메뉴 건너뛰기




Volumn 191, Issue , 1999, Pages 201-255

Synaptic-like microuesicles in mammalian pinealocytes

Author keywords

Melatonin; Neuroactive amino acids; Neuroendocrine cells; Paracrine communication; Pineal gland; Secretory vesicles; Synaptic membrane proteins

Indexed keywords

MEMBRANE PROTEIN;

EID: 0033010378     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)60160-6     Document Type: Article
Times cited : (22)

References (294)
  • 1
    • 0026516633 scopus 로고
    • A family of proteins involved in intracellular transport
    • Aalto, M. K., Keranen, S., and Rönne, H. (1992). A family of proteins involved in intracellular transport. Cell 68, 181-182.
    • (1992) Cell , vol.68 , pp. 181-182
    • Aalto, M.K.1    Keranen, S.2    Rönne, H.3
  • 2
    • 0026526404 scopus 로고
    • The amphicrine pancreatic cell line, AR42J, secretes GABA and amylase by separate regulated pathways
    • Ahnert-Hilger, G., and Wiedenmann, B. (1992). The amphicrine pancreatic cell line, AR42J, secretes GABA and amylase by separate regulated pathways. FEBS Lett. 314, 41-44.
    • (1992) FEBS Lett. , vol.314 , pp. 41-44
    • Ahnert-Hilger, G.1    Wiedenmann, B.2
  • 4
    • 0026757008 scopus 로고
    • Calcium-dependent transmitter secretion reconstituted in Xenopus oocytes: Requirement for synaptophysin
    • Alder, J., Lu, B., Valtorta, F., Greengard, P., and Poo, M. (1992a). Calcium-dependent transmitter secretion reconstituted in Xenopus oocytes: Requirement for synaptophysin. Science 257, 657-661.
    • (1992) Science , vol.257 , pp. 657-661
    • Alder, J.1    Lu, B.2    Valtorta, F.3    Greengard, P.4    Poo, M.5
  • 5
    • 0026767456 scopus 로고
    • Antibodies to synaptophysin interfere with transmitter secretion at neuromuscular synapses
    • Alder, J., Xie, Z., Valtorta, F., Greengard, P., and Poo, M. (1992b). Antibodies to synaptophysin interfere with transmitter secretion at neuromuscular synapses. Neuron 9, 759-768.
    • (1992) Neuron , vol.9 , pp. 759-768
    • Alder, J.1    Xie, Z.2    Valtorta, F.3    Greengard, P.4    Poo, M.5
  • 6
    • 0028800496 scopus 로고
    • Overexpression of synaptophysin enhances neurotransmitter secretion at Xenopus neuromuscular synapses
    • Alder, J., Kanki, H., Valtorta, F., Greengard, P., and Poo, M. (1995). Overexpression of synaptophysin enhances neurotransmitter secretion at Xenopus neuromuscular synapses. J. Neurosci. 15, 511-519.
    • (1995) J. Neurosci. , vol.15 , pp. 511-519
    • Alder, J.1    Kanki, H.2    Valtorta, F.3    Greengard, P.4    Poo, M.5
  • 7
    • 0027322820 scopus 로고
    • Catecholamines are present in a synaptic-like microvesicle-enriched fraction from bovine adrenal medulla
    • Annaert, W. G., Llona, I., Backer, A. C, Jacob, W. A., and De Potter, V. P. (1993). Catecholamines are present in a synaptic-like microvesicle-enriched fraction from bovine adrenal medulla. J. Neurochem. 60, 1746-1754
    • (1993) J. Neurochem. , vol.60 , pp. 1746-1754
    • Annaert, W.G.1    Llona, I.2    Backer, A.C.3    Jacob, W.A.4    De Potter, V.P.5
  • 9
    • 0002847716 scopus 로고
    • Electron microscopic studies on the structure and histochemistry of the pineal gland of the rat
    • Arstila, A. U. (1967). Electron microscopic studies on the structure and histochemistry of the pineal gland of the rat. Neiiroendocrinology 2(Suppl.), 1-101.
    • (1967) Neiiroendocrinology , vol.2 , Issue.SUPPL. , pp. 1-101
    • Arstila, A.U.1
  • 10
    • 0023201681 scopus 로고
    • Synapsin I bundles F-actin in a phosphorylationdependent manner
    • Bähler, M., and Greengard, P. (1987). Synapsin I bundles F-actin in a phosphorylationdependent manner. Nature 326, 704-707.
    • (1987) Nature , vol.326 , pp. 704-707
    • Bähler, M.1    Greengard, P.2
  • 11
    • 0025280151 scopus 로고
    • Synaptophysin: A substrate for the protein tyrosine kinase pp60c-src in intact synaptic vesicles
    • Barnekow, A., Jahn, R., and Schartl, M. (1990). Synaptophysin: A substrate for the protein tyrosine kinase pp60c-src in intact synaptic vesicles. Oncogene 5, 1019-1024.
    • (1990) Oncogene , vol.5 , pp. 1019-1024
    • Barnekow, A.1    Jahn, R.2    Schartl, M.3
  • 12
    • 0027305511 scopus 로고
    • Glutamate and GABA in retinal circuitry
    • Barnstable, C. J. (1993). Glutamate and GABA in retinal circuitry. Curr. Opin. Neurobiol. 3, 520-525.
    • (1993) Curr. Opin. Neurobiol. , vol.3 , pp. 520-525
    • Barnstable, C.J.1
  • 14
    • 0022071726 scopus 로고
    • A marker of early amacrine cell development in rat retina
    • Barnstable, C. J., Hofstein, R., and Akagawa, K. (1985). A marker of early amacrine cell development in rat retina. Dev. Brain Res. 20, 286-290.
    • (1985) Dev. Brain Res. , vol.20 , pp. 286-290
    • Barnstable, C.J.1    Hofstein, R.2    Akagawa, K.3
  • 15
    • 0027179911 scopus 로고
    • Selective storage of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin
    • Bauerfeind, R., Régnier-Vigouroux, A., Flatmark, T., and Huttner, W. B. (1993). Selective storage of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin. Neuron 11,105-121.
    • (1993) Neuron , vol.11 , pp. 105-121
    • Bauerfeind, R.1    Régnier-Vigouroux, A.2    Flatmark, T.3    Huttner, W.B.4
  • 16
    • 0029037547 scopus 로고
    • Synaptotagmin I- And II-deficient PC12 cells exhibit calcium-independent depolarization-induced neurotransmitter release from synaptic-like microvesicles
    • Bauerfeind, R., Jelinek, R., and Huttner, W. B. (1995). Synaptotagmin I- and II-deficient PC12 cells exhibit calcium-independent depolarization-induced neurotransmitter release from synaptic-like microvesicles. FEBS Lett. 364, 328-334.
    • (1995) FEBS Lett. , vol.364 , pp. 328-334
    • Bauerfeind, R.1    Jelinek, R.2    Huttner, W.B.3
  • 17
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
    • Baumert, M., Maycox, P. R., Navone, F., De Camilli, P., and Jahn, R. (1989). Synaptobrevin: An integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO J. 8, 379-384.
    • (1989) EMBO J. , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De Camilli, P.4    Jahn, R.5
  • 19
    • 0017659682 scopus 로고
    • Orcadian rhythm in the number of granulated vesicles in the pinealocytes of mice
    • Benson, B., and Krasovich, M. (1977). Orcadian rhythm in the number of granulated vesicles in the pinealocytes of mice. Cell Tissue Res. 184, 499-506.
    • (1977) Cell Tissue Res. , vol.184 , pp. 499-506
    • Benson, B.1    Krasovich, M.2
  • 20
    • 0025356030 scopus 로고
    • Homology and analogy in transmembrane channel design: Lessons from synaptic membrane proteins
    • Betz, H. (1990). Homology and analogy in transmembrane channel design: Lessons from synaptic membrane proteins. Biochemistry 29, 3591-3599.
    • (1990) Biochemistry , vol.29 , pp. 3591-3599
    • Betz, H.1
  • 21
    • 0030862358 scopus 로고    scopus 로고
    • Developmental expression pattern of phototransduction components in mammalian pineal implies a light-sensing function
    • Blackshaw, S., and Snyder, S. H. (1997). Developmental expression pattern of phototransduction components in mammalian pineal implies a light-sensing function.J. Neitrosci. 17,8074-8082.
    • (1997) J. Neitrosci. , vol.17 , pp. 8074-8082
    • Blackshaw, S.1    Snyder, S.H.2
  • 23
    • 0027432376 scopus 로고
    • Botulinum neurotoxin Cl blocks neurotransmitter release by means of cleaving HPC-1/syntaxin
    • Blasi, J., Chapman, E. R., Yamasaki, S., Binz, T., Niemann, H., and Jahn, R. (1993b). Botulinum neurotoxin Cl blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J. 12, 4821-4828.
    • (1993) EMBO J. , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamasaki, S.3    Binz, T.4    Niemann, H.5    Jahn, R.6
  • 25
    • 0343118137 scopus 로고    scopus 로고
    • Cholecystokinin (CCK-8) modulates vesicular release of excitatory amino acids in rat hippocampal nerve endings
    • Breukel, A. I., Lopes-da-Silva, F. H., and Ghijsen, W. E. (1997). Cholecystokinin (CCK-8) modulates vesicular release of excitatory amino acids in rat hippocampal nerve endings. Neurosci. Lett. 234, 67-70.
    • (1997) Neurosci. Lett. , vol.234 , pp. 67-70
    • Breukel, A.I.1    Lopes-da-Silva, F.H.2    Ghijsen, W.E.3
  • 26
    • 0029093329 scopus 로고
    • Deletion of syntaxin (t-SNARE) and synaptobrevin (v-SNARE) from the synapse: A test of the SNARE hypothesis of targeted vesicle exocytosis
    • Broadie, K., Prokop, A., Bellen, H. J., O'Kane, C. J., Schulze, K. L., and Sweeney, S. T. (1995). Deletion of syntaxin (t-SNARE) and synaptobrevin (v-SNARE) from the synapse: A test of the SNARE hypothesis of targeted vesicle exocytosis. Neuron 15, 663-673.
    • (1995) Neuron , vol.15 , pp. 663-673
    • Broadie, K.1    Prokop, A.2    Bellen, H.J.3    O'Kane, C.J.4    Schulze, K.L.5    Sweeney, S.T.6
  • 27
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose, N., Petrenko, A. G., Südhof, T. C-, and Jahn, R. (1992). Synaptotagmin: A calcium sensor on the synaptic vesicle surface. Science 256,1021-1025.
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Südhof, T.C.3    Jahn, R.4
  • 28
    • 0031149356 scopus 로고    scopus 로고
    • The DnaJ-like cystein string protein and exocytotic neurotransmitter release
    • Buchner, E., and Gundersen, C. B. (1997). The DnaJ-like cystein string protein and exocytotic neurotransmitter release. Trends Neurosci. 20, 223-227.
    • (1997) Trends Neurosci. , vol.20 , pp. 223-227
    • Buchner, E.1    Gundersen, C.B.2
  • 29
    • 0023576669 scopus 로고
    • Cloning and sequence analysis of cDNA encoding p38, a major synaptic vesicle protein
    • Buckley, K. M., Floor, E., and Kelly, R. B. (1987). Cloning and sequence analysis of cDNA encoding p38, a major synaptic vesicle protein. J. Cell Biol. 105, 2447-2456.
    • (1987) J. Cell Biol. , vol.105 , pp. 2447-2456
    • Buckley, K.M.1    Floor, E.2    Kelly, R.B.3
  • 30
    • 0027971368 scopus 로고
    • Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle
    • Calakos, N., and Scheller, R. H. (1994). Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle. J. Biol. Chem. 269, 24534-24537.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24534-24537
    • Calakos, N.1    Scheller, R.H.2
  • 31
    • 0030051050 scopus 로고    scopus 로고
    • Synaptic vesicle biogenesis, docking, and fusion: A molecular description
    • Calakos, N., and Scheller, R. H. (1996). Synaptic vesicle biogenesis, docking, and fusion: A molecular description. Physiol. Rev. 76, 1-29.
    • (1996) Physiol. Rev. , vol.76 , pp. 1-29
    • Calakos, N.1    Scheller, R.H.2
  • 32
    • 0026048669 scopus 로고
    • Colocalization ofsynaptophysin with transferrin receptors: Implications for synaptic vesicle biogenesis
    • Cameron, P. L., Südhof, T. C, Jahn, R., and De Camilli, P. (1991). Colocalization ofsynaptophysin with transferrin receptors: Implications for synaptic vesicle biogenesis. J. Cell Biol. 115, 151-164.
    • (1991) J. Cell Biol. , vol.115 , pp. 151-164
    • Cameron, P.L.1    Südhof, T.C.2    Jahn, R.3    De Camilli, P.4
  • 33
    • 0027748731 scopus 로고
    • Traffic of synaptic vesicle proteins in polarized and nonpolarized cells
    • Cameron, P., Mundigl, O., and De Camilli, P. (1993). Traffic of synaptic vesicle proteins in polarized and nonpolarized cells. J. Cell Sci. (Suppl. 17), 93-100.
    • (1993) J. Cell Sci. , Issue.17 SUPPL. , pp. 93-100
    • Cameron, P.1    Mundigl, O.2    De Camilli, P.3
  • 34
    • 0023614160 scopus 로고
    • Cellular and molecular mechanisms controlling melatonin release by mammalian pineal glands
    • Cardinal!, D. P., and Vacas, M. I. (1987). Cellular and molecular mechanisms controlling melatonin release by mammalian pineal glands. Cell. Mol. Neiirobiol. 7, 323-337.
    • (1987) Cell. Mol. Neiirobiol. , vol.7 , pp. 323-337
    • Cardinal, D.P.1    Vacas, M.I.2
  • 35
    • 0030330932 scopus 로고    scopus 로고
    • SV2 proteoglycan: A potential synaptic vesicle transporter and nerve terminal extracellular matrix receptor
    • Carlson, S. S. (1996). SV2 proteoglycan: A potential synaptic vesicle transporter and nerve terminal extracellular matrix receptor. Perspect. Dev. Neurobiol. 3, 373-386.
    • (1996) Perspect. Dev. Neurobiol. , vol.3 , pp. 373-386
    • Carlson, S.S.1
  • 36
    • 0023905895 scopus 로고
    • Dual receptor regulation of cyclic nucleotides: ArAdrenergic potentiation of vasoactive intestinal peptide stimulation of pinealocyte adenosine 3',5'-monophosphate
    • Chik, C. L., Ho, A. K., and Klein, D. C. (1988). Dual receptor regulation of cyclic nucleotides: arAdrenergic potentiation of vasoactive intestinal peptide stimulation of pinealocyte adenosine 3',5'-monophosphate. Endocrinology 122,1646-1651.
    • (1988) Endocrinology , vol.122 , pp. 1646-1651
    • Chik, C.L.1    Ho, A.K.2    Klein, D.C.3
  • 37
    • 0028919858 scopus 로고
    • Cellubrevin and synaptobrevins: Similar subcellular localization and biochemical properties in PC12 cells
    • Chilcote, T. J., Galli, T., Mundigl, O., Edelmann, L., McPherson, P. S., Takei, K., and De Camilli, P. (1995). Cellubrevin and synaptobrevins: Similar subcellular localization and biochemical properties in PC12 cells. J. Cell Biol. 129, 219-231.
    • (1995) J. Cell Biol. , vol.129 , pp. 219-231
    • Chilcote, T.J.1    Galli, T.2    Mundigl, O.3    Edelmann, L.4    McPherson, P.S.5    Takei, K.6    De Camilli, P.7
  • 38
    • 0025333225 scopus 로고
    • Biogenesis of synaptic vesicle-like structures in a pheochromocytoma cell line PC-12
    • Clift-O'Grady, L., Linstedt, A. D., Lowe, A. W., Grote, E., and Kelly, R. B. (1990). Biogenesis of synaptic vesicle-like structures in a pheochromocytoma cell line PC-12. J. Cell Biol. 110,1693-1703.
    • (1990) J. Cell Biol. , vol.110 , pp. 1693-1703
    • Clift-O'Grady, L.1    Linstedt, A.D.2    Lowe, A.W.3    Grote, E.4    Kelly, R.B.5
  • 39
    • 0002061266 scopus 로고
    • Structural and functional relationships in the nonmammalian pineal gland
    • R. J. Reiter, Ed., CRC Press, Boca Raton, FL
    • Collin, J.-P., and Oksche, A. (1981). Structural and functional relationships in the nonmammalian pineal gland. In "The Pineal Gland" (R. J. Reiter, Ed.), pp. 27-67. CRC Press, Boca Raton, FL.
    • (1981) The Pineal Gland , pp. 27-67
    • Collin, J.-P.1    Oksche, A.2
  • 40
    • 0023240455 scopus 로고
    • Pineocytoma with neuronal differentiation demonstrated immunocytochemically
    • Collins, V. P. (1987). Pineocytoma with neuronal differentiation demonstrated immunocytochemically. Ada Pathol. Microbiol. Immunol. Scand. A 95, 113-117.
    • (1987) Ada Pathol. Microbiol. Immunol. Scand. A , vol.95 , pp. 113-117
    • Collins, V.P.1
  • 42
    • 0027332736 scopus 로고
    • A single Q domain from synaptotagmin I is sufficient for high affinity Ca2t/phospholipid binding
    • Davletov, B. A., and Südhof, T. C. (1993). A single Q domain from synaptotagmin I is sufficient for high affinity Ca2t/phospholipid binding. J. Biol. Chem. 268, 26386-26390.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26386-26390
    • Davletov, B.A.1    Südhof, T.C.2
  • 43
    • 0026043679 scopus 로고
    • Co-secretion of multiple signal molecules from endocrine cells via distinct exocytotic pathways
    • De Camilli, P. (1991). Co-secretion of multiple signal molecules from endocrine cells via distinct exocytotic pathways. Trends Pharmacol. Sci. 12, 446-448.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 446-448
    • De Camilli, P.1
  • 44
    • 0027194875 scopus 로고
    • A plethora of GTPases, large and small
    • De Lisle, R. C. (1993). A plethora of GTPases, large and small. Digestion 54, 3-8.
    • (1993) Digestion , vol.54 , pp. 3-8
    • De Lisle, R.C.1
  • 45
    • 1842319782 scopus 로고
    • Plurivesicular secretory processes and nerve endings in the pineal gland of the rat
    • De Robertis, E., and De Iraldi, A. P. (1961). Plurivesicular secretory processes and nerve endings in the pineal gland of the rat. J. Biophys. Biochem. Cytol. 10, 361-372.
    • (1961) J. Biophys. Biochem. Cytol. , vol.10 , pp. 361-372
    • De Robertis, E.1    De Iraldi, A.P.2
  • 46
    • 0030592135 scopus 로고    scopus 로고
    • Parasympathetic inhibition of pineal indole metabolism by prejunctional modulation of noradrenaline release
    • Drijfhout, W. J., Grol, C. J., and Westerink, B. H. C. (1996a). Parasympathetic inhibition of pineal indole metabolism by prejunctional modulation of noradrenaline release. Etir. J. Pharmacol. 308, 117-124.
    • (1996) Etir. J. Pharmacol. , vol.308 , pp. 117-124
    • Drijfhout, W.J.1    Grol, C.J.2    Westerink, B.H.C.3
  • 47
    • 0030048246 scopus 로고    scopus 로고
    • Microdialysis reveals dynamics of coupling between noradrenaline release and melatonin secretion in conscious rats
    • Drijfhout, W. J., van der Linde, A. G., de Vries, J. B., Grol, C. J., and Westerink, B. H. C. (1996b). Microdialysis reveals dynamics of coupling between noradrenaline release and melatonin secretion in conscious rats. Neurosci. Lett. 202, 185-188.
    • (1996) Neurosci. Lett. , vol.202 , pp. 185-188
    • Drijfhout, W.J.1    Van Der Linde, A.G.2    De Vries, J.B.3    Grol, C.J.4    Westerink, B.H.C.5
  • 48
    • 8044245877 scopus 로고
    • The presence and function of glutamate receptors in the pineal gland
    • R. J. Reiter and M. Karasek, Eds. Libbey, New York
    • Ebadi, M., Govitrapong, P., and Murrine, L. C. (1986). The presence and function of glutamate receptors in the pineal gland. In "Advances in Pineal Research" (R. J. Reiter and M. Karasek, Eds.), pp. 99-109. Libbey, New York.
    • (1986) Advances in Pineal Research , pp. 99-109
    • Ebadi, M.1    Govitrapong, P.2    Murrine, L.C.3
  • 49
    • 0028819440 scopus 로고
    • Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine
    • Edelmann, L., Hanson, P. I., Chapman, E. R., and Jahn, R. (1995). Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine. EMBO J. 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
  • 50
    • 0024308501 scopus 로고
    • Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system
    • Elferink, L. A., Trimble, W. S., and Scheller, R. H. (1989). Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J. Biol. Chem. 264, 11061-11064.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11061-11064
    • Elferink, L.A.1    Trimble, W.S.2    Scheller, R.H.3
  • 51
    • 0028839811 scopus 로고
    • Mice lacking synaptophysin reproduce and form typical synaptic vesicles
    • Eshkind, L. G., and Leube, R. E. (1995). Mice lacking synaptophysin reproduce and form typical synaptic vesicles. Cell Tissue Res. 282, 423-433.
    • (1995) Cell Tissue Res. , vol.282 , pp. 423-433
    • Eshkind, L.G.1    Leube, R.E.2
  • 52
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- And R-SNAREs
    • Fasshauer, D., Sutton, R. B., Brunger, A. T., and Jahn, R. (1998). Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA 95, 15781-15786.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 53
    • 0032076102 scopus 로고    scopus 로고
    • A function for the AP3 coat complex in synaptic vesicle formation from endosomes
    • FaUndez, V., Horng, J.-T., and Kelly, R. B. (1998). A function for the AP3 coat complex in synaptic vesicle formation from endosomes. Cell 93, 423-432.
    • (1998) Cell , vol.93 , pp. 423-432
    • Faundez, V.1    Horng, J.-T.2    Kelly, R.B.3
  • 54
    • 0028306953 scopus 로고
    • Aberrant neurites and synaptic vesicle protein deficiency in synapsin II-depleted neurons
    • Ferreira, A., Kosik, K. S., Greengard, P., and Han, H.-Q.-(1994). Aberrant neurites and synaptic vesicle protein deficiency in synapsin II-depleted neurons. Science 264, 977-979.
    • (1994) Science , vol.264 , pp. 977-979
    • Ferreira, A.1    Kosik, K.S.2    Greengard, P.3    Han, H.-Q.4
  • 55
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novik, S., and Jahn, R. (1994). Vesicle fusion from yeast to man. Nature 3370,191-193.
    • (1994) Nature , vol.3370 , pp. 191-193
    • Ferro-Novik, S.1    Jahn, R.2
  • 58
    • 0026067472 scopus 로고
    • A small GTP-binding protein dissociates from synaptic vesicles during exocytosis
    • Fischer von Mollard, G., Südhof, T. C, and Jahn, R. (1991). A small GTP-binding protein dissociates from synaptic vesicles during exocytosis. Nature 349, 79-81.
    • (1991) Nature , vol.349 , pp. 79-81
    • Fischer Von Mollard, G.1    Südhof, T.C.2    Jahn, R.3
  • 59
    • 0028309740 scopus 로고
    • Rab3C is a synaptic vesicle protein that dissociates from synaptic vesicles after stimulation of exocytosis
    • Fischer von Mollard, G., Stahl, B., Khokhlatchev, A., Südhof, T. C, and Jahn, R. (1994). Rab3C is a synaptic vesicle protein that dissociates from synaptic vesicles after stimulation of exocytosis. J. Biol. Cliem. 269, 10971-10974.
    • (1994) J. Biol. Cliem. , vol.269 , pp. 10971-10974
    • Fischer Von Mollard, G.1    Stahl, B.2    Khokhlatchev, A.3    Südhof, T.C.4    Jahn, R.5
  • 60
    • 0031059276 scopus 로고    scopus 로고
    • Remodeling of pineal epithelium in the fetal rat as delineated by immunohistochemistry of laminin and cadherin
    • Fujieda, H., Sato, T., Shi, J., and Wake, K. (1997). Remodeling of pineal epithelium in the fetal rat as delineated by immunohistochemistry of laminin and cadherin. Cell Tissue Res. 287, 263-274.
    • (1997) Cell Tissue Res. , vol.287 , pp. 263-274
    • Fujieda, H.1    Sato, T.2    Shi, J.3    Wake, K.4
  • 62
    • 0029801022 scopus 로고    scopus 로고
    • Amino acid neurotransmission: Dynamics of vesicular uptake
    • Fykse, E. M., and Fonnum, F. (1996). Amino acid neurotransmission: Dynamics of vesicular uptake. Neureichem. Res. 21, 1053-1060.
    • (1996) Neureichem. Res. , vol.21 , pp. 1053-1060
    • Fykse, E.M.1    Fonnum, F.2
  • 63
    • 0027429034 scopus 로고
    • Relative properties and localizations of synaptic vesicle protein isoforms: The case of the synaptophysins
    • Fykse, E. M., Takei, K., Walch-Solimena, C., Geppert, M., Jahn, R., De Camilli, P., and Südhof, T. C. (1993). Relative properties and localizations of synaptic vesicle protein isoforms: The case of the synaptophysins. J. Neurosci. 13, 4997-5007.
    • (1993) J. Neurosci. , vol.13 , pp. 4997-5007
    • Fykse, E.M.1    Takei, K.2    Walch-Solimena, C.3    Geppert, M.4    Jahn, R.5    De Camilli, P.6    Südhof, T.C.7
  • 65
    • 0028945592 scopus 로고
    • RbSecl a and B colocalize with syntaxin l and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin
    • Garcia, E. P., McPherson, P. S., Chilcote, T. J., Takei, K., and De Camilli, P. (1995). RbSecl A and B colocalize with syntaxin l and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin. J. Cell Biol. 129, 105-120.
    • (1995) J. Cell Biol. , vol.129 , pp. 105-120
    • Garcia, E.P.1    McPherson, P.S.2    Chilcote, T.J.3    Takei, K.4    De Camilli, P.5
  • 66
    • 0029417333 scopus 로고
    • Glucose modulates -aminobutyric acid release from the pancreatic 0TC6 cell line
    • Gaskins, H. R., Baldeon, M. E., Selassie, L., and Beverly, J. L. (1995). Glucose modulates -aminobutyric acid release from the pancreatic 0TC6 cell line. J. Biol. Cliem. 270, 30286-30289.
    • (1995) J. Biol. Cliem. , vol.270 , pp. 30286-30289
    • Gaskins, H.R.1    Baldeon, M.E.2    Selassie, L.3    Beverly, J.L.4
  • 67
    • 0029967978 scopus 로고    scopus 로고
    • A murine neural-specific homolog corrects cholinergic defects in caenorhabditis elegans unc-18 mutants
    • Gengyo-Ando, K., Kitayama, H., Mukaida, M., and Ikawa, Y. (1996). A murine neural-specific homolog corrects cholinergic defects in caenorhabditis elegans unc-18 mutants. J. Neurosci. 16, 6695-6702.
    • (1996) J. Neurosci. , vol.16 , pp. 6695-6702
    • Gengyo-Ando, K.1    Kitayama, H.2    Mukaida, M.3    Ikawa, Y.4
  • 68
    • 0031898897 scopus 로고    scopus 로고
    • RAB3 and synaptotagmin: The yin and yang of synaptic membrane fusion
    • Geppert, M., and Südhof, T. C. (1998). RAB3 and synaptotagmin: The yin and yang of synaptic membrane fusion. Annu. Rev. Neurosci. 21, 75-95.
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 75-95
    • Geppert, M.1    Südhof, T.C.2
  • 70
    • 0028061861 scopus 로고
    • Synaptotagmin I: A major calcium sensor for transmitter release at a central synapse
    • Geppert, M., Goda, Y., Hammer, R. E., Li, C, Rosahl, T. W., Stevens, C. F., and Südhof, T. C. (1994b). Synaptotagmin I: A major calcium sensor for transmitter release at a central synapse. Cell 79, 717-727.
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1    Goda, Y.2    Hammer, R.E.3    Li, C.4    Rosahl, T.W.5    Stevens, C.F.6    Südhof, T.C.7
  • 71
    • 0030980279 scopus 로고    scopus 로고
    • The small GTP-binding protein rab3A regulates a late step in synaptic vesicle fusion
    • Geppert, M., Goda, Y., Stevens, C. F., and Südhof, T. C. (1997). The small GTP-binding protein rab3A regulates a late step in synaptic vesicle fusion. Nature 387, 810-814.
    • (1997) Nature , vol.387 , pp. 810-814
    • Geppert, M.1    Goda, Y.2    Stevens, C.F.3    Südhof, T.C.4
  • 72
    • 0031017219 scopus 로고    scopus 로고
    • SNAREs and regulated vesicle exocytosis
    • Goda, Y. (1997). SNAREs and regulated vesicle exocytosis. Proc. Natl. Acad. Sci. USA 94, 769-772.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 769-772
    • Goda, Y.1
  • 73
    • 0023816385 scopus 로고
    • The inhibition of pineal arylalkylamine N-acetyltransferase by glutamic acid and its analogues
    • Govitrapong, P., and Ebadi, M. (1988). The inhibition of pineal arylalkylamine N-acetyltransferase by glutamic acid and its analogues. Neurochem. Int. 13, 223-230.
    • (1988) Neurochem. Int. , vol.13 , pp. 223-230
    • Govitrapong, P.1    Ebadi, M.2
  • 74
    • 0022929899 scopus 로고
    • 2+-dependent glutamate (quisqualate) binding site in bovine pineal organ
    • 2+-dependent glutamate (quisqualate) binding site in bovine pineal organ. J. Pineal Res. 3, 223-234.
    • (1986) J. Pineal Res. , vol.3 , pp. 223-234
    • Govitrapong, P.1    Ebadi, M.2    Murrin, L.C.3
  • 75
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard, P., Valtorta, F., Czernik, A. J., and Benfenati, F. (1993). Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259, 780-785.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 76
    • 0022913488 scopus 로고
    • The endocrine cells of the digestive system: Amines, peptides, and modes of action
    • Grube, D. (1986). The endocrine cells of the digestive system: Amines, peptides, and modes of action. Anat. Embryol. 175, 151-162.
    • (1986) Anat. Embryol. , vol.175 , pp. 151-162
    • Grube, D.1
  • 77
    • 0026795692 scopus 로고
    • Suppression cloning of the cDNA for a candidate subunit of a presynaptic calcium channel
    • Gundersen, C. B., and Umbach, J. A. (1992). Suppression cloning of the cDNA for a candidate subunit of a presynaptic calcium channel. Neuron 9, 527-537.
    • (1992) Neuron , vol.9 , pp. 527-537
    • Gundersen, C.B.1    Umbach, J.A.2
  • 78
    • 0032529722 scopus 로고    scopus 로고
    • Synaptic vesicular localization and exocytosis of L-aspartate in excitatory nerve terminals: A quantitative immunogold analysis in rat hippocampus
    • Gundersen, V., Chaudhry, F. A., Bjaalie, J. G., Fonnum, F., Ottersen, O. P., and StormMathisen, J. (1998). Synaptic vesicular localization and exocytosis of L-aspartate in excitatory nerve terminals: A quantitative immunogold analysis in rat hippocampus. J. Neitrosci. 18, 6059-6070.
    • (1998) J. Neitrosci. , vol.18 , pp. 6059-6070
    • Gundersen, V.1    Chaudhry, F.A.2    Bjaalie, J.G.3    Fonnum, F.4    Ottersen, O.P.5    Stormmathisen, J.6
  • 79
    • 0028813810 scopus 로고
    • Anti-syntaxin antibodies inhibit calcium-dependent catecholamine secretion from permeabilized chromaffin cells
    • Gutierrez, L. M., Quintanar, J. L., Viniegra, S., Saunas, E., Moya, F., and Reig, J. A. (1995). Anti-syntaxin antibodies inhibit calcium-dependent catecholamine secretion from permeabilized chromaffin cells. Biochem. Biophys. Res. Commun. 206, 1-7.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 1-7
    • Gutierrez, L.M.1    Quintanar, J.L.2    Viniegra, S.3    Saunas, E.4    Moya, F.5    Reig, J.A.6
  • 80
    • 0026061136 scopus 로고
    • Induction of formation of presynaptic terminals in neuroblastoma cells by synapsin I b
    • Han, H.-Q., Nichols, R. A., Rubin, M. R., Bahler, M., and Greengard, P. (1991). Induction of formation of presynaptic terminals in neuroblastoma cells by synapsin I b. Nad/re 349,697-700.
    • (1991) Nad/re , vol.349 , pp. 697-700
    • Han, H.-Q.1    Nichols, R.A.2    Rubin, M.R.3    Bahler, M.4    Greengard, P.5
  • 81
    • 0030612955 scopus 로고    scopus 로고
    • Trafficking of amino acids between neurons and glia in vivo. Effects of inhibition of glial metabolism by fluoroacetate
    • Hassel, B., Bachelard, H., Jones, P., Fonnum, F., and Sonnewald, U. (1997). Trafficking of amino acids between neurons and glia in vivo. Effects of inhibition of glial metabolism by fluoroacetate. J. Cereb. Blood Flow Metab. 17, 1230-1238.
    • (1997) J. Cereb. Blood Flow Metab. , vol.17 , pp. 1230-1238
    • Hassel, B.1    Bachelard, H.2    Jones, P.3    Fonnum, F.4    Sonnewald, U.5
  • 82
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata, Y., Slaughter, C. A., and Südhof, T. C. (1993). Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366, 347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Südhof, T.C.3
  • 83
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi, T., McMahon, H., Yamasaki, S., Binz, T., Hata, Y., Südhof, T. C., and Niemann, H. (1994). Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly. EMBO J. 13, 5051-5061.
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Südhof, T.C.6    Niemann, H.7
  • 84
    • 0031844735 scopus 로고    scopus 로고
    • Synaptic vesicle protein SV2B, but not SV2A, is predominantly expressed and associated with microvesicles in rat pinealocytes
    • Hayashi, M., Yamamoto, A., Yatsushiro, S., Yamada, H., Futai, M., Yamaguchi, A., and Moriyama, Y. (1998). Synaptic vesicle protein SV2B, but not SV2A, is predominantly expressed and associated with microvesicles in rat pinealocytes. J. Neurochem. 71,356-365.
    • (1998) J. Neurochem. , vol.71 , pp. 356-365
    • Hayashi, M.1    Yamamoto, A.2    Yatsushiro, S.3    Yamada, H.4    Futai, M.5    Yamaguchi, A.6    Moriyama, Y.7
  • 85
    • 0026471991 scopus 로고
    • The 25 kDa synaptosomalassociated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess, D. T., Slater, T. M., Wilson, M. C, and Skene, J. H. P. (1992). The 25 kDa synaptosomalassociated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J. Neurosci. 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.P.4
  • 87
    • 0028244421 scopus 로고
    • In chromaffin cells, the mammalian seclp homologue is a syntaxin l A-binding protein associated with chromaffin granules
    • Hodel, A., Schäfer, T., Gerosa, D., and Burger, M. M. (1994). In chromaffin cells, the mammalian seclp homologue is a syntaxin l A-binding protein associated with chromaffin granules. J. Biol. Client. 269, 8623-8626.
    • (1994) J. Biol. Client. , vol.269 , pp. 8623-8626
    • Hodel, A.1    Schäfer, T.2    Gerosa, D.3    Burger, M.M.4
  • 88
    • 0031453767 scopus 로고    scopus 로고
    • Functional importance of synaptobrevin and SNAP-25 during exocytosis of histamine by rat gastric enterochromaffin-like cells
    • Höhne-Zell, B., Galler, A., Schepp, W., Gratzl, M., and Prinz, C. (1997). Functional importance of synaptobrevin and SNAP-25 during exocytosis of histamine by rat gastric enterochromaffin-like cells. Endocrinology 138, 5518-5526.
    • (1997) Endocrinology , vol.138 , pp. 5518-5526
    • Höhne-Zell, B.1    Galler, A.2    Schepp, W.3    Gratzl, M.4    Prinz, C.5
  • 89
    • 2642713311 scopus 로고    scopus 로고
    • Synapsins I and II are ATP-binding proteins with differential Ca2t regulation
    • Hosaka, M., and Südhof, T. C. (1998). Synapsins I and II are ATP-binding proteins with differential Ca2t regulation. J. Biol. Client. 273,1425-1429.
    • (1998) J. Biol. Client. , vol.273 , pp. 1425-1429
    • Hosaka, M.1    Südhof, T.C.2
  • 90
    • 0026582816 scopus 로고
    • The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans
    • Hosono, R., Hekimi, S., Kamiya, Y., Sassa, T., Murakami, S., Nishiwaki, K., Miwa, J., Taketo, A., and Kodaira, K.-I. (1992). The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans. J. Neurochem. 58, 1517-1525.
    • (1992) J. Neurochem. , vol.58 , pp. 1517-1525
    • Hosono, R.1    Hekimi, S.2    Kamiya, Y.3    Sassa, T.4    Murakami, S.5    Nishiwaki, K.6    Miwa, J.7    Taketo, A.8    Kodaira, K.-I.9
  • 91
    • 0026573292 scopus 로고
    • Immunocytochemical demonstration of rod-opsin, S-antigen, and neuron-specific proteins in the human pineal gland
    • Huang, S.-K., Klein, D. C, and Korf, H.-W. (1992). Immunocytochemical demonstration of rod-opsin, S-antigen, and neuron-specific proteins in the human pineal gland. Cell Tissue Res. 267, 493-498.
    • (1992) Cell Tissue Res. , vol.267 , pp. 493-498
    • Huang, S.-K.1    Klein, D.C.2    Korf, H.-W.3
  • 93
    • 0026660586 scopus 로고
    • Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1
    • Inoue, A., Obata, K., and Akagawa, K. (1992). Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1. J. Biol. Client. 267, 10613-10619.
    • (1992) J. Biol. Client. , vol.267 , pp. 10613-10619
    • Inoue, A.1    Obata, K.2    Akagawa, K.3
  • 95
    • 0014384031 scopus 로고
    • Electron microscopic observations on the mouse pineal, with particular emphasis on its secretory nature
    • Ito, T., and Matsushima, S. (1968). Electron microscopic observations on the mouse pineal, with particular emphasis on its secretory nature. Arch. Histol. Jpn. 30,1-15.
    • (1968) Arch. Histol. Jpn. , vol.30 , pp. 1-15
    • Ito, T.1    Matsushima, S.2
  • 96
    • 0030457774 scopus 로고    scopus 로고
    • Molecular components of the exocytotic machinery in the rat pituitary gland
    • Jacobsson, G., and Meister, B. (1996). Molecular components of the exocytotic machinery in the rat pituitary gland. Endocrinology 137, 5344-5356.
    • (1996) Endocrinology , vol.137 , pp. 5344-5356
    • Jacobsson, G.1    Meister, B.2
  • 98
    • 0032492779 scopus 로고    scopus 로고
    • SNAREs line up in new environment
    • Jahn, R., and Hanson, P. I. (1998). SNAREs line up in new environment. Nature 393,14-15.
    • (1998) Nature , vol.393 , pp. 14-15
    • Jahn, R.1    Hanson, P.I.2
  • 99
    • 0344237032 scopus 로고
    • A 38,000-dalton membrane protein (p38) present in synaptic vesicles
    • Jahn, R., Schiebler, W., Ouimet, C., and Greengard, P. (1985). A 38,000-dalton membrane protein (p38) present in synaptic vesicles. Proc. Natl. Acad. Sci. USA 82, 4137-4141.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4137-4141
    • Jahn, R.1    Schiebler, W.2    Ouimet, C.3    Greengard, P.4
  • 100
    • 0028177963 scopus 로고
    • Redistribution of a Rab3-like GTP-binding protein from secretory granules to the golgi complex in pancreatic acinar cells during regulated exocytosis
    • Jena, B. P., Gumkowski, F. D., Konieczko, E. M., Fischer von Mollard, G., Jahn, R., and Jamieson, J. D. (1994). Redistribution of a Rab3-like GTP-binding protein from secretory granules to the golgi complex in pancreatic acinar cells during regulated exocytosis. J. Cell Biol. 124, 43-53.
    • (1994) J. Cell Biol. , vol.124 , pp. 43-53
    • Jena, B.P.1    Gumkowski, F.D.2    Konieczko, E.M.3    Von Fischer Mollard, G.4    Jahn, R.5    Jamieson, J.D.6
  • 102
    • 0024497166 scopus 로고
    • Transmembrane topography and evolutionary conservation of synaptophysin
    • Johnston, P. A., Jahn, R., and Südhof, T. C. (1989b). Transmembrane topography and evolutionary conservation of synaptophysin. J. Biol. Client. 264, 1268-1273.
    • (1989) J. Biol. Client. , vol.264 , pp. 1268-1273
    • Johnston, P.A.1    Jahn, R.2    Südhof, T.C.3
  • 103
    • 0025784181 scopus 로고
    • Rab3A attachment to the synaptic vesicle membrane mediated by a conserved polyisoprenylated carboxy-terminal sequence
    • Johnston, P. A., Archer, B. T., Ill, Robinson, K., Mignery, G. A., Jahn, R., and Südhof, T. C. (1991). Rab3A attachment to the synaptic vesicle membrane mediated by a conserved polyisoprenylated carboxy-terminal sequence. Neuron 7, 101-109.
    • (1991) Neuron , vol.7 , pp. 101-109
    • Johnston, P.A.1    Archer III, B.T.2    Robinson, K.3    Mignery, G.A.4    Jahn, R.5    Südhof, T.C.6
  • 105
    • 0019157429 scopus 로고
    • Pools of serotonin in the pineal gland of the mouse: The mammalian pinealocyte as a component of the diffuse neuroendocrine system
    • Juillard, M.-T., and Collin, J. P. (1980). Pools of serotonin in the pineal gland of the mouse: The mammalian pinealocyte as a component of the diffuse neuroendocrine system. Cell Tissue Res. 213, 273-291.
    • (1980) Cell Tissue Res. , vol.213 , pp. 273-291
    • Juillard, M.-T.1    Collin, J.P.2
  • 106
    • 0030068913 scopus 로고    scopus 로고
    • Information processing by graded-potential transmission through tonically active synapses
    • Juusola, M., French, A. S., Uusitalo, R. O., and Weckström, M. (1996). Information processing by graded-potential transmission through tonically active synapses. Trends Neurosci. 19, 292-297.
    • (1996) Trends Neurosci. , vol.19 , pp. 292-297
    • Juusola, M.1    French, A.S.2    Uusitalo, R.O.3    Weckström, M.4
  • 108
    • 77956908115 scopus 로고
    • Survey of the innervation of the epiphysis cerebri and the accessory pineal organs of vertebrates
    • Kappers, J. A. (1965). Survey of the innervation of the epiphysis cerebri and the accessory pineal organs of vertebrates. Prog. Brain Res. 10, 87-151.
    • (1965) Prog. Brain Res. , vol.10 , pp. 87-151
    • Kappers, J.A.1
  • 109
    • 0026776282 scopus 로고
    • Ultrastructure of the mammalian pinealocyte under natural and experimental conditions: Quantitative aspects
    • Karasek, M. (1992). Ultrastructure of the mammalian pinealocyte under natural and experimental conditions: Quantitative aspects. Microsc. Res. Tech. 21,116-123.
    • (1992) Microsc. Res. Tech. , vol.21 , pp. 116-123
    • Karasek, M.1
  • 110
    • 0026740235 scopus 로고
    • Morphofunctional aspects of the mammalian pineal gland
    • Karasek, M., and Reiter, R. J. (1992). Morphofunctional aspects of the mammalian pineal gland. Microsc. Res. Tech. 21, 136-157.
    • (1992) Microsc. Res. Tech. , vol.21 , pp. 136-157
    • Karasek, M.1    Reiter, R.J.2
  • 111
    • 0030208011 scopus 로고    scopus 로고
    • Beyond the neuronal circuitry
    • Kettenmann, H. (1996). Beyond the neuronal circuitry. Trends Neurosci. 19, 305-306.
    • (1996) Trends Neurosci. , vol.19 , pp. 305-306
    • Kettenmann, H.1
  • 112
    • 0025146949 scopus 로고
    • Synaptoporin, a novel putative channel protein of synaptic vesicles
    • Knaus, P., Marqueze-Pouey, B., Scherer, H., and Betz, H. (1990). Synaptoporin, a novel putative channel protein of synaptic vesicles. Neuron 5, 453-462.
    • (1990) Neuron , vol.5 , pp. 453-462
    • Knaus, P.1    Marqueze-Pouey, B.2    Scherer, H.3    Betz, H.4
  • 113
    • 0029807825 scopus 로고    scopus 로고
    • Synaptic vesicles have two distinct recycling pathways
    • Koenig, J. H., and Ikeda, K. (1996). Synaptic vesicles have two distinct recycling pathways. J. Cell Biol. 135, 797-808.
    • (1996) J. Cell Biol. , vol.135 , pp. 797-808
    • Koenig, J.H.1    Ikeda, K.2
  • 114
    • 0028322286 scopus 로고
    • The pineal organ as a component of the biological clock
    • Korf, H.-W. (1994). The pineal organ as a component of the biological clock. Ann. N. Y. Acad. Sci. 719, 13-42.
    • (1994) Ann. N. Y. Acad. Sci. , vol.719 , pp. 13-42
    • Korf, H.-W.1
  • 115
    • 0000955127 scopus 로고    scopus 로고
    • Innervation of the pineal gland
    • G. Burnstock, Ed., Autonomie-Endocrine Interactions (K. Unsicker, Ed.), Harwood, Amsterdam
    • Korf, H.-W. (1996). Innervation of the pineal gland. In "The Autonomie Nervous System" (G. Burnstock, Ed.), Vol. 10, Autonomie-Endocrine Interactions (K. Unsicker, Ed.), pp. 129-180. Harwood, Amsterdam.
    • (1996) The Autonomie Nervous System , vol.10 , pp. 129-180
    • Korf, H.-W.1
  • 116
    • 0031626997 scopus 로고    scopus 로고
    • The pineal organ, its hormone melatonin, and the photoneuroendocrine system
    • Korf, H.-W., Schomerus, C, and Stehle, J. H. (1998). The pineal organ, its hormone melatonin, and the photoneuroendocrine system. Adv. Anat. Embryol. Cell Biol. 146.
    • (1998) Adv. Anat. Embryol. Cell Biol. , pp. 146
    • Korf, H.-W.1    Schomerus, C.2    Stehle, J.H.3
  • 117
    • 0030272807 scopus 로고    scopus 로고
    • Colocalization on the same synaptic vesicles of syntaxin and SNAP-25 with synaptic vesicle proteins: A reevaluation of functional models required?
    • Kretzschmar, S., Volknandt, W., and Zimmermann, H. (1996). Colocalization on the same synaptic vesicles of syntaxin and SNAP-25 with synaptic vesicle proteins: A reevaluation of functional models required? Nenrosci. Res. 26, 141-148.
    • (1996) Nenrosci. Res. , vol.26 , pp. 141-148
    • Kretzschmar, S.1    Volknandt, W.2    Zimmermann, H.3
  • 118
    • 33645844757 scopus 로고
    • Glutamate inhibition of melatonin production in the rat pineal gland in vitro
    • Kus, L., Handa, R. J., and McNuIty, J. A. (1991). Glutamate inhibition of melatonin production in the rat pineal gland in vitro. Anat. Rec. 229, 47A.
    • (1991) Anat. Rec. , vol.229
    • Kus, L.1    Handa, R.J.2    McNuity, J.A.3
  • 119
    • 0028247171 scopus 로고
    • Glutamate inhibition of the adrenergicstimulated production of melatonin in rat pineal gland in vitro
    • Kus, L., Handa, R. J., and McNulty, J. A. (1994). Glutamate inhibition of the adrenergicstimulated production of melatonin in rat pineal gland in vitro. J. Neiirochem. 62,2241 -2245.
    • (1994) J. Neiirochem. , vol.62 , pp. 2241-2245
    • Kus, L.1    Handa, R.J.2    McNulty, J.A.3
  • 121
    • 0014166499 scopus 로고
    • uber axonähnliche Fortsätze, Sekretbildung und Extrusion der hellen Pinealocyten des Kaninchens
    • Leonhardt, H. (1967). uber axonähnliche Fortsätze, Sekretbildung und Extrusion der hellen Pinealocyten des Kaninchens. Z. Zellforsch. 82, 307-320.
    • (1967) Z. Zellforsch. , vol.82 , pp. 307-320
    • Leonhardt, H.1
  • 122
    • 33947460818 scopus 로고
    • Isolation of melatonin, the pineal gland factor that lightens melanocytes
    • Lerner, A. B., Case, J. D., Takahashi, Y., Lee, T. H., and Mori, W. (1958). Isolation of melatonin, the pineal gland factor that lightens melanocytes. J. Am. Chem. Soc. 80, 2587.
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 2587
    • Lerner, A.B.1    Case, J.D.2    Takahashi, Y.3    Lee, T.H.4    Mori, W.5
  • 124
    • 0028300004 scopus 로고
    • Expression of the synaptophysin gene family is not restricted to neuronal and neuroendocrine differentiation in rat and human
    • Leube, R. E. (1994). Expression of the synaptophysin gene family is not restricted to neuronal and neuroendocrine differentiation in rat and human. Differentiation 56, 163-171.
    • (1994) Differentiation , vol.56 , pp. 163-171
    • Leube, R.E.1
  • 126
    • 0028099995 scopus 로고
    • Sorting of synaptophysin into special vesicles in nonneuroendocrine epithelial cells
    • Leube, R. E., Leimer, U., Grund, C., Franke, W. W., Harth, N., and Wiedenmann, B. (1994). Sorting of synaptophysin into special vesicles in nonneuroendocrine epithelial cells. J. Cell Biol. 127, 1589-1601.
    • (1994) J. Cell Biol. , vol.127 , pp. 1589-1601
    • Leube, R.E.1    Leimer, U.2    Grund, C.3    Franke, W.W.4    Harth, N.5    Wiedenmann, B.6
  • 127
    • 0028989281 scopus 로고
    • Ca2+-dependent and independent activities of neural and non-neural synaptotagmins
    • Li, C., Ullrich, B., Zhang, J. Z., Anderson, R. G. W., Brose, N., and Südhof, T. C. (1995). Ca2+-dependent and independent activities of neural and non-neural synaptotagmins. Nature 375, 594-599.
    • (1995) Nature , vol.375 , pp. 594-599
    • Li, C.1    Ullrich, B.2    Zhang, J.Z.3    Anderson, R.G.W.4    Brose, N.5    Südhof, T.C.6
  • 129
    • 0030000277 scopus 로고    scopus 로고
    • Deciphering neuronal secretion: Tools of the trade
    • Lineal, M., and Parnas, D. (1996). Deciphering neuronal secretion: Tools of the trade. Biochim. Biophys. Ada 1286, 117-152.
    • (1996) Biochim. Biophys. Ada , vol.1286 , pp. 117-152
    • Lineal, M.1    Parnas, D.2
  • 130
    • 0027438591 scopus 로고
    • Mutational analysis of Drosophila synaptotagmin demonstrates its essential role in calcium-activated neurotransmitter release
    • Littleton, J. T., Stern, M., Schulze, K., Perm, M., and Bellen, H. J. (1993). Mutational analysis of Drosophila synaptotagmin demonstrates its essential role in calcium-activated neurotransmitter release. Cell 74, 1125-1134.
    • (1993) Cell , vol.74 , pp. 1125-1134
    • Littleton, J.T.1    Stern, M.2    Schulze, K.3    Perm, M.4    Bellen, H.J.5
  • 131
    • 0027974130 scopus 로고
    • Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants
    • Littleton, J. T., Stern, M., Perin, M., and Bellen, H. J. (1994). Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants. Proc. Natl. Acad. Sci. USA 91, 10888-10892.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10888-10892
    • Littleton, J.T.1    Stern, M.2    Perin, M.3    Bellen, H.J.4
  • 132
    • 0027283011 scopus 로고
    • Inhibition of Rab3B expression attenuates Ca2*-dependent exocytosis in rat anterior pituitary cells
    • Lledo, P.-M, Vernier, P., Vincent, J.-D., Mason, W. T., and Zorec, R. (1993). Inhibition of Rab3B expression attenuates Ca2*-dependent exocytosis in rat anterior pituitary cells. Nature 364, 540-544.
    • (1993) Nature , vol.364 , pp. 540-544
    • Lledo, P.-M.1    Vernier, P.2    Vincent, J.-D.3    Mason, W.T.4    Zorec, R.5
  • 135
    • 0001823841 scopus 로고
    • Die Feinstruktur der Zirbeldrüse normaler, trächtiger und experimentell beeinfluter Meerschweinchen
    • Lues, G. (1971). Die Feinstruktur der Zirbeldrüse normaler, trächtiger und experimentell beeinfluter Meerschweinchen. Z. Zellforsch. 114, 38-60.
    • (1971) Z. Zellforsch. , vol.114 , pp. 38-60
    • Lues, G.1
  • 136
    • 0026778593 scopus 로고
    • The role of lipid anchors for small G proteins in membrane trafficking
    • Magee, T., and Newman, C. (1992). The role of lipid anchors for small G proteins in membrane trafficking. Trends Cell Biol. 2, 318-323.
    • (1992) Trends Cell Biol. , vol.2 , pp. 318-323
    • Magee, T.1    Newman, C.2
  • 137
    • 0030703675 scopus 로고    scopus 로고
    • Immunocytochemical analysis of the synaptic proteins SNAP-25 and Rab3A in human pituitary adenomas. Overexpression of SNAP-25 in the mammosomatotroph lineages
    • Majo, G., Ferrer, I., Marsal, J., Blasi, J., and Aguado, F. (1997). Immunocytochemical analysis of the synaptic proteins SNAP-25 and Rab3A in human pituitary adenomas. Overexpression of SNAP-25 in the mammosomatotroph lineages. J. Palhol. 183, 440-446.
    • (1997) J. Palhol. , vol.183 , pp. 440-446
    • Majo, G.1    Ferrer, I.2    Marsal, J.3    Blasi, J.4    Aguado, F.5
  • 138
    • 0025345021 scopus 로고
    • Synapsins in the vertebrate retina: Absence from ribbon synapses and heterogeneous distribution among conventional synapses
    • Mandell, J.V., Townes-Anderson, E., Czernik, A. J., Cameron, R., Greengard, P., and De Camilli, P. (1990). Synapsins in the vertebrate retina: Absence from ribbon synapses and heterogeneous distribution among conventional synapses. Neuron 5, 19-33.
    • (1990) Neuron , vol.5 , pp. 19-33
    • Mandell, J.V.1    Townes-Anderson, E.2    Czernik, A.J.3    Cameron, R.4    Greengard, P.5    De Camilli, P.6
  • 139
    • 0030208826 scopus 로고    scopus 로고
    • Intracellular calcium release mediated by noradrenaline and acetylcholine in mammalian pineal cells
    • Marin, A., Urena, J., and Tabares, L. (1996). Intracellular calcium release mediated by noradrenaline and acetylcholine in mammalian pineal cells. J. Pineal Res. 21, 15-28.
    • (1996) J. Pineal Res. , vol.21 , pp. 15-28
    • Marin, A.1    Urena, J.2    Tabares, L.3
  • 140
    • 0029019102 scopus 로고
    • Cellular localization of synaptotagmin I, II, and III mRNAs in the central nervous system and pituitary and adrenal glands of the rat
    • Marqueze, B., Boudier, J. A., Mizuta, M., Inagaki, N., Seino, S., and Seagar, M. (1995). Cellular localization of synaptotagmin I, II, and III mRNAs in the central nervous system and pituitary and adrenal glands of the rat. J. Neurosci. 15, 4906-4917.
    • (1995) J. Neurosci. , vol.15 , pp. 4906-4917
    • Marqueze, B.1    Boudier, J.A.2    Mizuta, M.3    Inagaki, N.4    Seino, S.5    Seagar, M.6
  • 141
    • 0028797142 scopus 로고
    • The nucleotide and deduced amino acid sequence of a rat cysteine string protein
    • Mastrogiacomo, A., and Gundersen, C. B. (1995). The nucleotide and deduced amino acid sequence of a rat cysteine string protein. Mol. Brain Res. 28, 12-18.
    • (1995) Mol. Brain Res. , vol.28 , pp. 12-18
    • Mastrogiacomo, A.1    Gundersen, C.B.2
  • 142
    • 0028350829 scopus 로고
    • Cysteine string proteins: A potential link between synaptic vesicles and presynaptic Ca2t channels
    • Mastrogiacomo, A., Parsons, S. M., Zampighi, G. A., Jenden, D. J., Umbach, J. A., and Gundersen, C. B. (1994). Cysteine string proteins: A potential link between synaptic vesicles and presynaptic Ca2t channels. Science 263, 981-982.
    • (1994) Science , vol.263 , pp. 981-982
    • Mastrogiacomo, A.1    Parsons, S.M.2    Zampighi, G.A.3    Jenden, D.J.4    Umbach, J.A.5    Gundersen, C.B.6
  • 143
    • 0026719481 scopus 로고
    • Exoendocytotic recycling of synaptic vesicles in developing processes of cultured hippocampal neurons
    • Matteoli, M., Takei, K., Perin, M. S., Südhof, T. C, and De Camilli, P. (1992). Exoendocytotic recycling of synaptic vesicles in developing processes of cultured hippocampal neurons. J. Cell Biol. 117, 849-861.
    • (1992) J. Cell Biol. , vol.117 , pp. 849-861
    • Matteoli, M.1    Takei, K.2    Perin, M.S.3    Südhof, T.C.4    De Camilli, P.5
  • 144
    • 0027265710 scopus 로고
    • Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein
    • McMahon, H. T., Ushkaryov, Y. A., Edelmann, L., Link, E., Binz, T., Niemann, H., Jahn, R., and Südhof, T. C. (1993). Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature 364, 346-349.
    • (1993) Nature , vol.364 , pp. 346-349
    • McMahon, H.T.1    Ushkaryov, Y.A.2    Edelmann, L.3    Link, E.4    Binz, T.5    Niemann, H.6    Jahn, R.7    Südhof, T.C.8
  • 145
    • 0026717823 scopus 로고
    • Pinealocyte synaptic ribbons and neuroendocrine function
    • McNulty, J. A., and Fox, L. M. (1992). Pinealocyte synaptic ribbons and neuroendocrine function. Microsc. Res. Tech. 21, 175-187.
    • (1992) Microsc. Res. Tech. , vol.21 , pp. 175-187
    • McNulty, J.A.1    Fox, L.M.2
  • 146
    • 0023117782 scopus 로고
    • Pinealocyte dense-cored vesicles and synaptic ribbons: A correlative ultrastructural-biochemical investigation in rats and mice
    • McNulty, J. A., Fox, L. M., and Lisco, S. J. (1987). Pinealocyte dense-cored vesicles and synaptic ribbons: A correlative ultrastructural-biochemical investigation in rats and mice. J. Pineal Res. 4, 45-59.
    • (1987) J. Pineal Res. , vol.4 , pp. 45-59
    • McNulty, J.A.1    Fox, L.M.2    Lisco, S.J.3
  • 147
    • 0026706712 scopus 로고
    • Immunocytochemical and circadian biochemical analysis of neuroactive amino acids in the pineal gland of the rat: Effect of superior ganglionectomy
    • McNulty, J. A., Kus, L., and Ottersen, O. P. (1992). Immunocytochemical and circadian biochemical analysis of neuroactive amino acids in the pineal gland of the rat: Effect of superior ganglionectomy. Cell Tissue Res. 269, 515-523.
    • (1992) Cell Tissue Res. , vol.269 , pp. 515-523
    • McNulty, J.A.1    Kus, L.2    Ottersen, O.P.3
  • 148
    • 0021345577 scopus 로고
    • Photosensory properties of the pineal organ. Microiontophoretic application of excitatory amino acids onto pineal neurons
    • Meissl, H., and George, S. R. (1984). Photosensory properties of the pineal organ. Microiontophoretic application of excitatory amino acids onto pineal neurons. Ophthalmic Res. 16, 114-118.
    • (1984) Ophthalmic Res. , vol.16 , pp. 114-118
    • Meissl, H.1    George, S.R.2
  • 149
    • 0028901009 scopus 로고
    • Non-A'-methyl-D-aspartate glutamate receptors in glial cells and neurons of the pineal gland in a higher primate
    • Mick, G. (1995). Non-A'-methyl-D-aspartate glutamate receptors in glial cells and neurons of the pineal gland in a higher primate. Neiiroendocrinology 61, 256-264.
    • (1995) Neiiroendocrinology , vol.61 , pp. 256-264
    • Mick, G.1
  • 150
    • 0028305903 scopus 로고
    • Synaptotagmin III is a novel isoform of rat synaptotagmin expressed in endocrine and neuronal cells
    • Mizuta, M., Inagaki, N., Nemoto, Y., Matsukura, S., Takahashi, M., and Seino, S. (1994). Synaptotagmin III is a novel isoform of rat synaptotagmin expressed in endocrine and neuronal cells. J. Biol. Chem. 269, 11675-11678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11675-11678
    • Mizuta, M.1    Inagaki, N.2    Nemoto, Y.3    Matsukura, S.4    Takahashi, M.5    Seino, S.6
  • 151
    • 0029655243 scopus 로고    scopus 로고
    • The chemical neuroanatomy of the mammalian pineal gland: Neuropeptides
    • M011er, M., Ravault, J.-P., and Cozzi, B. (1996). The chemical neuroanatomy of the mammalian pineal gland: Neuropeptides. Neurochem. Int. 28, 23-33.
    • (1996) Neurochem. Int. , vol.28 , pp. 23-33
    • Moller, M.1    Ravault, J.-P.2    Cozzi, B.3
  • 152
    • 0029020844 scopus 로고
    • Microvesicles isolated from bovine pineal gland specifically accumulate L-glutamate
    • Moriyama, Y., and Yamamoto, A. (1995a). Microvesicles isolated from bovine pineal gland specifically accumulate L-glutamate. FEBS Lett. 367, 233-236.
    • (1995) FEBS Lett. , vol.367 , pp. 233-236
    • Moriyama, Y.1    Yamamoto, A.2
  • 153
    • 0029121814 scopus 로고
    • Vesicular L-glutamate transporter in microvesicles from bovine pineal glands
    • Moriyama, Y., and Yamamoto, A. (1995b). Vesicular L-glutamate transporter in microvesicles from bovine pineal glands. J. Biol. Chem. 270, 22314-22320.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22314-22320
    • Moriyama, Y.1    Yamamoto, A.2
  • 154
    • 0029077242 scopus 로고
    • Localization of A'-ethylmaleimide-sensitive fusion protein in pinealocytes
    • Moriyama, Y., Yamamoto, A., Tagaya, M., Tashiro, Y., and Michibata, H. (1995). Localization of A'-ethylmaleimide-sensitive fusion protein in pinealocytes. Neuroreport 6, 1757-1760.
    • (1995) Neuroreport , vol.6 , pp. 1757-1760
    • Moriyama, Y.1    Yamamoto, A.2    Tagaya, M.3    Tashiro, Y.4    Michibata, H.5
  • 156
    • 0032473998 scopus 로고    scopus 로고
    • Synaptic vesicles retain their identity through the endocytic cycle
    • Murthy, V. N., and Stevens, C. F. (1998). Synaptic vesicles retain their identity through the endocytic cycle. Nature 392, 497-501.
    • (1998) Nature , vol.392 , pp. 497-501
    • Murthy, V.N.1    Stevens, C.F.2
  • 157
    • 0023032310 scopus 로고
    • Protein p38: An integral membrane protein specific for small vesicles of neurons and neuroendocrine cells
    • Navone, F., Jahn, R., DiGioia, G., Stukenbrok, H., Greengard, P., and De Camilli, P. (1986). Protein p38: An integral membrane protein specific for small vesicles of neurons and neuroendocrine cells.J. Cell Dial. 103, 2511-2527.
    • (1986) J. Cell Dial. , vol.103 , pp. 2511-2527
    • Navone, F.1    Jahn, R.2    Digioia, G.3    Stukenbrok, H.4    Greengard, P.5    De Camilli, P.6
  • 159
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann, H., Blasi, J., and Jahn, R. (1994). Clostridial neurotoxins: New tools for dissecting exocytosis. Trends Cell Biol. 4, 179-185.
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 161
    • 0027319325 scopus 로고
    • Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin
    • Nonet, M. L., Grundahl, K., Meyer, B. J., and Rand, J. B. (1993). Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin. Cell 73, 1291-1305.
    • (1993) Cell , vol.73 , pp. 1291-1305
    • Nonet, M.L.1    Grundahl, K.2    Meyer, B.J.3    Rand, J.B.4
  • 163
    • 0027525103 scopus 로고
    • Friends and family: The role of the rab GTPases in vesicular traffic
    • Novick, P., and Brennwald, P. (1993). Friends and family: The role of the rab GTPases in vesicular traffic. Cell 75, 597-601.
    • (1993) Cell , vol.75 , pp. 597-601
    • Novick, P.1    Brennwald, P.2
  • 164
    • 0031975381 scopus 로고    scopus 로고
    • Glutamate release inhibitors: A critical assessment of their action mechanism
    • Obrenovitch, T. P., and Urenjak, J. (1998). Glutamate release inhibitors: A critical assessment of their action mechanism. Amino Acids 14, 143-150.
    • (1998) Amino Acids , vol.14 , pp. 143-150
    • Obrenovitch, T.P.1    Urenjak, J.2
  • 165
    • 0020521968 scopus 로고
    • Microvasculature as studied by the microvascular corrosion casting/scanning electron microscope method. I. Endocrine and digestive system
    • Ohtani, O., Kikuta, A., Ohtsuka, A., Taguchi, T., and Murakami, T. (1983). Microvasculature as studied by the microvascular corrosion casting/scanning electron microscope method. I. Endocrine and digestive system. Arch. Histol. Jpn. 46, 1-42.
    • (1983) Arch. Histol. Jpn. , vol.46 , pp. 1-42
    • Ohtani, O.1    Kikuta, A.2    Ohtsuka, A.3    Taguchi, T.4    Murakami, T.5
  • 166
    • 0002248136 scopus 로고
    • Pinealocytes as photoneuroendocrine units of neuronal origin: Concepts and evidence
    • R. J. Reiter and F. Fraschini, Eds., Libbey, London
    • Oksche, A., Korf, H.-W., and Rodrfguez, E. M. (1987). Pinealocytes as photoneuroendocrine units of neuronal origin: Concepts and evidence. In "Advances in Pineal Research" (R. J. Reiter and F. Fraschini, Eds.), Vol. 2, pp. 1-18. Libbey, London.
    • (1987) Advances in Pineal Research , vol.2 , pp. 1-18
    • Oksche, A.1    Korf, H.-W.2    Rodrfguez, E.M.3
  • 167
    • 33645867607 scopus 로고    scopus 로고
    • Species heterogeneity in pineal signal transduction mechanisms
    • S. M. Webb, M. Puig-Domingo, M. M011er, and P. Pévet, Eds., PJD, Westbury
    • Olcese, J., and Maronde, E. (1997). Species heterogeneity in pineal signal transduction mechanisms. In "Pineal Update. From Molecular Mechanisms to Clinical Implications" (S. M. Webb, M. Puig-Domingo, M. M011er, and P. Pévet, Eds.), pp. 161-171. PJD, Westbury.
    • (1997) Pineal Update. from Molecular Mechanisms to Clinical Implications , pp. 161-171
    • Olcese, J.1    Maronde, E.2
  • 169
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein, SNAP-25, differently expressed by neuronal subpopulations
    • Oyler, G. A., Higgins, G. A., Hart, R. A., Battenberg, E., Billingsley, M. L., Bloom, F. E., and Wilson, M. C. (1989). The identification of a novel synaptosomal-associated protein, SNAP-25, differently expressed by neuronal subpopulations. J. Cell Biol. 109, 3039-3052.
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, E.4    Billingsley, M.L.5    Bloom, F.E.6    Wilson, M.C.7
  • 170
    • 0026047660 scopus 로고
    • Developmental expression of the synaptosomal-associated protein SNAP-25 in the rat brain
    • Oyler, G. A., Polli, J. W., Wilson, M. C, and Billingsley, M. L. (1991). Developmental expression of the synaptosomal-associated protein SNAP-25 in the rat brain. Proc. Natl. Acad. Sci. USA 88, 785-789.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 785-789
    • Oyler, G.A.1    Polli, J.W.2    Wilson, M.C.3    Billingsley, M.L.4
  • 171
    • 0018582030 scopus 로고
    • Embryology of the diffuse neuroendocrine system and its relationship to the common peptides
    • Pearse, A. G. E., and Takor Takor, T. (1979). Embryology of the diffuse neuroendocrine system and its relationship to the common peptides. Fed. Proc. Fed. Am. Soc. Exp. Biol. 38, 2288-2294.
    • (1979) Fed. Proc. Fed. Am. Soc. Exp. Biol. , vol.38 , pp. 2288-2294
    • Pearse, A.G.E.1    Takor Takor, T.2
  • 172
    • 0027309505 scopus 로고
    • Immunocytochemical and electron microscopic characterization of macrophage/microglia cells and expression of class II major histocompatibility complex in the pineal gland of the rat
    • Pedersen, E. B., Fox, L. M., Castro, A. J., and McNulty, J. A. (1993). Immunocytochemical and electron microscopic characterization of macrophage/microglia cells and expression of class II major histocompatibility complex in the pineal gland of the rat. Cell Tissue Res. 272, 257-265
    • (1993) Cell Tissue Res. , vol.272 , pp. 257-265
    • Pedersen, E.B.1    Fox, L.M.2    Castro, A.J.3    McNulty, J.A.4
  • 173
    • 0027915355 scopus 로고
    • Neurotransmission and secretion
    • Pelham, H. R. B. (1993). Neurotransmission and secretion. Nature 364, 582.
    • (1993) Nature , vol.364 , pp. 582
    • Pelham, H.R.B.1
  • 174
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin, M. S., Fried, V. A., Mignery, G. A., Jahn, R., and Südhof, T. C. (1990). Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 345, 260-263.
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Südhof, T.C.5
  • 175
    • 0028157362 scopus 로고
    • Light and electron microscope distribution of the NMDA receptor subunit NMDAR1 in the rat nervous system using a selective anti-peptide antibody
    • Petralia, R. S., Yokotani, N., and Wenthold, R. J. (1994). Light and electron microscope distribution of the NMDA receptor subunit NMDAR1 in the rat nervous system using a selective anti-peptide antibody. J. Neurosd. 14, 667-696.
    • (1994) J. Neurosd. , vol.14 , pp. 667-696
    • Petralia, R.S.1    Yokotani, N.2    Wenthold, R.J.3
  • 176
    • 0029874694 scopus 로고    scopus 로고
    • The metabotropic glutamate receptors, mGIuR2 and mGluR3, show unique
    • Petralia, R. S., Wang, Y.-X., Niedzielski, A. S., and Wenthold, R. J. (1996). The metabotropic glutamate receptors, mGIuR2 and mGluR3, show unique postsynaptic, presynaptic and glial localizations. Neuroscience 71, 949-976.
    • (1996) Neuroscience , vol.71 , pp. 949-976
    • Petralia, R.S.1    Wang, Y.-X.2    Niedzielski, A.S.3    Wenthold, R.J.4
  • 177
    • 0025776680 scopus 로고
    • Binding of synaptotagmin to the alpha-latrotoxin receptor implicates both in synaptic exocytosis
    • Petrenko, A. G., Perin, M. S., Davletov, B. A., Ushkaryov, Y. A., Geppert, M., and Südhof, T. C. (1991). Binding of synaptotagmin to the alpha-latrotoxin receptor implicates both in synaptic exocytosis. Nature 353, 65-68.
    • (1991) Nature , vol.353 , pp. 65-68
    • Petrenko, A.G.1    Perin, M.S.2    Davletov, B.A.3    Ushkaryov, Y.A.4    Geppert, M.5    Südhof, T.C.6
  • 178
    • 0017409197 scopus 로고
    • On the presence of different populations of pinealocytes in the mammalian pineal gland
    • Pévet, P. (1977). On the presence of different populations of pinealocytes in the mammalian pineal gland. J. Neural Transmission 40, 289-304.
    • (1977) J. Neural Transmission , vol.40 , pp. 289-304
    • Pévet, P.1
  • 179
    • 0018559772 scopus 로고
    • Secretory processes in the mammalian pinealocyte under natural and experimental conditions
    • Pévet, P. (1979). Secretory processes in the mammalian pinealocyte under natural and experimental conditions. Prog. Brain Res. 52, 149-192.
    • (1979) Prog. Brain Res. , vol.52 , pp. 149-192
    • Pévet, P.1
  • 180
    • 0028156925 scopus 로고
    • N-Sec-1: A neural-specific syntaxin-binding protein
    • Pevsner, J., Hsu, S. C, and Scheller, R. H. (1994a). N-Sec-1: A neural-specific syntaxin-binding protein. Proc. Natl. Acad. Sci. USA 91, 1445-1449.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1445-1449
    • Pevsner, J.1    Hsu, C.S.2    Scheller, R.H.3
  • 182
    • 0028107932 scopus 로고
    • Rab GTPases: Master regulators of membrane trafficking
    • Pfeffer, S. R. (1994). Rab GTPases: Master regulators of membrane trafficking. Cun. Opin. Cell Biol. 6, 522-526.
    • (1994) Cun. Opin. Cell Biol. , vol.6 , pp. 522-526
    • Pfeffer, S.R.1
  • 183
    • 0016719353 scopus 로고
    • A light and electron microscopic study of the pineal gland of the groundsquirrel,Citellustridecemlineatus
    • Povlishock, J. T., Kriebel, R. M., and Seibel, H. R. (1975). A light and electron microscopic study of the pineal gland of the groundsquirrel,Citellustridecemlineatus. ./4 m.J./l/Mr. 143,465-484.
    • (1975) /4 M.J./l/Mr. , vol.143 , pp. 465-484
    • Povlishock, J.T.1    Kriebel, R.M.2    Seibel, H.R.3
  • 184
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • Protopopov, V., Govindan, B., Novick, P., and Gerst, J. E. (1993). Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell 74, 855-861.
    • (1993) Cell , vol.74 , pp. 855-861
    • Protopopov, V.1    Govindan, B.2    Novick, P.3    Gerst, J.E.4
  • 185
    • 0025884651 scopus 로고
    • Ultrastructural visualization of exocytosis in the pig pineal gland
    • Przybylska, B., Masson-Pévet, M., and Pévet, P. (1991). Ultrastructural visualization of exocytosis in the pig pineal gland. Cell Tissue Res. 264, 377-379.
    • (1991) Cell Tissue Res. , vol.264 , pp. 377-379
    • Przybylska, B.1    Masson-Pévet, M.2    Pévet, P.3
  • 186
    • 0026021015 scopus 로고
    • Ultrastructural demonstration of neurohaemal contacts in the internal zone of the median eminence of the Mongolian gerbil (Meriones unguiculatus): Correlation with synaptophysin immunohistochemistry
    • Redecker, P. (1991). Ultrastructural demonstration of neurohaemal contacts in the internal zone of the median eminence of the Mongolian gerbil (Meriones unguiculatus): Correlation with synaptophysin immunohistochemistry. Histochemistry 95, 503-511.
    • (1991) Histochemistry , vol.95 , pp. 503-511
    • Redecker, P.1
  • 187
    • 0027279610 scopus 로고
    • Dense accumulations of synaptic-Iike microvesicles in "dark" pinealocytes of the gerbil pineal gland
    • Redecker, P. (1993a). Dense accumulations of synaptic-Iike microvesicles in "dark" pinealocytes of the gerbil pineal gland. J. Neurocytol. 22, 572-581.
    • (1993) J. Neurocytol. , vol.22 , pp. 572-581
    • Redecker, P.1
  • 188
    • 0027690386 scopus 로고
    • Close microtopographical relationships between sympathetic nerve terminals and bulbous process endings of pinealocytes in the pineal gland of the Mongolian gerbil
    • Redecker, P. (1993b). Close microtopographical relationships between sympathetic nerve terminals and bulbous process endings of pinealocytes in the pineal gland of the Mongolian gerbil. J. Pineal Res. 15, 199-207.
    • (1993) J. Pineal Res. , vol.15 , pp. 199-207
    • Redecker, P.1
  • 189
    • 0028829924 scopus 로고
    • The ras-like rabSA protein is present in pinealocytes of the gerbil pineal gland
    • Redecker, P. (1995). The ras-like rabSA protein is present in pinealocytes of the gerbil pineal gland. Neurosci. Lett. 184, 117-120.
    • (1995) Neurosci. Lett. , vol.184 , pp. 117-120
    • Redecker, P.1
  • 190
    • 0030030910 scopus 로고    scopus 로고
    • Synaptotagmin I, synaptobrevin II, and syntaxin I are coexpressed in rat and gerbil pinealocytes
    • Redecker, P. (1996). Synaptotagmin I, synaptobrevin II, and syntaxin I are coexpressed in rat and gerbil pinealocytes. Cell Tissue Res. 283, 443-454.
    • (1996) Cell Tissue Res. , vol.283 , pp. 443-454
    • Redecker, P.1
  • 191
    • 0032515388 scopus 로고    scopus 로고
    • Developmental pattern of cell type-specific calretinin immunoreactivity in the postnatal gerbil pineal gland
    • Redecker, P. (1998). Developmental pattern of cell type-specific calretinin immunoreactivity in the postnatal gerbil pineal gland. Dev. Brain Res. 105, 43-50.
    • (1998) Dev. Brain Res. , vol.105 , pp. 43-50
    • Redecker, P.1
  • 192
    • 0027505663 scopus 로고
    • Synaptophysin-A common constituent of presumptive secretory microvesicles in the mammalian pinealocyte: A study of rat and gerbil pineal glands
    • Redecker, P., and Bargsten, G. (1993). Synaptophysin-A common constituent of presumptive secretory microvesicles in the mammalian pinealocyte: A study of rat and gerbil pineal glands. J. Neurosci. Res. 34, 79-96.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 79-96
    • Redecker, P.1    Bargsten, G.2
  • 193
    • 0028126776 scopus 로고
    • Glutamate immunoreactivity is enriched over pinealocytes of the gerbil pineal gland
    • Redecker, P., and Veh, R. W. (1994). Glutamate immunoreactivity is enriched over pinealocytes of the gerbil pineal gland. Cell Tissue Res. 278, 579-588.
    • (1994) Cell Tissue Res. , vol.278 , pp. 579-588
    • Redecker, P.1    Veh, R.W.2
  • 194
    • 0025166796 scopus 로고
    • Immunohistochemical localization of synaptophysin (p38) in the pineal gland of the Mongolian gerbil (Meriones unguiculatus)
    • Redecker, P., Grube, D., and Jahn, R. (1990). Immunohistochemical localization of synaptophysin (p38) in the pineal gland of the Mongolian gerbil (Meriones unguiculatus). Anat. Embryol. 181, 433-440.
    • (1990) Anat. Embryol. , vol.181 , pp. 433-440
    • Redecker, P.1    Grube, D.2    Jahn, R.3
  • 195
    • 0025890975 scopus 로고
    • Synaptophysin immunoreactivity in the mammalian endocrine pancreas
    • Redecker, P., Jörns, A., Jahn, R., and Grube, D. (1991). Synaptophysin immunoreactivity in the mammalian endocrine pancreas. Cell Tissue Res. 264, 461-467.
    • (1991) Cell Tissue Res. , vol.264 , pp. 461-467
    • Redecker, P.1    Jörns, A.2    Jahn, R.3    Grube, D.4
  • 196
    • 0028997620 scopus 로고
    • Differential distribution of synaptotagmin I and rab3 in the anterior pituitary of four mammalian species
    • Redecker, P., Cetin, Y., and Grube, D. (1995). Differential distribution of synaptotagmin I and rab3 in the anterior pituitary of four mammalian species. Neuroendocrinology 62,101-110.
    • (1995) Neuroendocrinology , vol.62 , pp. 101-110
    • Redecker, P.1    Cetin, Y.2    Grube, D.3
  • 197
    • 0030002032 scopus 로고    scopus 로고
    • Differential immunocytochemical localization of calretinin in the pineal gland of three mammalian species
    • Redecker, P., Cetin, Y., and Korf, H.-W. (1996a). Differential immunocytochemical localization of calretinin in the pineal gland of three mammalian species. J. Neurocytol. 25, 9-18.
    • (1996) J. Neurocytol. , vol.25 , pp. 9-18
    • Redecker, P.1    Cetin, Y.2    Korf, H.-W.3
  • 198
    • 0030208747 scopus 로고    scopus 로고
    • Rat and gerbil pinealocytes contain the synaptosomal-associated protein 25 (SNAP-25)
    • Redecker, P., Weyer, C, and Grube, D. (1996b). Rat and gerbil pinealocytes contain the synaptosomal-associated protein 25 (SNAP-25). J. Pineal Res. 21, 29-34.
    • (1996) J. Pineal Res. , vol.21 , pp. 29-34
    • Redecker, P.1    Weyer, C.2    Grube, D.3
  • 199
    • 0031055844 scopus 로고    scopus 로고
    • Expression of synaptic membrane proteins in gerbil pinealocytes in primary culture
    • Redecker, P., Pabst, H., Gebert, A., and Steinlechner, S. (1997). Expression of synaptic membrane proteins in gerbil pinealocytes in primary culture. J. Neurosci. Res. 47,509-520.
    • (1997) J. Neurosci. Res. , vol.47 , pp. 509-520
    • Redecker, P.1    Pabst, H.2    Gebert, A.3    Steinlechner, S.4
  • 200
    • 0031874732 scopus 로고    scopus 로고
    • Munc-18-1 and cysteine string protein (csp) in pinealocytes of the gerbil pineal gland
    • Redecker, P., Pabst, H., and Grube, D. (1998). Munc-18-1 and cysteine string protein (csp) in pinealocytes of the gerbil pineal gland. Cell Tissue Res. 293, 245-252.
    • (1998) Cell Tissue Res. , vol.293 , pp. 245-252
    • Redecker, P.1    Pabst, H.2    Grube, D.3
  • 201
    • 0025875235 scopus 로고
    • GABA and pancreatic /3-cells: Colocalization of glutamic acid decarboxylase (GAD) and GABA with synaptic-like microvesicles suggests their role in GABA storage and secretion
    • Reetz, A., Solimena, M., Matteoli, M., Folli, F., Takei, K., and De Camilli, P. (1991). GABA and pancreatic /3-cells: Colocalization of glutamic acid decarboxylase (GAD) and GABA with synaptic-like microvesicles suggests their role in GABA storage and secretion. EMBO J. 10,1275-1284.
    • (1991) EMBO J. , vol.10 , pp. 1275-1284
    • Reetz, A.1    Solimena, M.2    Matteoli, M.3    Folli, F.4    Takei, K.5    De Camilli, P.6
  • 202
  • 204
    • 0019781433 scopus 로고
    • The mammalian pineal gland: Structure and function
    • Reiter, R. J. (1981). The mammalian pineal gland: Structure and function. Am. J. Anat. 162, 287-313.
    • (1981) Am. J. Anat. , vol.162 , pp. 287-313
    • Reiter, R.J.1
  • 205
    • 0025915557 scopus 로고
    • Melatonin: The chemical expression of darkness
    • Reiter, R. J. (1991a). Melatonin: The chemical expression of darkness. Mol. Cell. Endocrinol. 79, C153-C158.
    • (1991) Mol. Cell. Endocrinol. , vol.79
    • Reiter, R.J.1
  • 206
    • 0025758136 scopus 로고
    • Pineal melatonin: Cell biology of its synthesis and of its physiological interactions
    • Reiter, R. J. (1991b). Pineal melatonin: Cell biology of its synthesis and of its physiological interactions. Endocr. Rev. 12, 151-180.
    • (1991) Endocr. Rev. , vol.12 , pp. 151-180
    • Reiter, R.J.1
  • 207
    • 0026955748 scopus 로고
    • Remembrance: Growing up with the pineal gland: Early recollections
    • Reiter, R. J. (1992). Remembrance: Growing up with the pineal gland: Early recollections. Endocrinology 131, 2039-2041.
    • (1992) Endocrinology , vol.131 , pp. 2039-2041
    • Reiter, R.J.1
  • 208
    • 0028793087 scopus 로고
    • Functional pleiotropy of the neurohormone melatonin: Antioxidant protection and neuroendocrine regulation
    • Reiter, R. J. (1995). Functional pleiotropy of the neurohormone melatonin: Antioxidant protection and neuroendocrine regulation. Front. Neuroendocrinol. 16, 383-415.
    • (1995) Front. Neuroendocrinol. , vol.16 , pp. 383-415
    • Reiter, R.J.1
  • 209
    • 0029617713 scopus 로고
    • Melatonin madness
    • Reppert, S. M., and Weaver, D. R. (1995). Melatonin madness. Cell S3, 1059-1062.
    • (1995) Cell S , vol.3 , pp. 1059-1062
    • Reppert, S.M.1    Weaver, D.R.2
  • 210
    • 0021245635 scopus 로고
    • Electrophysiological properties of rat pinealocytes: Evidence for circadian and ultradian rhythms
    • Reuss, S., and Vollrath, L. (1984). Electrophysiological properties of rat pinealocytes: Evidence for circadian and ultradian rhythms. Exp. Brain Res. 55, 455-461.
    • (1984) Exp. Brain Res. , vol.55 , pp. 455-461
    • Reuss, S.1    Vollrath, L.2
  • 211
    • 0022998061 scopus 로고
    • Rat pineal exhibits two electrophysiological patterns of response to microiontophoretic norepinephrine application
    • Reyes-Vazquez, C., Prieto-Gomez, B., Aides, L. D., and Dafny, N. (1986). Rat pineal exhibits two electrophysiological patterns of response to microiontophoretic norepinephrine application. J. Pineal Res. 3, 213-222.
    • (1986) J. Pineal Res. , vol.3 , pp. 213-222
    • Reyes-Vazquez, C.1    Prieto-Gomez, B.2    Aides, L.D.3    Dafny, N.4
  • 213
    • 0031693296 scopus 로고    scopus 로고
    • Mechanics of membrane fusion
    • Rizo, J., and Südhof, T. C. (1998). Mechanics of membrane fusion. Nature Struct. Biol. 5, 839-842.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 839-842
    • Rizo, J.1    Südhof, T.C.2
  • 214
    • 0015794529 scopus 로고
    • Structure and innervation of the pineal gland of the rabbit, Oryctolagus cuniculus (L.). II. An electron microscopic investigation of the pinealocytes
    • Romijn, H. J. (1973). Structure and innervation of the pineal gland of the rabbit, Oryctolagus cuniculus (L.). II. An electron microscopic investigation of the pinealocytes. Z. Zellforscli. 141, 545-560.
    • (1973) Z. Zellforscli. , vol.141 , pp. 545-560
    • Romijn, H.J.1
  • 217
    • 0025163589 scopus 로고
    • GABA as a presumptive paracrine signal in the pineal gland. Evidence on an intrapineal GABAergic system
    • Rosenstein, R. E., Chuluyan, H. E., Diaz, M. C., and Cardinal!, D. P. (1990). GABA as a presumptive paracrine signal in the pineal gland. Evidence on an intrapineal GABAergic system. Brain Res. Bull. 25, 339-344.
    • (1990) Brain Res. Bull. , vol.25 , pp. 339-344
    • Rosenstein, R.E.1    Chuluyan, H.E.2    Diaz, M.C.3    Cardinal, D.P.4
  • 218
    • 0030023904 scopus 로고    scopus 로고
    • Vamp/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues
    • Rossetto, O., Gorza, L., Schiavo, G., Schiavo, N., Scheller, R. H., and Montecucco, C. (1996). Vamp/synaptobrevin isoforms 1 and 2 are widely and differentially expressed in nonneuronal tissues. J. Cell Biol. 132, 167-179.
    • (1996) J. Cell Biol. , vol.132 , pp. 167-179
    • Rossetto, O.1    Gorza, L.2    Schiavo, G.3    Schiavo, N.4    Scheller, R.H.5    Montecucco, C.6
  • 219
    • 0027203579 scopus 로고
    • Gene expression of KA type and NMD a receptors and of a glycine transporter in the rat pineal gland
    • Sato, K., Kiyama, H., Shimada, S., and Tohyama, M. (1993). Gene expression of KA type and NMD A receptors and of a glycine transporter in the rat pineal gland. Neiiroendocrinology 58, 77-79.
    • (1993) Neiiroendocrinology , vol.58 , pp. 77-79
    • Sato, K.1    Kiyama, H.2    Shimada, S.3    Tohyama, M.4
  • 220
    • 0028335647 scopus 로고
    • Analysis of the heterogeneity within bovine pineal gland by immunohistochemistry and in situ hybridization
    • Sato, T., Kaneko, M., Fujieda, H., Deguchi, T., and Wake, K. (1994). Analysis of the heterogeneity within bovine pineal gland by immunohistochemistry and in situ hybridization. Cell Tissue Res. 277, 201-209.
    • (1994) Cell Tissue Res. , vol.277 , pp. 201-209
    • Sato, T.1    Kaneko, M.2    Fujieda, H.3    Deguchi, T.4    Wake, K.5
  • 221
    • 17444446041 scopus 로고    scopus 로고
    • Cholinergic neurons and terminal Fields revealed by immunohistochemistry for the vesicular acetylcholine transporter. I. Central nervous system
    • Schäfer, M. K.-H., Eiden, L. E., and Weihe, E. (1998). Cholinergic neurons and terminal Fields revealed by immunohistochemistry for the vesicular acetylcholine transporter. I. Central nervous system. Neitroscience 84, 331-359.
    • (1998) Neitroscience , vol.84 , pp. 331-359
    • Schäfer, M.K.-H.1    Eiden, L.E.2    Weihe, E.3
  • 222
    • 0018219518 scopus 로고
    • Membrane recycling in the cone cell endings in the turtle retina
    • Schaeffer, S. F., and Raviola, E. (1978). Membrane recycling in the cone cell endings in the turtle retina. J. Cell Biol. 79, 802-825.
    • (1978) J. Cell Biol. , vol.79 , pp. 802-825
    • Schaeffer, S.F.1    Raviola, E.2
  • 223
    • 0031033690 scopus 로고    scopus 로고
    • Nitric oxide inhibits electrically active units in the rat pineal gland
    • Schenda, J., and Vollrath, L. (1997). Nitric oxide inhibits electrically active units in the rat pineal gland. J. Neural Transmission 104, 53-58.
    • (1997) J. Neural Transmission , vol.104 , pp. 53-58
    • Schenda, J.1    Vollrath, L.2
  • 225
    • 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, J. E., and Söllner, T. H. (1997). 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 94, 997-1001.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Söllner, T.H.4
  • 226
    • 0025952638 scopus 로고
    • Synaptin/synaptophysin, p65 and SV2: Their presence in adrenal chromaffin granules and sympathetic large dense core vesicles
    • Schmidle, T., Weiler, R., Desnos, C., Scherman, D., Fischer-Colbrie, R., Floor, E., and Winkler, H. (1991). Synaptin/synaptophysin, p65 and SV2: Their presence in adrenal chromaffin granules and sympathetic large dense core vesicles. Biochim. Biophys. Ada 1060,251-256.
    • (1991) Biochim. Biophys. Ada , vol.1060 , pp. 251-256
    • Schmidle, T.1    Weiler, R.2    Desnos, C.3    Scherman, D.4    Fischer-Colbrie, R.5    Floor, E.6    Winkler, H.7
  • 227
    • 0030936274 scopus 로고    scopus 로고
    • Synaptic-like microvesicles of neuroendocrine cells originate from a novel compartment that is continuous with the plasma membrane and devoid of transferrin receptor
    • Schmidt, A., Hannah, M. J., and Huttner, W. B. (1997). Synaptic-like microvesicles of neuroendocrine cells originate from a novel compartment that is continuous with the plasma membrane and devoid of transferrin receptor. J. Cell Biol. 137, 445-458.
    • (1997) J. Cell Biol. , vol.137 , pp. 445-458
    • Schmidt, A.1    Hannah, M.J.2    Huttner, W.B.3
  • 228
    • 0027321736 scopus 로고
    • Intermediate stages in the disassembly of synaptic ribbons in cone photoreceptors of the crucian carp, Carassius carassius
    • Schmilz, F., and Drenckhahn, D. (1993). Intermediate stages in the disassembly of synaptic ribbons in cone photoreceptors of the crucian carp, Carassius carassius. Cell Tissue Res. 272, 487-490.
    • (1993) Cell Tissue Res. , vol.272 , pp. 487-490
    • Schmilz, F.1    Drenckhahn, D.2
  • 229
    • 0027938284 scopus 로고
    • Photoreceptor-specific proteins in the mammalian pineal organ: Immunocytochemical data and functional considerations
    • Schomerus, C., Ruth, P., and Korf, H.-W. (1994). Photoreceptor-specific proteins in the mammalian pineal organ: Immunocytochemical data and functional considerations. Acta Neitrobiol. Exp. 54(Suppl.), 9-17.
    • (1994) Acta Neitrobiol. Exp. , vol.54 , Issue.SUPPL. , pp. 9-17
    • Schomerus, C.1    Ruth, P.2    Korf, H.-W.3
  • 230
    • 0029004897 scopus 로고
    • Calcium responses of isolated, immunocytochemically identified rat pinealocytes to noradrenergic, cholinergic and vasopressinergic stimulations
    • Schomerus, C, Laedtke, E., and Korf, H.-W. (1995). Calcium responses of isolated, immunocytochemically identified rat pinealocytes to noradrenergic, cholinergic and vasopressinergic stimulations. Nenrochem. Int. 27, 163-175.
    • (1995) Nenrochem. Int. , vol.27 , pp. 163-175
    • Schomerus, C.1    Laedtke, E.2    Korf, H.-W.3
  • 231
    • 0025315191 scopus 로고
    • Neuronal markers in the rodent pineal gland-An immunohistochemical investigation
    • Schröder, H., Bendig, A., Dahl, D., Gröschel-Stewart, U., and Vollrath, L. (1990). Neuronal markers in the rodent pineal gland-An immunohistochemical investigation. Histochemistry 94, 309-314.
    • (1990) Histochemistry , vol.94 , pp. 309-314
    • Schröder, H.1    Bendig, A.2    Dahl, D.3    Gröschel-Stewart, U.4    Vollrath, L.5
  • 232
    • 0018900967 scopus 로고
    • Electrophysiological evidence for arcadian rhythmicity in a mammalian pineal organ
    • Semm, P., and Vollrath, L. (1990). Electrophysiological evidence for arcadian rhythmicity in a mammalian pineal organ. J. Neural Transmission 47, 181-190.
    • (1990) J. Neural Transmission , vol.47 , pp. 181-190
    • Semm, P.1    Vollrath, L.2
  • 233
    • 0014260126 scopus 로고
    • The fine structure of the hamster pineal gland
    • Sheridan, M. N., and Reiter, R. J. (1968). The fine structure of the hamster pineal gland. Am. J. Anat. 122, 357-376.
    • (1968) Am. J. Anat. , vol.122 , pp. 357-376
    • Sheridan, M.N.1    Reiter, R.J.2
  • 234
    • 0032538838 scopus 로고    scopus 로고
    • Neuroendocrine synaptic vesicles are formed in vitro by both clathrin-dependent and clathrin-independent pathways
    • Shi, G., Faündez, V., Roos, J., Dell'Angelica, E. C, and Kelly, R.B. (1998). Neuroendocrine synaptic vesicles are formed in vitro by both clathrin-dependent and clathrin-independent pathways. J. Cell Biol. 143, 947-955.
    • (1998) J. Cell Biol. , vol.143 , pp. 947-955
    • Shi, G.1    Faündez, V.2    Roos, J.3    Dell'Angelica, E.C.4    Kelly, R.B.5
  • 235
    • 0027436941 scopus 로고
    • Rab proteins and the road maps for intracellular transport
    • Simons, K., and Zerial, M. (1993). Rab proteins and the road maps for intracellular transport. Neuron 11, 789-799.
    • (1993) Neuron , vol.11 , pp. 789-799
    • Simons, K.1    Zerial, M.2
  • 236
    • 0031438061 scopus 로고    scopus 로고
    • Nutrient regulation of gamma-aminobutyric acid release from islet beta cells
    • Smismans, A., Schult, F., and Pipeleers, D. (1997). Nutrient regulation of gamma-aminobutyric acid release from islet beta cells. Diabelologia 40, 1411-1415.
    • (1997) Diabelologia , vol.40 , pp. 1411-1415
    • Smismans, A.1    Schult, F.2    Pipeleers, D.3
  • 237
    • 0032567834 scopus 로고    scopus 로고
    • Synapses: Glia help synapses form and function
    • Smith, S. J. (1998). Synapses: Glia help synapses form and function. Curr. Biol. 8, R158-R160.
    • (1998) Curr. Biol. , vol.8
    • Smith, S.J.1
  • 238
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of vesicle docking, activation, and fusion
    • Söllner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H., and Rothman, J. E. (1993a). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 240
    • 0029295355 scopus 로고
    • Pineal gene expression: Dawn in a dark matter
    • Stehle, J. H. (1995). Pineal gene expression: Dawn in a dark matter. J. Pineal Res. 18,179-190.
    • (1995) J. Pineal Res. , vol.18 , pp. 179-190
    • Stehle, J.H.1
  • 241
    • 0023276866 scopus 로고
    • Electrophysiological characterization of the pineal gland of golden hamsters
    • Stehle, J. H., Reuss, S., and Vollrath, L. (1987). Electrophysiological characterization of the pineal gland of golden hamsters. Exp. Brain Res. 67, 27-32.
    • (1987) Exp. Brain Res. , vol.67 , pp. 27-32
    • Stehle, J.H.1    Reuss, S.2    Vollrath, L.3
  • 242
    • 0024409697 scopus 로고
    • Day-night differences in the sensitivity of adrenoceptors in the Syrian hamster pineal gland: An in vivo iontophoretic study
    • Stehle, J. H., Reuss, S., and Vollrath, L. (1989). Day-night differences in the sensitivity of adrenoceptors in the Syrian hamster pineal gland: An in vivo iontophoretic study. Brain Res. 488, 275-282
    • (1989) Brain Res. , vol.488 , pp. 275-282
    • Stehle, J.H.1    Reuss, S.2    Vollrath, L.3
  • 243
    • 0002060125 scopus 로고
    • Impact of photoperiod and melatonin on reproduc-tion in small mammals
    • Steinlechner, S., and Niklowitz, P. (1992). Impact of photoperiod and melatonin on reproduc-tion in small mammals. Anim. Reprod. Sci. 30,1-28.
    • (1992) Anim. Reprod. Sci. , vol.30 , pp. 1-28
    • Steinlechner, S.1    Niklowitz, P.2
  • 244
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof, T. C. (1995). The synaptic vesicle cycle: A cascade of protein-protein interactions. Nature 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 245
    • 0023661124 scopus 로고
    • A synaptic vesicle protein with a novel cytoplasmic domain and four transmembrane regions
    • Südhof, T. C, Lottspeich, F., Greengard, P., Mehl, E., and Jahn, R. (1987). A synaptic vesicle protein with a novel cytoplasmic domain and four transmembrane regions. Science 238, 1142-1144.
    • (1987) Science , vol.238 , pp. 1142-1144
    • Südhof, T.C.1    Lottspeich, F.2    Greengard, P.3    Mehl, E.4    Jahn, R.5
  • 246
    • 0024659539 scopus 로고
    • A synaptic vesicle membrane protein is conserved from mammals to Drosophila
    • Südhof, T. C., Baumert, M., Perin, M. S., and Jahn, R. (1989a). A synaptic vesicle membrane protein is conserved from mammals to Drosophila. Neuron 2, 1475-1481.
    • (1989) Neuron , vol.2 , pp. 1475-1481
    • Südhof, T.C.1    Baumert, M.2    Perin, M.S.3    Jahn, R.4
  • 248
    • 0029894198 scopus 로고    scopus 로고
    • The synaptic vesicle cycle: A single vesicle budding step involving clathrin and dynamin
    • Takei, K., Mundigl, O., Daniell, L., and DeCamilli, P. (1996). The synaptic vesicle cycle: A single vesicle budding step involving clathrin and dynamin. J. Cell Dial. 133, 1237-1250.
    • (1996) J. Cell Dial. , vol.133 , pp. 1237-1250
    • Takei, K.1    Mundigl, O.2    Daniell, L.3    DeCamilli, P.4
  • 249
    • 0030025674 scopus 로고    scopus 로고
    • Rab3D protein is a specific marker for zymogen granules in gastric chief cells of rats and rabbits
    • Tang, L. H., Gumkowski, F. D., Sengupta, D., Modlin, I. M., and Jamieson, J. D. (1996). Rab3D protein is a specific marker for zymogen granules in gastric chief cells of rats and rabbits. Gastroenterology 110, 809-820.
    • (1996) Gastroenterology , vol.110 , pp. 809-820
    • Tang, L.H.1    Gumkowski, F.D.2    Sengupta, D.3    Modlin, I.M.4    Jamieson, J.D.5
  • 250
    • 0023685654 scopus 로고
    • Identification of synaptophysin as a hexameric channel protein of the synaptic vesicle membrane
    • Thomas, L., Härtung, K., Langosch, D., Rehm, H., Bamberg, E., Franke, W. W., and Betz, H. (1988). Identification of synaptophysin as a hexameric channel protein of the synaptic vesicle membrane. Science 242, 1050-1053.
    • (1988) Science , vol.242 , pp. 1050-1053
    • Thomas, L.1    Härtung, K.2    Langosch, D.3    Rehm, H.4    Bamberg, E.5    Franke, W.W.6    Betz, H.7
  • 251
    • 0028014432 scopus 로고
    • A role for synaptic vesicles in nonneuronal cells: Clues from pancreatic cells and from chromaffin cells
    • Thomas-Reetz, A., and De Camilli, P. (1994). A role for synaptic vesicles in nonneuronal cells: Clues from pancreatic cells and from chromaffin cells. FASEB J. 8, 209-216.
    • (1994) FASEB J. , vol.8 , pp. 209-216
    • Thomas-Reetz, A.1    De Camilli, P.2
  • 252
    • 0027265223 scopus 로고
    • A y-aminobutyric acid transporter driven by a proton pump is present in synapticlike microvesicles of pancreatic cells
    • Thomas-Reetz, A., Hell, J. W., During, M. J., Walch-Solimena, C, Jahn, R., and De Camilli, P. (1993). A y-aminobutyric acid transporter driven by a proton pump is present in synapticlike microvesicles of pancreatic cells. Proc. Natl. Acad. Sci. USA 90, 5317-5321.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5317-5321
    • Thomas-Reetz, A.1    Hell, J.W.2    During, M.J.3    Walch-Solimena, C.4    Jahn, R.5    De Camilli, P.6
  • 253
    • 0027141312 scopus 로고
    • The differential expression of 16 NMDA and non-NMDA receptor subunits in the rat spinal cord and in periaqueductal gray
    • Tolle, T. R., Berthele, A., Zieglgänsberger, W., Seeburg, P. H., and Wisden, W. (1993). The differential expression of 16 NMDA and non-NMDA receptor subunits in the rat spinal cord and in periaqueductal gray. J. Neitrosci. 13, 5009-5028.
    • (1993) J. Neitrosci. , vol.13 , pp. 5009-5028
    • Tolle, T.R.1    Berthele, A.2    Zieglgänsberger, W.3    Seeburg, P.H.4    Wisden, W.5
  • 254
    • 0006602702 scopus 로고
    • VAMP-1: A synaptic vesicle-associated integral membrane protein
    • Trimble, W. S., Cowan, D. M., and Scheller, R. H. (1988). VAMP-1: A synaptic vesicle-associated integral membrane protein. Proc. Natl. Acad. Sci. USA 85, 4538-4542.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 255
    • 0028803946 scopus 로고
    • Differential distributions of novel synaptotagmins: Comparison to synapsins
    • Ullrich, B., and Südhof, T. C. (1995). Differential distributions of novel synaptotagmins: Comparison to synapsins. Neiirophannacology 34, 1371-1377.
    • (1995) Neiirophannacology , vol.34 , pp. 1371-1377
    • Ullrich, B.1    Südhof, T.C.2
  • 257
    • 0032080204 scopus 로고    scopus 로고
    • Attenuated influx of calcium ions at nerve endings of csp and shibire mutant Drosophila
    • Umbach, J. A., Saitoe, M., Kidokoro, Y., and Gundersen, C. B. (1998). Attenuated influx of calcium ions at nerve endings of csp and shibire mutant Drosophila. J. Neurosci. 18, 3233-3240.
    • (1998) J. Neurosci. , vol.18 , pp. 3233-3240
    • Umbach, J.A.1    Saitoe, M.2    Kidokoro, Y.3    Gundersen, C.B.4
  • 258
    • 0027969112 scopus 로고
    • Glutamate inhibits the isoprenaline-induced raise in melatonin synthesis by organ cultures of rat pineal glands
    • an Wyk, E., and Daya, S. (1994). Glutamate inhibits the isoprenaline-induced raise in melatonin synthesis by organ cultures of rat pineal glands. Med. Sci. Res. 22, 635-636.
    • (1994) Med. Sci. Res. , vol.22 , pp. 635-636
    • Wyk, E.1    Daya, S.2
  • 259
    • 0030932857 scopus 로고    scopus 로고
    • DOC2 proteins in rat brain: Complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion
    • Verhage, M., de Vries, K. J., Roshol, H., Burbach, J. P. H., Gispen, W. H., and Südhof, T. C. (1997). DOC2 proteins in rat brain: Complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion. Neuron 18, 453-461.
    • (1997) Neuron , vol.18 , pp. 453-461
    • Verhage, M.1    De Vries, K.J.2    Roshol, H.3    Burbach, J.P.H.4    Gispen, W.H.5    Südhof, T.C.6
  • 260
    • 0028909684 scopus 로고
    • Similar fine-structural localization of immunoreactive glutamate in the pineal complex and retina of frogs
    • Vigh, B., Vigh-Teichmann, I., Debreceni, K., and Takacs, J. (1995). Similar fine-structural localization of immunoreactive glutamate in the pineal complex and retina of frogs. Arch. Histol. Cytol. 58, 37-44.
    • (1995) Arch. Histol. Cytol. , vol.58 , pp. 37-44
    • Vigh, B.1    Vigh-Teichmann, I.2    Debreceni, K.3    Takacs, J.4
  • 261
    • 0002528154 scopus 로고
    • The pineal organ
    • A. Oksche and L. Vollrath, Eds., Springer, Berlin
    • Vollrath, L. (1981). The pineal organ. In "Handbuch der Mikroskopischen Anatomie des Menschen" (A. Oksche and L. Vollrath, Eds.), Vol. VI/7. Springer, Berlin.
    • (1981) Handbuch der Mikroskopischen Anatomie des Menschen , vol.6-7
    • Vollrath, L.1
  • 262
    • 0002411507 scopus 로고
    • Functional anatomy of the human pineal gland
    • R. J. Reiter, Ed., Raven Press, New York
    • Vollrath, L. (1984). Functional anatomy of the human pineal gland. In "The Pineal Gland" (R. J. Reiter, Ed.), pp. 285-322. Raven Press, New York.
    • (1984) The Pineal Gland , pp. 285-322
    • Vollrath, L.1
  • 263
    • 0015880323 scopus 로고
    • The synaptic ribbons of the guinea-pig pineal gland under normal and experimental conditions
    • Vollrath, L., and Huss, H. (1973). The synaptic ribbons of the guinea-pig pineal gland under normal and experimental conditions. Z. Zellforsch. Mikrosk. Anat. 139, 417-429.
    • (1973) Z. Zellforsch. Mikrosk. Anat. , vol.139 , pp. 417-429
    • Vollrath, L.1    Huss, H.2
  • 264
    • 0344301706 scopus 로고
    • Neuronal properties of mammalian pinealocytes?
    • G. P. Trentini, C. de Gaetani, and P. Pévet, Eds., Raven Press, New York
    • Vollrath, L., and Schröder, H. (1987). Neuronal properties of mammalian pinealocytes? In "Fundamentals and Clinics in Pineal Research" (G. P. Trentini, C. de Gaetani, and P. Pévet, Eds.), Vol. 44, pp. 13-23. Raven Press, New York.
    • (1987) Fundamentals and Clinics in Pineal Research , vol.44 , pp. 13-23
    • Vollrath, L.1    Schröder, H.2
  • 265
    • 0024950543 scopus 로고
    • The plasticity of synaptic ribbons
    • Vollrath, L., and Seidel, A. (1989). The plasticity of synaptic ribbons. Biomed. Res. 10(Suppl. 3), 207-212.
    • (1989) Biomed. Res. , vol.10 , Issue.3 SUPPL. , pp. 207-212
    • Vollrath, L.1    Seidel, A.2
  • 266
  • 267
    • 0031034980 scopus 로고    scopus 로고
    • Depletion and replenishment of vesicle pools at a ribbon-type synaptic terminal
    • von Gersdorff, H., and Matthews, G. (1997). Depletion and replenishment of vesicle pools at a ribbon-type synaptic terminal. J. Neurosci. 15, 1919-1927.
    • (1997) J. Neurosci. , vol.15 , pp. 1919-1927
    • Von Gersdorff, H.1    Matthews, G.2
  • 268
    • 0030175780 scopus 로고    scopus 로고
    • Evidence that vesicles on the synaptic ribbon of retinal bipolar neurons can be rapidly released
    • von Gersdorff, H., Vardi, E., Matthews, G., and Sterling, P. (1996). Evidence that vesicles on the synaptic ribbon of retinal bipolar neurons can be rapidly released. Neuron 16,1221-1277.
    • (1996) Neuron , vol.16 , pp. 1221-1277
    • Von Gersdorff, H.1    Vardi, E.2    Matthews, G.3    Sterling, P.4
  • 269
    • 0030952081 scopus 로고    scopus 로고
    • The evolutionary pressure to inactivate. a subclass of synaptotagmin with an amino acid substitution that abolishes Ca2+ binding
    • von Poser, C., Ichtchenko, K., Shao, X., Rizo, J., and Südhof, T. C. (1997). The evolutionary pressure to inactivate. A subclass of synaptotagmin with an amino acid substitution that abolishes Ca2+ binding. J. Biol. Cliem. 272, 14314-14319.
    • (1997) J. Biol. Cliem. , vol.272 , pp. 14314-14319
    • Von Poser, C.1    Ichtchenko, K.2    Shao, X.3    Rizo, J.4    Südhof, T.C.5
  • 270
    • 0031048269 scopus 로고    scopus 로고
    • Presynaptic bodies ("ribbons"): From ultrastructural observations to molecular perspectives
    • Wagner, H.-J. (1997). Presynaptic bodies ("ribbons"): From ultrastructural observations to molecular perspectives. Cell Tissue Res. 287, 435-446.
    • (1997) Cell Tissue Res. , vol.287 , pp. 435-446
    • Wagner, H.-J.1
  • 271
    • 0028815453 scopus 로고
    • The t-SNAREs syntaxin l and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
    • Walch-Solimena, C., Blasi, J., Edelmann, L., Chapman, E. R., von Mollard, G. F., and Jahn, R. (1995). The t-SNAREs syntaxin l and SNAP-25 are present on organelles that participate in synaptic vesicle recycling. J. Cell Biol. 128, 637-645.
    • (1995) J. Cell Biol. , vol.128 , pp. 637-645
    • Walch-Solimena, C.1    Blasi, J.2    Edelmann, L.3    Chapman, E.R.4    Von Mollard, G.F.5    Jahn, R.6
  • 272
    • 0014378807 scopus 로고
    • The mammalian pineal organ: Electron microscopic studies on the fine structure of pinealocytes, glial cells and on the perivascular compartment
    • Wartenberg, H. (1968). The mammalian pineal organ: Electron microscopic studies on the fine structure of pinealocytes, glial cells and on the perivascular compartment. Z. Zellforsch. 86, 74-97.
    • (1968) Z. Zellforsch. , vol.86 , pp. 74-97
    • Wartenberg, H.1
  • 273
    • 0028942065 scopus 로고
    • Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin
    • Washbourne, P., Schiavo, G., and Montecucco, C. (1995). Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin. Biochem. J. 305, 721-724.
    • (1995) Biochem. J. , vol.305 , pp. 721-724
    • Washbourne, P.1    Schiavo, G.2    Montecucco, C.3
  • 275
    • 0018144991 scopus 로고
    • The pineal gland of the gerbil, Meriones unguiculatus
    • Welsh, M. G., and Reiter, R. J. (1978). The pineal gland of the gerbil, Meriones unguiculatus. Cell Tissue Res. 193, 323-336.
    • (1978) Cell Tissue Res. , vol.193 , pp. 323-336
    • Welsh, M.G.1    Reiter, R.J.2
  • 276
    • 0018605756 scopus 로고
    • The pineal gland of the gerbil, Meriones unguiculatus. II. Morphometric analysis over a 24-hour period
    • Welsh, M. G., Cameron, I. L., and Reiter, R. J. (1979). The pineal gland of the gerbil, Meriones unguiculatus. II. Morphometric analysis over a 24-hour period. Cell Tissue Res. 204,95-109.
    • (1979) Cell Tissue Res. , vol.204 , pp. 95-109
    • Welsh, M.G.1    Cameron, I.L.2    Reiter, R.J.3
  • 279
    • 0022391791 scopus 로고
    • Identification and localization of synaptophysin, an integral membrane glycoprotein of Mr 38,000 characteristic of presynaptic vesicles
    • Wiedenmann, B., and Franke, W. W. (1985). Identification and localization of synaptophysin, an integral membrane glycoprotein of Mr 38,000 characteristic of presynaptic vesicles. Cell 41, 1017-1028.
    • (1985) Cell , vol.41 , pp. 1017-1028
    • Wiedenmann, B.1    Franke, W.W.2
  • 280
    • 0029812286 scopus 로고    scopus 로고
    • SNAP-25, enSNAREd in neurotransmission ' and regulation of behaviour
    • Wilson, M. C., Mehta, P. P., and Hess, E. J. (1996). SNAP-25, enSNAREd in neurotransmission ' and regulation of behaviour. Biochem. Soc. Trans. 24, 670-676.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 670-676
    • Wilson, M.C.1    Mehta, P.P.2    Hess, E.J.3
  • 281
    • 0027198558 scopus 로고
    • A complex mosaic of high-affinity kainate receptors in rat brain
    • Wisden, W., and Seeburg, P. H. (1993). A complex mosaic of high-affinity kainate receptors in rat brain. J. Nenrosci. 13, 3582-3598.
    • (1993) J. Nenrosci. , vol.13 , pp. 3582-3598
    • Wisden, W.1    Seeburg, P.H.2
  • 282
    • 0030992881 scopus 로고    scopus 로고
    • The roles of NSF, SNAPs and SNAREs during membrane fusion
    • Woodman, P. G. (1997). The roles of NSF, SNAPs and SNAREs during membrane fusion. Biochim. Biophys. Acta 1357, 155-172.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 155-172
    • Woodman, P.G.1
  • 284
    • 0030254346 scopus 로고    scopus 로고
    • Microvesicle-mediated exocytosis of glutamate is a novel paracrine-like chemical transduction mechanism and inhibits melatonin secretion in rat pinealocytes
    • Yamada, H., Yamamoto, A., Yodozawa, S., Kozaki, S., Takahashi, M., Monta, M., Michibata, H., Furuichi.T., Mikoshiba, K., and Moriyama, Y. (1996b). Microvesicle-mediated exocytosis of glutamate is a novel paracrine-like chemical transduction mechanism and inhibits melatonin secretion in rat pinealocytes. J. Pineal Res. 21,175-191.
    • (1996) J. Pineal Res. , vol.21 , pp. 175-191
    • Yamada, H.1    Yamamoto, A.2    Yodozawa, S.3    Kozaki, S.4    Takahashi, M.5    Monta, M.6    Michibata, H.7    Furuichi, T.8    Mikoshiba, K.9    Moriyama, Y.10
  • 285
    • 0030849897 scopus 로고    scopus 로고
    • L-Aspartate-evoked inhibition of melatonin production in rat pineal glands
    • Yamada, H., Yamaguchi, A., and Moriyama, Y. (1997a). L-Aspartate-evoked inhibition of melatonin production in rat pineal glands. Neurosci. Lett. 228, 103-106.
    • (1997) Neurosci. Lett. , vol.228 , pp. 103-106
    • Yamada, H.1    Yamaguchi, A.2    Moriyama, Y.3
  • 287
    • 0032125275 scopus 로고    scopus 로고
    • Acetylcholine triggers L-glutamate exocytosis via nicotinic receptors and inhibits melatonin synthesis in rat pinealocytes
    • Yamada, H., Ogura, A., Koizumi, S., Yamaguchi, A., and Moriyama, Y. (1998a). Acetylcholine triggers L-glutamate exocytosis via nicotinic receptors and inhibits melatonin synthesis in rat pinealocytes. J. Neurosci. 18, 4946-4952.
    • (1998) J. Neurosci. , vol.18 , pp. 4946-4952
    • Yamada, H.1    Ogura, A.2    Koizumi, S.3    Yamaguchi, A.4    Moriyama, Y.5
  • 290
  • 291
    • 0028168590 scopus 로고
    • Synaptotagmin I is a high affinity receptor for clathrin AP-2: Implications for membrane recycling
    • Zhang, J. Z., Davletov, B. A., Südhof, T. C, and Anderson, R. G. W. (1994). Synaptotagmin I is a high affinity receptor for clathrin AP-2: Implications for membrane recycling. Cell 78, 751-760.
    • (1994) Cell , vol.78 , pp. 751-760
    • Zhang, J.Z.1    Davletov, B.A.2    Südhof, T.C.3    Anderson, R.G.W.4
  • 292
    • 0026602071 scopus 로고
    • Molecular cloning of a cDNA encoding a novel protein related to the neuronal vesicle protein synaptophysin
    • Zhong, C., Hayzer, D. J., and Runge, M. S. (1992). Molecular cloning of a cDNA encoding a novel protein related to the neuronal vesicle protein synaptophysin. Biochim. Biophys. Acta 1129, 235-238.
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 235-238
    • Zhong, C.1    Hayzer, D.J.2    Runge, M.S.3
  • 294
    • 0028281387 scopus 로고
    • Paralysis and early death in cysteine string protein mutants of Drosophila
    • Zinsmaier, K. E., Eberle, K. K., Buchner, E., Walter, N., and Benzer, S. (1994). Paralysis and early death in cysteine string protein mutants of Drosophila. Science 263, 977-980.
    • (1994) Science , vol.263 , pp. 977-980
    • Zinsmaier, K.E.1    Eberle, K.K.2    Buchner, E.3    Walter, N.4    Benzer, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.