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The biochemistry or neurotransmitter secretion
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Exocytosis: A molecular and physiological perspective
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An excellent up-to-date review that describes recent advances pertaining to the mechanisms of exocytosis and their relationships to short-term synaptic plasticity (i.e. facilitation augmentation, and post-tetanic potentiation) and vesicle pool dynamics. of special interest
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Zucker RS. Exocytosis: a molecular and physiological perspective. Neuron. 17:1996;1049-1055 An excellent up-to-date review that describes recent advances pertaining to the mechanisms of exocytosis and their relationships to short-term synaptic plasticity (i.e. facilitation augmentation, and post-tetanic potentiation) and vesicle pool dynamics. of special interest.
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Zucker, R.S.1
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2+-sensitive release machinery. of special interest
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2+-sensitive release machinery. of special interest.
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Hsu, S.F.1
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Ultrafast exocytosis elicited by calcium current in synaptic terminals of retinal bipolar neurons
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Definition of the readily releasable pool of vesicles at hippocampal synapses
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Rosenmund C, Stevens CF. Definition of the readily releasable pool of vesicles at hippocampal synapses. Neuron. 16:1996;1197-1207.
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Bittner MA, Holz RW. Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components. J Biol Chem. 267:1992;16219-16225.
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Neher E, Zucker RS. Multiple calcium-dependent processes related to secretion in bovine chromaffin cells. Neuron. 10:1993;21-30.
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Synaptotagmins: C2-domain proteins that regulate membrane traffic
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An excellent, comprehensive review of the synaptotagmin family, with an emphasis on recent advances in the study of synaptotagmin I structure and function. of special interest
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Südhof TC, Rizo J. Synaptotagmins: C2-domain proteins that regulate membrane traffic. Neuron. 17:1996;379-388 An excellent, comprehensive review of the synaptotagmin family, with an emphasis on recent advances in the study of synaptotagmin I structure and function. of special interest.
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Südhof, T.C.1
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Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants
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Littleton JT, Stem M, Perin M, Bellen HJ. Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants. Proc Natl Acad Sci USA. 91:1994;10888-10892.
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Absence of synaptotagmin disrupts excitation-secretion coupling during synaptic transmission
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Broadie K, Bellen HJ, DiAntonio A, Littleton JT, Schwarz TL. Absence of synaptotagmin disrupts excitation-secretion coupling during synaptic transmission. Proc Natl Acad Sci USA. 91:1994;10727-10731.
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Broadie, K.1
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Evidence for synaptotagmin as an inhibitor clamp on synaptic vesicle release in Aplysia neurons
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Martin KC, Hu Y, Armitage BA, Siegelbaum SA, Kandel ER, Kaang B-K. Evidence for synaptotagmin as an inhibitor clamp on synaptic vesicle release in Aplysia neurons. Proc Natl Acad Sci USA. 92:1995;11307-11311.
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Martin, K.C.1
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19
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0028799119
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Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse preterminal
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Mikoshiba K, Fukuda M, Moreira JE, Lewis FM, Sugimori M, Niinobe M, Llinas R. Role of the C2A domain of synaptotagmin in transmitter release as determined by specific antibody injection into the squid giant synapse preterminal. Proc Natl Acad Sci USA. 92:1995;10703-10707.
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Mikoshiba, K.1
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Llinas, R.7
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20
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0028986240
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2+/phospholipid-binding fold
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2+-binding site formed by two loops connecting the β-strands. These results provide a prototype structure for comparison with, and modeling of, other C2 domain sequences. of special interest
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2+-binding site formed by two loops connecting the β-strands. These results provide a prototype structure for comparison with, and modeling of, other C2 domain sequences. of special interest.
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(1995)
Cell
, vol.80
, pp. 929-938
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Sutton, R.B.1
Davletov, B.A.2
Berghuis, A.M.3
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Sprang, S.R.5
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21
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0029666292
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2+-binding motif in C2 domains of synaptotagmin and protein kinase C
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2+ binding is not associated with large conformational changes. of special interest
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2+ binding is not associated with large conformational changes. of special interest.
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(1996)
Science
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Shao, X.1
Davletov, B.A.2
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Südhof, T.C.4
Rizo, J.5
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22
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0031019191
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2+-dependent electrostatic switch
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2+-binding site were found to have no apparent effect on C2 structure but abolished syntaxin binding. Contrary to previous reports [25,26], the amino-terminal domain of syntaxin was found to interact with the C2A domain. of special interest
-
2+-binding site were found to have no apparent effect on C2 structure but abolished syntaxin binding. Contrary to previous reports [25,26], the amino-terminal domain of syntaxin was found to interact with the C2A domain. of special interest.
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(1997)
Neuron
, vol.18
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Shao, X.1
Li, C.2
Fernandez, I.3
Zhang, X.4
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Rizo, J.6
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23
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0028989281
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2+-dependent and -independent activities of neural and non-neural synaptotagmins
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2+] that promoted the interaction of syntaxin with some of the synaptotagmins was found to be comparable to that required to promote neurotransmitter release. of special interest
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2+] that promoted the interaction of syntaxin with some of the synaptotagmins was found to be comparable to that required to promote neurotransmitter release. of special interest.
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(1995)
Nature
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, pp. 594-599
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Li, C.1
Ullrich, B.2
Zhang, J.Z.3
Anderson, R.G.4
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26
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0029917101
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Localization of synaptotagmin-binding domains on syntaxin
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2+-independent interactions with syntaxin, respectively. Furthermore, a carboxyl-terminal region of syntaxin adjacent to the membrane anchor was shown to be sufficient for synaptotagmin interactions (but see [22]). of special interest
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2+-independent interactions with syntaxin, respectively. Furthermore, a carboxyl-terminal region of syntaxin adjacent to the membrane anchor was shown to be sufficient for synaptotagmin interactions (but see [22]). of special interest.
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(1996)
J Neurosci
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Kee, Y.1
Scheller, R.H.2
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30
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0029861418
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Isoform-specific, calcium-regulated interaction of the synaptic vesicle proteins SV2 and synaptotagmin
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50 of 10μM. These results suggest a regulatory relationship between synaptotagmin I and SV2A. of special interest
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50 of 10μM. These results suggest a regulatory relationship between synaptotagmin I and SV2A. of special interest.
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(1996)
J Biol Chem
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Schivell, A.E.1
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Nature
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2+-dependent conformational change in synaptotagmin I. J Biol Chem. 269:1994;28547-28550.
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J Biol Chem
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0028791349
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Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins
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2+), as well as a C1 domain (suggesting possible direct regulation by phorbol ester). Munc13-1 was shown to be a peripheral membrane protein enriched in a synaptic plasma membrane fraction, lending further support to a possible function in neurotransmitter release. of special interest
-
2+), as well as a C1 domain (suggesting possible direct regulation by phorbol ester). Munc13-1 was shown to be a peripheral membrane protein enriched in a synaptic plasma membrane fraction, lending further support to a possible function in neurotransmitter release. of special interest.
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(1995)
J Biol Chem
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Brose, N.1
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Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin
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Shirataki H, Kaibuchi K, Sakoda T, Kishida S, Yamaguchi T, Wada K, Miyazaki M, Takai Y. Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin. Mol Cell Biol. 13:1993;2061-2068.
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Shirataki, H.1
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Wada, K.6
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Takai, Y.8
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35
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0028897324
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Doc2: A novel brain protein having two repeated C2-like domains
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Orita S, Sasaki T, Naito A, Komuro R, Ohtsuka T, Maeda M, Suzuki H, Igarashi H, Takai Y. Doc2: a novel brain protein having two repeated C2-like domains. Biochem Biophys Res Commun. 206:1995;439-448.
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Orita, S.1
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2+ sensors for the fast and slow components of neurotransmitter release
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2+ sensors for the fast and slow components of neurotransmitter release. J Biol Chem. 270:1995;24898-24902.
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J Biol Chem
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Li, C.1
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2+/phospholipid-binding protein, depends on rab3A/3C
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2+/phospholipid-binding protein, depends on rab3A/3C. Neuron. 13:1994;885-898.
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Li, C.1
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2+-binding domains. J Biol Chem. 268:1993;27164-27170.
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Yamaguchi, T.1
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39
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0029077932
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Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. Studies in adrenal chromaffin cells
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See annotation [41]. of special interest
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Chung SH, Takai Y, Holz RW. Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. Studies in adrenal chromaffin cells. J Biol Chem. 270:1995;16714-16718 See annotation [41]. of special interest.
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J Biol Chem
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Chung, S.H.1
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Holz, R.W.3
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41
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0030461545
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Involvement of Rabphilin-3A in cortical granule exocytosis in mouse eggs
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Along with [39] and [40], this article provides evidence of a role for rabphilin in the regulation of exocytosis. In chromaffin cells [39], overexpression of rabphilin enhanced regulated secretion while anti-sense downregulation of expression, as well as introduction of soluble fragments, reduced regulated secretion from both chromaffin cells [39] and PC12 cells [40]. Rabphilin was also found to be expressed in mouse eggs (demonstrating that it is not restricted to neuroendocrine cells), where soluble rabphilin fragments were shown to inhibit cortical granule exocytosis [41]. of special interest
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Masumoto N, Sasaki T, Tahara M, Mammoto A, Ikebuchi Y, Tasaka K, Tokunaga M, Takai Y, Miyake A. Involvement of Rabphilin-3A in cortical granule exocytosis in mouse eggs. J Cell Biol. 135:1996;1741-1747 Along with [39] and [40], this article provides evidence of a role for rabphilin in the regulation of exocytosis. In chromaffin cells [39], overexpression of rabphilin enhanced regulated secretion while anti-sense downregulation of expression, as well as introduction of soluble fragments, reduced regulated secretion from both chromaffin cells [39] and PC12 cells [40]. Rabphilin was also found to be expressed in mouse eggs (demonstrating that it is not restricted to neuroendocrine cells), where soluble rabphilin fragments were shown to inhibit cortical granule exocytosis [41]. of special interest.
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(1996)
J Cell Biol
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Masumoto, N.1
Sasaki, T.2
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Tasaka, K.6
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Takai, Y.8
Miyake, A.9
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42
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0029665075
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2+-dependent exocytosis from PC12 cells
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2+-dependent secretion, while anti-sense downregulation of expression and production of truncated doc2 fragments had the opposite effect. of special interest
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2+-dependent secretion, while anti-sense downregulation of expression and production of truncated doc2 fragments had the opposite effect. of special interest.
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(1996)
J Biol Chem
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Orita, S.1
Sasaki, T.2
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Takai, Y.7
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43
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0027370160
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Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein
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Kishida S, Shirataki H, Sasaki T, Kato M, Kaibuchi K, Takai Y. Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein. J Biol Chem. 268:1993;22259-22261.
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Kishida, S.1
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0029935431
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Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras
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Stahl B, Chou JH, Li C, Südhof TC, Jahn R. Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras. EMBO J. 15:1996;1799-1809.
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0026475394
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The Caenorhabditis elegans unc-13 gene product is a phospholipid-dependent high-affinity phorbol ester receptor
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Ahmed S, Maruyama IN, Kozma R, Lee J, Brenner S, Lim L. The Caenorhabditis elegans unc-13 gene product is a phospholipid-dependent high-affinity phorbol ester receptor. Biochem J. 287:1992;995-999.
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Ahmed, S.1
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46
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0031027591
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Direct interaction of the rat unc-13 homologue munc13-1 with the N terminus of syntaxin
-
2+-independent interaction requires a region between the second and third C2 domains of munc13-1. In addition, the amino-terminal region of syntaxin was found to be sufficient for munc13-1 interaction, making this the first of syntaxin's many interactions to displays this property. of special interest
-
2+-independent interaction requires a region between the second and third C2 domains of munc13-1. In addition, the amino-terminal region of syntaxin was found to be sufficient for munc13-1 interaction, making this the first of syntaxin's many interactions to displays this property. of special interest.
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(1997)
J Biol Chem
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Betz, A.1
Okamoto, M.2
Benseler, F.3
Brose, N.4
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0026778460
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Syntaxin: A synaptic protein implicated in the docking of synaptic vesicles at presynaptic active zones
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Bennett MK, Calakos N, Scheller RH. Syntaxin: a synaptic protein implicated in the docking of synaptic vesicles at presynaptic active zones. Science. 257:1992;255-259.
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Science
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Bennett, M.K.1
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Scheller, R.H.3
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48
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0029935177
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Interaction of SNARE complexes with P/Q-type calcium channels in rat cerebellar synaptosomes
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Martin MN, Charvin N, Leveque C, Sato K, Nishiki T, Kozaki S, Takahashi M, Seagar M. Interaction of SNARE complexes with P/Q-type calcium channels in rat cerebellar synaptosomes. J Biol Chem. 271:1996;6567-6570.
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Martin, M.N.1
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49
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0028595727
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Identification of a syntaxin-binding site on N-type calcium channels
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Sheng ZH, Rettig J, Takahashi M, Catterall WA. Identification of a syntaxin-binding site on N-type calcium channels. Neuron. 13:1994;1303-1313.
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Sheng, Z.H.1
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52
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0030273248
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2+ channels.
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2+-channel complex being functionally important, although other cations of the channel peptide have not been ruled out. of special interest
-
2+-channel complex being functionally important, although other cations of the channel peptide have not been ruled out. of special interest.
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(1996)
Neuron
, vol.17
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Mochida, S.1
Sheng, Z.H.2
Baker, C.3
Kobayashi, H.4
Catterall, W.A.5
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53
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0028783997
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Functional impact of syntaxin on gating of N-type and Q-type calcium channels
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2+ that triggers neurotransmitter release and also raises the possibility that syntaxin could act as a regulator of channel activity independent of its role in exocytosis. of special interest
-
2+ that triggers neurotransmitter release and also raises the possibility that syntaxin could act as a regulator of channel activity independent of its role in exocytosis. of special interest.
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(1995)
Nature
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Bezprozvanny, I.1
Scheller, R.H.2
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Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins
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Hay JC, Martin TF. Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins. J Cell Biol. 119:1992;139-151.
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Hay, J.C.1
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