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A cDNA that suppresses MPP+ toxicity encodes a vesicular amine transporter
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Erickson JD, Eiden LE, Hoffman BJ. Expression cloning of a reserpine-sensitive vesicular monoamine transporter. Proc Natl Acad Sci USA. 89:1992;10993-10997.
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The Caenorhabditis elegans unc-17 gene: A putative vesicular acetylcholine transporter
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Alfonso A, Grundahl K, Duerr JS, Han H-P, Rand JB. The Caenorhabditis elegans unc-17 gene: a putative vesicular acetylcholine transporter. Science. 261:1993;617-619.
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0028048214
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Functional identification of a vesicular acetylcholine transporter and its expression from a 'cholinergic' gene locus
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Erickson JD, Varoqui H, Schafer MD, Modi W, Diebler MF, Weihe E, Rand J, Eiden LE, Bonner TI, Usdin TB. Functional identification of a vesicular acetylcholine transporter and its expression from a 'cholinergic' gene locus. J Biol Chem. 269:1994;21929-21932.
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Differential localization of vesicular acetylcholine and monoamine transporters in PC12 cells but not CHO cells
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of special interest. This report documents the differential localization of VMATs and VAChT in PC12 cells that was suggested by Bauerfeind et al. 1993 [33]. VMATs localize preferentially to LDCVs whereas VAChT localizes preferentially to light vesicles, including SLMVs, in PC12 cells.
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Liu Y, Edwards RH. Differential localization of vesicular acetylcholine and monoamine transporters in PC12 cells but not CHO cells. of special interest J Cell Biol. 139:1997;907-916 This report documents the differential localization of VMATs and VAChT in PC12 cells that was suggested by Bauerfeind et al. 1993 [33]. VMATs localize preferentially to LDCVs whereas VAChT localizes preferentially to light vesicles, including SLMVs, in PC12 cells.
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Liu, Y.1
Edwards, R.H.2
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0029861246
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Active transport of acetylcholine by the human vesicular acetylcholine transporter
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Varoqui H, Erickson JD. Active transport of acetylcholine by the human vesicular acetylcholine transporter. J Biol Chem. 271:1996;27229-27232.
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Varoqui, H.1
Erickson, J.D.2
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16
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0030968854
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Expression of putative vesicular acetylcholine transporter facilitates quantal transmitter packaging
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of outstanding interest. Using a Xenopus culture system in which motor neurons form synapses with muscle cells, expression of VAChT in the motor neurons but not the muscle cells increases quantal size, indicating that the transporter can limit the rate of SV filling. VAChT expression also increases the frequency of release, presumably by increasing the detection of events, but increased VAChT expression may also increase the number of SVs capable of transmitter release. Neutralization of an aspartate in TMD10 of VAChT reduces the amount of transmitter packaged by the endogeneous wild-type transporter, possibly by promoting efflux.
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Song H-j, Ming G-I, Fon E, Bellocchio E, Edwards RH, Poo M-m. Expression of putative vesicular acetylcholine transporter facilitates quantal transmitter packaging. of outstanding interest Neuron. 18:1997;815-826 Using a Xenopus culture system in which motor neurons form synapses with muscle cells, expression of VAChT in the motor neurons but not the muscle cells increases quantal size, indicating that the transporter can limit the rate of SV filling. VAChT expression also increases the frequency of release, presumably by increasing the detection of events, but increased VAChT expression may also increase the number of SVs capable of transmitter release. Neutralization of an aspartate in TMD10 of VAChT reduces the amount of transmitter packaged by the endogeneous wild-type transporter, possibly by promoting efflux.
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Neuron
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Song H-J1
Ming G-I2
Fon, E.3
Bellocchio, E.4
Edwards, R.H.5
Poo M-M6
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17
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0028263975
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The chromaffin granule and synaptic vesicle amine transporters differ in substrate recognition and sensitivity to inhibitors
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Peter D, Jimenez J, Liu Y, Kim J, Edwards RH. The chromaffin granule and synaptic vesicle amine transporters differ in substrate recognition and sensitivity to inhibitors. J Biol Chem. 269:1994;7231-7237.
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Peter, D.1
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Gracz LM, Wang W-C, Parsons SM. Cholinergic synaptic vesicle heterogeneity: evidence for regulation of acetylcholine transport. Biochemistry. 27:1988;5268-5274.
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0030931721
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VMAT2 knockout mice: Heterozygous display reduced amphetamine-conditioned reward, enhanced amphetamine locomotion and enhanced MPTP toxicity
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+/- mice show slightly increased sensitivity to the neurotoxin MPTP, consistent with a role for VMAT2 in protection against this form of toxicity (see Liu et al., 1992 [8]).
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+/- mice show slightly increased sensitivity to the neurotoxin MPTP, consistent with a role for VMAT2 in protection against this form of toxicity (see Liu et al., 1992 [8]).
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Takahashi, N.1
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Kostic, V.6
Jackson-Lewis, V.7
Przedborski, S.8
Uhl, G.R.9
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20
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0031458637
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Vesicular transport regulates monoamine storage and release but is not essential for amphetamine action
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-/- animals and permits survival to several weeks. Heterozygotes show substantially reduced brain monoamine levels, presumably accounting for the behavioral defects observed in Takahashi et al., 1997 [19] and Wang et al., 1997 [21] and supporting a role for the vesicular transporters in regulating transmitter release.
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-/- animals and permits survival to several weeks. Heterozygotes show substantially reduced brain monoamine levels, presumably accounting for the behavioral defects observed in Takahashi et al., 1997 [19] and Wang et al., 1997 [21] and supporting a role for the vesicular transporters in regulating transmitter release.
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Neuron
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Fon, E.A.1
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Sun B-C3
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Edwards, R.H.6
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21
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0031458923
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Knockout of the vesicular monoamine transporter 2 gene results in neonatal death and supersensitivity to cocaine and amphetamine
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+/- animals show dramatically increased sensitivity to apomorphine, cocaine, amphetamine and ethanol.
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+/- animals show dramatically increased sensitivity to apomorphine, cocaine, amphetamine and ethanol.
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Neuron
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Wang Y-M1
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Miller, G.W.7
Wightman, R.M.8
Caron, M.G.9
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0025122167
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Induction of the vesicular monoamine transporter by elevated potassium concentration in culture of rat sympathetic neurons
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Regulation of the chromaffin granule catecholamine transporter in cultured bovine adrenal medullary cell-stimulus biosynthesis coupling
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Desnos C, Laran M, Scherman D. Regulation of the chromaffin granule catecholamine transporter in cultured bovine adrenal medullary cell-stimulus biosynthesis coupling. J Neurochem. 59:1992;2105-2112.
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24
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Expression and regulation of the bovine vesicular monoamine transporter gene
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ATP-dependent uptake of 5-hydroxytryptamine by secretory granules isolated from thyroid parafollicular cells
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Secretagogue-induced gating of chloride channels in the secretory vesicles of parafollicular cells
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Tamir H, Piscopo I, Liu KP, Hsiung SC, Adlersberg M, Nicolaides M, al-Awqati Q, Nunez EA, Gershon MD. Secretagogue-induced gating of chloride channels in the secretory vesicles of parafollicular cells. Endocrinology. 135:1994;2045-2057.
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Al-Awqati, Q.7
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27
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0029147857
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Effects of protein kinase inhibitors and protein phosphatase inhibitors on cyclic AMP-dependent down-regulation of vesicular monoamine transport in pheochromocytoma PC12 cells
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Nakanishi N, Onozawa S, Matsumoto R, Hasegawa H, Yamada S. Effects of protein kinase inhibitors and protein phosphatase inhibitors on cyclic AMP-dependent down-regulation of vesicular monoamine transport in pheochromocytoma PC12 cells. FEBS Lett. 368:1995;411-414.
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0030965452
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Phosphorylation of a vesicular monoamine transporter by casein kinase II
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Krantz DE, Peter D, Liu Y, Edwards RH. Phosphorylation of a vesicular monoamine transporter by casein kinase II. J Biol Chem. 272:1997;6752-6759.
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Krantz, D.E.1
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Time course of extracellular dopamine and behavioral sensitization to cocaine. II. Dopamine perikarya
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Kalivas PW, Duffy P. Time course of extracellular dopamine and behavioral sensitization to cocaine. II. Dopamine perikarya. J Neurosci. 13:1993;276-284.
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Kalivas, P.W.1
Duffy, P.2
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30
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0029071155
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The vesicular monoamine transporter-2 is present in small synaptic vesicles and preferentially localizes to large dense core vesicles in rat solitary tract nuclei
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Nirenberg MJ, Liu Y, Peter D, Edwards RH, Pickel VM. The vesicular monoamine transporter-2 is present in small synaptic vesicles and preferentially localizes to large dense core vesicles in rat solitary tract nuclei. Proc Natl Acad Sci USA. 92:1995;8773-8777.
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Nirenberg, M.J.1
Liu, Y.2
Peter, D.3
Edwards, R.H.4
Pickel, V.M.5
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31
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0029898811
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Ultrastructural localization of the vesicular monoamine transporter-2 in midbrain dopaminergic neurons: Potential sites for somatodendritic storage and release of dopamine
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of special interest. VMAT2 occurs in tubulovesicular structures of midbrain dopamine cell bodies and dendrites as well as in SVs and LDCVs in striatal terminals. Although these structures may simply represent an intermediate in transit from one compartment to another, these vesicles may also mediate the release of dopamine from midbrain cell bodies and dendrites described in Kalivas and Duffy, 1993 [29].
-
Nirenberg MJ, Chan J, Liu Y, Edwards RH, Pickel VM. Ultrastructural localization of the vesicular monoamine transporter-2 in midbrain dopaminergic neurons: potential sites for somatodendritic storage and release of dopamine. of special interest J Neurosci. 16:1996;4135-4145 VMAT2 occurs in tubulovesicular structures of midbrain dopamine cell bodies and dendrites as well as in SVs and LDCVs in striatal terminals. Although these structures may simply represent an intermediate in transit from one compartment to another, these vesicles may also mediate the release of dopamine from midbrain cell bodies and dendrites described in Kalivas and Duffy, 1993 [29].
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Nirenberg, M.J.1
Chan, J.2
Liu, Y.3
Edwards, R.H.4
Pickel, V.M.5
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32
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0027971587
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Preferential localization of a vesicular monoamine transporter to dense core vesicles in PC12 cells
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Liu Y, Schweitzer ES, Nirenberg MJ, Pickel VM, Evans CJ, Edwards RH. Preferential localization of a vesicular monoamine transporter to dense core vesicles in PC12 cells. J Cell Biol. 127:1994;1419-1433.
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Liu, Y.1
Schweitzer, E.S.2
Nirenberg, M.J.3
Pickel, V.M.4
Evans, C.J.5
Edwards, R.H.6
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33
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0027179911
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Selective storge of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin
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Bauerfeind R, Regnier-Vigouroux A, Flatmark T, Huttner WB. Selective storge of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin. Neuron. 11:1993;105-121.
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Bauerfeind, R.1
Regnier-Vigouroux, A.2
Flatmark, T.3
Huttner, W.B.4
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34
-
-
0029939094
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Visualization of the vesicular acetylcholine transporter in cholinergic nerve terminals and its targeting to a specific population of small synaptic vesicles
-
of special interest. Immuno-electron microscopy demonstrates VAChT in SVs of rat brain and in SLMVs of PC12 cells, supporting the difference in localization from that of the VMATs.
-
Weihe E, Tao-Cheng J-H, Schafer MK-H, Erickson JD, Eiden LE. Visualization of the vesicular acetylcholine transporter in cholinergic nerve terminals and its targeting to a specific population of small synaptic vesicles. of special interest Proc Natl Acad Sci USA. 93:1996;3547-3552 Immuno-electron microscopy demonstrates VAChT in SVs of rat brain and in SLMVs of PC12 cells, supporting the difference in localization from that of the VMATs.
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Proc Natl Acad Sci USA
, vol.93
, pp. 3547-3552
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Weihe, E.1
Tao-Cheng J-H2
Schafer Mk-H3
Erickson, J.D.4
Eiden, L.E.5
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35
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0028845359
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Identification of residues involved in substrate recognition by a vesicular monoamine transporter
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Merickel A, Rosandich P, Peter D, Edwards RH. Identification of residues involved in substrate recognition by a vesicular monoamine transporter. J Biol Chem. 270:1995;25798-25804.
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J Biol Chem
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Merickel, A.1
Rosandich, P.2
Peter, D.3
Edwards, R.H.4
-
36
-
-
0031054527
-
Charged residues in transmembrane domains II and XI of a vesicular monoamine transporter form a charge pair that promotes high affinity substrates recognition
-
of special interest. of special interest. A highly conserved lysine in TMD2 of VMAT2 forms a charge pair with a highly conserved aspartate in TMD11. Neutralization of each residues alone eliminates transport activity but neutralization of both restores function, providing some of the first information about the packing of helices in these proteins.
-
of special interest Merickel A, Kaback HR, Edwards RH. Charged residues in transmembrane domains II and XI of a vesicular monoamine transporter form a charge pair that promotes high affinity substrates recognition. of special interest J Biol Chem. 272:1997;5403-5408 A highly conserved lysine in TMD2 of VMAT2 forms a charge pair with a highly conserved aspartate in TMD11. Neutralization of each residues alone eliminates transport activity but neutralization of both restores function, providing some of the first information about the packing of helices in these proteins.
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(1997)
J Biol Chem
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Merickel, A.1
Kaback, H.R.2
Edwards, R.H.3
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37
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17544366949
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Modification of the pH profile and tetrabenazine sensitivity of rat VMAT1 by replacement of aspartate 404 with glutamate
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+ as measured by reserpine binding. Supporting a role for this residue in proton translocation, replacement of the aspartate with glutamate alters the pH profile for transport.
-
+ as measured by reserpine binding. Supporting a role for this residue in proton translocation, replacement of the aspartate with glutamate alters the pH profile for transport.
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J Biol Chem
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Steiner-Mordoch, S.1
Shirvan, A.2
Schuldiner, S.3
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0027272707
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Genes required for GABA function in Caenorhabditis elegans
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McIntire, S.1
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Horvitz, H.R.3
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39
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0030734546
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Identification and characterization of the vesicular GABA transporter
-
of special interest. This report describes the identification of a genomic fragment from C. elegans that complements the defect in unc-47, a mutant with a presynaptic defect in GABAergic transmission. A vertebrate homolog has a pattern of expression restricted to GABAergic cell groups and, further, confers vesicular GABA transport with the expected properties on heterologous expression. The sequence predicts 10 TMDs and a relatively large cytoplasmic amino terminus.In addition, it defines a novel family of vesicular neurotransmitter transports that may also include a transporter for the principal excitatory neurotransmitter, glutamate.
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McIntire SL, Reimer RJ, Schuske K, Edwards RH, Jorgensen EM. Identification and characterization of the vesicular GABA transporter. of special interest Nature. 389:1997;870-876 This report describes the identification of a genomic fragment from C. elegans that complements the defect in unc-47, a mutant with a presynaptic defect in GABAergic transmission. A vertebrate homolog has a pattern of expression restricted to GABAergic cell groups and, further, confers vesicular GABA transport with the expected properties on heterologous expression. The sequence predicts 10 TMDs and a relatively large cytoplasmic amino terminus.In addition, it defines a novel family of vesicular neurotransmitter transports that may also include a transporter for the principal excitatory neurotransmitter, glutamate.
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Nature
, vol.389
, pp. 870-876
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McIntire, S.L.1
Reimer, R.J.2
Schuske, K.3
Edwards, R.H.4
Jorgensen, E.M.5
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Active transport of gamma-aminobutyric acid and glycine into synaptic vesicles
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