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Volumn 110, Issue 15, 2013, Pages

Identification of molecular hinge points mediating alternating access in the vesicular monoamine transporter VMAT2

Author keywords

Homology modeling; Ion coupling; Membrane proteins; Multidrug resistance; Neurotransmitter transporter

Indexed keywords

GLUTAMIC ACID; VESICULAR MONOAMINE TRANSPORTER 2;

EID: 84876049537     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1220497110     Document Type: Article
Times cited : (34)

References (61)
  • 1
    • 10744231003 scopus 로고    scopus 로고
    • The vesicular amine transporter family (SLC18): Amine/proton antiporters required for vesicular accumulation and regulated exocytotic secretion of monoamines and acetylcholine
    • Eiden LE, Schäfer MK, Weihe E, Schütz B (2004) The vesicular amine transporter family (SLC18): Amine/proton antiporters required for vesicular accumulation and regulated exocytotic secretion of monoamines and acetylcholine. Pflugers Arch 447(5):636-640.
    • (2004) Pflugers Arch , vol.447 , Issue.5 , pp. 636-640
    • Eiden, L.E.1    Schäfer, M.K.2    Weihe, E.3    Schütz, B.4
  • 2
    • 0028912433 scopus 로고
    • Vesicular neurotransmitter transporters: From bacteria to humans
    • Schuldiner S, Shirvan A, Linial M (1995) Vesicular neurotransmitter transporters: From bacteria to humans. Physiol Rev 75(2):369-392.
    • (1995) Physiol Rev , vol.75 , Issue.2 , pp. 369-392
    • Schuldiner, S.1    Shirvan, A.2    Linial, M.3
  • 3
    • 41149115776 scopus 로고    scopus 로고
    • Vesicular neurotransmitter transporters as targets for endogenous and exogenous toxic substances
    • Chaudhry FA, Edwards RH, Fonnum F (2008) Vesicular neurotransmitter transporters as targets for endogenous and exogenous toxic substances. Annu Rev Pharmacol Toxicol 48:277-301.
    • (2008) Annu Rev Pharmacol Toxicol , vol.48 , pp. 277-301
    • Chaudhry, F.A.1    Edwards, R.H.2    Fonnum, F.3
  • 4
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y, Lemieux MJ, Song J, Auer M, Wang DN (2003) Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301(5633):616-620.
    • (2003) Science , vol.301 , Issue.5633 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 5
    • 78751604619 scopus 로고    scopus 로고
    • Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2
    • Newstead S, et al. (2011) Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2. EMBO J 30(2):417-426.
    • (2011) EMBO J , vol.30 , Issue.2 , pp. 417-426
    • Newstead, S.1
  • 6
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson J, et al. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301(5633):610-615.
    • (2003) Science , vol.301 , Issue.5633 , pp. 610-615
    • Abramson, J.1
  • 7
    • 77958010505 scopus 로고    scopus 로고
    • Structure of a fucose transporter in an outward-open conformation
    • Dang S, et al. (2010) Structure of a fucose transporter in an outward-open conformation. Nature 467(7316):734-738.
    • (2010) Nature , vol.467 , Issue.7316 , pp. 734-738
    • Dang, S.1
  • 8
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin Y, He X, Szewczyk P, Nguyen T, Chang G (2006) Structure of the multidrug transporter EmrD from Escherichia coli. Science 312(5774):741-744.
    • (2006) Science , vol.312 , Issue.5774 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 9
    • 84867657593 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of glucose transporters GLUT1-4
    • Sun L, et al. (2012) Crystal structure of a bacterial homologue of glucose transporters GLUT1-4. Nature 490(7420):361-366.
    • (2012) Nature , vol.490 , Issue.7420 , pp. 361-366
    • Sun, L.1
  • 10
    • 79952738070 scopus 로고    scopus 로고
    • The alternating-access mechanism of MFS transporters arises from inverted-topology repeats
    • Radestock S, Forrest LR (2011) The alternating-access mechanism of MFS transporters arises from inverted-topology repeats. J Mol Biol 407(5):698-715.
    • (2011) J Mol Biol , vol.407 , Issue.5 , pp. 698-715
    • Radestock, S.1    Forrest, L.R.2
  • 11
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O (1966) Simple allosteric model for membrane pumps. Nature 211(5052):969-970.
    • (1966) Nature , vol.211 , Issue.5052 , pp. 969-970
    • Jardetzky, O.1
  • 12
    • 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) 24:377-386.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 13
    • 80755122853 scopus 로고    scopus 로고
    • Lactose permease and the alternating access mechanism
    • Smirnova I, Kasho V, Kaback HR (2011) Lactose permease and the alternating access mechanism. Biochemistry 50(45):9684-9693.
    • (2011) Biochemistry , vol.50 , Issue.45 , pp. 9684-9693
    • Smirnova, I.1    Kasho, V.2    Kaback, H.R.3
  • 14
    • 48349140230 scopus 로고    scopus 로고
    • Mechanism for alternating access in neurotransmitter transporters
    • Forrest LR, et al. (2008) Mechanism for alternating access in neurotransmitter transporters. Proc Natl Acad Sci USA 105(30):10338-10343.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.30 , pp. 10338-10343
    • Forrest, L.R.1
  • 15
    • 73949133608 scopus 로고    scopus 로고
    • Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats
    • Crisman TJ, Qu S, Kanner BI, Forrest LR (2009) Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats. Proc Natl Acad Sci USA 106(49):20752-20757.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.49 , pp. 20752-20757
    • Crisman, T.J.1    Qu, S.2    Kanner, B.I.3    Forrest, L.R.4
  • 16
    • 3042665547 scopus 로고    scopus 로고
    • Structural conservation in the major facilitator superfamily as revealed by comparative modeling
    • Vardy E, Arkin IT, Gottschalk KE, Kaback HR, Schuldiner S (2004) Structural conservation in the major facilitator superfamily as revealed by comparative modeling. Protein Sci 13(7):1832-1840.
    • (2004) Protein Sci , vol.13 , Issue.7 , pp. 1832-1840
    • Vardy, E.1    Arkin, I.T.2    Gottschalk, K.E.3    Kaback, H.R.4    Schuldiner, S.5
  • 17
    • 0031054527 scopus 로고    scopus 로고
    • Charged residues in transmembrane domains II and XI of a vesicular monoamine transporter form a charge pair that promotes high affinity substrate recognition
    • Merickel A, Kaback HR, Edwards RH (1997) Charged residues in transmembrane domains II and XI of a vesicular monoamine transporter form a charge pair that promotes high affinity substrate recognition. J Biol Chem 272(9):5403-5408.
    • (1997) J Biol Chem , vol.272 , Issue.9 , pp. 5403-5408
    • Merickel, A.1    Kaback, H.R.2    Edwards, R.H.3
  • 18
    • 17544366949 scopus 로고    scopus 로고
    • Modification of the pH profile and tetrabenazine sensitivity of rat VMAT1 by replacement of aspartate 404 with glutamate
    • Steiner-Mordoch S, Shirvan A, Schuldiner S (1996) Modification of the pH profile and tetrabenazine sensitivity of rat VMAT1 by replacement of aspartate 404 with glutamate. J Biol Chem 271(22):13048-13054.
    • (1996) J Biol Chem , vol.271 , Issue.22 , pp. 13048-13054
    • Steiner-Mordoch, S.1    Shirvan, A.2    Schuldiner, S.3
  • 19
    • 0034105641 scopus 로고    scopus 로고
    • Mutational analysis of basic residues in the rat vesicular acetylcholine transporter. Identification of a transmembrane ion pair and evidence that histidine is not involved in proton translocation
    • Kim MH, Lu M, Kelly M, Hersh LB (2000) Mutational analysis of basic residues in the rat vesicular acetylcholine transporter. Identification of a transmembrane ion pair and evidence that histidine is not involved in proton translocation. J Biol Chem 275(9):6175-6180.
    • (2000) J Biol Chem , vol.275 , Issue.9 , pp. 6175-6180
    • Kim, M.H.1    Lu, M.2    Kelly, M.3    Hersh, L.B.4
  • 20
    • 0029845047 scopus 로고    scopus 로고
    • Proton-dependent multidrug efflux systems
    • Paulsen IT, Brown MH, Skurray RA (1996) Proton-dependent multidrug efflux systems. Microbiol Rev 60(4):575-608.
    • (1996) Microbiol Rev , vol.60 , Issue.4 , pp. 575-608
    • Paulsen, I.T.1    Brown, M.H.2    Skurray, R.A.3
  • 21
    • 27144520233 scopus 로고    scopus 로고
    • Characterization of bacterial drug antiporters homologous to mammalian neurotransmitter transporters
    • Vardy E, Steiner-Mordoch S, Schuldiner S (2005) Characterization of bacterial drug antiporters homologous to mammalian neurotransmitter transporters. J Bacteriol 187(21):7518-7525.
    • (2005) J Bacteriol , vol.187 , Issue.21 , pp. 7518-7525
    • Vardy, E.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 22
    • 0034725629 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of transmembrane segments 4 and 5 of the Tn10-encoded metal-tetracycline/H+ antiporter reveals a permeability barrier in the middle of a transmembrane water-filled channel
    • Iwaki S, Tamura N, Kimura-Someya T, Nada S, Yamaguchi A (2000) Cysteine-scanning mutagenesis of transmembrane segments 4 and 5 of the Tn10-encoded metal-tetracycline/H+ antiporter reveals a permeability barrier in the middle of a transmembrane water-filled channel. J Biol Chem 275(30):22704-22712.
    • (2000) J Biol Chem , vol.275 , Issue.30 , pp. 22704-22712
    • Iwaki, S.1    Tamura, N.2    Kimura-Someya, T.3    Nada, S.4    Yamaguchi, A.5
  • 23
    • 0029382408 scopus 로고
    • Mutational analysis and molecular modelling of an amino acid sequence motif conserved in antiporters but not symporters in a transporter superfamily
    • Varela MF, Sansom CE, Griffith JK (1995) Mutational analysis and molecular modelling of an amino acid sequence motif conserved in antiporters but not symporters in a transporter superfamily. Mol Membr Biol 12(4):313-319.
    • (1995) Mol Membr Biol , vol.12 , Issue.4 , pp. 313-319
    • Varela, M.F.1    Sansom, C.E.2    Griffith, J.K.3
  • 24
    • 19644392529 scopus 로고    scopus 로고
    • Interhelical packing modulates conformational flexibility in the lactose permease of Escherichia coli
    • Ermolova NV, Smirnova IN, Kasho VN, Kaback HR (2005) Interhelical packing modulates conformational flexibility in the lactose permease of Escherichia coli. Biochemistry 44(21):7669-7677.
    • (2005) Biochemistry , vol.44 , Issue.21 , pp. 7669-7677
    • Ermolova, N.V.1    Smirnova, I.N.2    Kasho, V.N.3    Kaback, H.R.4
  • 25
    • 0033534625 scopus 로고    scopus 로고
    • Mutational analysis of aspartate residues in the transmembrane regions and cytoplasmic loops of rat vesicular acetylcholine transporter
    • Kim MH, Lu M, Lim EJ, Chai YG, Hersh LB (1999) Mutational analysis of aspartate residues in the transmembrane regions and cytoplasmic loops of rat vesicular acetylcholine transporter. J Biol Chem 274(2):673-680.
    • (1999) J Biol Chem , vol.274 , Issue.2 , pp. 673-680
    • Kim, M.H.1    Lu, M.2    Lim, E.J.3    Chai, Y.G.4    Hersh, L.B.5
  • 26
    • 0025097871 scopus 로고
    • Energetics of reserpine binding and occlusion by the chromaffin granule biogenic amine transporter
    • Rudnick G, Steiner-Mordoch SS, Fishkes H, Stern-Bach Y, Schuldiner S (1990) Energetics of reserpine binding and occlusion by the chromaffin granule biogenic amine transporter. Biochemistry 29(3):603-608.
    • (1990) Biochemistry , vol.29 , Issue.3 , pp. 603-608
    • Rudnick, G.1    Steiner-Mordoch, S.S.2    Fishkes, H.3    Stern-Bach, Y.4    Schuldiner, S.5
  • 27
    • 0032571364 scopus 로고    scopus 로고
    • Missense mutations that inactivate Escherichia coli lac permease
    • Bailey J, Manoil C (1998) Missense mutations that inactivate Escherichia coli lac permease. J Mol Biol 277(2):199-213.
    • (1998) J Mol Biol , vol.277 , Issue.2 , pp. 199-213
    • Bailey, J.1    Manoil, C.2
  • 28
    • 20444419395 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease
    • Kaback HR (2005) Structure and mechanism of the lactose permease. C R Biol 328(6):557-567.
    • (2005) C R Biol , vol.328 , Issue.6 , pp. 557-567
    • Kaback, H.R.1
  • 29
    • 36749095723 scopus 로고    scopus 로고
    • The fast release of sticky protons: Kinetics of substrate binding and proton release in a multidrug transporter
    • Adam Y, Tayer N, Rotem D, Schreiber G, Schuldiner S (2007) The fast release of sticky protons: Kinetics of substrate binding and proton release in a multidrug transporter. Proc Natl Acad Sci USA 104(46):17989-17994.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.46 , pp. 17989-17994
    • Adam, Y.1    Tayer, N.2    Rotem, D.3    Schreiber, G.4    Schuldiner, S.5
  • 30
    • 64649106418 scopus 로고    scopus 로고
    • EmrE, a model for studying evolution and mechanism of ion-coupled transporters
    • Schuldiner S (2009) EmrE, a model for studying evolution and mechanism of ion-coupled transporters. Biochim Biophys Acta 1794(5):748-762.
    • (2009) Biochim Biophys Acta , vol.1794 , Issue.5 , pp. 748-762
    • Schuldiner, S.1
  • 31
    • 77957854951 scopus 로고    scopus 로고
    • A flexible cation binding site in the multidrug major facilitator superfamily transporter LmrP is associated with variable proton coupling
    • Schaedler TA, van Veen HW (2010) A flexible cation binding site in the multidrug major facilitator superfamily transporter LmrP is associated with variable proton coupling. FASEB J 24(10):3653-3661.
    • (2010) FASEB J , vol.24 , Issue.10 , pp. 3653-3661
    • Schaedler, T.A.1    Van Veen, H.W.2
  • 32
    • 84864513575 scopus 로고    scopus 로고
    • Manipulating the drug/proton antiport stoichiometry of the secondary multidrug transporter MdfA
    • Tirosh O, et al. (2012) Manipulating the drug/proton antiport stoichiometry of the secondary multidrug transporter MdfA. Proc Natl Acad Sci USA 109(31):12473-12478.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.31 , pp. 12473-12478
    • Tirosh, O.1
  • 33
    • 77950635341 scopus 로고    scopus 로고
    • Possible important pair of acidic residues in vesicular acetylcholine transporter
    • Khare P, Ojeda AM, Chandrasekaran A, Parsons SM (2010) Possible important pair of acidic residues in vesicular acetylcholine transporter. Biochemistry 49(14):3049-3059.
    • (2010) Biochemistry , vol.49 , Issue.14 , pp. 3049-3059
    • Khare, P.1    Ojeda, A.M.2    Chandrasekaran, A.3    Parsons, S.M.4
  • 34
    • 84863173801 scopus 로고    scopus 로고
    • Mechanism of proton/substrate coupling in the heptahelical lysosomal transporter cystinosin
    • Ruivo R, et al. (2012) Mechanism of proton/substrate coupling in the heptahelical lysosomal transporter cystinosin. Proc Natl Acad Sci USA 109(5):E210-E217.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.5
    • Ruivo, R.1
  • 35
    • 80053351510 scopus 로고    scopus 로고
    • Towards a structural understanding of drug and peptide transport within the proton-dependent oligopeptide transporter (POT) family
    • Newstead S (2011) Towards a structural understanding of drug and peptide transport within the proton-dependent oligopeptide transporter (POT) family. Biochem Soc Trans 39(5):1353-1358.
    • (2011) Biochem Soc Trans , vol.39 , Issue.5 , pp. 1353-1358
    • Newstead, S.1
  • 37
    • 77956189075 scopus 로고    scopus 로고
    • Structural perspectives on secondary active transporters
    • Boudker O, Verdon G (2010) Structural perspectives on secondary active transporters. Trends Pharmacol Sci 31(9):418-426.
    • (2010) Trends Pharmacol Sci , vol.31 , Issue.9 , pp. 418-426
    • Boudker, O.1    Verdon, G.2
  • 38
    • 0030771680 scopus 로고    scopus 로고
    • Interaction between residues Glu269 (helix VIII) and His322 (helix X) of the lactose permease of Escherichia coli is essential for substrate binding
    • He MM, Kaback HR (1997) Interaction between residues Glu269(helix VIII) and His322 (helix X) of the lactose permease of Escherichia coli is essential for substrate binding. Biochemistry 36 (44):13688-13692.
    • (1997) Biochemistry , vol.36 , Issue.44 , pp. 13688-13692
    • He, M.M.1    Kaback, H.R.2
  • 39
    • 0037036449 scopus 로고    scopus 로고
    • Structure/function relationships in OxlT, the oxalate/formate antiporter of Oxalobacter formigenes: Assignment of transmembrane helix 2 to the translocation pathway
    • Ye L, Maloney PC (2002) Structure/function relationships in OxlT, the oxalate/formate antiporter of Oxalobacter formigenes: Assignment of transmembrane helix 2 to the translocation pathway. J Biol Chem 277(23):20372-20378.
    • (2002) J Biol Chem , vol.277 , Issue.23 , pp. 20372-20378
    • Ye, L.1    Maloney, P.C.2
  • 40
    • 0035965315 scopus 로고    scopus 로고
    • Helix proximity in OxlT, the oalate: Formate antiporter of oxalobacter formigenes. Cross-linking between TM2 and TM11
    • Kim YM, Ye L, Maloney PC (2001) Helix proximity in OxlT, the oalate: formate antiporter of oxalobacter formigenes. Cross-linking between TM2 and TM11. J Biol Chem 276(39):36681-36686.
    • (2001) J Biol Chem , vol.276 , Issue.39 , pp. 36681-36686
    • Kim, Y.M.1    Ye, L.2    Maloney, P.C.3
  • 41
    • 0035830595 scopus 로고    scopus 로고
    • Physiological evidence for an interaction between helices II and XI in the melibiose carrier of Escherichia coli
    • Franco PJ, Jena AB, Wilson TH (2001) Physiological evidence for an interaction between helices II and XI in the melibiose carrier of Escherichia coli. Biochim Biophys Acta 1510(1-2):231-242.
    • (2001) Biochim Biophys Acta , vol.1510 , Issue.1-2 , pp. 231-242
    • Franco, P.J.1    Jena, A.B.2    Wilson, T.H.3
  • 42
    • 0037373068 scopus 로고    scopus 로고
    • Structural model for 12-helix transporters belonging to the major facilitator superfamily
    • Hirai T, Heymann J A W, Maloney PC, Subramaniam S (2003) Structural model for 12-helix transporters belonging to the major facilitator superfamily. J Bacteriol 185(5):1712-1718.
    • (2003) J Bacteriol , vol.185 , Issue.5 , pp. 1712-1718
    • Hirai, T.1    Heymann, J.A.W.2    Maloney, P.C.3    Subramaniam, S.4
  • 43
    • 33750212348 scopus 로고    scopus 로고
    • Crystal structure and mechanism of GlpT, the glycerol-3-phosphate transporter from E
    • Lemieux MJ, Huang Y, Wang N (2005) Crystal structure and mechanism of GlpT, the glycerol-3-phosphate transporter from E. coli. J Electron Microsc (Tokyo) 54(Suppl 1):i43-i46.
    • (2005) Coli. J Electron Microsc (Tokyo) , vol.54 , Issue.SUPPL. 1
    • Lemieux, M.J.1    Huang, Y.2    Wang, N.3
  • 44
    • 36749074450 scopus 로고    scopus 로고
    • Sugar binding induces an outward facing conformation of LacY
    • Smirnova I, et al. (2007) Sugar binding induces an outward facing conformation of LacY. Proc Natl Acad Sci USA 104(42):16504-16509.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.42 , pp. 16504-16509
    • Smirnova, I.1
  • 45
    • 84868095500 scopus 로고    scopus 로고
    • Apo-intermediate in the transport cycle of lactose permease (LacY)
    • Madej MG, Soro SN, Kaback HR (2012) Apo-intermediate in the transport cycle of lactose permease (LacY). Proc Natl Acad Sci USA 109(44):E2970-E2978.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.44
    • Madej, M.G.1    Soro, S.N.2    Kaback, H.R.3
  • 46
    • 33749109860 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul S, et al. (1998) Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. FASEB J 12:A1326-A1326.
    • (1998) FASEB J , vol.12
    • Altschul, S.1
  • 48
    • 33745634395 scopus 로고    scopus 로고
    • Cd-hit: A fast program for clustering and comparing large sets of protein or nucleotide sequences
    • Li WZ, Godzik A (2006) Cd-hit: A fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics 22(13):1658-1659.
    • (2006) Bioinformatics , vol.22 , Issue.13 , pp. 1658-1659
    • Li, W.Z.1    Godzik, A.2
  • 49
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32(5):1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 50
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T, Bell RE, Mayrose I, Glaser F., Ben-Tal N (2002) Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues. Bioinformatics 18(Suppl 1):S71-S77.
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 51
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser F, et al. (2003) ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19(1):163-164.
    • (2003) Bioinformatics , vol.19 , Issue.1 , pp. 163-164
    • Glaser, F.1
  • 52
    • 33745714411 scopus 로고    scopus 로고
    • On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins
    • Forrest LR, Tang CL, Honig B (2006) On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins. Biophys J 91(2):508-517.
    • (2006) Biophys J , vol.91 , Issue.2 , pp. 508-517
    • Forrest, L.R.1    Tang, C.L.2    Honig, B.3
  • 53
    • 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(3):779-815.
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 54
    • 77952850689 scopus 로고    scopus 로고
    • Quality assessment of protein model-structures using evolutionary conservation
    • Kalman M, Ben-Tal N (2010) Quality assessment of protein model-structures using evolutionary conservation. Bioinformatics 26(10):1299-1307.
    • (2010) Bioinformatics , vol.26 , Issue.10 , pp. 1299-1307
    • Kalman, M.1    Ben-Tal, N.2
  • 55
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • Laskowski RA, Macarthur MW, Moss DS, Thornton JM (1993) Procheck - A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 56
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16(6):566-567.
    • (2000) Bioinformatics , vol.16 , Issue.6 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 57
    • 84986512474 scopus 로고
    • Charmm - A program for macromolecular energy, minimization, and dynamics calculations
    • Brooks BR, et al. (1983) Charmm - A program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 4:187-217.
    • (1983) J Comput Chem , vol.4 , pp. 187-217
    • Brooks, B.R.1
  • 58
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word JM, Lovell SC, Richardson JS, Richardson DC (1999) Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation. J Mol Biol 285(4):1735-1747.
    • (1999) J Mol Biol , vol.285 , Issue.4 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 59
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell AD, et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102:3586-3616.
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 60
    • 77955416344 scopus 로고    scopus 로고
    • Expression of neurotransmitter transporters for structural and biochemical studies
    • Elbaz Y, Danieli T, Kanner BI, Schuldiner S (2010) Expression of neurotransmitter transporters for structural and biochemical studies. Protein Expr Purif 73(2):152-160.
    • (2010) Protein Expr Purif , vol.73 , Issue.2 , pp. 152-160
    • Elbaz, Y.1    Danieli, T.2    Kanner, B.I.3    Schuldiner, S.4
  • 61
    • 41949089632 scopus 로고    scopus 로고
    • Expression and function of the rat vesicular monoamine transporter 2
    • Adam Y, Edwards RH, Schuldiner S (2008) Expression and function of the rat vesicular monoamine transporter 2. Am J Physiol Cell Physiol 294(4):C1004-C1011.
    • (2008) Am J Physiol Cell Physiol , vol.294 , Issue.4
    • Adam, Y.1    Edwards, R.H.2    Schuldiner, S.3


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