메뉴 건너뛰기




Volumn 11, Issue 2, 2012, Pages 1163-1174

Protein composition of immunoprecipitated synaptic ribbons

Author keywords

active zone; cochlea; proteomics; retina; synapse; synaptic ribbon; vesicle release

Indexed keywords

IMMUNOGLOBULIN G;

EID: 84856631137     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr2008972     Document Type: Article
Times cited : (28)

References (74)
  • 3
    • 11144256172 scopus 로고    scopus 로고
    • Structure and function of ribbon synapses
    • Sterling, P.; Matthews, G. Structure and function of ribbon synapses Trends Neurosci. 2005, 28, 20-9
    • (2005) Trends Neurosci. , vol.28 , pp. 20-9
    • Sterling, P.1    Matthews, G.2
  • 4
    • 68949150979 scopus 로고    scopus 로고
    • The role of ribbons at sensory synapses
    • LoGiudice, L.; Matthews, G. The role of ribbons at sensory synapses Neuroscientist 2009, 15, 380-91
    • (2009) Neuroscientist , vol.15 , pp. 380-91
    • Logiudice, L.1    Matthews, G.2
  • 5
    • 77953204546 scopus 로고    scopus 로고
    • Onset coding is degraded in auditory nerve fibers from mutant mice lacking synaptic ribbons
    • Buran, B. N.; Strenzke, N.; Neef, A.; Gundelfinger, E. D.; Moser, T.; Liberman, M. C. Onset coding is degraded in auditory nerve fibers from mutant mice lacking synaptic ribbons J. Neurosci. 2010, 30, 7587-97
    • (2010) J. Neurosci. , vol.30 , pp. 7587-97
    • Buran, B.N.1    Strenzke, N.2    Neef, A.3    Gundelfinger, E.D.4    Moser, T.5    Liberman, M.C.6
  • 7
    • 77956850256 scopus 로고    scopus 로고
    • Molecular anatomy of the hair cell's ribbon synapse
    • Uthaiah, R. C.; Hudspeth, A. J. Molecular anatomy of the hair cell's ribbon synapse J. Neurosci. 2010, 30, 12387-99
    • (2010) J. Neurosci. , vol.30 , pp. 12387-99
    • Uthaiah, R.C.1    Hudspeth, A.J.2
  • 8
    • 0029826498 scopus 로고    scopus 로고
    • Purification of synaptic ribbons, structural components of the photoreceptor active zone complex
    • Schmitz, F.; Bechmann, M.; Drenckhahn, D. Purification of synaptic ribbons, structural components of the photoreceptor active zone complex J. Neurosci. 1996, 16, 7109-16
    • (1996) J. Neurosci. , vol.16 , pp. 7109-16
    • Schmitz, F.1    Bechmann, M.2    Drenckhahn, D.3
  • 9
    • 0034525302 scopus 로고    scopus 로고
    • RIBEYE, a component of synaptic ribbons: A protein's journey through evolution provides insight into synaptic ribbon function
    • Schmitz, F.; Konigstorfer, A.; Sudhof, T. C. RIBEYE, a component of synaptic ribbons: a protein's journey through evolution provides insight into synaptic ribbon function Neuron 2000, 28, 857-72
    • (2000) Neuron , vol.28 , pp. 857-72
    • Schmitz, F.1    Konigstorfer, A.2    Sudhof, T.C.3
  • 10
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y.; Oda, Y.; Tabata, T.; Sato, T.; Nagasu, T.; Rappsilber, J.; Mann, M. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein Mol. Cell. Proteomics 2005, 4, 1265-72
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1265-72
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 11
    • 33644745471 scopus 로고    scopus 로고
    • MPP3 is recruited to the MPP5 protein scaffold at the retinal outer limiting membrane
    • Kantardzhieva, A.; Alexeeva, S.; Versteeg, I.; Wijnholds, J. MPP3 is recruited to the MPP5 protein scaffold at the retinal outer limiting membrane FEBS J. 2006, 273, 1152-65
    • (2006) FEBS J. , vol.273 , pp. 1152-65
    • Kantardzhieva, A.1    Alexeeva, S.2    Versteeg, I.3    Wijnholds, J.4
  • 12
    • 21844479018 scopus 로고    scopus 로고
    • ELKS, a protein structurally related to the active zone-associated protein CAST, is expressed in pancreatic beta cells and functions in insulin exocytosis: Interaction of ELKS with exocytotic machinery analyzed by total internal reflection fluorescence microscopy
    • Ohara-Imaizumi, M.; Ohtsuka, T.; Matsushima, S.; Akimoto, Y.; Nishiwaki, C.; Nakamichi, Y.; Kikuta, T.; Nagai, S.; Kawakami, H.; Watanabe, T.; Nagamatsu, S. ELKS, a protein structurally related to the active zone-associated protein CAST, is expressed in pancreatic beta cells and functions in insulin exocytosis: interaction of ELKS with exocytotic machinery analyzed by total internal reflection fluorescence microscopy Mol. Biol. Cell 2005, 16, 3289-300
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3289-300
    • Ohara-Imaizumi, M.1    Ohtsuka, T.2    Matsushima, S.3    Akimoto, Y.4    Nishiwaki, C.5    Nakamichi, Y.6    Kikuta, T.7    Nagai, S.8    Kawakami, H.9    Watanabe, T.10    Nagamatsu, S.11
  • 14
    • 0842324001 scopus 로고    scopus 로고
    • CAST2: Identification and characterization of a protein structurally related to the presynaptic cytomatrix protein CAST
    • Deguchi-Tawarada, M.; Inoue, E.; Takao-Rikitsu, E.; Inoue, M.; Ohtsuka, T.; Takai, Y. CAST2: identification and characterization of a protein structurally related to the presynaptic cytomatrix protein CAST Genes Cells 2004, 9, 15-23
    • (2004) Genes Cells , vol.9 , pp. 15-23
    • Deguchi-Tawarada, M.1    Inoue, E.2    Takao-Rikitsu, E.3    Inoue, M.4    Ohtsuka, T.5    Takai, Y.6
  • 15
    • 1642499114 scopus 로고    scopus 로고
    • Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release
    • Takao-Rikitsu, E.; Mochida, S.; Inoue, E.; Deguchi-Tawarada, M.; Inoue, M.; Ohtsuka, T.; Takai, Y. Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release J. Cell Biol. 2004, 164, 301-11
    • (2004) J. Cell Biol. , vol.164 , pp. 301-11
    • Takao-Rikitsu, E.1    Mochida, S.2    Inoue, E.3    Deguchi-Tawarada, M.4    Inoue, M.5    Ohtsuka, T.6    Takai, Y.7
  • 16
    • 0142242179 scopus 로고    scopus 로고
    • Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins
    • Ko, J.; Na, M.; Kim, S.; Lee, J. R.; Kim, E. Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins J. Biol. Chem. 2003, 278, 42377-85
    • (2003) J. Biol. Chem. , vol.278 , pp. 42377-85
    • Ko, J.1    Na, M.2    Kim, S.3    Lee, J.R.4    Kim, E.5
  • 17
    • 1542289732 scopus 로고    scopus 로고
    • Interaction of ATP sensor, cAMP sensor, Ca2+ sensor, and voltage-dependent Ca2+ channel in insulin granule exocytosis
    • Shibasaki, T.; Sunaga, Y.; Fujimoto, K.; Kashima, Y.; Seino, S. Interaction of ATP sensor, cAMP sensor, Ca2+ sensor, and voltage-dependent Ca2+ channel in insulin granule exocytosis J. Biol. Chem. 2004, 279, 7956-61
    • (2004) J. Biol. Chem. , vol.279 , pp. 7956-61
    • Shibasaki, T.1    Sunaga, Y.2    Fujimoto, K.3    Kashima, Y.4    Seino, S.5
  • 18
    • 0037171801 scopus 로고    scopus 로고
    • RIM binding proteins (RBPs) couple Rab3-interacting molecules (RIMs) to voltage-gated Ca(2+) channels
    • Hibino, H.; Pironkova, R.; Onwumere, O.; Vologodskaia, M.; Hudspeth, A. J.; Lesage, F. RIM binding proteins (RBPs) couple Rab3-interacting molecules (RIMs) to voltage-gated Ca(2+) channels Neuron 2002, 34, 411-23
    • (2002) Neuron , vol.34 , pp. 411-23
    • Hibino, H.1    Pironkova, R.2    Onwumere, O.3    Vologodskaia, M.4    Hudspeth, A.J.5    Lesage, F.6
  • 19
    • 33751298557 scopus 로고    scopus 로고
    • Impact of subunit positioning on GABAA receptor function
    • Sigel, E.; Baur, R.; Boulineau, N.; Minier, F. Impact of subunit positioning on GABAA receptor function Biochem. Soc. Trans. 2006, 34, 868-71
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 868-71
    • Sigel, E.1    Baur, R.2    Boulineau, N.3    Minier, F.4
  • 20
    • 57549108331 scopus 로고    scopus 로고
    • ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas
    • Table of Contents
    • Hong, S.; Pedersen, P. L. ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas Microbiol. Mol. Biol. Rev 2008, 72, 590-641; see Table of Contents
    • (2008) Microbiol. Mol. Biol. Rev , vol.72 , pp. 590-641
    • Hong, S.1    Pedersen, P.L.2
  • 21
    • 0028114231 scopus 로고
    • Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J. P.; Leslie, A. G.; Lutter, R.; Walker, J. E. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria Nature 1994, 370, 621-8
    • (1994) Nature , vol.370 , pp. 621-8
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 26
    • 0028987102 scopus 로고
    • GABAA receptor subunits have differential distributions in the rat retina: In situ hybridization and immunohistochemistry
    • Greferath, U.; Grunert, U.; Fritschy, J. M.; Stephenson, A.; Mohler, H.; Wassle, H. GABAA receptor subunits have differential distributions in the rat retina: in situ hybridization and immunohistochemistry J. Comp. Neurol. 1995, 353, 553-71
    • (1995) J. Comp. Neurol. , vol.353 , pp. 553-71
    • Greferath, U.1    Grunert, U.2    Fritschy, J.M.3    Stephenson, A.4    Mohler, H.5    Wassle, H.6
  • 28
    • 34648840323 scopus 로고    scopus 로고
    • Synaptic contact between melanopsin-containing retinal ganglion cells and rod bipolar cells
    • Ostergaard, J.; Hannibal, J.; Fahrenkrug, J. Synaptic contact between melanopsin-containing retinal ganglion cells and rod bipolar cells Invest. Ophthalmol. Vis. Sci. 2007, 48, 3812-20
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , pp. 3812-20
    • Ostergaard, J.1    Hannibal, J.2    Fahrenkrug, J.3
  • 29
    • 33845981493 scopus 로고    scopus 로고
    • PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex
    • Lo, S. C.; Hannink, M. PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex J. Biol. Chem. 2006, 281, 37893-903
    • (2006) J. Biol. Chem. , vol.281 , pp. 37893-903
    • Lo, S.C.1    Hannink, M.2
  • 30
    • 42649130014 scopus 로고    scopus 로고
    • PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria
    • Lo, S. C.; Hannink, M. PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria Exp. Cell Res. 2008, 314, 1789-803
    • (2008) Exp. Cell Res. , vol.314 , pp. 1789-803
    • Lo, S.C.1    Hannink, M.2
  • 32
    • 1042278171 scopus 로고    scopus 로고
    • Synergistic effects of coactivators GRIP1 and beta-catenin on gene activation: Cross-talk between androgen receptor and Wnt signaling pathways
    • Li, H.; Kim, J. H.; Koh, S. S.; Stallcup, M. R. Synergistic effects of coactivators GRIP1 and beta-catenin on gene activation: cross-talk between androgen receptor and Wnt signaling pathways J. Biol. Chem. 2004, 279, 4212-20
    • (2004) J. Biol. Chem. , vol.279 , pp. 4212-20
    • Li, H.1    Kim, J.H.2    Koh, S.S.3    Stallcup, M.R.4
  • 33
    • 0028981208 scopus 로고
    • Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm, D. L.; Koslov, E. R.; Kebriaei, P.; Cianci, C. D.; Morrow, J. S. Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 8813-7
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8813-7
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 34
    • 0025374899 scopus 로고
    • Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule
    • Ozawa, M.; Ringwald, M.; Kemler, R. Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 4246-50
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4246-50
    • Ozawa, M.1    Ringwald, M.2    Kemler, R.3
  • 35
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; Calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke, V.; Weber, K. Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin EMBO J. 1984, 3, 227-33
    • (1984) EMBO J. , vol.3 , pp. 227-33
    • Gerke, V.1    Weber, K.2
  • 36
    • 0020460868 scopus 로고
    • Nonerythrocyte spectrins: Actin-membrane attachment proteins occurring in many cell types
    • Burridge, K.; Kelly, T.; Mangeat, P. Nonerythrocyte spectrins: actin-membrane attachment proteins occurring in many cell types J. Cell Biol. 1982, 95, 478-86
    • (1982) J. Cell Biol. , vol.95 , pp. 478-86
    • Burridge, K.1    Kelly, T.2    Mangeat, P.3
  • 38
    • 0009470593 scopus 로고
    • Purification of two spectrin-binding proteins: Biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1
    • Tyler, J. M.; Hargreaves, W. R.; Branton, D. Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1 Proc. Natl. Acad. Sci. U.S.A. 1979, 76, 5192-6
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 5192-6
    • Tyler, J.M.1    Hargreaves, W.R.2    Branton, D.3
  • 39
    • 0033598182 scopus 로고    scopus 로고
    • Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrin-vimentin complexes in macrophages
    • Correia, I.; Chu, D.; Chou, Y. H.; Goldman, R. D.; Matsudaira, P. Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrin-vimentin complexes in macrophages J. Cell Biol. 1999, 146, 831-42
    • (1999) J. Cell Biol. , vol.146 , pp. 831-42
    • Correia, I.1    Chu, D.2    Chou, Y.H.3    Goldman, R.D.4    Matsudaira, P.5
  • 40
    • 0025371817 scopus 로고
    • The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction
    • Katsumoto, T.; Mitsushima, A.; Kurimura, T. The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction Biol. Cell 1990, 68, 139-46
    • (1990) Biol. Cell , vol.68 , pp. 139-46
    • Katsumoto, T.1    Mitsushima, A.2    Kurimura, T.3
  • 41
    • 0033790324 scopus 로고    scopus 로고
    • Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery
    • Faigle, W.; Colucci-Guyon, E.; Louvard, D.; Amigorena, S.; Galli, T. Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery Mol. Biol. Cell 2000, 11, 3485-94
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3485-94
    • Faigle, W.1    Colucci-Guyon, E.2    Louvard, D.3    Amigorena, S.4    Galli, T.5
  • 42
    • 0141987893 scopus 로고    scopus 로고
    • Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses
    • Lonart, G.; Schoch, S.; Kaeser, P. S.; Larkin, C. J.; Sudhof, T. C.; Linden, D. J. Phosphorylation of RIM1alpha by PKA triggers presynaptic long-term potentiation at cerebellar parallel fiber synapses Cell 2003, 115, 49-60
    • (2003) Cell , vol.115 , pp. 49-60
    • Lonart, G.1    Schoch, S.2    Kaeser, P.S.3    Larkin, C.J.4    Sudhof, T.C.5    Linden, D.J.6
  • 43
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard, P.; Valtorta, F.; Czernik, A. J.; Benfenati, F. Synaptic vesicle phosphoproteins and regulation of synaptic function Science 1993, 259, 780-5
    • (1993) Science , vol.259 , pp. 780-5
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 44
    • 34047107208 scopus 로고    scopus 로고
    • Liprinalpha1 degradation by calcium/calmodulin-dependent protein kinase II regulates LAR receptor tyrosine phosphatase distribution and dendrite development
    • Hoogenraad, C. C.; Feliu-Mojer, M. I.; Spangler, S. A.; Milstein, A. D.; Dunah, A. W.; Hung, A. Y.; Sheng, M. Liprinalpha1 degradation by calcium/calmodulin-dependent protein kinase II regulates LAR receptor tyrosine phosphatase distribution and dendrite development Dev. Cell 2007, 12, 587-602
    • (2007) Dev. Cell , vol.12 , pp. 587-602
    • Hoogenraad, C.C.1    Feliu-Mojer, M.I.2    Spangler, S.A.3    Milstein, A.D.4    Dunah, A.W.5    Hung, A.Y.6    Sheng, M.7
  • 45
    • 72749107691 scopus 로고    scopus 로고
    • Differential distribution of exchange proteins directly activated by cyclic AMP within the adult rat retina
    • Whitaker, C. M.; Cooper, N. G. Differential distribution of exchange proteins directly activated by cyclic AMP within the adult rat retina Neuroscience 2010, 165, 955-67
    • (2010) Neuroscience , vol.165 , pp. 955-67
    • Whitaker, C.M.1    Cooper, N.G.2
  • 46
    • 25844507819 scopus 로고    scopus 로고
    • CAMP increases Ca2+-dependent exocytosis through both PKA and Epac2 in mouse melanotrophs from pituitary tissue slices
    • Sedej, S.; Rose, T.; Rupnik, M. cAMP increases Ca2+-dependent exocytosis through both PKA and Epac2 in mouse melanotrophs from pituitary tissue slices J. Physiol. 2005, 567, 799-813
    • (2005) J. Physiol. , vol.567 , pp. 799-813
    • Sedej, S.1    Rose, T.2    Rupnik, M.3
  • 48
    • 0038504029 scopus 로고    scopus 로고
    • Interactions between Piccolo and the actin/dynamin-binding protein Abp1 link vesicle endocytosis to presynaptic active zones
    • Fenster, S. D.; Kessels, M. M.; Qualmann, B.; Chung, W. J.; Nash, J.; Gundelfinger, E. D.; Garner, C. C. Interactions between Piccolo and the actin/dynamin-binding protein Abp1 link vesicle endocytosis to presynaptic active zones J. Biol. Chem. 2003, 278, 20268-77
    • (2003) J. Biol. Chem. , vol.278 , pp. 20268-77
    • Fenster, S.D.1    Kessels, M.M.2    Qualmann, B.3    Chung, W.J.4    Nash, J.5    Gundelfinger, E.D.6    Garner, C.C.7
  • 55
    • 33644821441 scopus 로고    scopus 로고
    • The multiple activities of CtBP/BARS proteins: The Golgi view
    • Corda, D.; Colanzi, A.; Luini, A. The multiple activities of CtBP/BARS proteins: the Golgi view Trends Cell Biol. 2006, 16, 167-73
    • (2006) Trends Cell Biol. , vol.16 , pp. 167-73
    • Corda, D.1    Colanzi, A.2    Luini, A.3
  • 56
    • 65649126338 scopus 로고    scopus 로고
    • CtBP1/BARS is an activator of phospholipase D1 necessary for agonist-induced macropinocytosis
    • Haga, Y.; Miwa, N.; Jahangeer, S.; Okada, T.; Nakamura, S. CtBP1/BARS is an activator of phospholipase D1 necessary for agonist-induced macropinocytosis EMBO J. 2009, 28, 1197-207
    • (2009) EMBO J. , vol.28 , pp. 1197-207
    • Haga, Y.1    Miwa, N.2    Jahangeer, S.3    Okada, T.4    Nakamura, S.5
  • 57
    • 0345687308 scopus 로고    scopus 로고
    • Mechanism of constitutive export from the golgi: Bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains
    • Polishchuk, E. V.; Di Pentima, A.; Luini, A.; Polishchuk, R. S. Mechanism of constitutive export from the golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains Mol. Biol. Cell 2003, 14, 4470-85
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4470-85
    • Polishchuk, E.V.1    Di Pentima, A.2    Luini, A.3    Polishchuk, R.S.4
  • 59
    • 0036221752 scopus 로고    scopus 로고
    • Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport
    • Monier, S.; Jollivet, F.; Janoueix-Lerosey, I.; Johannes, L.; Goud, B. Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport Traffic 2002, 3, 289-97
    • (2002) Traffic , vol.3 , pp. 289-97
    • Monier, S.1    Jollivet, F.2    Janoueix-Lerosey, I.3    Johannes, L.4    Goud, B.5
  • 60
    • 0037195108 scopus 로고    scopus 로고
    • A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones
    • Wang, Y.; Liu, X.; Biederer, T.; Sudhof, T. C. A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 14464-9
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14464-9
    • Wang, Y.1    Liu, X.2    Biederer, T.3    Sudhof, T.C.4
  • 61
    • 67649344114 scopus 로고    scopus 로고
    • Involvement of ELKS, an active zone protein, in exocytotic release from RBL-2H3 cells
    • Nomura, H.; Ohtsuka, T.; Tadokoro, S.; Tanaka, M.; Hirashima, N. Involvement of ELKS, an active zone protein, in exocytotic release from RBL-2H3 cells Cell Immunol. 2009, 258, 204-11
    • (2009) Cell Immunol. , vol.258 , pp. 204-11
    • Nomura, H.1    Ohtsuka, T.2    Tadokoro, S.3    Tanaka, M.4    Hirashima, N.5
  • 73
    • 0037442516 scopus 로고    scopus 로고
    • Bulk membrane retrieval in the synaptic terminal of retinal bipolar cells
    • Holt, M.; Cooke, A.; Wu, M. M.; Lagnado, L. Bulk membrane retrieval in the synaptic terminal of retinal bipolar cells J. Neurosci. 2003, 23, 1329-39
    • (2003) J. Neurosci. , vol.23 , pp. 1329-39
    • Holt, M.1    Cooke, A.2    Wu, M.M.3    Lagnado, L.4
  • 74
    • 0037079068 scopus 로고    scopus 로고
    • Depolarization redistributes synaptic membrane and creates a gradient of vesicles on the synaptic body at a ribbon synapse
    • Lenzi, D.; Crum, J.; Ellisman, M. H.; Roberts, W. M. Depolarization redistributes synaptic membrane and creates a gradient of vesicles on the synaptic body at a ribbon synapse Neuron 2002, 36, 649-59
    • (2002) Neuron , vol.36 , pp. 649-59
    • Lenzi, D.1    Crum, J.2    Ellisman, M.H.3    Roberts, W.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.