메뉴 건너뛰기




Volumn 94, Issue 1, 2000, Pages 10-17

Regulated exocytosis in immune function: Are SNARE-proteins involved?

Author keywords

[No Author keywords available]

Indexed keywords

CD11B ANTIGEN; CD18 ANTIGEN; CELL SURFACE RECEPTOR; RAB PROTEIN; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOPHYSIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN; SYNTAXIN;

EID: 0033997225     PISSN: 09546111     EISSN: None     Source Type: Journal    
DOI: 10.1053/rmed.1999.0700     Document Type: Article
Times cited : (15)

References (72)
  • 1
    • 0030633641 scopus 로고    scopus 로고
    • Asthma: A dynamic disease of inflammation and repair
    • Holgate ST. Asthma: a dynamic disease of inflammation and repair. Ciba Found Symp 1997; 206: 5-28.
    • (1997) Ciba Found Symp , vol.206 , pp. 5-28
    • Holgate, S.T.1
  • 2
    • 0028605507 scopus 로고
    • The role of eosinophils in the pathogenesis of asthma
    • Seminario MC, Gleich GJ. The role of eosinophils in the pathogenesis of asthma. Curr Opin Immunol 1994; 6: 860-864.
    • (1994) Curr Opin Immunol , vol.6 , pp. 860-864
    • Seminario, M.C.1    Gleich, G.J.2
  • 3
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade G. Intracellular aspects of the process of protein synthesis. Science 1975; 189: 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 4
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess TL, Kelly RB. Constitutive and regulated secretion of proteins. Annu Rev Cell Bio! 1987; 3: 243-293.
    • (1987) Annu Rev Cell Bio! , vol.3 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 6
    • 0028143698 scopus 로고
    • Mechanism of intracellular protein transport
    • Rothman JE. Mechanism of intracellular protein transport. Nature 1994; 372: 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 7
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner T, Bennett MK, Whiteheart Sw, Scheller RH, Rothman JE. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 1993; 75: 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Sw, W.3    Scheller, R.H.4    Rothman, J.E.5
  • 8
    • 0030051050 scopus 로고    scopus 로고
    • Synaptic vesicle biogenesis, docking, and fusion: A molecular description
    • Calakos N, Scheller RH. Synaptic vesicle biogenesis, docking, and fusion: a molecular description. Physiol Rev 1996; 76: 1-29.
    • (1996) Physiol Rev , vol.76 , pp. 1-29
    • Calakos, N.1    Scheller, R.H.2
  • 9
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof TC. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 1995; 375: 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Sudhof, T.C.1
  • 10
    • 0027959617 scopus 로고
    • Inhibition of neurotransmitter release by clostridial neurotoxins correlates with specific proteolysis of synaptosomal proteins
    • Blasi J, Binz T, Yamasaki S, Link E, Niemann H, Jahn R. Inhibition of neurotransmitter release by clostridial neurotoxins correlates with specific proteolysis of synaptosomal proteins. J Physiol Paris 1994; 88: 235-241.
    • (1994) J Physiol Paris , vol.88 , pp. 235-241
    • Blasi, J.1    Binz, T.2    Yamasaki, S.3    Link, E.4    Niemann, H.5    Jahn, R.6
  • 11
    • 0031019926 scopus 로고    scopus 로고
    • Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses
    • Schiavo G, Stenbeck G, Rothman JE, Sollner TH. Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses. Proc Natl Acad Sci USA 1997; 94: 997-1001.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Sollner, T.H.4
  • 12
    • 0028963427 scopus 로고
    • Synaptic core complex of synaptobrevin, syntaxin, and SNAP25 forms high affinity alpha-SNAP binding site
    • McMahon HT, Sudhof TC. Synaptic core complex of synaptobrevin, syntaxin, and SNAP25 forms high affinity alpha-SNAP binding site. J Biol Chem 1995; 270:2213-2217.
    • (1995) J Biol Chem , vol.270 , pp. 2213-2217
    • McMahon, H.T.1    Sudhof, T.C.2
  • 13
    • 0028132782 scopus 로고
    • N-ethymaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart SW, Rossnagel K, Buhrow SA, Brunner M, Jaenicke M, Rothman JE. N-ethymaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J Cell Biol 1994; 126: 945-954.
    • (1994) J Cell Biol , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, M.5    Rothman, J.E.6
  • 15
    • 0027328483 scopus 로고
    • The syntaxin family of vesicular transport receptors
    • Bennett MK, Garcia-Arraras JE, Elferink LA, et al. The syntaxin family of vesicular transport receptors. Cell 1993; 74: 863-873.
    • (1993) Cell , vol.74 , pp. 863-873
    • Bennett, M.K.1    Garcia-Arraras, J.E.2    Elferink, L.A.3
  • 16
    • 0032007835 scopus 로고    scopus 로고
    • Endogenous syntaxins 2, 3 and 4 exhibit distinct but overlapping patterns of expression at the hepatocyte plasma membrane
    • Fujita H, Tuma PL, Finnegan CM, Locco L, Hubbard AL. Endogenous syntaxins 2, 3 and 4 exhibit distinct but overlapping patterns of expression at the hepatocyte plasma membrane. Biochem J 1998; 329: 527-538.
    • (1998) Biochem J , vol.329 , pp. 527-538
    • Fujita, H.1    Tuma, P.L.2    Finnegan, C.M.3    Locco, L.4    Hubbard, A.L.5
  • 17
    • 0028260065 scopus 로고
    • Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25
    • Bark IC, Wilson MC. Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25. Gene 1994; 139: 291-292.
    • (1994) Gene , vol.139 , pp. 291-292
    • Bark, I.1    Wilson, M.C.2
  • 18
    • 0026471991 scopus 로고
    • The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess DT, Slater TM, Wilson MC, Skene JH. The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J Neurosci 1992; 12: 4634-4641.
    • (1992) J Neurosci , vol.12 , pp. 4634-4641
    • Hess, D.T.1    Slater, T.M.2    Wilson, M.C.3    Skene, J.H.4
  • 19
    • 0030735370 scopus 로고    scopus 로고
    • Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor formation
    • Fasshauer D, Otto H, Eliason WK, Jahn R, Brunger AT. Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor formation. J Biol Chem 1997; 272: 28036-28041.
    • (1997) J Biol Chem , vol.272 , pp. 28036-28041
    • Fasshauer, D.1    Otto, H.2    Eliason, W.K.3    Jahn, R.4    Brunger, A.T.5
  • 20
    • 0029929223 scopus 로고    scopus 로고
    • Identification of a novel syntaxin- And synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues
    • Ravichandran V, Chawla A, Roche PA. Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues. J Biol Chem 1996; 271: 13300-13303.
    • (1996) J Biol Chem , vol.271 , pp. 13300-13303
    • Ravichandran, V.1    Chawla, A.2    Roche, P.A.3
  • 21
    • 0032562808 scopus 로고    scopus 로고
    • Seven novel mammalian SNARE proteins localize to distinct membrane compartments
    • Advani RJ, Bae HR, Bock JB, et al. Seven novel mammalian SNARE proteins localize to distinct membrane compartments. J Biol Chem 1998; 273: 10317-10324.
    • (1998) J Biol Chem , vol.273 , pp. 10317-10324
    • Advani, R.J.1    Bae, H.R.2    Bock, J.B.3
  • 23
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick S, Jahn R. Vesicle fusion from yeast to man. Nature 1994; 370: 191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 24
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay JC, Scheller RH. SNAREs and NSF in targeted membrane fusion. Curr Opin Cell Biol 1997; 9: 505-512.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 25
    • 0030222771 scopus 로고    scopus 로고
    • Synaptotagmins: C2-domain proteins that regulate membrane traffic
    • Sudhof TC, Rizo J. Synaptotagmins: C2-domain proteins that regulate membrane traffic. Neuron 1996; 17: 379-388.
    • (1996) Neuron , vol.17 , pp. 379-388
    • Sudhof, T.C.1    Rizo, J.2
  • 29
    • 0024328734 scopus 로고    scopus 로고
    • The human Rab genes encode a family of GTP-binding proteins related to yeast YPTI and SEC4 products involved in secretion
    • Zahraoui, A, Touchot N, Chardin P, Tavitian A. The human Rab genes encode a family of GTP-binding proteins related to yeast YPTI and SEC4 products involved in secretion. J Biol Chem 1998; 264: 12394-12401.
    • (1998) J Biol Chem , vol.264 , pp. 12394-12401
    • Zahraoui1    Touchot, N.2    Chardin, P.3    Tavitian, A.4
  • 30
    • 0025221853 scopus 로고
    • Small GTP-binding proteins in vesicular transport
    • Balch WE. Small GTP-binding proteins in vesicular transport. Trends Biochem Sci 1990; 15: 473-477.
    • (1990) Trends Biochem Sci , vol.15 , pp. 473-477
    • Balch, W.E.1
  • 31
    • 0031591692 scopus 로고    scopus 로고
    • Differential expression of Rab3 isoforms during differentiation of pancreatic acinar cell line AR42J
    • Klengel R, Paper A, Pittelkow S, Zeuzem S. Differential expression of Rab3 isoforms during differentiation of pancreatic acinar cell line AR42J. Biochem Biophys Res Commun 1997; 236: 719-722.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 719-722
    • Klengel, R.1    Paper, A.2    Pittelkow, S.3    Zeuzem, S.4
  • 32
    • 0028343430 scopus 로고
    • The role of Rab3A in neurotransmitter release
    • Geppert M, Bolshakov VY, Siegelbaum SA, et al. The role of Rab3A in neurotransmitter release. Nature 1994; 369: 493-497.
    • (1994) Nature , vol.369 , pp. 493-497
    • Geppert, M.1    Bolshakov, V.Y.2    Siegelbaum, S.A.3
  • 33
    • 0030980279 scopus 로고    scopus 로고
    • The small GTP-binding protein Rab3 regulates a late step in synaptic vesicle fusion
    • Geppert M, Goda Y, Stevens CF, Sudhof TC. The small GTP-binding protein Rab3 regulates a late step in synaptic vesicle fusion. Nature 1997; 387: 810-814.
    • (1997) Nature , vol.387 , pp. 810-814
    • Geppert, M.1    Goda, Y.2    Stevens, C.F.3    Sudhof, T.C.4
  • 34
    • 0031052719 scopus 로고    scopus 로고
    • Hrs-2 is an ATPase implicated in calcium-regulated secretion
    • Bean AJ, Seifert R, Chen YA, Sacks R, Scheller RH. Hrs-2 is an ATPase implicated in calcium-regulated secretion. Nature 1997; 385: 826-829.
    • (1997) Nature , vol.385 , pp. 826-829
    • Bean, A.J.1    Seifert, R.2    Chen, Y.A.3    Sacks, R.4    Scheller, R.H.5
  • 35
    • 0028819440 scopus 로고
    • Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine
    • Edelmann L, Hanson PI, Chapman ER, Jahn R. Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. EMBO J 1995; 14: 224-231.
    • (1995) EMBO J , vol.14 , pp. 224-231
    • Edelmann, L.1    Hanson, P.I.2    Chapman, E.R.3    Jahn, R.4
  • 37
    • 0027174208 scopus 로고
    • Control of exocytosis in early neutrophil activation
    • Sengelov H, Kjeldsen L, Borregaard N. Control of exocytosis in early neutrophil activation. J Immunol 1993; 150: 1535-1543.
    • (1993) J Immunol , vol.150 , pp. 1535-1543
    • Sengelov, H.1    Kjeldsen, L.2    Borregaard, N.3
  • 38
    • 0028321701 scopus 로고
    • Calcium-induced translocation of annexins to subcellular organelles of human neutrophils
    • Sjolin C, Stendahl O, Dahlgren C. Calcium-induced translocation of annexins to subcellular organelles of human neutrophils. Biochem J 1994; 300: 325-330.
    • (1994) Biochem J , vol.300 , pp. 325-330
    • Sjolin, C.1    Stendahl, O.2    Dahlgren, C.3
  • 39
    • 0028892237 scopus 로고
    • Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments
    • Brumell JH, Volchuk A, Sengelov H, et al. Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments. J Immunol 1995; 155: 5750-5759.
    • (1995) J Immunol , vol.155 , pp. 5750-5759
    • Brumell, J.H.1    Volchuk, A.2    Sengelov, H.3
  • 41
    • 0031584796 scopus 로고    scopus 로고
    • Identification of two isoforms of the vesicle-membrane fusion protein SNAP-23 in human neutrophils and HL-60 cells
    • Mollinedo F, Lazo PA. Identification of two isoforms of the vesicle-membrane fusion protein SNAP-23 in human neutrophils and HL-60 cells. Biochem Biophys Res Commun 1997; 231: 808-812.
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 808-812
    • Mollinedo, F.1    Lazo, P.A.2
  • 42
    • 0032192480 scopus 로고    scopus 로고
    • Mast cells and basophils in innate immunity
    • Abraham SN, Arock M. Mast cells and basophils in innate immunity. Semin Immunol 1998; 10: 373-381.
    • (1998) Semin Immunol , vol.10 , pp. 373-381
    • Abraham, S.N.1    Arock, M.2
  • 43
    • 0027361976 scopus 로고
    • 2+ and guanine nucleotides: An all-or-none event
    • 2+ and guanine nucleotides: an all-or-none event. J Cell Biol 1993; 123: 585-593.
    • (1993) J Cell Biol , vol.123 , pp. 585-593
    • Hide, I.1    Bennett, J.P.2    Pizzey, A.3
  • 44
    • 0032555722 scopus 로고    scopus 로고
    • Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells
    • Guo Z, Turner C, Castle D. Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells. Cell 1998; 94: 537-548.
    • (1998) Cell , vol.94 , pp. 537-548
    • Guo, Z.1    Turner, C.2    Castle, D.3
  • 46
    • 0027536245 scopus 로고
    • Elevated release of tumor necrosis factor-alpha and interferon-gamma by bronchoalveolar leukocytes from patients with bronchial asthma
    • Cembrzynaska-Nowak M, Szklarz E, Inglot AD, Teodorczyk-Ingeyan JA. Elevated release of tumor necrosis factor-alpha and interferon-gamma by bronchoalveolar leukocytes from patients with bronchial asthma. Am Rev Respir Dis 1993; 147: 291-295.
    • (1993) Am Rev Respir Dis , vol.147 , pp. 291-295
    • Cembrzynaska-Nowak, M.1    Szklarz, E.2    Inglot, A.D.3    Teodorczyk-Ingeyan, J.A.4
  • 48
    • 0029949540 scopus 로고    scopus 로고
    • macrophages. Syntaxins 2, 3, and 4 are present on phagosomal membranes. J Immunol 1996; 156: 4377-4383.
    • (1996) J Immunol , vol.156 , pp. 4377-4383
    • Membranes, A.P.1
  • 49
    • 0029864604 scopus 로고    scopus 로고
    • Tetanus toxin-sensitive VAMP-related proteins are present in murine macrophages
    • Pitzurra L, Rossetto O, Chimienti AR, Blasi E, Bistoni F. Tetanus toxin-sensitive VAMP-related proteins are present in murine macrophages. Cell Immunol 1996; 169: 113-116.
    • (1996) Cell Immunol , vol.169 , pp. 113-116
    • Pitzurra, L.1    Rossetto, O.2    Chimienti, A.R.3    Blasi, E.4    Bistoni, F.5
  • 50
    • 0030991567 scopus 로고    scopus 로고
    • Internalized Listeria monocytogenes modulates intracellular trafficking and delays maturation of the phagosome
    • Alvarez-Dominguez C, Roberts R, Stahl PD. Internalized Listeria monocytogenes modulates intracellular trafficking and delays maturation of the phagosome. J Cell Sei 1997; 110: 731-743.
    • (1997) J Cell Sei , vol.110 , pp. 731-743
    • Alvarez-Dominguez, C.1    Roberts, R.2    Stahl, P.D.3
  • 51
    • 0021299354 scopus 로고
    • Basophils and mast cells: Morphologic insights into their biology, secretory patterns, and function
    • Galli SJ, Dvorak AM, Dovrak HF. Basophils and mast cells: morphologic insights into their biology, secretory patterns, and function. Prog Allergy 1984; 34: 1-141.
    • (1984) Prog Allergy , vol.34 , pp. 1-141
    • Galli, S.J.1    Dvorak, A.M.2    Dovrak, H.F.3
  • 52
    • 0025341908 scopus 로고
    • Intracellular application of guanosine-5′-O-(3-thiotriphosphate) induces exocytotic granule fusion in guinea pig eosinophils
    • Nusse O, Lindau M, Cromwell O, Kay AB, Gomperts BD. Intracellular application of guanosine-5′-O-(3-thiotriphosphate) induces exocytotic granule fusion in guinea pig eosinophils. J Exp Med 1990; 171: 775-786.
    • (1990) J Exp Med , vol.171 , pp. 775-786
    • Nusse, O.1    Lindau, M.2    Cromwell, O.3    Kay, A.B.4    Gomperts, B.D.5
  • 53
    • 33646109224 scopus 로고    scopus 로고
    • Tetanus toxin light chain cleaves a vesicle associated membrane protein (VAMP) isoform 2 in human blood eosinophils and inhibits the release of granule protein
    • Bjerke T, Hoffmann HJH, Karawajczyk M, Dahl R, Knepper M, Nielsen S. Tetanus toxin light chain cleaves a vesicle associated membrane protein (VAMP) isoform 2 in human blood eosinophils and inhibits the release of granule protein. J Exp Med 1999; submitted.
    • (1999) J Exp Med
    • Bjerke, T.1    Hjh, H.2    Karawajczyk, M.3    Dahl, R.4    Knepper, M.5    Nielsen, S.6
  • 55
    • 0030807624 scopus 로고    scopus 로고
    • A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole
    • Darsow T, Reider SE, Emr SD. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. J Ceil Biol 1997; 138: 517-529.
    • (1997) J Ceil Biol , vol.138 , pp. 517-529
    • Darsow, T.1    Reider, S.E.2    Emr, S.D.3
  • 59
    • 0028124309 scopus 로고
    • Association of N-ethylmaleimide-sensitive factor with synaptic vesicles
    • Hong RM, Mori H, Fukui T, et al. Association of N-ethylmaleimide-sensitive factor with synaptic vesicles. FEBS Lett 1994; 350: 253-257.
    • (1994) FEBS Lett , vol.350 , pp. 253-257
    • Hong, R.M.1    Mori, H.2    Fukui, T.3
  • 60
    • 0030954439 scopus 로고    scopus 로고
    • Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles
    • Otto H, Hanson PI, Jahn R. Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles. Proc Natl Acad Sei USA 1997; 94: 6197-6201.
    • (1997) Proc Natl Acad Sei USA , vol.94 , pp. 6197-6201
    • Otto, H.1    Hanson, P.I.2    Jahn, R.3
  • 61
    • 0029075363 scopus 로고
    • The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin
    • Hanson PI, Otto H, Barton N, Jahn R. The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. J Biol Chem 1995; 270: 16955-16961.
    • (1995) J Biol Chem , vol.270 , pp. 16955-16961
    • Hanson, P.I.1    Otto, H.2    Barton, N.3    Jahn, R.4
  • 62
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett MK, Calakos N, Scheller RH. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 1992; 257: 255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 64
    • 0024828306 scopus 로고
    • protein, SNAP-25, differentially expressed by neuronal subpopulations. J Cell Biol 1989; 109: 3039-3052.
    • (1989) J Cell Biol , vol.109 , pp. 3039-3052
  • 65
    • 0031550236 scopus 로고    scopus 로고
    • Tissue distribution of SNAP-23 and its subcellular localization in 3T3-L1 cells
    • Wong PP, Daneman N, Volchuk A, et al. Tissue distribution of SNAP-23 and its subcellular localization in 3T3-L1 cells. Biochem Biophys Res Commun 1997; 230: 64-68.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 64-68
    • Wong, P.P.1    Daneman, N.2    Volchuk, A.3
  • 66
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
    • Baumert M, Maycox PR, Navone F, De CP, Jahn R. Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO J 1989; 8: 379-384.
    • (1989) EMBO J , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De, C.P.4    Jahn, R.5
  • 67
    • 0028919858 scopus 로고
    • Cellubrevin and synaptobrevins: Similar subcellular localization and biochemical properties in PC12 cells
    • Chilcote TJ, Galli T, Mundigl O, et al. Cellubrevin and synaptobrevins: similar subcellular localization and biochemical properties in PC12 cells. J Cell Biol 1995; 129: 219-231.
    • (1995) J Cell Biol , vol.129 , pp. 219-231
    • Chilcote, T.J.1    Galli, T.2    Mundigl, O.3
  • 68
    • 0006602702 scopus 로고    scopus 로고
    • VAMP-1: A synaptic vesicle-associated integral membrane protein
    • Trimble WS, Cowan DM, Scheller RH. VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc Nad Acad Sci USA 1998; 85: 4538-4542.
    • (1998) Proc Nad Acad Sci USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 69
    • 0027402091 scopus 로고
    • SNAP family of NSF attachment proteins includes a brain-specific isoform
    • Whiteheart SW, Griff IC, Brunner M, et al. SNAP family of NSF attachment proteins includes a brain-specific isoform. Nature 1993; 362: 353-355.
    • (1993) Nature , vol.362 , pp. 353-355
    • Whiteheart, S.W.1    Griff, I.C.2    Brunner, M.3
  • 70
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose N, Petrenko AG, Sudhof TC, Jahn R. Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science 1992; 256: 1021-1025.
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Sudhof, T.C.3    Jahn, R.4
  • 71
    • 0028942065 scopus 로고
    • Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin
    • Washbourne P, Schiavo G, Montecucco C. Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin. Biochem J 1995; 305: 721-724.
    • (1995) Biochem J , vol.305 , pp. 721-724
    • Washbourne, P.1    Schiavo, G.2    Montecucco, C.3
  • 72
    • 0022391791 scopus 로고
    • Identification and localization of synaptophysin, an integral membrane glycoprotein of Mr 38,000 characteristic of presynaptic vesicles
    • Wiedenmann B, Franke WW. Identification and localization of synaptophysin, an integral membrane glycoprotein of Mr 38,000 characteristic of presynaptic vesicles. Cell 1985; 41: 1017-1028.
    • (1985) Cell , vol.41 , pp. 1017-1028
    • Wiedenmann, B.1    Franke, W.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.