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Volumn 84, Issue 6, 2014, Pages 1287-1301

Vesicular glutamate transporters use flexible anion and cation binding sites for efficient accumulation of neurotransmitter

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE; GLUTAMIC ACID; LIPOSOME; POTASSIUM ION; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; VESICULAR GLUTAMATE TRANSPORTER 1; AGENTS INTERACTING WITH TRANSMITTER, HORMONE OR DRUG RECEPTORS; ANION; MONOVALENT CATION; POTASSIUM;

EID: 84926284521     PISSN: 08966273     EISSN: 10974199     Source Type: Journal    
DOI: 10.1016/j.neuron.2014.11.008     Document Type: Article
Times cited : (67)

References (72)
  • 3
    • 0020680992 scopus 로고
    • Effects of extracellular fluid volume and plasma bicarbonate concentration on proximal acidification in the rat
    • Alpern R.J., Cogan M.G., Rector F.C. Effects of extracellular fluid volume and plasma bicarbonate concentration on proximal acidification in the rat. J.Clin. Invest. 1983, 71:736-746.
    • (1983) J.Clin. Invest. , vol.71 , pp. 736-746
    • Alpern, R.J.1    Cogan, M.G.2    Rector, F.C.3
  • 4
    • 77956665248 scopus 로고    scopus 로고
    • A fluorescence-based invitro assay for investigating early endosome dynamics
    • Barysch S.V., Jahn R., Rizzoli S.O. A fluorescence-based invitro assay for investigating early endosome dynamics. Nat. Protoc. 2010, 5:1127-1137.
    • (2010) Nat. Protoc. , vol.5 , pp. 1127-1137
    • Barysch, S.V.1    Jahn, R.2    Rizzoli, S.O.3
  • 5
    • 0034637146 scopus 로고    scopus 로고
    • Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter
    • Bellocchio E.E., Reimer R.J., Fremeau R.T., Edwards R.H. Uptake of glutamate into synaptic vesicles by an inorganic phosphate transporter. Science 2000, 289:957-960.
    • (2000) Science , vol.289 , pp. 957-960
    • Bellocchio, E.E.1    Reimer, R.J.2    Fremeau, R.T.3    Edwards, R.H.4
  • 6
    • 0028321554 scopus 로고
    • Long-wavelength chloride-sensitive fluorescent indicators
    • Biwersi J., Tulk B., Verkman A.S. Long-wavelength chloride-sensitive fluorescent indicators. Anal. Biochem. 1994, 219:139-143.
    • (1994) Anal. Biochem. , vol.219 , pp. 139-143
    • Biwersi, J.1    Tulk, B.2    Verkman, A.S.3
  • 7
  • 8
    • 0029865294 scopus 로고    scopus 로고
    • PH regulation and proton signalling by glial cells
    • Deitmer J.W., Rose C.R. pH regulation and proton signalling by glial cells. Prog. Neurobiol. 1996, 48:73-103.
    • (1996) Prog. Neurobiol. , vol.48 , pp. 73-103
    • Deitmer, J.W.1    Rose, C.R.2
  • 9
    • 34548565630 scopus 로고    scopus 로고
    • The neurotransmitter cycle and quantal size
    • Edwards R.H. The neurotransmitter cycle and quantal size. Neuron 2007, 55:835-858.
    • (2007) Neuron , vol.55 , pp. 835-858
    • Edwards, R.H.1
  • 11
    • 84877262325 scopus 로고    scopus 로고
    • Neurotransmitter transporters: structure meets function
    • Focke P.J., Wang X., Larsson H.P. Neurotransmitter transporters: structure meets function. Structure 2013, 21:694-705.
    • (2013) Structure , vol.21 , pp. 694-705
    • Focke, P.J.1    Wang, X.2    Larsson, H.P.3
  • 12
    • 0020007085 scopus 로고
    • 31P-NMR analysis of synaptic vesicles. Status of ATP and internal pH
    • 31P-NMR analysis of synaptic vesicles. Status of ATP and internal pH. Eur. J. Biochem. 1982, 121:519-524.
    • (1982) Eur. J. Biochem. , vol.121 , pp. 519-524
    • Füldner, H.H.1    Stadler, H.2
  • 14
    • 0026604813 scopus 로고
    • Relationship between intracellular proton buffering capacity and intracellular pH
    • Goldsmith D.J., Hilton P.J. Relationship between intracellular proton buffering capacity and intracellular pH. Kidney Int. 1992, 41:43-49.
    • (1992) Kidney Int. , vol.41 , pp. 43-49
    • Goldsmith, D.J.1    Hilton, P.J.2
  • 15
    • 61449361479 scopus 로고    scopus 로고
    • Review. The molecular logic of sodium-coupled neurotransmitter transporters
    • Gouaux E. Review. The molecular logic of sodium-coupled neurotransmitter transporters. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2009, 364:149-154.
    • (2009) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.364 , pp. 149-154
    • Gouaux, E.1
  • 16
    • 74849093404 scopus 로고    scopus 로고
    • Quantitative comparison of glutamatergic and GABAergic synaptic vesicles unveils selectivity for few proteins including MAL2, a novel synaptic vesicle protein
    • Grønborg M., Pavlos N.J., Brunk I., Chua J.J., Münster-Wandowski A., Riedel D., Ahnert-Hilger G., Urlaub H., Jahn R. Quantitative comparison of glutamatergic and GABAergic synaptic vesicles unveils selectivity for few proteins including MAL2, a novel synaptic vesicle protein. J.Neurosci. 2010, 30:2-12.
    • (2010) J.Neurosci. , vol.30 , pp. 2-12
    • Grønborg, M.1    Pavlos, N.J.2    Brunk, I.3    Chua, J.J.4    Münster-Wandowski, A.5    Riedel, D.6    Ahnert-Hilger, G.7    Urlaub, H.8    Jahn, R.9
  • 17
    • 0027425518 scopus 로고
    • An anion binding site that regulates the glutamate transporter of synaptic vesicles
    • Hartinger J., Jahn R. An anion binding site that regulates the glutamate transporter of synaptic vesicles. J.Biol. Chem. 1993, 268:23122-23127.
    • (1993) J.Biol. Chem. , vol.268 , pp. 23122-23127
    • Hartinger, J.1    Jahn, R.2
  • 18
    • 0025041769 scopus 로고
    • Energy dependence and functional reconstitution of the gamma-aminobutyric acid carrier from synaptic vesicles
    • Hell J.W., Maycox P.R., Jahn R. Energy dependence and functional reconstitution of the gamma-aminobutyric acid carrier from synaptic vesicles. J.Biol. Chem. 1990, 265:2111-2117.
    • (1990) J.Biol. Chem. , vol.265 , pp. 2111-2117
    • Hell, J.W.1    Maycox, P.R.2    Jahn, R.3
  • 19
    • 0015197327 scopus 로고
    • Ion transport by energy-conserving biological membranes
    • Henderson P.J. Ion transport by energy-conserving biological membranes. Annu. Rev. Microbiol. 1971, 25:393-428.
    • (1971) Annu. Rev. Microbiol. , vol.25 , pp. 393-428
    • Henderson, P.J.1
  • 21
    • 62149138458 scopus 로고    scopus 로고
    • Baculovirus expression systems for recombinant protein production in insect cells
    • Hitchman R.B., Possee R.D., King L.A. Baculovirus expression systems for recombinant protein production in insect cells. Recent Pat. Biotechnol. 2009, 3:46-54.
    • (2009) Recent Pat. Biotechnol. , vol.3 , pp. 46-54
    • Hitchman, R.B.1    Possee, R.D.2    King, L.A.3
  • 23
    • 0020955120 scopus 로고
    • Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation
    • Huttner W.B., Schiebler W., Greengard P., De Camilli P. Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation. J.Cell Biol. 1983, 96:1374-1388.
    • (1983) J.Cell Biol. , vol.96 , pp. 1374-1388
    • Huttner, W.B.1    Schiebler, W.2    Greengard, P.3    De Camilli, P.4
  • 25
    • 0023872141 scopus 로고
    • Accumulation of biological amines into chromaffin granules: a model for hormone and neurotransmitter transport
    • Johnson R.G. Accumulation of biological amines into chromaffin granules: a model for hormone and neurotransmitter transport. Physiol. Rev. 1988, 68:232-307.
    • (1988) Physiol. Rev. , vol.68 , pp. 232-307
    • Johnson, R.G.1
  • 26
    • 33846003157 scopus 로고    scopus 로고
    • Vesicular glutamate transporter contains two independent transport machineries
    • Juge N., Yoshida Y., Yatsushiro S., Omote H., Moriyama Y. Vesicular glutamate transporter contains two independent transport machineries. J.Biol. Chem. 2006, 281:39499-39506.
    • (2006) J.Biol. Chem. , vol.281 , pp. 39499-39506
    • Juge, N.1    Yoshida, Y.2    Yatsushiro, S.3    Omote, H.4    Moriyama, Y.5
  • 28
    • 0035543198 scopus 로고    scopus 로고
    • One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag
    • Keefe A.D., Wilson D.S., Seelig B., Szostak J.W. One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag. Protein Expr. Purif. 2001, 23:440-446.
    • (2001) Protein Expr. Purif. , vol.23 , pp. 440-446
    • Keefe, A.D.1    Wilson, D.S.2    Seelig, B.3    Szostak, J.W.4
  • 29
    • 66249098083 scopus 로고    scopus 로고
    • Unlocking the molecular secrets of sodium-coupled transporters
    • Krishnamurthy H., Piscitelli C.L., Gouaux E. Unlocking the molecular secrets of sodium-coupled transporters. Nature 2009, 459:347-355.
    • (2009) Nature , vol.459 , pp. 347-355
    • Krishnamurthy, H.1    Piscitelli, C.L.2    Gouaux, E.3
  • 30
    • 0027209690 scopus 로고
    • Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli
    • Luckow V.A., Lee S.C., Barry G.F., Olins P.O. Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli. J.Virol. 1993, 67:4566-4579.
    • (1993) J.Virol. , vol.67 , pp. 4566-4579
    • Luckow, V.A.1    Lee, S.C.2    Barry, G.F.3    Olins, P.O.4
  • 32
    • 0023715532 scopus 로고
    • Glutamate uptake by brain synaptic vesicles. Energy dependence of transport and functional reconstitution in proteoliposomes
    • Maycox P.R., Deckwerth T., Hell J.W., Jahn R. Glutamate uptake by brain synaptic vesicles. Energy dependence of transport and functional reconstitution in proteoliposomes. J.Biol. Chem. 1988, 263:15423-15428.
    • (1988) J.Biol. Chem. , vol.263 , pp. 15423-15428
    • Maycox, P.R.1    Deckwerth, T.2    Hell, J.W.3    Jahn, R.4
  • 33
    • 0025021999 scopus 로고
    • Amino acid neurotransmission: spotlight on synaptic vesicles
    • Maycox P.R., Hell J.W., Jahn R. Amino acid neurotransmission: spotlight on synaptic vesicles. Trends Neurosci. 1990, 13:83-87.
    • (1990) Trends Neurosci. , vol.13 , pp. 83-87
    • Maycox, P.R.1    Hell, J.W.2    Jahn, R.3
  • 34
    • 0019308646 scopus 로고
    • Determination of delta pH in cholinergic synaptic vesicles: its effect on storage and release of acetylcholine
    • Michaelson D.M., Angel I. Determination of delta pH in cholinergic synaptic vesicles: its effect on storage and release of acetylcholine. Life Sci. 1980, 27:39-44.
    • (1980) Life Sci. , vol.27 , pp. 39-44
    • Michaelson, D.M.1    Angel, I.2
  • 37
    • 0017076072 scopus 로고
    • The preparation and characterization of synaptic vesicles of high purity
    • Nagy A., Baker R.R., Morris S.J., Whittaker V.P. The preparation and characterization of synaptic vesicles of high purity. Brain Res. 1976, 109:285-309.
    • (1976) Brain Res. , vol.109 , pp. 285-309
    • Nagy, A.1    Baker, R.R.2    Morris, S.J.3    Whittaker, V.P.4
  • 38
    • 0021965984 scopus 로고
    • Characterization of glutamate uptake into synaptic vesicles
    • Naito S., Ueda T. Characterization of glutamate uptake into synaptic vesicles. J.Neurochem. 1985, 44:99-109.
    • (1985) J.Neurochem. , vol.44 , pp. 99-109
    • Naito, S.1    Ueda, T.2
  • 39
    • 12544258841 scopus 로고    scopus 로고
    • + exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation
    • + exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation. J.Biol. Chem. 2005, 280:1561-1572.
    • (2005) J.Biol. Chem. , vol.280 , pp. 1561-1572
    • Nakamura, N.1    Tanaka, S.2    Teko, Y.3    Mitsui, K.4    Kanazawa, H.5
  • 40
    • 0028895648 scopus 로고
    • Effects of internal pH on the acetylcholine transporter of synaptic vesicles
    • Nguyen M.L., Parsons S.M. Effects of internal pH on the acetylcholine transporter of synaptic vesicles. J.Neurochem. 1995, 64:1137-1142.
    • (1995) J.Neurochem. , vol.64 , pp. 1137-1142
    • Nguyen, M.L.1    Parsons, S.M.2
  • 41
    • 0032558426 scopus 로고    scopus 로고
    • Kinetic parameters for the vesicular acetylcholine transporter: two protons are exchanged for one acetylcholine
    • Nguyen M.L., Cox G.D., Parsons S.M. Kinetic parameters for the vesicular acetylcholine transporter: two protons are exchanged for one acetylcholine. Biochemistry 1998, 37:13400-13410.
    • (1998) Biochemistry , vol.37 , pp. 13400-13410
    • Nguyen, M.L.1    Cox, G.D.2    Parsons, S.M.3
  • 42
    • 0028233971 scopus 로고
    • Cloning and expression of a cDNA encoding a brain-specific Na(+)-dependent inorganic phosphate cotransporter
    • Ni B., Rosteck P.R., Nadi N.S., Paul S.M. Cloning and expression of a cDNA encoding a brain-specific Na(+)-dependent inorganic phosphate cotransporter. Proc. Natl. Acad. Sci. USA 1994, 91:5607-5611.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5607-5611
    • Ni, B.1    Rosteck, P.R.2    Nadi, N.S.3    Paul, S.M.4
  • 43
    • 0035907355 scopus 로고    scopus 로고
    • + exchanger localized to the trans-Golgi network
    • + exchanger localized to the trans-Golgi network. J.Biol. Chem. 2001, 276:17387-17394.
    • (2001) J.Biol. Chem. , vol.276 , pp. 17387-17394
    • Numata, M.1    Orlowski, J.2
  • 44
    • 84871905410 scopus 로고    scopus 로고
    • Vesicular neurotransmitter transporters: an approach for studying transporters with purified proteins
    • Omote H., Moriyama Y. Vesicular neurotransmitter transporters: an approach for studying transporters with purified proteins. Physiology (Bethesda) 2013, 28:39-50.
    • (2013) Physiology (Bethesda) , vol.28 , pp. 39-50
    • Omote, H.1    Moriyama, Y.2
  • 45
    • 0026069460 scopus 로고
    • Acridine orange as a probe for measuring pH gradients across membranes: mechanism and limitations
    • Palmgren M.G. Acridine orange as a probe for measuring pH gradients across membranes: mechanism and limitations. Anal. Biochem. 1991, 192:316-321.
    • (1991) Anal. Biochem. , vol.192 , pp. 316-321
    • Palmgren, M.G.1
  • 46
    • 33746915109 scopus 로고    scopus 로고
    • N- to C-terminal SNARE complex assembly promotes rapid membrane fusion
    • Pobbati A.V., Stein A., Fasshauer D. N- to C-terminal SNARE complex assembly promotes rapid membrane fusion. Science 2006, 313:673-676.
    • (2006) Science , vol.313 , pp. 673-676
    • Pobbati, A.V.1    Stein, A.2    Fasshauer, D.3
  • 47
    • 33750950509 scopus 로고    scopus 로고
    • Estimate of the chloride concentration in a central glutamatergic terminal: a gramicidin perforated-patch study on the calyx of Held
    • Price G.D., Trussell L.O. Estimate of the chloride concentration in a central glutamatergic terminal: a gramicidin perforated-patch study on the calyx of Held. J.Neurosci. 2006, 26:11432-11436.
    • (2006) J.Neurosci. , vol.26 , pp. 11432-11436
    • Price, G.D.1    Trussell, L.O.2
  • 49
    • 0242317916 scopus 로고    scopus 로고
    • Reconstitution of membrane proteins into liposomes
    • Rigaud J.L., Lévy D. Reconstitution of membrane proteins into liposomes. Methods Enzymol. 2003, 372:65-86.
    • (2003) Methods Enzymol. , vol.372 , pp. 65-86
    • Rigaud, J.L.1    Lévy, D.2
  • 50
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins
    • Rigaud J.L., Pitard B., Levy D. Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins. Biochim. Biophys. Acta 1995, 1231:223-246.
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 51
    • 80052190918 scopus 로고    scopus 로고
    • Cytoplasmic permeation pathway of neurotransmitter transporters
    • Rudnick G. Cytoplasmic permeation pathway of neurotransmitter transporters. Biochemistry 2011, 50:7462-7475.
    • (2011) Biochemistry , vol.50 , pp. 7462-7475
    • Rudnick, G.1
  • 52
    • 0021179651 scopus 로고
    • 2+ ATPase in neurosecretory vesicles isolated from bovine neurohypophyses
    • 2+ ATPase in neurosecretory vesicles isolated from bovine neurohypophyses. J.Biol. Chem. 1984, 259:9496-9507.
    • (1984) J.Biol. Chem. , vol.259 , pp. 9496-9507
    • Russell, J.T.1
  • 53
    • 34247648737 scopus 로고    scopus 로고
    • The uncoupled chloride conductance of a bacterial glutamate transporter homolog
    • Ryan R.M., Mindell J.A. The uncoupled chloride conductance of a bacterial glutamate transporter homolog. Nat. Struct. Mol. Biol. 2007, 14:365-371.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 365-371
    • Ryan, R.M.1    Mindell, J.A.2
  • 54
    • 58849125253 scopus 로고    scopus 로고
    • A chloride conductance in VGLUT1 underlies maximal glutamate loading into synaptic vesicles
    • Schenck S., Wojcik S.M., Brose N., Takamori S. A chloride conductance in VGLUT1 underlies maximal glutamate loading into synaptic vesicles. Nat. Neurosci. 2009, 12:156-162.
    • (2009) Nat. Neurosci. , vol.12 , pp. 156-162
    • Schenck, S.1    Wojcik, S.M.2    Brose, N.3    Takamori, S.4
  • 55
    • 0024502672 scopus 로고
    • Glutamate uptake into synaptic vesicles of bovine cerebral cortex and electrochemical potential difference of proton across the membrane
    • Shioi J., Naito S., Ueda T. Glutamate uptake into synaptic vesicles of bovine cerebral cortex and electrochemical potential difference of proton across the membrane. Biochem. J. 1989, 258:499-504.
    • (1989) Biochem. J. , vol.258 , pp. 499-504
    • Shioi, J.1    Naito, S.2    Ueda, T.3
  • 56
    • 0020532148 scopus 로고
    • Molecular engineering of the Autographa californica nuclear polyhedrosis virus genome: deletion mutations within the polyhedrin gene
    • Smith G.E., Fraser M.J., Summers M.D. Molecular engineering of the Autographa californica nuclear polyhedrosis virus genome: deletion mutations within the polyhedrin gene. J.Virol. 1983, 46:584-593.
    • (1983) J.Virol. , vol.46 , pp. 584-593
    • Smith, G.E.1    Fraser, M.J.2    Summers, M.D.3
  • 59
    • 0037066772 scopus 로고    scopus 로고
    • F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring
    • Suzuki T., Ueno H., Mitome N., Suzuki J., Yoshida M. F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring. J.Biol. Chem. 2002, 277:13281-13285.
    • (2002) J.Biol. Chem. , vol.277 , pp. 13281-13285
    • Suzuki, T.1    Ueno, H.2    Mitome, N.3    Suzuki, J.4    Yoshida, M.5
  • 60
    • 0026755199 scopus 로고
    • Glutamate transport into synaptic vesicles. Roles of membrane potential, pH gradient, and intravesicular pH
    • Tabb J.S., Kish P.E., Van Dyke R., Ueda T. Glutamate transport into synaptic vesicles. Roles of membrane potential, pH gradient, and intravesicular pH. J.Biol. Chem. 1992, 267:15412-15418.
    • (1992) J.Biol. Chem. , vol.267 , pp. 15412-15418
    • Tabb, J.S.1    Kish, P.E.2    Van Dyke, R.3    Ueda, T.4
  • 61
    • 0034648770 scopus 로고    scopus 로고
    • Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons
    • Takamori S., Rhee J.S., Rosenmund C., Jahn R. Identification of a vesicular glutamate transporter that defines a glutamatergic phenotype in neurons. Nature 2000, 407:189-194.
    • (2000) Nature , vol.407 , pp. 189-194
    • Takamori, S.1    Rhee, J.S.2    Rosenmund, C.3    Jahn, R.4
  • 62
    • 0035891724 scopus 로고    scopus 로고
    • Identification of differentiation-associated brain-specific phosphate transporter as a second vesicular glutamate transporter (VGLUT2)
    • Takamori S., Rhee J.S., Rosenmund C., Jahn R. Identification of differentiation-associated brain-specific phosphate transporter as a second vesicular glutamate transporter (VGLUT2). J.Neurosci. 2001, 21:RC182.
    • (2001) J.Neurosci. , vol.21 , pp. RC182
    • Takamori, S.1    Rhee, J.S.2    Rosenmund, C.3    Jahn, R.4
  • 64
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • Toei M., Saum R., Forgac M. Regulation and isoform function of the V-ATPases. Biochemistry 2010, 49:4715-4723.
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 66
    • 84885820366 scopus 로고    scopus 로고
    • Mechanisms of glutamate transport
    • Vandenberg R.J., Ryan R.M. Mechanisms of glutamate transport. Physiol. Rev. 2013, 93:1621-1657.
    • (2013) Physiol. Rev. , vol.93 , pp. 1621-1657
    • Vandenberg, R.J.1    Ryan, R.M.2
  • 67
    • 0025032271 scopus 로고
    • Development and biological applications of chloride-sensitive fluorescent indicators
    • Verkman A.S. Development and biological applications of chloride-sensitive fluorescent indicators. Am. J. Physiol. 1990, 259:C375-C388.
    • (1990) Am. J. Physiol. , vol.259 , pp. C375-C388
    • Verkman, A.S.1
  • 68
    • 79952750323 scopus 로고    scopus 로고
    • Interplay between VGLUT isoforms and endophilin A1 regulates neurotransmitter release and short-term plasticity
    • Weston M.C., Nehring R.B., Wojcik S.M., Rosenmund C. Interplay between VGLUT isoforms and endophilin A1 regulates neurotransmitter release and short-term plasticity. Neuron 2011, 69:1147-1159.
    • (2011) Neuron , vol.69 , pp. 1147-1159
    • Weston, M.C.1    Nehring, R.B.2    Wojcik, S.M.3    Rosenmund, C.4
  • 70
    • 17544376990 scopus 로고    scopus 로고
    • Regulation of glutamate transport into synaptic vesicles by chloride and proton gradient
    • Wolosker H., de Souza D.O., de Meis L. Regulation of glutamate transport into synaptic vesicles by chloride and proton gradient. J.Biol. Chem. 1996, 271:11726-11731.
    • (1996) J.Biol. Chem. , vol.271 , pp. 11726-11731
    • Wolosker, H.1    de Souza, D.O.2    de Meis, L.3
  • 71
    • 0021112876 scopus 로고
    • Determinants of clathrin-coated vesicle acidification
    • Xie X.S., Stone D.K., Racker E. Determinants of clathrin-coated vesicle acidification. J.Biol. Chem. 1983, 258:14834-14838.
    • (1983) J.Biol. Chem. , vol.258 , pp. 14834-14838
    • Xie, X.S.1    Stone, D.K.2    Racker, E.3


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