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Volumn 9, Issue 3, 2014, Pages

Molecular dynamics simulations of the mammalian glutamate transporter EAAT3

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; EXCITATORY AMINO ACID TRANSPORTER 1; EXCITATORY AMINO ACID TRANSPORTER 2; EXCITATORY AMINO ACID TRANSPORTER 3; POTASSIUM ION; PROTON; SODIUM ION; GLUTAMIC ACID; POTASSIUM; PROTEIN BINDING; SLC1A1 PROTEIN, HUMAN; SLC1A1 PROTEIN, RAT; SODIUM;

EID: 84898662786     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0092089     Document Type: Article
Times cited : (16)

References (72)
  • 1
    • 0035001341 scopus 로고    scopus 로고
    • Glutamate uptake
    • DOI 10.1016/S0301-0082(00)00067-8, PII S0301008200000678
    • Danbolt NC (2001) Glutamate uptake. Prog Neurobiol. 65:1-105. (Pubitemid 32479155)
    • (2001) Progress in Neurobiology , vol.65 , Issue.1 , pp. 1-105
    • Danbolt, N.C.1
  • 2
    • 0020448447 scopus 로고
    • Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain
    • Kanner BI, Bendahan A (1982) Binding order of substrates to the sodium and potassium-ion coupled L-glutamic acid transporter from rat-brain. Biochemistry 21:6327-6330. (Pubitemid 13141637)
    • (1982) Biochemistry , vol.21 , Issue.24 , pp. 6327-6330
    • Kanner, B.I.1    Bendahan, A.2
  • 3
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • DOI 10.1038/383634a0
    • Zerangue N, Kavanaugh MP (1996) Flux coupling in a neuronal glutamate transporter. Nature 383:634-637. (Pubitemid 26347587)
    • (1996) Nature , vol.383 , Issue.6601 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 4
    • 77953857777 scopus 로고    scopus 로고
    • The position of an arginine residue inuences substrate affinity and K+ coupling in the human glutamate transporter, EAAT1
    • Ryan RM, Kortt NC, Sirivanta T, Vandenberg RJ (2010) The position of an arginine residue inuences substrate affinity and K+ coupling in the human glutamate transporter, EAAT1. J Neurochem 114: 565-575.
    • (2010) J Neurochem , vol.114 , pp. 565-575
    • Ryan, R.M.1    Kortt, N.C.2    Sirivanta, T.3    Vandenberg, R.J.4
  • 5
    • 63249114685 scopus 로고    scopus 로고
    • The role of cation binding in determining substrate selectivity of glutamate transporters
    • Huang S, Ryan RM, Vandenberg RJ (2009) The role of cation binding in determining substrate selectivity of glutamate transporters. J Biol Chem 284:4510-4515.
    • (2009) J Biol Chem , vol.284 , pp. 4510-4515
    • Huang, S.1    Ryan, R.M.2    Vandenberg, R.J.3
  • 6
    • 84858110981 scopus 로고    scopus 로고
    • Position of the third Na site in the aspartate transporter GltPh and the human glutamate transporter EAAT1
    • Bastug T, Heinzelmann G, Kuyucak S, Salim M, Vandenberg RJ, et al. (2012) Position of the third Na site in the aspartate transporter GltPh and the human glutamate transporter EAAT1. PLoS ONE 7:e33058.
    • (2012) PLoS ONE , vol.7
    • Bastug, T.1    Heinzelmann, G.2    Kuyucak, S.3    Salim, M.4    Vandenberg, R.J.5
  • 7
    • 0031028206 scopus 로고    scopus 로고
    • Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange
    • DOI 10.1074/jbc.272.3.1703
    • Kavanaugh MP, Bendahan A, Zerangue N, Zhang Y, Kanner BI (1997) Mutation of an amino acid residue inuencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange. J Biol Chem 272:1703-1708. (Pubitemid 27043256)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.3 , pp. 1703-1708
    • Kavanaugh, M.P.1    Bendahan, A.2    Zerangue, N.3    Zhang, Y.4    Kanner, B.I.5
  • 8
    • 0036896927 scopus 로고    scopus 로고
    • Comparison of coupled and uncoupled currents during glutamate uptake by GLT-1 transporters
    • Bergles DE, Tzingounis AV, Jahr CE (2002) Comparison of coupled and uncoupled currents during glutamate uptake by GLT-1 transporters. J Neurosci 22:10153-10162. (Pubitemid 35416854)
    • (2002) Journal of Neuroscience , vol.22 , Issue.23 , pp. 10153-10162
    • Bergles, D.E.1    Tzingounis, A.V.2    Jahr, C.E.3
  • 10
    • 0033573907 scopus 로고    scopus 로고
    • Two serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitter
    • DOI 10.1073/pnas.96.4.1710
    • Zhang Y, Kanner BI (1999) Two serine residues of the glutamate transporter GLT-1 are crucial for coupling the uxes of sodium and the neurotransmitter. Proc Natl Acad Sci USA 96:1710-1715. (Pubitemid 29098516)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.4 , pp. 1710-1715
    • Zhang, Y.1    Kanner, B.I.2
  • 11
    • 33947726549 scopus 로고    scopus 로고
    • + binding to the glutamate transporter EAAC1
    • DOI 10.1085/jgp.200609678
    • Tao Z, Grewer C (2007) Cooperation of the conserved aspartate 439 and bound amino acid substrate is important for high-affinity Na+ binding to the glutamate transporter EAAC1. J Gen Physiol 129:331-344. (Pubitemid 46506983)
    • (2007) Journal of General Physiology , vol.129 , Issue.4 , pp. 331-344
    • Tao, Z.1    Grewer, C.2
  • 12
    • 0035798626 scopus 로고    scopus 로고
    • Coupled, but not uncoupled, uxes in a neuronal glutamate transporter can be activated by lithium ions
    • Borre L, Kanner BI (2001) Coupled, but not uncoupled, uxes in a neuronal glutamate transporter can be activated by lithium ions. J Biol Chem 276:40396-40401.
    • (2001) J Biol Chem , vol.276 , pp. 40396-40401
    • Borre, L.1    Kanner, B.I.2
  • 13
    • 33744518437 scopus 로고    scopus 로고
    • + to the glutamate-free form and cycling of the glutamate transporter EAAC1
    • DOI 10.1074/jbc.M510739200
    • Tao Z, Zhang Z, Grewer C (2006) Neutralization of the aspartic acid residue Asp-367, but not Asp-454, inhibits binding of Na+ to the glutamate-free form and cycling of the glutamate transporter EAAC1. J Biol Chem 281:10263-10272. (Pubitemid 43864564)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10263-10272
    • Tao, Z.1    Zhang, Z.2    Grewer, C.3
  • 14
    • 77952907248 scopus 로고    scopus 로고
    • Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101
    • Tao Z, Rosental N, Kanner BI, Gameiro A, Mwaura J, et al. (2010) Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101. J Biol Chem 285:17725-17733.
    • (2010) J Biol Chem , vol.285 , pp. 17725-17733
    • Tao, Z.1    Rosental, N.2    Kanner, B.I.3    Gameiro, A.4    Mwaura, J.5
  • 15
    • 14644419554 scopus 로고    scopus 로고
    • The conserved histidine 295 does not contribute to proton cotransport by the glutamate transporter EAAC1
    • DOI 10.1021/bi047812i
    • Tao Z, Grewer C (2005) The conserved histidine 295 does not contribute to proton cotransport by the glutamate transporter EAAC1. Biochemistry 44:3466-3476. (Pubitemid 40322016)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3466-3476
    • Tao, Z.1    Grewer, C.2
  • 16
    • 33748765517 scopus 로고    scopus 로고
    • Multiple consequences of mutating two conserved β-bridge forming residues in the translocation cycle of a neuronal glutamate transporter
    • DOI 10.1074/jbc.M600331200
    • Rosental N, Bendahan A, Kanner BI (2006) Multiple consequences of mutating two conserved b-bridge forming residues in the translocation cycle of a neuronal glutamate transporter. J Biol Chem 281:27905-27915. (Pubitemid 44414502)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.38 , pp. 27905-27915
    • Rosental, N.1    Bendahan, A.2    Kanner, B.I.3
  • 17
    • 84861204243 scopus 로고    scopus 로고
    • Conserved asparagine residue located in binding pocket controls cation selectivity and substrate interactions in neuronal glutamate transporters
    • Teichman S, Qu S, Kanner BI (2012) Conserved asparagine residue located in binding pocket controls cation selectivity and substrate interactions in neuronal glutamate transporters. J Biol Chem 287:17198-17205.
    • (2012) J Biol Chem , vol.287 , pp. 17198-17205
    • Teichman, S.1    Qu, S.2    Kanner, B.I.3
  • 18
    • 77956362466 scopus 로고    scopus 로고
    • Evidence for a third sodium-binding site in glutamate transporters suggests an ion/ substrate coupling model
    • Larsson HP, Wang XY, Lev B, Baconguis I, Caplan DA, et al. (2010) Evidence for a third sodium-binding site in glutamate transporters suggests an ion/ substrate coupling model. Proc Natl Acad Sci USA 107:13912-13917.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13912-13917
    • Larsson, H.P.1    Wang, X.Y.2    Lev, B.3    Baconguis, I.4    Caplan, D.A.5
  • 19
    • 0037462748 scopus 로고    scopus 로고
    • Is the glutamate residue Glu-373 the proton acceptor of the excitatory amino acid carrier 1?
    • DOI 10.1074/jbc.M207956200
    • Grewer C, Watzke N, Rauen T, Bicho A (2003) Is the glutamate residue glu-373 the proton acceptor of the excitatory amino acid carrier 1? J Biol Chem 278:2585-2592. (Pubitemid 36801337)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2585-2592
    • Grewer, C.1    Watzke, N.2    Rauen, T.3    Bicho, A.4
  • 20
    • 82355184476 scopus 로고    scopus 로고
    • A conserved aspartate residue located at the end of the binding pocket controls cation interactions in brain glutamate transporters
    • Rosental N, Gameiro A, Grewer C, Kanner BI (2011) A conserved aspartate residue located at the end of the binding pocket controls cation interactions in brain glutamate transporters. J Biol Chem 286:41381-41390.
    • (2011) J Biol Chem , vol.286 , pp. 41381-41390
    • Rosental, N.1    Gameiro, A.2    Grewer, C.3    Kanner, B.I.4
  • 21
    • 34249788444 scopus 로고    scopus 로고
    • Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporter
    • DOI 10.1085/jgp.200609707
    • Teichman S, Kanner BI (2007) Aspartate-444 is essential for productive substrate interactions in a neuronal glutamate transporter. J Gen Physiol 129:527-539. (Pubitemid 46849151)
    • (2007) Journal of General Physiology , vol.129 , Issue.6 , pp. 527-539
    • Teichman, S.1    Kanner, B.I.2
  • 22
    • 1642494714 scopus 로고    scopus 로고
    • Arginine 445 Controls the Coupling between Glutamate and Cations in the Neuronal Transporter EAAC-1
    • DOI 10.1074/jbc.M311446200
    • Borre L, Kanner BI (2004) Arginine 445 controls the coupling between glutamate and cations in the neuronal transporter EAAC-1. J Biol Chem 279:2513-2519. (Pubitemid 38114235)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2513-2519
    • Borre, L.1    Kanner, B.I.2
  • 23
    • 0034529012 scopus 로고    scopus 로고
    • Arginine 447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter
    • DOI 10.1074/jbc.M006536200
    • Bendahan A, Armon A, Madani N, Kavanaugh MP, Kanner BI (2000) Arginine 447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter. J Biol Chem 275:37436-37442. (Pubitemid 32004848)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37436-37442
    • Bendahan, A.1    Armon, A.2    Madani, N.3    Kavanaugh, M.P.4    Kanner, B.I.5
  • 24
    • 70149086286 scopus 로고    scopus 로고
    • The equivalent of a thallium binding residue from an archaeal homolog controls cation interactions in brain glutamate transporters
    • Teichman S, Qu S, Kanner BI (2009) The equivalent of a thallium binding residue from an archaeal homolog controls cation interactions in brain glutamate transporters. Proc Natl Acad Sci USA 106:14297-14302.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14297-14302
    • Teichman, S.1    Qu, S.2    Kanner, B.I.3
  • 25
    • 84871346150 scopus 로고    scopus 로고
    • Protonation state of a conserved acidic amino acid involved in Na+ binding to the glutamate transporter EAAC1
    • Mwaura J, Tao Z, James H, Albers T, Schwartz A, et al. (2012) Protonation state of a conserved acidic amino acid involved in Na+ binding to the glutamate transporter EAAC1. ACS Chem Neurosci 3:1073-1083.
    • (2012) ACS Chem Neurosci , vol.3 , pp. 1073-1083
    • Mwaura, J.1    Tao, Z.2    James, H.3    Albers, T.4    Schwartz, A.5
  • 26
    • 57049106850 scopus 로고    scopus 로고
    • Thallium ions can replace both sodium and potassium ions in the glutamate transporter excitatory amino acid carrier 1
    • Tao Z, Gameiro A, Grewer C (2008) Thallium ions can replace both sodium and potassium ions in the glutamate transporter excitatory amino acid carrier 1. Biochemistry 47:12923-12930.
    • (2008) Biochemistry , vol.47 , pp. 12923-12930
    • Tao, Z.1    Gameiro, A.2    Grewer, C.3
  • 27
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • DOI 10.1038/nature03018
    • Yernool D, Boudker O, Jin Y, Gouaux E (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431:811-818. (Pubitemid 39434071)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 28
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • DOI 10.1038/nature05455, PII NATURE05455
    • Boudker O, Ryan RM, Yernool D, Shimamoto K, Gouaux E (2007) Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445:387-393. (Pubitemid 46160902)
    • (2007) Nature , vol.445 , Issue.7126 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 29
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • Reyes N, Ginter C, Boudker O (2009) Transport mechanism of a bacterial homologue of glutamate transporters. Nature 462:880-885.
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 30
    • 0029023101 scopus 로고
    • Constitutive ion uxes and substrate binding domains of human glutamate transporters
    • Vandenberg RJ, Arriza JL, Amara SG, Kavanaugh MP (1995) Constitutive ion uxes and substrate binding domains of human glutamate transporters. J Biol Chem 270:17668-17671.
    • (1995) J Biol Chem , vol.270 , pp. 17668-17671
    • Vandenberg, R.J.1    Arriza, J.L.2    Amara, S.G.3    Kavanaugh, M.P.4
  • 31
    • 0033681163 scopus 로고    scopus 로고
    • A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines
    • Seal RP, Leighton BH, Amara SG (2000) A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines. Neuron 25:695-706.
    • (2000) Neuron , vol.25 , pp. 695-706
    • Seal, R.P.1    Leighton, B.H.2    Amara, S.G.3
  • 32
    • 67650526059 scopus 로고    scopus 로고
    • Functional characterization of a Na+-dependent as-partate transporter from Pyrococcus horikoshii
    • Ryan RM, Compton EL, Mindell JA (2009) Functional characterization of a Na+-dependent as-partate transporter from Pyrococcus horikoshii. J Biol Chem 284:17540-17548.
    • (2009) J Biol Chem , vol.284 , pp. 17540-17548
    • Ryan, R.M.1    Compton, E.L.2    Mindell, J.A.3
  • 33
    • 77951680965 scopus 로고    scopus 로고
    • Na+:aspartate coupling stoichiometry in the glutamate trans-porter homologue GltPh
    • Groeneveld M, Slotboom DJ (2010) Na+:aspartate coupling stoichiometry in the glutamate trans-porter homologue GltPh. Biochemistry 49:3511-3513.
    • (2010) Biochemistry , vol.49 , pp. 3511-3513
    • Groeneveld, M.1    Slotboom, D.J.2
  • 34
    • 78149499345 scopus 로고    scopus 로고
    • New views of glutamate transporter structure and function: Advances and challenges
    • Jiang J, Amara SG (2011) New views of glutamate transporter structure and function: advances and challenges. Neuropharmacology 60:172-181.
    • (2011) Neuropharmacology , vol.60 , pp. 172-181
    • Jiang, J.1    Amara, S.G.2
  • 35
    • 78650297251 scopus 로고    scopus 로고
    • The Structural basis of secondary active transport mech-anisms
    • Forrest LR, Kramer R, Ziegler C (2011) The Structural basis of secondary active transport mech-anisms. Biochim Biophys Acta 1807:167-188.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Kramer, R.2    Ziegler, C.3
  • 36
    • 57649119782 scopus 로고    scopus 로고
    • Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter
    • Shrivastava IH, Jiang J, Amara SG, Bahar I (2008) Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter. J Biol Chem 283:28680-28690.
    • (2008) J Biol Chem , vol.283 , pp. 28680-28690
    • Shrivastava, I.H.1    Jiang, J.2    Amara, S.G.3    Bahar, I.4
  • 37
    • 51649088013 scopus 로고    scopus 로고
    • Dynamics of the extracellular gate and ionsubstrate coupling in the glutamate transporter
    • Huang Z, Tajkhorshid E (2008) Dynamics of the extracellular gate and ionsubstrate coupling in the glutamate transporter. Biophys J 95:2292-2300.
    • (2008) Biophys J , vol.95 , pp. 2292-2300
    • Huang, Z.1    Tajkhorshid, E.2
  • 38
    • 84855716593 scopus 로고    scopus 로고
    • Investigating the mechanism of substrate uptake and release in the glutamate transporter homologue GltPh through metadynamics simulations
    • Grazioso G, Limongelli V, Branduardi D, Novellino E, De Micheli C, et al. (2012) Investigating the mechanism of substrate uptake and release in the glutamate transporter homologue GltPh through metadynamics simulations. J Am Chem Soc 134:453-463.
    • (2012) J Am Chem Soc , vol.134 , pp. 453-463
    • Grazioso, G.1    Limongelli, V.2    Branduardi, D.3    Novellino, E.4    De Micheli, C.5
  • 39
    • 84875446139 scopus 로고    scopus 로고
    • Intracellular gating in an inward-facing state of aspartate transporter Glt(Ph) is regulated by the movements of the helical hairpin HP2
    • Zomot E, Bahar I (2013) Intracellular gating in an inward-facing state of aspartate transporter Glt(Ph) is regulated by the movements of the helical hairpin HP2. J Biol Chem 288:8231-8237.
    • (2013) J Biol Chem , vol.288 , pp. 8231-8237
    • Zomot, E.1    Bahar, I.2
  • 40
    • 84877702735 scopus 로고    scopus 로고
    • Mechanism and energetics of ligand release in the aspartate transporter GltPh
    • Heinzelmann G, Bastug T, Kuyucak S (2013) Mechanism and energetics of ligand release in the aspartate transporter GltPh. J Phys Chem B 117:5486-5496.
    • (2013) J Phys Chem B , vol.117 , pp. 5486-5496
    • Heinzelmann, G.1    Bastug, T.2    Kuyucak, S.3
  • 41
    • 77956527543 scopus 로고    scopus 로고
    • Identification of the third Na+ site and the sequence of extracellular binding events in the glutamate transporter
    • Huang Z, Tajkhorshid E (2010) Identification of the third Na+ site and the sequence of extracellular binding events in the glutamate transporter. Biophys J 99:1416-1425.
    • (2010) Biophys J , vol.99 , pp. 1416-1425
    • Huang, Z.1    Tajkhorshid, E.2
  • 42
    • 81255200359 scopus 로고    scopus 로고
    • Free energy simulations of ligand binding to the aspartate transporter GltPh
    • Heinzelmann G, Bastug T, Kuyucak S (2011) Free energy simulations of ligand binding to the aspartate transporter GltPh. Biophys J 101:2380-2388.
    • (2011) Biophys J , vol.101 , pp. 2380-2388
    • Heinzelmann, G.1    Bastug, T.2    Kuyucak, S.3
  • 43
    • 62449268980 scopus 로고    scopus 로고
    • Molecular simulations elucidate the substrate translocation pathway in a glutamate transporter
    • Gu Y, Shrivastava IH, Amara SG, Bahar I (2009) Molecular simulations elucidate the substrate translocation pathway in a glutamate transporter. Proc Natl Acad Sci USA 106:2589-2594.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2589-2594
    • Gu, Y.1    Shrivastava, I.H.2    Amara, S.G.3    Bahar, I.4
  • 44
    • 80053084303 scopus 로고    scopus 로고
    • Large collective motions regulate the functional properties of glutamate transporter trimers
    • Jiang J, Shrivastava IH, Watts SD, Bahar I, Amara SG (2011) Large collective motions regulate the functional properties of glutamate transporter trimers. Proc Natl Acad Sci USA 108:15141-15146.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 15141-15146
    • Jiang, J.1    Shrivastava, I.H.2    Watts, S.D.3    Bahar, I.4    Amara, S.G.5
  • 45
    • 84861090698 scopus 로고    scopus 로고
    • Structural intermediates in a model of the sub-strate translocation path of the bacterial glutamate transporter GltPh
    • Stolzenberg S, Khelashvili G, Weinstein H (2012) Structural intermediates in a model of the sub-strate translocation path of the bacterial glutamate transporter GltPh. J Phys Chem B 116:5372-5383.
    • (2012) J Phys Chem B , vol.116 , pp. 5372-5383
    • Stolzenberg, S.1    Khelashvili, G.2    Weinstein, H.3
  • 46
    • 61449430457 scopus 로고    scopus 로고
    • Interactions of alkali cations with glutamate transporters
    • Holley DC, Kavanaugh MP (2009) Interactions of alkali cations with glutamate transporters. Phil Trans R Soc B 364:155-161.
    • (2009) Phil Trans R Soc B , vol.364 , pp. 155-161
    • Holley, D.C.1    Kavanaugh, M.P.2
  • 47
    • 0033767399 scopus 로고    scopus 로고
    • On the mechanism of proton transport by the neuronal excitatory amino acid carrier 1
    • Watzke N, Rauen T, Bamberg E, Grewer C (2000) On the mechanism of proton transport by the neuronal excitatory amino acid carrier 1. J Gen Physiol 116:609-621.
    • (2000) J Gen Physiol , vol.116 , pp. 609-621
    • Watzke, N.1    Rauen, T.2    Bamberg, E.3    Grewer, C.4
  • 49
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • DOI 10.1110/ps.0217002
    • Zhou H, Zhou Y (2002) Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci 11:2714-2726. (Pubitemid 35191145)
    • (2002) Protein Science , vol.11 , Issue.11 , pp. 2714-2726
    • Zhou, H.1    Zhou, Y.2
  • 50
    • 79551613290 scopus 로고    scopus 로고
    • Toward the estimation of the absolute quality of individual protein structure models
    • Benkert P, Biasini M, Schwede T (2011) Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics 27:343-350.
    • (2011) Bioinformatics , vol.27 , pp. 343-350
    • Benkert, P.1    Biasini, M.2    Schwede, T.3
  • 51
    • 34548300005 scopus 로고    scopus 로고
    • Voltage-independent sodium-binding events reported by the 4B-4C loop in the human glutamate transporter excitatory amino acid transporter 3
    • DOI 10.1074/jbc.M704087200
    • Koch HP, Hubbard JM, Larsson HP (2007) Voltage-independent sodiumbinding events reported by the 4B-4C loop in the human glutamate transporter excitatory amino acid transporter 3. J Biol Chem 282:24547-24553. (Pubitemid 47347537)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24547-24553
    • Koch, H.P.1    Hubbard, J.M.2    Larsson, H.P.3
  • 52
    • 0031056670 scopus 로고    scopus 로고
    • The role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis
    • Frillingos S, Ujwal ML, Sun JZ, Kaback HR (1997) The role of helix VIII in the lactose permease of Escherichia coli. 1. Cys-scanning mutagenesis. Protein Sci 6:431-437. (Pubitemid 27079936)
    • (1997) Protein Science , vol.6 , Issue.2 , pp. 431-437
    • Frillingos, S.1    Ujwal, M.L.2    Sun, J.3    Kaback, H.R.4
  • 53
    • 14044263640 scopus 로고    scopus 로고
    • Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters
    • DOI 10.1523/JNEUROSCI.4138-04.2005
    • Koch HP, Larsson HP (2005) Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters. J Neurosci 25:1730-1736. (Pubitemid 40279278)
    • (2005) Journal of Neuroscience , vol.25 , Issue.7 , pp. 1730-1736
    • Koch, H.P.1    Larsson, H.P.2
  • 54
    • 84873029441 scopus 로고    scopus 로고
    • Role of protein matrix rigidity and local polarization effects in the monovalent cation selectivity of crystallographic sites in the Nacoupled aspartate transporter GltPh
    • Lev B, Noskov SY (2013) Role of protein matrix rigidity and local polarization effects in the monovalent cation selectivity of crystallographic sites in the Nacoupled aspartate transporter GltPh. Phys Chem Chem Phys 15:2397-2404.
    • (2013) Phys Chem Chem Phys , vol.15 , pp. 2397-2404
    • Lev, B.1    Noskov, S.Y.2
  • 55
    • 84881364525 scopus 로고    scopus 로고
    • Novel dicarboxylate selectivity in an insect glutamate transporter homolog
    • Wang H, Rascoe AM, Holley DC, Gouaux E, Kavanaugh MP (2013) Novel dicarboxylate selectivity in an insect glutamate transporter homolog. PLoS ONE 8:e70947.
    • (2013) PLoS ONE , vol.8
    • Wang, H.1    Rascoe, A.M.2    Holley, D.C.3    Gouaux, E.4    Kavanaugh, M.P.5
  • 58
    • 84885669136 scopus 로고    scopus 로고
    • Transport dynamics in a glutamate transporter homologue
    • Akyuz N, Altman RB, Blanchard SC, Boudker O (2013) Transport dynamics in a glutamate transporter homologue. Nature 502:114-118.
    • (2013) Nature , vol.502 , pp. 114-118
    • Akyuz, N.1    Altman, R.B.2    Blanchard, S.C.3    Boudker, O.4
  • 59
    • 84885606528 scopus 로고    scopus 로고
    • Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters
    • Erkens GB, Hnelt I, Goudsmits JMH, Slotboom DJ, van Oijen AM (2013) Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters. Nature 502:119-123.
    • (2013) Nature , vol.502 , pp. 119-123
    • Erkens, G.B.1    Hnelt, I.2    Jmh, G.3    Slotboom, D.J.4    Van Oijen, A.M.5
  • 62
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • Klauda JB, Venable RM, Freites JA, OConnor JW, Tobias DJ, et al. (2012) Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types. J Phys Chem B 114:7830-7843.
    • (2012) J Phys Chem B , vol.114 , pp. 7830-7843
    • Klauda, J.B.1    Venable, R.M.2    Freites, J.A.3    Oconnor, J.W.4    Tobias, D.J.5
  • 63
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics: The Langevin piston method
    • Feller S, Zhang Y, Pastor R, Brooks B (1995) Constant pressure molecular dynamics: the Langevin piston method. J Chem Phys 103:4613-4621.
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.1    Zhang, Y.2    Pastor, R.3    Brooks, B.4
  • 64
    • 0024578173 scopus 로고
    • Free energy via molecular simulation: Applications to chemical and biomolecular systems
    • Beveridge DL, DiCapua FM (1989) Free energy via molecular simulation: applications to chemical and biomolecular systems. Ann Rev Biophys Biophys Chem 18:431-492.
    • (1989) Ann Rev Biophys Biophys Chem , vol.18 , pp. 431-492
    • Beveridge, D.L.1    Dicapua, F.M.2
  • 65
    • 85027948926 scopus 로고    scopus 로고
    • Binding thermodynamics of a glutamate transporter homolog
    • Reyes N, Oh S, Boudker O (2013) Binding thermodynamics of a glutamate transporter homolog. Nat Struct Mol Biol 20: 634-641.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 634-641
    • Reyes, N.1    Oh, S.2    Boudker, O.3
  • 66
    • 17044372385 scopus 로고    scopus 로고
    • Absolute and relative entropies from computer simulation with applications to ligand binding
    • DOI 10.1021/jp046022f
    • Carlson J, Aqvist J (2005) Absolute and relative entropies from computer simulation with appli-cations to ligand binding. J Phys Chem B 109:6448-6456. (Pubitemid 40496862)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.13 , pp. 6448-6456
    • Carlsson, J.1    Aqvist, J.2
  • 68
    • 0031058541 scopus 로고    scopus 로고
    • The statistical-thermodynamic basis for computation of binding affinities: A critical review
    • Gilson MK, Given JA, Bush BL, McCammon JA (1997) The statisticalthermodynamic basis for computation of binding affinities: A critical review. Biophys J 72:1047-1069. (Pubitemid 27113632)
    • (1997) Biophysical Journal , vol.72 , Issue.3 , pp. 1047-1069
    • Gilson, M.K.1    Given, J.A.2    Bush, B.L.3    McCammon, J.A.4
  • 69
    • 0141682863 scopus 로고    scopus 로고
    • Absolute binding free energies: A quantitative approach for their calculation
    • Boresch S, Tettinger F, Leitgeb M, Karplus M (2003) Absolute binding free energies: A quantitative approach for their calculation. J Phys Chem B 107:9535-9551.
    • (2003) J Phys Chem B , vol.107 , pp. 9535-9551
    • Boresch, S.1    Tettinger, F.2    Leitgeb, M.3    Karplus, M.4
  • 70
    • 84894549950 scopus 로고    scopus 로고
    • Computation of standard binding free energies of polar and charged ligands to the glutamate receptor GluA2
    • Heinzelmann G, Chen PC, Kuyucak S (2014) Computation of standard binding free energies of polar and charged ligands to the glutamate receptor GluA2. J Phys Chem B 118:1813-1824.
    • (2014) J Phys Chem B , vol.118 , pp. 1813-1824
    • Heinzelmann, G.1    Chen, P.C.2    Kuyucak, S.3
  • 71
    • 84876214497 scopus 로고    scopus 로고
    • Funnel metadynamics as accurate binding free-energy method
    • Limongelli V, Bonomi M, Parrinello M (2013) Funnel metadynamics as accurate binding free-energy method. Proc Natl Acad Sci USA 110:6358-6363.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 6358-6363
    • Limongelli, V.1    Bonomi, M.2    Parrinello, M.3
  • 72
    • 45149123917 scopus 로고    scopus 로고
    • Comment on free energy simulations of single and double ion occupancy in gramicidin A [J. Chem. Phys.126, 105103 (2007)]
    • Roux B, Andersen OS, Allen TA (2008) Comment on Free energy simulations of single and double ion occupancy in gramicidin A [J. Chem. Phys.126, 105103 (2007)] J Chem Phys 128:227101.
    • (2008) J. Chem. Phys. , vol.26 , pp. 105103
    • Roux, B.1    Andersen, O.S.2    Allen, T.A.3


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