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Volumn 9, Issue 2, 2013, Pages

Mutational Analysis of the High-Affinity Zinc Binding Site Validates a Refined Human Dopamine Transporter Homology Model

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; CRYSTAL STRUCTURE; ENZYME ACTIVITY; NEUROPHYSIOLOGY; SUBSTRATES; ZINC;

EID: 84874785148     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002909     Document Type: Article
Times cited : (58)

References (96)
  • 1
    • 0035224834 scopus 로고    scopus 로고
    • Evolution of transport proteins
    • Saier MH, (2001) Evolution of transport proteins. Genet Eng 23: 1-10.
    • (2001) Genet Eng , vol.23 , pp. 1-10
    • Saier, M.H.1
  • 2
    • 0037264650 scopus 로고    scopus 로고
    • Plasma membrane monoamine transporters: structure, regulation and function
    • Torres GE, Gainetdinov RR, Caron MG, (2003) Plasma membrane monoamine transporters: structure, regulation and function. Nat Rev Neurosci 4: 13-25.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 13-25
    • Torres, G.E.1    Gainetdinov, R.R.2    Caron, M.G.3
  • 3
    • 79951702177 scopus 로고    scopus 로고
    • How addictive drugs disrupt presynaptic dopamine neurotransmission
    • Sulzer D, (2011) How addictive drugs disrupt presynaptic dopamine neurotransmission. Neuron 69: 628-649.
    • (2011) Neuron , vol.69 , pp. 628-649
    • Sulzer, D.1
  • 4
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O, (1966) Simple allosteric model for membrane pumps. Nature 211: 969-970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 5
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • Krishnamurthy H, Gouaux E, (2012) X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481: 469-474.
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 7
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters
    • Yamashita A, Singh SK, Kawate T, Jin Y, Gouaux E, (2005) Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters. Nature 437: 215-223.
    • (2005) Nature , vol.437 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 9
    • 73949083478 scopus 로고    scopus 로고
    • The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters
    • Forrest LR, Rudnick G, (2009) The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters. Physiology (Bethesda, Md) 24: 377-386.
    • (2009) Physiology (Bethesda, Md) , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 10
    • 55349092991 scopus 로고    scopus 로고
    • Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter
    • Weyand S, Shimamura T, Yajima S, Suzuki S, Mirza O, et al. (2008) Structure and molecular mechanism of a nucleobase-cation-symport-1 family transporter. Science (New York, NY) 322: 709-713.
    • (2008) Science (New York, NY) , vol.322 , pp. 709-713
    • Weyand, S.1    Shimamura, T.2    Yajima, S.3    Suzuki, S.4    Mirza, O.5
  • 11
    • 78951490668 scopus 로고    scopus 로고
    • Reconstructing a chloride-binding site in a bacterial neurotransmitter transporter homologue
    • Tavoulari S, Rizwan AN, Forrest LR, Rudnick G, (2011) Reconstructing a chloride-binding site in a bacterial neurotransmitter transporter homologue. J Biol Chem 286: 2834-2842.
    • (2011) J Biol Chem , vol.286 , pp. 2834-2842
    • Tavoulari, S.1    Rizwan, A.N.2    Forrest, L.R.3    Rudnick, G.4
  • 13
    • 35148815052 scopus 로고    scopus 로고
    • Mechanism of chloride interaction with neurotransmitter:sodium symporters
    • Zomot E, Bendahan A, Quick M, Zhao Y, Javitch JA, et al. (2007) Mechanism of chloride interaction with neurotransmitter:sodium symporters. Nature 449: 726-730.
    • (2007) Nature , vol.449 , pp. 726-730
    • Zomot, E.1    Bendahan, A.2    Quick, M.3    Zhao, Y.4    Javitch, J.A.5
  • 14
    • 78951476578 scopus 로고    scopus 로고
    • A glutamine residue conserved in the neurotransmitter:sodium:symporters is essential for the interaction of chloride with the GABA transporter GAT-1
    • Ben-Yona A, Bendahan A, Kanner BI, (2011) A glutamine residue conserved in the neurotransmitter:sodium:symporters is essential for the interaction of chloride with the GABA transporter GAT-1. J Biol Chem 286: 2826-2833.
    • (2011) J Biol Chem , vol.286 , pp. 2826-2833
    • Ben-Yona, A.1    Bendahan, A.2    Kanner, B.I.3
  • 15
    • 0028341658 scopus 로고
    • Delineation of discrete domains for substrate, cocaine, and tricyclic antidepressant interactions using chimeric dopamine-norepinephrine transporters
    • Giros B, Wang YM, Suter S, McLeskey SB, Pifl C, et al. (1994) Delineation of discrete domains for substrate, cocaine, and tricyclic antidepressant interactions using chimeric dopamine-norepinephrine transporters. J Biol Chem 269: 15985-15988.
    • (1994) J Biol Chem , vol.269 , pp. 15985-15988
    • Giros, B.1    Wang, Y.M.2    Suter, S.3    McLeskey, S.B.4    Pifl, C.5
  • 16
    • 0034695678 scopus 로고    scopus 로고
    • Transport-dependent accessibility of a cytoplasmic loop cysteine in the human dopamine transporter
    • Chen N, Ferrer JV, Javitch JA, Justice JB, (2000) Transport-dependent accessibility of a cytoplasmic loop cysteine in the human dopamine transporter. J Biol Chem 275: 1608-1614.
    • (2000) J Biol Chem , vol.275 , pp. 1608-1614
    • Chen, N.1    Ferrer, J.V.2    Javitch, J.A.3    Justice, J.B.4
  • 18
    • 0032480011 scopus 로고    scopus 로고
    • Delineation of an endogenous zinc-binding site in the human dopamine transporter
    • Norregaard L, Frederiksen D, Nielsen EO, Gether U, (1998) Delineation of an endogenous zinc-binding site in the human dopamine transporter. EMBO J 17: 4266-4273.
    • (1998) EMBO J , vol.17 , pp. 4266-4273
    • Norregaard, L.1    Frederiksen, D.2    Nielsen, E.O.3    Gether, U.4
  • 19
    • 0027455744 scopus 로고
    • Zinc modulation of drug binding, cocaine affinity states, and dopamine uptake on the dopamine uptake complex
    • Richfield EK, (1993) Zinc modulation of drug binding, cocaine affinity states, and dopamine uptake on the dopamine uptake complex. Mol Pharmacol 43: 100-108.
    • (1993) Mol Pharmacol , vol.43 , pp. 100-108
    • Richfield, E.K.1
  • 20
    • 0033601168 scopus 로고    scopus 로고
    • Defining proximity relationships in the tertiary structure of the dopamine transporter
    • Loland CJ, Norregaard L, Gether U, (1999) Defining proximity relationships in the tertiary structure of the dopamine transporter. J Biol Chem 274: 36928-36934.
    • (1999) J Biol Chem , vol.274 , pp. 36928-36934
    • Loland, C.J.1    Norregaard, L.2    Gether, U.3
  • 21
    • 0037077196 scopus 로고    scopus 로고
    • The role of zinc ions in reverse transport mediated by monoamine transporters
    • Scholze P, Nørregaard L, Singer EA, Freissmuth M, Gether U, et al. (2002) The role of zinc ions in reverse transport mediated by monoamine transporters. J Biol Chem 277: 21505-21513.
    • (2002) J Biol Chem , vol.277 , pp. 21505-21513
    • Scholze, P.1    Nørregaard, L.2    Singer, E.A.3    Freissmuth, M.4    Gether, U.5
  • 22
    • 2642549055 scopus 로고    scopus 로고
    • Structure and function of extracellular loop 4 of the serotonin transporter as revealed by cysteine-scanning mutagenesis
    • Mitchell SM, Lee E, Garcia ML, Stephan MM, (2004) Structure and function of extracellular loop 4 of the serotonin transporter as revealed by cysteine-scanning mutagenesis. J Biol Chem 279: 24089-24099.
    • (2004) J Biol Chem , vol.279 , pp. 24089-24099
    • Mitchell, S.M.1    Lee, E.2    Garcia, M.L.3    Stephan, M.M.4
  • 23
    • 0035887735 scopus 로고    scopus 로고
    • Induction of mossy fiber→Ca3 long-term potentiation requires translocation of synaptically released Zn2+
    • Li Y, Hough CJ, Frederickson CJ, Sarvey JM, (2001) Induction of mossy fiber→Ca3 long-term potentiation requires translocation of synaptically released Zn2+. J Neurosci 21: 8015-8025.
    • (2001) J Neurosci , vol.21 , pp. 8015-8025
    • Li, Y.1    Hough, C.J.2    Frederickson, C.J.3    Sarvey, J.M.4
  • 24
    • 0033712121 scopus 로고    scopus 로고
    • The actions of synaptically released zinc at hippocampal mossy fiber synapses
    • Vogt K, Mellor J, Tong G, Nicoll R, (2000) The actions of synaptically released zinc at hippocampal mossy fiber synapses. Neuron 26: 187-196.
    • (2000) Neuron , vol.26 , pp. 187-196
    • Vogt, K.1    Mellor, J.2    Tong, G.3    Nicoll, R.4
  • 25
    • 0035964795 scopus 로고    scopus 로고
    • Dendrodendritic inhibition through reversal of dopamine transport
    • Falkenburger BH, Barstow KL, Mintz IM, (2001) Dendrodendritic inhibition through reversal of dopamine transport. Science (New York, NY) 293: 2465-2470.
    • (2001) Science (New York, NY) , vol.293 , pp. 2465-2470
    • Falkenburger, B.H.1    Barstow, K.L.2    Mintz, I.M.3
  • 26
    • 0348110567 scopus 로고    scopus 로고
    • Zn2+ modulates currents generated by the dopamine transporter: parallel effects on amphetamine-induced charge transfer and release
    • Pifl C, Rebernik P, Kattinger A, Reither H, (2004) Zn2+ modulates currents generated by the dopamine transporter: parallel effects on amphetamine-induced charge transfer and release. Neuropharmacology 46: 223-231.
    • (2004) Neuropharmacology , vol.46 , pp. 223-231
    • Pifl, C.1    Rebernik, P.2    Kattinger, A.3    Reither, H.4
  • 27
    • 9644295740 scopus 로고    scopus 로고
    • Zinc potentiates an uncoupled anion conductance associated with the dopamine transporter
    • Meinild A-K, Sitte HH, Gether U, (2004) Zinc potentiates an uncoupled anion conductance associated with the dopamine transporter. J Biol Chem 279: 49671-49679.
    • (2004) J Biol Chem , vol.279 , pp. 49671-49679
    • Meinild, A.-K.1    Sitte, H.H.2    Gether, U.3
  • 28
    • 0037022356 scopus 로고    scopus 로고
    • Generation of an activating Zn(2+) switch in the dopamine transporter: mutation of an intracellular tyrosine constitutively alters the conformational equilibrium of the transport cycle
    • Loland CJ, Norregaard L, Litman T, Gether U, (2002) Generation of an activating Zn(2+) switch in the dopamine transporter: mutation of an intracellular tyrosine constitutively alters the conformational equilibrium of the transport cycle. Proc Natl Acad Sci U S A 99: 1683-1688.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1683-1688
    • Loland, C.J.1    Norregaard, L.2    Litman, T.3    Gether, U.4
  • 29
    • 84861337783 scopus 로고    scopus 로고
    • Substrate binding and translocation of the serotonin transporter studied by docking and molecular dynamics simulations
    • Gabrielsen M, Ravna AW, Kristiansen K, Sylte I, (2012) Substrate binding and translocation of the serotonin transporter studied by docking and molecular dynamics simulations. J Mol Model 18: 1073-1085.
    • (2012) J Mol Model , vol.18 , pp. 1073-1085
    • Gabrielsen, M.1    Ravna, A.W.2    Kristiansen, K.3    Sylte, I.4
  • 30
    • 28844506362 scopus 로고    scopus 로고
    • Putative drug binding conformations of monoamine transporters
    • Ravna AW, Sylte I, Kristiansen K, Dahl SG, (2006) Putative drug binding conformations of monoamine transporters. Bioorg Med Chem 14: 666-675.
    • (2006) Bioorg Med Chem , vol.14 , pp. 666-675
    • Ravna, A.W.1    Sylte, I.2    Kristiansen, K.3    Dahl, S.G.4
  • 31
    • 78649920349 scopus 로고    scopus 로고
    • The high-affinity binding site for tricyclic antidepressants resides in the outer vestibule of the serotonin transporter
    • Sarker S, Weissensteiner R, Steiner I, Sitte HH, Ecker GF, et al. (2010) The high-affinity binding site for tricyclic antidepressants resides in the outer vestibule of the serotonin transporter. Mol Pharmacol 78: 1026-1035.
    • (2010) Mol Pharmacol , vol.78 , pp. 1026-1035
    • Sarker, S.1    Weissensteiner, R.2    Steiner, I.3    Sitte, H.H.4    Ecker, G.F.5
  • 32
    • 76249105122 scopus 로고    scopus 로고
    • Mutational mapping and modeling of the binding site for (S)-citalopram in the human serotonin transporter
    • Andersen J, Olsen L, Hansen KB, Taboureau O, Jørgensen FS, et al. (2010) Mutational mapping and modeling of the binding site for (S)-citalopram in the human serotonin transporter. J Biol Chem 285: 2051-2063.
    • (2010) J Biol Chem , vol.285 , pp. 2051-2063
    • Andersen, J.1    Olsen, L.2    Hansen, K.B.3    Taboureau, O.4    Jørgensen, F.S.5
  • 33
    • 80053167954 scopus 로고    scopus 로고
    • Structure-based discovery of prescription drugs that interact with the norepinephrine transporter, NET
    • Schlessinger A, Geier E, Fan H, Irwin JJ, Shoichet BK, et al. (2011) Structure-based discovery of prescription drugs that interact with the norepinephrine transporter, NET. Proc Natl Acad Sci U S A 108: 15810-15815.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 15810-15815
    • Schlessinger, A.1    Geier, E.2    Fan, H.3    Irwin, J.J.4    Shoichet, B.K.5
  • 34
    • 77349101044 scopus 로고    scopus 로고
    • Bivalent phenethylamines as novel dopamine transporter inhibitors: evidence for multiple substrate-binding sites in a single transporter
    • Schmitt KC, Mamidyala S, Biswas S, Dutta AK, Reith MEA, (2010) Bivalent phenethylamines as novel dopamine transporter inhibitors: evidence for multiple substrate-binding sites in a single transporter. J Neurochem 112: 1605-1618.
    • (2010) J Neurochem , vol.112 , pp. 1605-1618
    • Schmitt, K.C.1    Mamidyala, S.2    Biswas, S.3    Dutta, A.K.4    Reith, M.E.A.5
  • 35
    • 75749102552 scopus 로고    scopus 로고
    • The two enantiomers of citalopram bind to the human serotonin transporter in reversed orientations
    • Koldsø H, Severinsen K, Tran TT, Celik L, Jensen HH, et al. (2010) The two enantiomers of citalopram bind to the human serotonin transporter in reversed orientations. J Am Chem Soc 132: 1311-1322.
    • (2010) J Am Chem Soc , vol.132 , pp. 1311-1322
    • Koldsø, H.1    Severinsen, K.2    Tran, T.T.3    Celik, L.4    Jensen, H.H.5
  • 36
    • 36549031819 scopus 로고    scopus 로고
    • How dopamine transporter interacts with dopamine: insights from molecular modeling and simulation
    • Huang X, Zhan C-G, (2007) How dopamine transporter interacts with dopamine: insights from molecular modeling and simulation. Biophys J 93: 3627-3639.
    • (2007) Biophys J , vol.93 , pp. 3627-3639
    • Huang, X.1    Zhan, C.-G.2
  • 37
    • 72449145780 scopus 로고    scopus 로고
    • Mechanism for cocaine blocking the transport of dopamine: insights from molecular modeling and dynamics simulations
    • Huang X, Gu HH, Zhan C-G, (2009) Mechanism for cocaine blocking the transport of dopamine: insights from molecular modeling and dynamics simulations. J Phys Chem B 113: 15057-15066.
    • (2009) J Phys Chem B , vol.113 , pp. 15057-15066
    • Huang, X.1    Gu, H.H.2    Zhan, C.-G.3
  • 38
    • 46049086729 scopus 로고    scopus 로고
    • The binding sites for cocaine and dopamine in the dopamine transporter overlap
    • Beuming T, Kniazeff J, Bergmann ML, Shi L, Gracia L, et al. (2008) The binding sites for cocaine and dopamine in the dopamine transporter overlap. Nature Neurosci 11: 780-789.
    • (2008) Nature Neurosci , vol.11 , pp. 780-789
    • Beuming, T.1    Kniazeff, J.2    Bergmann, M.L.3    Shi, L.4    Gracia, L.5
  • 39
    • 38549139110 scopus 로고    scopus 로고
    • Dopamine transporter comparative molecular modeling and binding site prediction using the LeuT(Aa) leucine transporter as a template
    • Indarte M, Madura JD, Surratt CK, (2008) Dopamine transporter comparative molecular modeling and binding site prediction using the LeuT(Aa) leucine transporter as a template. Proteins 70: 1033-1046.
    • (2008) Proteins , vol.70 , pp. 1033-1046
    • Indarte, M.1    Madura, J.D.2    Surratt, C.K.3
  • 40
    • 33751194447 scopus 로고    scopus 로고
    • A comprehensive structure-based alignment of prokaryotic and eukaryotic neurotransmitter/Na+ symporters (NSS) aids in the use of the LeuT structure to probe NSS structure and function
    • Beuming T, Shi L, Javitch JA, Weinstein H, (2006) A comprehensive structure-based alignment of prokaryotic and eukaryotic neurotransmitter/Na+ symporters (NSS) aids in the use of the LeuT structure to probe NSS structure and function. Mol Pharmacol 70: 1630-1642.
    • (2006) Mol Pharmacol , vol.70 , pp. 1630-1642
    • Beuming, T.1    Shi, L.2    Javitch, J.A.3    Weinstein, H.4
  • 41
    • 77951230460 scopus 로고    scopus 로고
    • The N terminus of monoamine transporters is a lever required for the action of amphetamines
    • Sucic S, Dallinger S, Zdrazil B, Weissensteiner R, Jørgensen TN, et al. (2010) The N terminus of monoamine transporters is a lever required for the action of amphetamines. J Biol Chem 285: 10924-10938.
    • (2010) J Biol Chem , vol.285 , pp. 10924-10938
    • Sucic, S.1    Dallinger, S.2    Zdrazil, B.3    Weissensteiner, R.4    Jørgensen, T.N.5
  • 42
    • 41149175461 scopus 로고    scopus 로고
    • Binding of serotonin to the human serotonin transporter. Molecular modeling and experimental validation
    • Celik L, Sinning S, Severinsen K, Hansen CG, Møller MS, et al. (2008) Binding of serotonin to the human serotonin transporter. Molecular modeling and experimental validation. J Am Chem Soc 130: 3853-3865.
    • (2008) J Am Chem Soc , vol.130 , pp. 3853-3865
    • Celik, L.1    Sinning, S.2    Severinsen, K.3    Hansen, C.G.4    Møller, M.S.5
  • 43
    • 59849093622 scopus 로고    scopus 로고
    • Structural determinants of species-selective substrate recognition in human and Drosophila serotonin transporters revealed through computational docking studies
    • Kaufmann KW, Dawson ES, Henry LK, Field JR, Blakely RD, et al. (2009) Structural determinants of species-selective substrate recognition in human and Drosophila serotonin transporters revealed through computational docking studies. Proteins 74: 630-642.
    • (2009) Proteins , vol.74 , pp. 630-642
    • Kaufmann, K.W.1    Dawson, E.S.2    Henry, L.K.3    Field, J.R.4    Blakely, R.D.5
  • 44
    • 77949313326 scopus 로고    scopus 로고
    • Molecular dynamics of leucine and dopamine transporter proteins in a model cell membrane lipid bilayer
    • Gedeon PC, Indarte M, Surratt CK, Madura JD, (2010) Molecular dynamics of leucine and dopamine transporter proteins in a model cell membrane lipid bilayer. Proteins 78: 797-811.
    • (2010) Proteins , vol.78 , pp. 797-811
    • Gedeon, P.C.1    Indarte, M.2    Surratt, C.K.3    Madura, J.D.4
  • 45
    • 80055067598 scopus 로고    scopus 로고
    • Unbiased simulations reveal the inward-facing conformation of the human serotonin transporter and Na(+) ion release
    • Koldsø H, Noer P, Grouleff J, Autzen HE, Sinning S, et al. (2011) Unbiased simulations reveal the inward-facing conformation of the human serotonin transporter and Na(+) ion release. PLoS Comput Biol 7: e1002246.
    • (2011) PLoS Comput Biol , vol.7
    • Koldsø, H.1    Noer, P.2    Grouleff, J.3    Autzen, H.E.4    Sinning, S.5
  • 46
    • 80052245062 scopus 로고    scopus 로고
    • A conserved asparagine residue in TM1 of the serotonin transporter dictates chloride-coupled neurotransmitter transport
    • Henry LK, Iwamoto H, Field JR, Kaufmann K, Dawson ES, et al. (2011) A conserved asparagine residue in TM1 of the serotonin transporter dictates chloride-coupled neurotransmitter transport. J Biol Chem 286: 30823-30836.
    • (2011) J Biol Chem , vol.286 , pp. 30823-30836
    • Henry, L.K.1    Iwamoto, H.2    Field, J.R.3    Kaufmann, K.4    Dawson, E.S.5
  • 47
    • 79551598571 scopus 로고    scopus 로고
    • The substrate-driven transition to an inward-facing conformation in the functional mechanism of the dopamine transporter
    • Shan J, Javitch JA, Shi L, Weinstein H, (2011) The substrate-driven transition to an inward-facing conformation in the functional mechanism of the dopamine transporter. PloS one 6: e16350.
    • (2011) PloS One , vol.6
    • Shan, J.1    Javitch, J.A.2    Shi, L.3    Weinstein, H.4
  • 48
    • 62149131065 scopus 로고    scopus 로고
    • A Juxtamembrane Mutation in the N Terminus of the Dopamine Transporter Induces Preference for an Inward-Facing Conformation
    • Guptaroy B, Zhang M, Bowton E, Binda F, Shi L, et al. (2009) A Juxtamembrane Mutation in the N Terminus of the Dopamine Transporter Induces Preference for an Inward-Facing Conformation. Mol Pharmacol 75: 514-524.
    • (2009) Mol Pharmacol , vol.75 , pp. 514-524
    • Guptaroy, B.1    Zhang, M.2    Bowton, E.3    Binda, F.4    Shi, L.5
  • 49
    • 0034807252 scopus 로고    scopus 로고
    • The monoamine neurotransmitter transporters: structure, conformational changes and molecular gating
    • Norregaard L, Gether U, (2001) The monoamine neurotransmitter transporters: structure, conformational changes and molecular gating. Curr Opin Drug Discov 4: 591-601.
    • (2001) Curr Opin Drug Discov , vol.4 , pp. 591-601
    • Norregaard, L.1    Gether, U.2
  • 50
    • 26644465295 scopus 로고    scopus 로고
    • A comprehensive atlas of the topography of functional groups of the dopamine transporter
    • Volz TJ, Schenk JO, (2005) A comprehensive atlas of the topography of functional groups of the dopamine transporter. Synapse (New York, NY) 58: 72-94.
    • (2005) Synapse (New York, NY) , vol.58 , pp. 72-94
    • Volz, T.J.1    Schenk, J.O.2
  • 51
    • 2542420799 scopus 로고    scopus 로고
    • Mutation of Trp84 and Asp313 of the dopamine transporter reveals similar mode of binding interaction for GBR12909 and benztropine as opposed to cocaine
    • Chen N, Zhen J, Reith MEA, (2004) Mutation of Trp84 and Asp313 of the dopamine transporter reveals similar mode of binding interaction for GBR12909 and benztropine as opposed to cocaine. J Neurochem 89: 853-864.
    • (2004) J Neurochem , vol.89 , pp. 853-864
    • Chen, N.1    Zhen, J.2    Reith, M.E.A.3
  • 52
    • 0032801143 scopus 로고    scopus 로고
    • Dopamine transporter: transmembrane phenylalanine mutations can selectively influence dopamine uptake and cocaine analog recognition
    • Lin Z, Wang W, Kopajtic T, Revay RS, Uhl GR, (1999) Dopamine transporter: transmembrane phenylalanine mutations can selectively influence dopamine uptake and cocaine analog recognition. Mol Pharmacol 56: 434-447.
    • (1999) Mol Pharmacol , vol.56 , pp. 434-447
    • Lin, Z.1    Wang, W.2    Kopajtic, T.3    Revay, R.S.4    Uhl, G.R.5
  • 53
    • 0033669731 scopus 로고    scopus 로고
    • Dopamine transporter tryptophan mutants highlight candidate dopamine- and cocaine-selective domains
    • Lin Z, Wang W, Uhl GR, (2000) Dopamine transporter tryptophan mutants highlight candidate dopamine- and cocaine-selective domains. Mol Pharmacol 58: 1581-1592.
    • (2000) Mol Pharmacol , vol.58 , pp. 1581-1592
    • Lin, Z.1    Wang, W.2    Uhl, G.R.3
  • 54
    • 0026722234 scopus 로고
    • Dopamine transporter site-directed mutations differentially alter substrate transport and cocaine binding
    • Kitayama S, Shimada S, Xu H, Markham L, Donovan DM, et al. (1992) Dopamine transporter site-directed mutations differentially alter substrate transport and cocaine binding. Proc Natl Acad Sci U S A 89: 7782-7785.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7782-7785
    • Kitayama, S.1    Shimada, S.2    Xu, H.3    Markham, L.4    Donovan, D.M.5
  • 55
    • 0035020831 scopus 로고    scopus 로고
    • The role of conserved tryptophan and acidic residues in the human dopamine transporter as characterized by site-directed mutagenesis
    • Chen N, Vaughan RA, Reith ME, (2001) The role of conserved tryptophan and acidic residues in the human dopamine transporter as characterized by site-directed mutagenesis. J Neurochem 77: 1116-1127.
    • (2001) J Neurochem , vol.77 , pp. 1116-1127
    • Chen, N.1    Vaughan, R.A.2    Reith, M.E.3
  • 56
    • 47749083479 scopus 로고    scopus 로고
    • An intracellular interaction network regulates conformational transitions in the dopamine transporter
    • Kniazeff J, Shi L, Loland CJ, Javitch JA, Weinstein H, et al. (2008) An intracellular interaction network regulates conformational transitions in the dopamine transporter. J Biol Chem 283: 17691-17701.
    • (2008) J Biol Chem , vol.283 , pp. 17691-17701
    • Kniazeff, J.1    Shi, L.2    Loland, C.J.3    Javitch, J.A.4    Weinstein, H.5
  • 57
    • 0942276396 scopus 로고    scopus 로고
    • Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding
    • Loland CJ, Grånäs C, Javitch JA, Gether U, (2004) Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding. J Biol Chem 279: 3228-3238.
    • (2004) J Biol Chem , vol.279 , pp. 3228-3238
    • Loland, C.J.1    Grånäs, C.2    Javitch, J.A.3    Gether, U.4
  • 58
    • 38549121701 scopus 로고    scopus 로고
    • Currents in response to rapid concentration jumps of amphetamine uncover novel aspects of human dopamine transporter function
    • Erreger K, Grewer C, Javitch JA, Galli A, (2008) Currents in response to rapid concentration jumps of amphetamine uncover novel aspects of human dopamine transporter function. J Neurosci 28: 976-989.
    • (2008) J Neurosci , vol.28 , pp. 976-989
    • Erreger, K.1    Grewer, C.2    Javitch, J.A.3    Galli, A.4
  • 59
    • 0027364736 scopus 로고
    • From synapse to vesicle: the reuptake and storage of biogenic amine neurotransmitters
    • Rudnick G, Clark J, (1993) From synapse to vesicle: the reuptake and storage of biogenic amine neurotransmitters. Biochim Biophys Acta 1144: 249-263.
    • (1993) Biochim Biophys Acta , vol.1144 , pp. 249-263
    • Rudnick, G.1    Clark, J.2
  • 60
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • Sali A, Overington JP, (1994) Derivation of rules for comparative protein modeling from a database of protein structure alignments. Protein Sci 3: 1582-1596.
    • (1994) Protein Sci , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.P.2
  • 61
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen M-Y, Sali A, (2006) Statistical potential for assessment and prediction of protein structures. Protein Sci 15: 2507-2524.
    • (2006) Protein Sci , vol.15 , pp. 2507-2524
    • Shen, M.-Y.1    Sali, A.2
  • 62
    • 2442637536 scopus 로고    scopus 로고
    • The role of N-glycosylation in function and surface trafficking of the human dopamine transporter
    • Li L-B, Chen N, Ramamoorthy S, Chi L, Cui X-N, et al. (2004) The role of N-glycosylation in function and surface trafficking of the human dopamine transporter. J Biol Chem 279: 21012-21020.
    • (2004) J Biol Chem , vol.279 , pp. 21012-21020
    • Li, L.-B.1    Chen, N.2    Ramamoorthy, S.3    Chi, L.4    Cui, X.-N.5
  • 63
    • 0027291899 scopus 로고
    • Species differences in dopamine transporters: postmortem changes and glycosylation differences
    • Patel A, Uhl G, Kuhar MJ, (1993) Species differences in dopamine transporters: postmortem changes and glycosylation differences. J Neurochem 61: 496-500.
    • (1993) J Neurochem , vol.61 , pp. 496-500
    • Patel, A.1    Uhl, G.2    Kuhar, M.J.3
  • 64
    • 0028872648 scopus 로고
    • Dopamine transporter cysteine mutants: second extracellular loop cysteines are required for transporter expression
    • Wang JB, Moriwaki A, Uhl GR, (1995) Dopamine transporter cysteine mutants: second extracellular loop cysteines are required for transporter expression. J Neurochem 64: 1416-1419.
    • (1995) J Neurochem , vol.64 , pp. 1416-1419
    • Wang, J.B.1    Moriwaki, A.2    Uhl, G.R.3
  • 65
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley WC, White SH, (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nature Struct Biol 3: 842-848.
    • (1996) Nature Struct Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 66
    • 0034732952 scopus 로고    scopus 로고
    • Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins
    • Ridder AN, Morein S, Stam JG, Kuhn A, de Kruijff B, et al. (2000) Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins. Biochemistry 39: 6521-6528.
    • (2000) Biochemistry , vol.39 , pp. 6521-6528
    • Ridder, A.N.1    Morein, S.2    Stam, J.G.3    Kuhn, A.4    de Kruijff, B.5
  • 67
    • 43649094583 scopus 로고    scopus 로고
    • Distribution of amino acids in a lipid bilayer from computer simulations
    • MacCallum JL, Bennett WFD, Tieleman DP, (2008) Distribution of amino acids in a lipid bilayer from computer simulations. Biophys J 94: 3393-3404.
    • (2008) Biophys J , vol.94 , pp. 3393-3404
    • MacCallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 68
    • 0031030859 scopus 로고    scopus 로고
    • Mutation of tryptophan residues in lipoprotein lipase. Effects on stability, immunoreactivity, and catalytic properties
    • Lookene A, Groot NB, Kastelein JJ, Olivecrona G, Bruin T, (1997) Mutation of tryptophan residues in lipoprotein lipase. Effects on stability, immunoreactivity, and catalytic properties. J Biol Chem 272: 766-772.
    • (1997) J Biol Chem , vol.272 , pp. 766-772
    • Lookene, A.1    Groot, N.B.2    Kastelein, J.J.3    Olivecrona, G.4    Bruin, T.5
  • 69
    • 70350680995 scopus 로고    scopus 로고
    • Coordination dynamics of zinc in proteins
    • Maret W, Li Y, (2009) Coordination dynamics of zinc in proteins. Chem Rev 109: 4682-4707.
    • (2009) Chem Rev , vol.109 , pp. 4682-4707
    • Maret, W.1    Li, Y.2
  • 70
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld DS, (2001) Zinc coordination sphere in biochemical zinc sites. Biometals 14: 271-313.
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 71
    • 79959999377 scopus 로고    scopus 로고
    • R.E.D. Server: a web service for deriving RESP and ESP charges and building force field libraries for new molecules and molecular fragments
    • Vanquelef E, Simon S, Marquant G, Garcia E, Klimerak G, et al. (2011) R.E.D. Server: a web service for deriving RESP and ESP charges and building force field libraries for new molecules and molecular fragments. Nucl Acids Res 39: W511-W517.
    • (2011) Nucl Acids Res , vol.39
    • Vanquelef, E.1    Simon, S.2    Marquant, G.3    Garcia, E.4    Klimerak, G.5
  • 72
    • 77954566051 scopus 로고    scopus 로고
    • The R.E.D. tools: Advances in RESP and ESP charge derivation and force field library building,
    • Dupradeau F-Y, Pigache A, Zaffran T, Savineau C, Lelong R, et al. (2010) The R.E.D. tools: Advances in RESP and ESP charge derivation and force field library building,. Phys Chem Chem Phys 12: 7821-7839.
    • (2010) Phys Chem Chem Phys , vol.12 , pp. 7821-7839
    • Dupradeau, F.-Y.1    Pigache, A.2    Zaffran, T.3    Savineau, C.4    Lelong, R.5
  • 73
    • 84874544038 scopus 로고    scopus 로고
    • Carbonic anhydrase binding site parameterization in OPLS-AA force field
    • Bernadat G, Supuran CT, Iorga BI, (2012) Carbonic anhydrase binding site parameterization in OPLS-AA force field. Bioorg Med Chem In press. doi:http://dx.doi.org/10.1016/j.bmc.2012.10.040.
    • (2012) Bioorg Med Chem
    • Bernadat, G.1    Supuran, C.T.2    Iorga, B.I.3
  • 74
    • 30744471169 scopus 로고    scopus 로고
    • Counting the zinc-proteins encoded in the human genome
    • Andreini C, Banci L, Bertini I, Rosato A, (2006) Counting the zinc-proteins encoded in the human genome. J Proteome Res 5: 196-201.
    • (2006) J Proteome Res , vol.5 , pp. 196-201
    • Andreini, C.1    Banci, L.2    Bertini, I.3    Rosato, A.4
  • 75
    • 20144369025 scopus 로고    scopus 로고
    • Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1
    • Jin-Suk Han J-S, Kazuhiko Ishikawa K, (2005) Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1. Archaea 1: 311-317.
    • (2005) Archaea , vol.1 , pp. 311-317
    • Jin-Suk, H.J.-S.1    Kazuhiko Ishikawa, K.2
  • 76
    • 40849140675 scopus 로고    scopus 로고
    • Solution structure of NEMO zinc finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation
    • Cordier F, Vinolo E, Véron M, Delepierre M, Agou F, (2008) Solution structure of NEMO zinc finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation. J Mol Biol 377: 1419-32.
    • (2008) J Mol Biol , vol.377 , pp. 1419-1432
    • Cordier, F.1    Vinolo, E.2    Véron, M.3    Delepierre, M.4    Agou, F.5
  • 78
    • 1342265784 scopus 로고    scopus 로고
    • Uptake inhibitors but not substrates induce protease resistance in extracellular loop two of the dopamine transporter
    • Gaffaney JD, Vaughan RA, (2004) Uptake inhibitors but not substrates induce protease resistance in extracellular loop two of the dopamine transporter. Mol Pharmacol 65: 692-701.
    • (2004) Mol Pharmacol , vol.65 , pp. 692-701
    • Gaffaney, J.D.1    Vaughan, R.A.2
  • 80
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity
    • Edgar RC, (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5: 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 81
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 82
    • 77954256616 scopus 로고    scopus 로고
    • g _ membed: Efficient Insertion of a Membrane Protein into an Equilibrated Lipid Bilayer with Minimal Perturbation
    • Wolf MG, Hoefling M, Aponte-Santamaría C, Grubmüller H, Groenhof G, (2010) g _ membed: Efficient Insertion of a Membrane Protein into an Equilibrated Lipid Bilayer with Minimal Perturbation. J Comput Chem 31: 2169-2174.
    • (2010) J Comput Chem , vol.31 , pp. 2169-2174
    • Wolf, M.G.1    Hoefling, M.2    Aponte-Santamaría, C.3    Grubmüller, H.4    Groenhof, G.5
  • 84
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 85
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and Reparametrization of the OPLS-AA Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides
    • Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL, (2001) Evaluation and Reparametrization of the OPLS-AA Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides. J Phys Chem B 105: 6474-6487.
    • (2001) J Phys Chem B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 86
    • 0029912748 scopus 로고    scopus 로고
    • Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J, (1996) Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids. J Am Chem Soc 118: 11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 87
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger O, Edholm O, Jahnig F, (1997) Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys J 72: 2002-2013.
    • (1997) Biophys J , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 88
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • In: B P, editor, Dordrecht: D. Reidel Publishing Company
    • Berendsen HJC, Postma JPM, van Gunsteren WF, Hermans J (1981) Interaction models for water in relation to protein hydration. In: B P, editor. Intermolecular Forces. Dordrecht: D. Reidel Publishing Company pp. 331-342.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    van Gunsteren, W.F.3    Hermans, J.4
  • 89
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi G, Donadio D, Parrinello M, (2007) Canonical sampling through velocity rescaling. The J Chem Phys 126: 014101.
    • (2007) The J Chem Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 91
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N{dot operator}log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L, (1993) Particle mesh Ewald: An N{dot operator}log(N) method for Ewald sums in large systems. The J Chem Phys 98: 10089-10092.
    • (1993) The J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 92
    • 84986440341 scopus 로고
    • SETTLE - An Analytical Version of the SHAKE and RATTLE Algorithm for rigid Water Models
    • Miyamoto S, Kollman P, Peter A, Kiyamoto S, (1992) SETTLE- An Analytical Version of the SHAKE and RATTLE Algorithm for rigid Water Models. J Comput Chem 13: 952-962.
    • (1992) J Comput Chem , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.2    Peter, A.3    Kiyamoto, S.4
  • 93
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen H, Fraaije JGEM, (1997) LINCS: A linear constraint solver for molecular simulations. J Comput Chem 18: 1463-1472.
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.3    Fraaije, J.G.E.M.4
  • 94
    • 0026335164 scopus 로고
    • Cloning and functional characterization of a cocaine-sensitive dopamine transporter
    • Giros B, el Mestikawy S, Bertrand L, Caron MG, (1991) Cloning and functional characterization of a cocaine-sensitive dopamine transporter. FEBS Lett 295: 149-154.
    • (1991) FEBS Lett , vol.295 , pp. 149-154
    • Giros, B.1    el Mestikawy, S.2    Bertrand, L.3    Caron, M.G.4
  • 95
    • 65549089736 scopus 로고    scopus 로고
    • Physical and functional interaction between the dopamine transporter and the synaptic vesicle protein synaptogyrin-3
    • Egaña LA, Cuevas RA, Baust TB, Parra LA, Leak RK, et al. (2009) Physical and functional interaction between the dopamine transporter and the synaptic vesicle protein synaptogyrin-3. J Neurosci 29: 4592-4604.
    • (2009) J Neurosci , vol.29 , pp. 4592-4604
    • Egaña, L.A.1    Cuevas, R.A.2    Baust, T.B.3    Parra, L.A.4    Leak, R.K.5
  • 96
    • 33744948233 scopus 로고    scopus 로고
    • The conserved glutamate (Glu136) in transmembrane domain 2 of the serotonin transporter is required for the conformational switch in the transport cycle
    • Korkhov VM, Holy M, Freissmuth M, Sitte HH, (2006) The conserved glutamate (Glu136) in transmembrane domain 2 of the serotonin transporter is required for the conformational switch in the transport cycle. J Biol Chem 281: 13439-13448.
    • (2006) J Biol Chem , vol.281 , pp. 13439-13448
    • Korkhov, V.M.1    Holy, M.2    Freissmuth, M.3    Sitte, H.H.4


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