients
    • Llano I., Gonzalez J., Caputo C., Lai F. A., Blayney L. M., Tan Y. P., Marty A. (2000): Presynaptic calcium stores underlie large-amplitude miniature IPSCs and spontaneous calcium transients. Nat. Neurosci. 3, 1256-1265 http://dx.doi.org/10.1038/81781
    • (2000) Nat. Neurosci. , vol.3 , pp. 1256-1265
    • Llano, I.1    Gonzalez, J.2    Caputo, C.3    Lai, F.A.4    Blayney, L.M.5    Tan, Y.P.6    Marty, A.7
  • 35
    • 0018178434 scopus 로고
    • Modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell M. A. K., Haas S. M., Bieber L. L., Tolbert N. E. (1978): Modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87, 206-210 http://dx.doi.org/10.1016/0003-2697(78)90586-9
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 36
    • 0033785452 scopus 로고    scopus 로고
    • Racing lipid rafts for synaptic-vesicle formation
    • Martin T. F. (2000): Racing lipid rafts for synaptic-vesicle formation. Nat. Cell. Biol. 2, E9-E11 http://dx.doi.org/10.1038/71392
    • (2000) Nat. Cell. Biol. , vol.2
    • Martin, T.F.1
  • 38
    • 79959284253 scopus 로고    scopus 로고
    • Characterization of nanoparticles intended for drug delivery
    • (Eds.: S. E. McNeil), Humana Press., New Yourk
    • McNeil S. E. (2011): Characterization of nanoparticles intended for drug delivery. In: Methods in Molecular Biology 697 (Eds.: S. E. McNeil) p. 269, Humana Press., New Yourk
    • (2011) Methods in Molecular Biology , vol.697 , pp. 269
    • McNeil, S.E.1
  • 39
    • 84860545681 scopus 로고    scopus 로고
    • Particle size measurements. Fundamentals, practice, quality
    • (Eds. H. G. Merkus), Springer science + Business Media B.V
    • Merkus H. G. (2009): Particle size measurements. fundamentals, practice, quality. In: Particle Ttechnology Sseries. 13 (Eds. H. G. Merkus) p. 536, Springer science + Business Media B.V
    • (2009) Particle Ttechnology Sseries. , vol.13 , pp. 536
    • Merkus, H.G.1
  • 41
    • 36349010892 scopus 로고    scopus 로고
    • Probing the mechanism of exocytosis at the hair cell ribbon synapse
    • Neef A., Khimich D., Pirih P., Riedel D., Wolf F., Moser T. (2007): Probing the mechanism of exocytosis at the hair cell ribbon synapse. J. Neurosci. 27, 12933-12944 http://dx.doi.org/10.1523/JNEUROSCI.1996-07.2007
    • (2007) J. Neurosci. , vol.27 , pp. 12933-12944
    • Neef, A.1    Khimich, D.2    Pirih, P.3    Riedel, D.4    Wolf, F.5    Moser, T.6
  • 42
    • 0036303258 scopus 로고    scopus 로고
    • Facilitation at single synapses probed with optical quantal analysis
    • Oertner T. G., Sabatini B. L., Nimchinsky E. A., Svoboda K. (2002): Facilitation at single synapses probed with optical quantal analysis. Nat. Neurosci. 5, 657-664
    • (2002) Nat. Neurosci. , vol.5 , pp. 657-664
    • Oertner, T.G.1    Sabatini, B.L.2    Nimchinsky, E.A.3    Svoboda, K.4
  • 43
    • 33645123035 scopus 로고    scopus 로고
    • Compound exocytosis: Mechanisms and functional significance
    • Pickett J. A., Edwardson J. M. (2006): Compound exocytosis: mechanisms and functional significance. Traffic 7, 109-116 http://dx.doi.org/10.1111/j. 1600-0854.2005.00372.x
    • (2006) Traffic , vol.7 , pp. 109-116
    • Pickett, J.A.1    Edwardson, J.M.2
  • 45
    • 0032575524 scopus 로고    scopus 로고
    • Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormonestimulated phosphatidylinositol turnover
    • Pike L. J., Miller J. M. (1998): Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormonestimulated phosphatidylinositol turnover. J. Biol. Chem. 273, 22298-22304 http://dx.doi.org/10.1074/jbc.273.35.22298
    • (1998) J. Biol. Chem. , vol.273 , pp. 22298-22304
    • Pike, L.J.1    Miller, J.M.2
  • 46
    • 78651155480 scopus 로고
    • The dependence of contraction and relaxation of muscle fibers from the crab maia squinado on the internal concentration of free calcium ions
    • Portzehl H., Caldwell P. C., Ruegy J. C. (1964): The dependence of contraction and relaxation of muscle fibers from the crab maia squinado on the internal concentration of free calcium ions. Biochim. Biophys. Acta. 79, 581-591
    • (1964) Biochim. Biophys. Acta. , vol.79 , pp. 581-591
    • Portzehl, H.1    Caldwell, P.C.2    Ruegy, J.C.3
  • 47
    • 83255184235 scopus 로고    scopus 로고
    • Cholesterol and synaptic vesicle exocytosis
    • Rosa P., Fratangeli A. (2010): Cholesterol and synaptic vesicle exocytosis. Commun. Integr. Biol. 3, 352-353 http://dx.doi.org/10.4161/cib.3.4. 11831
    • (2010) Commun. Integr. Biol. , vol.3 , pp. 352-353
    • Rosa, P.1    Fratangeli, A.2
  • 48
    • 0037115113 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of a calyx of Held and its postsynaptic principal neuron in the medial nucleus of the trapezoid body
    • Satzler K., Sohl L. F., Bollmann J. H., Borst J. G., Frotscher M., Sakmann B., Lubke J. H. (2002): Three-dimensional reconstruction of a calyx of Held and its postsynaptic principal neuron in the medial nucleus of the trapezoid body. J. Neurosci. 22, 10567-10579
    • (2002) J. Neurosci. , vol.22 , pp. 10567-10579
    • Satzler, K.1    Sohl, L.F.2    Bollmann, J.H.3    Borst, J.G.4    Frotscher, M.5    Sakmann, B.6    Lubke, J.H.7
  • 49
    • 0035095914 scopus 로고    scopus 로고
    • Morphological correlates of functionally defined synaptic vesicle populations
    • Schikorski T., Stevens C. F. (2001): Morphological correlates of functionally defined synaptic vesicle populations. Nat. Neurosci. 4, 391-395 http://dx.doi.org/10.1038/86042
    • (2001) Nat. Neurosci. , vol.4 , pp. 391-395
    • Schikorski, T.1    Stevens, C.F.2
  • 50
    • 58149472205 scopus 로고    scopus 로고
    • The synaptic vesicle cluster: A source of endocytic proteins during neurotransmitter release
    • Shupliakov O. (2009): The synaptic vesicle cluster:a source of endocytic proteins during neurotransmitter release. Neuroscience 158, 204-210 http://dx.doi.org/10.1016/j.neuroscience.2008.03.035
    • (2009) Neuroscience , vol.158 , pp. 204-210
    • Shupliakov, O.1
  • 51
    • 84893696060 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof T. C. (2004): The synaptic vesicle cycle. Annu. Rev. Neurosci. 2, 7509-7547
    • (2004) Annu. Rev. Neurosci. , vol.2 , pp. 7509-7547
    • Sudhof, T.C.1
  • 54
    • 77954543290 scopus 로고    scopus 로고
    • Cholesterol depletion from the plasma membrane impairs proton and glutamate storage in synaptic vesicles of nerve terminals
    • Tarasenko A. S., Sivko R. V., Krisanova N. V., Himmelreich N. H., Borisova T. A. (2010): Cholesterol depletion from the plasma membrane impairs proton and glutamate storage in synaptic vesicles of nerve terminals. J. Mol. Neurosci. 41, 358-367 http://dx.doi.org/10.1007/s12031-010-9351-z
    • (2010) J. Mol. Neurosci. , vol.41 , pp. 358-367
    • Tarasenko, A.S.1    Sivko, R.V.2    Krisanova, N.V.3    Himmelreich, N.H.4    Borisova, T.A.5
  • 55
    • 0037137693 scopus 로고    scopus 로고
    • Optimizing synaptic architecture and efficiency for high-frequency transmission
    • Taschenberger H., Leao R. M., Rowland K. C., Spirou G. A., von Gersdorff H. (2002): Optimizing synaptic architecture and efficiency for high-frequency transmission. Neuron 36, 1127-1143 http://dx.doi.org/10.1016/S0896-6273(02) 01137-6
    • (2002) Neuron , vol.36 , pp. 1127-1143
    • Taschenberger, H.1    Leao, R.M.2    Rowland, K.C.3    Spirou, G.A.4    Von Gersdorff, H.5
  • 56
    • 0033792318 scopus 로고    scopus 로고
    • Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles
    • Thiele C., Hannah M. J., Fahrenholz F., Huttner W. B. (2000): Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles. Nat. Cell Biol. 2, 42-49 http://dx.doi.org/10.1038/71366
    • (2000) Nat. Cell Biol. , vol.2 , pp. 42-49
    • Thiele, C.1    Hannah, M.J.2    Fahrenholz, F.3    Huttner, W.B.4
  • 57
    • 0028028527 scopus 로고
    • Multivesicular release from excitatory synapses of cultured hippocampal neurons
    • Tong G., Jahr C. E. (1994): Multivesicular release from excitatory synapses of cultured hippocampal neurons. Neuron 12, 51-59 http://dx.doi.org/10. 1016/0896-6273(94)90151-1
    • (1994) Neuron , vol.12 , pp. 51-59
    • Tong, G.1    Jahr, C.E.2
  • 58
    • 1442351302 scopus 로고    scopus 로고
    • Modulating effect of the antiseizure drugs on Ca2+-dependent membrane fusion in cell-free model of neurosecretion
    • Trikash I., Humeniuk V. P., Hromov L. O., Syrovats'ka L. P. (2003): Modulating effect of the antiseizure drugs on Ca2+-dependent membrane fusion in cell-free model of neurosecretion. Ukr. Biokhim. Zh. 75, 81-86
    • (2003) Ukr. Biokhim. Zh. , vol.75 , pp. 81-86
    • Trikash, I.1    Humeniuk, V.P.2    Hromov, L.O.3    Syrovats'ka, L.P.4
  • 59
    • 15044345945 scopus 로고    scopus 로고
    • The fusion of isolated synaptic vesicles as a model of final step of exocytosis
    • Trikash I., Gumenyuk V. P., Chernyshov V. I. (2004): The fusion of isolated synaptic vesicles as a model of final step of exocytosis. Neurophysiology 36, 238-246
    • (2004) Neurophysiology , vol.36 , pp. 238-246
    • Trikash, I.1    Gumenyuk, V.P.2    Chernyshov, V.I.3
  • 60
    • 33745650231 scopus 로고    scopus 로고
    • Fusion of synaptic vesicles and plasma membrane in the presense of synaptosomal soluble proteins
    • Trikash I., Kolchinska L. (2006): Fusion of synaptic vesicles and plasma membrane in the presense of synaptosomal soluble proteins. Neurochem. Int. 49, 270-275 http://dx.doi.org/10.1016/j.neuint.2006.01.014
    • (2006) Neurochem. Int. , vol.49 , pp. 270-275
    • Trikash, I.1    Kolchinska, L.2
  • 61
    • 56349145637 scopus 로고    scopus 로고
    • Dockingfusion of synaptic vesicles in cell-free model system of exocytosis
    • Trikash I. O., Volynets G. P., Remenyak O. V., Gorchev V. F. (2008): Dockingfusion of synaptic vesicles in cell-free model system of exocytosis. Neurochem. Int. 53, 401-407 http://dx.doi.org/10.1016/j.neuint.2008.09.010
    • (2008) Neurochem. Int. , vol.53 , pp. 401-407
    • Trikash, I.O.1    Volynets, G.P.2    Remenyak, O.V.3    Gorchev, V.F.4
  • 62
    • 78049470093 scopus 로고    scopus 로고
    • The fusion of synaptic vesicle membranes studied by lipid mixing: The R18 fluorescence assay validity
    • Trikash I., Gumenyuk V., Lishko V. (2010): The fusion of synaptic vesicle membranes studied by lipid mixing: The R18 fluorescence assay validity. Chem. Phys. Lipids 163, 778-786 http://dx.doi.org/10.1016/j.chemphyslip.2010.09.003
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 778-786
    • Trikash, I.1    Gumenyuk, V.2    Lishko, V.3
  • 63
    • 49749084725 scopus 로고    scopus 로고
    • Vesicle docking in regulated exocytosis
    • Verhage M., Sorensen J. B. (2008): Vesicle docking in regulated exocytosis. Traffic 9, 1414-1424 http://dx.doi.org/10.1111/j.1600-0854.2008. 00759.x
    • (2008) Traffic , vol.9 , pp. 1414-1424
    • Verhage, M.1    Sorensen, J.B.2
  • 64
    • 33846785411 scopus 로고    scopus 로고
    • The coupling between synaptic vesicles and Ca2+ channels determines fast neurotransmitter release
    • Wadel K., Neher E., Sakaba T. (2007): The coupling between synaptic vesicles and Ca2+ channels determines fast neurotransmitter release. Neuron 53, 563-575 http://dx.doi.org/10.1016/j.neuron.2007.01.021
    • (2007) Neuron , vol.53 , pp. 563-575
    • Wadel, K.1    Neher, E.2    Sakaba, T.3
  • 65
    • 0035950191 scopus 로고    scopus 로고
    • Multivesicular release at climbing fiber Purkinje cell synapses
    • Wadiche J. I., Jahr C. E. (2001): Multivesicular release at climbing fiber Purkinje cell synapses. Neuron 32, 301-313 http://dx.doi.org/10.1016/ S0896-6273(01)00488-3
    • (2001) Neuron , vol.32 , pp. 301-313
    • Wadiche, J.I.1    Jahr, C.E.2
  • 66
    • 34047204206 scopus 로고    scopus 로고
    • Mechanisms of action of antiepileptic drugs
    • White H. S., Smith M. D., Wilcox K. S. (2007): Mechanisms of action of antiepileptic drugs. Int. Rev. Neurobiol. 81, 85-110 http://dx.doi.org/10.1016/ S0074-7742(06)81006-8
    • (2007) Int. Rev. Neurobiol. , vol.81 , pp. 85-110
    • White, H.S.1    Smith, M.D.2    Wilcox, K.S.3
  • 67
    • 33645891984 scopus 로고    scopus 로고
    • Cholesterol and synaptic transmitter release at crayfish neuromuscular junctions
    • Zamir O., Charlton M. P. (2006): Cholesterol and synaptic transmitter release at crayfish neuromuscular junctions. J. Physiol. 571, 83-99 http://dx.doi.org/10.1113/jphysiol.2005.098319
    • (2006) J. Physiol. , vol.571 , pp. 83-99
    • Zamir, O.1    Charlton, M.P.2
  • 68
    • 70349601231 scopus 로고    scopus 로고
    • Roles of cholesterol in vesicle fusion and motion
    • Zhang J., Xue R., Ong W. Y., Chen P. (2009): Roles of cholesterol in vesicle fusion and motion. Biophys. J. 97, 1371-1380 http://dx.doi.org/10.1016/ j.bpj.2009.06.025
    • (2009) Biophys. J. , vol.97 , pp. 1371-1380
    • Zhang, J.1    Xue, R.2    Ong, W.Y.3    Chen, P.4
  • 69
    • 50449112322 scopus 로고
    • A new method for the direct determination of serum cholesterol
    • Zlatkis A., Zak B., Boyle A. J. (1953): A new method for the direct determination of serum cholesterol. J. Lab. Clin. Med. 41, 486-492
    • (1953) J. Lab. Clin. Med. , vol.41 , pp. 486-492
    • Zlatkis, A.1    Zak, B.2    Boyle, A.J.3


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