메뉴 건너뛰기




Volumn 73, Issue 1, 2014, Pages 16-26

Antagonist-induced conformational changes in dopamine transporter extracellular loop two involve residues in a potential salt bridge

Author keywords

Amphetamine; Cocaine; Methamphetamine; Molecular modeling; SCAM

Indexed keywords

COCAINE; CYSTEINE; DOPAMINE TRANSPORTER; LEUCINE; PEPTIDE; PROTEINASE; SODIUM CHLORIDE; DOPAMINE; DOPAMINE RECEPTOR BLOCKING AGENT; DOPAMINE UPTAKE INHIBITOR; ENDOPROTEINASE ASP-N; METALLOPROTEINASE;

EID: 84902517787     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2013.11.003     Document Type: Article
Times cited : (7)

References (73)
  • 2
    • 0027446493 scopus 로고
    • Neurotransmitter transporters: Recent progress
    • S.G. Amara, and M.J. Kuhar Neurotransmitter transporters: recent progress Annu. Rev. Neurosci. 16 1993 73 93
    • (1993) Annu. Rev. Neurosci. , vol.16 , pp. 73-93
    • Amara, S.G.1    Kuhar, M.J.2
  • 3
    • 67649859504 scopus 로고    scopus 로고
    • Recent advances in the understanding of the interaction of antidepressant drugs with serotonin and norepinephrine transporters
    • J. Andersen, A.S. Kristensen, B. Bang-Andersen, and K. Stromgaard Recent advances in the understanding of the interaction of antidepressant drugs with serotonin and norepinephrine transporters Chem. Commun. (Camb.) 2009 3677 3692
    • (2009) Chem. Commun. (Camb.) , pp. 3677-3692
    • Andersen, J.1    Kristensen, A.S.2    Bang-Andersen, B.3    Stromgaard, K.4
  • 4
    • 65649109333 scopus 로고    scopus 로고
    • Location of the antidepressant binding site in the serotonin transporter: Importance of Ser-438 in recognition of citalopram and tricyclic antidepressants
    • J. Andersen, O. Taboureau, K.B. Hansen, L. Olsen, J. Egebjerg, K. Stromgaard, and A.S. Kristensen Location of the antidepressant binding site in the serotonin transporter: importance of Ser-438 in recognition of citalopram and tricyclic antidepressants J. Biol. Chem. 284 2009 10276 10284
    • (2009) J. Biol. Chem. , vol.284 , pp. 10276-10284
    • Andersen, J.1    Taboureau, O.2    Hansen, K.B.3    Olsen, L.4    Egebjerg, J.5    Stromgaard, K.6    Kristensen, A.S.7
  • 6
    • 84865425436 scopus 로고    scopus 로고
    • The solute carrier 6 family of transporters
    • S. Broer, and U. Gether The solute carrier 6 family of transporters Br. J. Pharmacol. 167 2012 256 278
    • (2012) Br. J. Pharmacol. , vol.167 , pp. 256-278
    • Broer, S.1    Gether, U.2
  • 7
    • 0030692041 scopus 로고    scopus 로고
    • The third transmembrane domain of the serotonin transporter contains residues associated with substrate and cocaine binding
    • J.G. Chen, A. Sachpatzidis, and G. Rudnick The third transmembrane domain of the serotonin transporter contains residues associated with substrate and cocaine binding J. Biol. Chem. 272 1997 28321 28327
    • (1997) J. Biol. Chem. , vol.272 , pp. 28321-28327
    • Chen, J.G.1    Sachpatzidis, A.2    Rudnick, G.3
  • 8
    • 0034695678 scopus 로고    scopus 로고
    • Transport-dependent accessibility of a cytoplasmic loop cysteine in the human dopamine transporter
    • N. Chen, J.V. Ferrer, J.A. Javitch, and J.B. Justice Jr. Transport-dependent accessibility of a cytoplasmic loop cysteine in the human dopamine transporter J. Biol. Chem. 275 2000 1608 1614
    • (2000) J. Biol. Chem. , vol.275 , pp. 1608-1614
    • Chen, N.1    Ferrer, J.V.2    Javitch, J.A.3    Justice, Jr.J.B.4
  • 9
    • 1242317021 scopus 로고    scopus 로고
    • Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation and cocaine binding
    • N. Chen, J. Rickey, J.L. Berfield, and M.E. Reith Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation and cocaine binding J. Biol. Chem. 279 2004 5508 5519
    • (2004) J. Biol. Chem. , vol.279 , pp. 5508-5519
    • Chen, N.1    Rickey, J.2    Berfield, J.L.3    Reith, M.E.4
  • 10
    • 34247276092 scopus 로고    scopus 로고
    • Direct evidence that two cysteines in the dopamine transporter form a disulfide bond
    • R. Chen, H. Wei, E.R. Hill, L. Chen, L. Jiang, D.D. Han, and H.H. Gu Direct evidence that two cysteines in the dopamine transporter form a disulfide bond Mol. Cell. Biochem. 298 2007 41 48
    • (2007) Mol. Cell. Biochem. , vol.298 , pp. 41-48
    • Chen, R.1    Wei, H.2    Hill, E.R.3    Chen, L.4    Jiang, L.5    Han, D.D.6    Gu, H.H.7
  • 11
    • 0242408732 scopus 로고    scopus 로고
    • Dopamine transporter as target for drug development of cocaine dependence medications
    • A.K. Dutta, S. Zhang, R. Kolhatkar, and M.E. Reith Dopamine transporter as target for drug development of cocaine dependence medications Eur. J. Pharmacol. 479 2003 93 106
    • (2003) Eur. J. Pharmacol. , vol.479 , pp. 93-106
    • Dutta, A.K.1    Zhang, S.2    Kolhatkar, R.3    Reith, M.E.4
  • 12
    • 0032482945 scopus 로고    scopus 로고
    • Cocaine alters the accessibility of endogenous cysteines in putative extracellular and intracellular loops of the human dopamine transporter
    • J.V. Ferrer, and J.A. Javitch Cocaine alters the accessibility of endogenous cysteines in putative extracellular and intracellular loops of the human dopamine transporter Proc. Natl. Acad. Sci. USA 95 1998 9238 9243
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9238-9243
    • Ferrer, J.V.1    Javitch, J.A.2
  • 13
    • 77951246287 scopus 로고    scopus 로고
    • Transmembrane domain 6 of the human serotonin transporter contributes to an aqueously accessible binding pocket for serotonin and the psychostimulant 3,4-methylene dioxymethamphetamine
    • J.R. Field, L.K. Henry, and R.D. Blakely Transmembrane domain 6 of the human serotonin transporter contributes to an aqueously accessible binding pocket for serotonin and the psychostimulant 3,4-methylene dioxymethamphetamine J. Biol. Chem. 285 2010 11270 11280
    • (2010) J. Biol. Chem. , vol.285 , pp. 11270-11280
    • Field, J.R.1    Henry, L.K.2    Blakely, R.D.3
  • 14
    • 73949083478 scopus 로고    scopus 로고
    • The rocking bundle: A mechanism for ion-coupled solute flux by symmetrical transporters
    • L.R. Forrest, and G. Rudnick The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters Physiology 24 2009 377 386
    • (2009) Physiology , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 15
    • 0037067690 scopus 로고    scopus 로고
    • Dopamine transporters are phosphorylated on N-terminal serines in rat striatum
    • J.D. Foster, B. Pananusorn, and R.A. Vaughan Dopamine transporters are phosphorylated on N-terminal serines in rat striatum J. Biol. Chem. 277 2002 25178 25186
    • (2002) J. Biol. Chem. , vol.277 , pp. 25178-25186
    • Foster, J.D.1    Pananusorn, B.2    Vaughan, R.A.3
  • 16
    • 1342265784 scopus 로고    scopus 로고
    • Uptake inhibitors but not substrates induce protease resistance in extracellular loop two of the dopamine transporter
    • J.D. Gaffaney, and R.A. Vaughan Uptake inhibitors but not substrates induce protease resistance in extracellular loop two of the dopamine transporter Mol. Pharmacol. 65 2004 692 701
    • (2004) Mol. Pharmacol. , vol.65 , pp. 692-701
    • Gaffaney, J.D.1    Vaughan, R.A.2
  • 17
    • 0030071106 scopus 로고    scopus 로고
    • Hyperlocomotion and indifference to cocaine and amphetamine in mice lacking the dopamine transporter
    • B. Giros, M. Jaber, S.R. Jones, R.M. Wightman, and M.G. Caron Hyperlocomotion and indifference to cocaine and amphetamine in mice lacking the dopamine transporter Nature 379 1996 606 612
    • (1996) Nature , vol.379 , pp. 606-612
    • Giros, B.1    Jaber, M.2    Jones, S.R.3    Wightman, R.M.4    Caron, M.G.5
  • 18
    • 0242665383 scopus 로고    scopus 로고
    • The human dopamine transporter forms a tetramer in the plasma membrane: Cross-linking of a cysteine in the fourth transmembrane segment is sensitive to cocaine analogs
    • H. Hastrup, N. Sen, and J.A. Javitch The human dopamine transporter forms a tetramer in the plasma membrane: cross-linking of a cysteine in the fourth transmembrane segment is sensitive to cocaine analogs J. Biol. Chem. 278 2003 45045 45048
    • (2003) J. Biol. Chem. , vol.278 , pp. 45045-45048
    • Hastrup, H.1    Sen, N.2    Javitch, J.A.3
  • 19
    • 0141844649 scopus 로고    scopus 로고
    • Serotonin and cocaine-sensitive inactivation of human serotonin transporters by methanethiosulfonates targeted to transmembrane domain i
    • L.K. Henry, E.M. Adkins, Q. Han, and R.D. Blakely Serotonin and cocaine-sensitive inactivation of human serotonin transporters by methanethiosulfonates targeted to transmembrane domain I J. Biol. Chem. 278 2003 37052 37063
    • (2003) J. Biol. Chem. , vol.278 , pp. 37052-37063
    • Henry, L.K.1    Adkins, E.M.2    Han, Q.3    Blakely, R.D.4
  • 20
    • 40849140989 scopus 로고    scopus 로고
    • Distinctions between dopamine transporter antagonists could be just around the bend
    • L.K. Henry, and R.D. Blakely Distinctions between dopamine transporter antagonists could be just around the bend Mol. Pharmacol. 73 2008 616 618
    • (2008) Mol. Pharmacol. , vol.73 , pp. 616-618
    • Henry, L.K.1    Blakely, R.D.2
  • 21
    • 33644856545 scopus 로고    scopus 로고
    • Tyr-95 and Ile-172 in transmembrane segments 1 and 3 of human serotonin transporters interact to establish high affinity recognition of antidepressants
    • L.K. Henry, J.R. Field, E.M. Adkins, M.L. Parnas, R.A. Vaughan, M.F. Zou, A.H. Newman, and R.D. Blakely Tyr-95 and Ile-172 in transmembrane segments 1 and 3 of human serotonin transporters interact to establish high affinity recognition of antidepressants J. Biol. Chem. 281 2006 2012 2023
    • (2006) J. Biol. Chem. , vol.281 , pp. 2012-2023
    • Henry, L.K.1    Field, J.R.2    Adkins, E.M.3    Parnas, M.L.4    Vaughan, R.A.5    Zou, M.F.6    Newman, A.H.7    Blakely, R.D.8
  • 22
    • 79957808687 scopus 로고    scopus 로고
    • Interaction of tyrosine 151 in norepinephrine transporter with the 2beta group of cocaine analog RTI-113
    • E.R. Hill, X. Huang, C.G. Zhan, F. Ivy Carroll, and H.H. Gu Interaction of tyrosine 151 in norepinephrine transporter with the 2beta group of cocaine analog RTI-113 Neuropharmacology 61 2011 112 120
    • (2011) Neuropharmacology , vol.61 , pp. 112-120
    • Hill, E.R.1    Huang, X.2    Zhan, C.G.3    Ivy Carroll, F.4    Gu, H.H.5
  • 23
    • 72449145780 scopus 로고    scopus 로고
    • Mechanism for cocaine blocking the transport of dopamine: Insights from molecular modeling and dynamics simulations
    • X. Huang, H.H. Gu, and C.G. Zhan Mechanism for cocaine blocking the transport of dopamine: insights from molecular modeling and dynamics simulations J. Phys. Chem. B 113 2009 15057 15066
    • (2009) J. Phys. Chem. B , vol.113 , pp. 15057-15066
    • Huang, X.1    Gu, H.H.2    Zhan, C.G.3
  • 24
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • O. Jardetzky Simple allosteric model for membrane pumps Nature 211 1966 969 970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 25
    • 0026722234 scopus 로고
    • Dopamine transporter site-directed mutations differentially alter substrate transport and cocaine binding
    • S. Kitayama, S. Shimada, H. Xu, L. Markham, D.M. Donovan, and G.R. Uhl Dopamine transporter site-directed mutations differentially alter substrate transport and cocaine binding Proc. Natl. Acad. Sci. USA 89 1992 7782 7785
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7782-7785
    • Kitayama, S.1    Shimada, S.2    Xu, H.3    Markham, L.4    Donovan, D.M.5    Uhl, G.R.6
  • 26
    • 47749083479 scopus 로고    scopus 로고
    • An intracellular interaction network regulates conformational transitions in the dopamine transporter
    • J. Kniazeff, L. Shi, C.J. Loland, J.A. Javitch, H. Weinstein, and U. Gether An intracellular interaction network regulates conformational transitions in the dopamine transporter J. Biol. Chem. 283 2008 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    Gether, U.6
  • 27
    • 84878940205 scopus 로고    scopus 로고
    • Ligand induced conformational changes of the human serotonin transporter revealed by molecular dynamics simulations
    • H. Koldso, H.E. Autzen, J. Grouleff, and B. Schiott Ligand induced conformational changes of the human serotonin transporter revealed by molecular dynamics simulations PLoS One 8 2013 e63635
    • (2013) PLoS One , vol.8 , pp. 63635
    • Koldso, H.1    Autzen, H.E.2    Grouleff, J.3    Schiott, B.4
  • 28
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • H. Krishnamurthy, and E. Gouaux X-ray structures of LeuT in substrate-free outward-open and apo inward-open states Nature 481 2012 469 474
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 30
    • 0025362328 scopus 로고
    • Kinetics and block of dopamine uptake in synaptosomes from rat caudate nucleus
    • B.K. Krueger Kinetics and block of dopamine uptake in synaptosomes from rat caudate nucleus J. Neurochem. 55 1990 260 267
    • (1990) J. Neurochem. , vol.55 , pp. 260-267
    • Krueger, B.K.1
  • 31
    • 84879411265 scopus 로고    scopus 로고
    • Simultaneous prediction of protein secondary structure and transmembrane spans
    • J.K. Leman, R. Mueller, M. Karakas, N. Woetzel, and J. Meiler Simultaneous prediction of protein secondary structure and transmembrane spans Proteins 81 2013 1127 1140
    • (2013) Proteins , vol.81 , pp. 1127-1140
    • Leman, J.K.1    Mueller, R.2    Karakas, M.3    Woetzel, N.4    Meiler, J.5
  • 32
    • 2442637536 scopus 로고    scopus 로고
    • The role of N-glycosylation in function and surface trafficking of the human dopamine transporter
    • L.B. Li, N. Chen, S. Ramamoorthy, L. Chi, X.N. Cui, L.C. Wang, and M.E. Reith The role of N-glycosylation in function and surface trafficking of the human dopamine transporter J. Biol. Chem. 279 2004 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    Wang, L.C.6    Reith, M.E.7
  • 33
    • 78751474117 scopus 로고    scopus 로고
    • N-substituted benztropine analogs: Selective dopamine transporter ligands with a fast onset of action and minimal cocaine-like behavioral effects
    • S.M. Li, T.A. Kopajtic, M.J. O'Callaghan, G.E. Agoston, J. Cao, A.H. Newman, and J.L. Katz N-substituted benztropine analogs: selective dopamine transporter ligands with a fast onset of action and minimal cocaine-like behavioral effects J. Pharmacol. Exp. Ther. 336 2011 575 585
    • (2011) J. Pharmacol. Exp. Ther. , vol.336 , pp. 575-585
    • Li, S.M.1    Kopajtic, T.A.2    O'Callaghan, M.J.3    Agoston, G.E.4    Cao, J.5    Newman, A.H.6    Katz, J.L.7
  • 34
    • 0033669731 scopus 로고    scopus 로고
    • Dopamine transporter tryptophan mutants highlight candidate dopamine- and cocaine-selective domains
    • Z. Lin, W. Wang, and G.R. Uhl Dopamine transporter tryptophan mutants highlight candidate dopamine- and cocaine-selective domains Mol. Pharmacol. 58 2000 1581 1592
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1581-1592
    • Lin, Z.1    Wang, W.2    Uhl, G.R.3
  • 36
    • 0942276396 scopus 로고    scopus 로고
    • Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding
    • C.J. Loland, C. Granas, J.A. Javitch, and U. Gether Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding J. Biol. Chem. 279 2004 3228 3238
    • (2004) J. Biol. Chem. , vol.279 , pp. 3228-3238
    • Loland, C.J.1    Granas, C.2    Javitch, J.A.3    Gether, U.4
  • 38
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • L.J. McGuffin, K. Bryson, and D.T. Jones The PSIPRED protein structure prediction server Bioinformatics 16 2000 404 405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 39
    • 9644295740 scopus 로고    scopus 로고
    • Zinc potentiates an uncoupled anion conductance associated with the dopamine transporter
    • A.K. Meinild, H.H. Sitte, and U. Gether Zinc potentiates an uncoupled anion conductance associated with the dopamine transporter J. Biol. Chem. 279 2004 49671 49679
    • (2004) J. Biol. Chem. , vol.279 , pp. 49671-49679
    • Meinild, A.K.1    Sitte, H.H.2    Gether, U.3
  • 42
    • 0032480011 scopus 로고    scopus 로고
    • Delineation of an endogenous zinc-binding site in the human dopamine transporter
    • L. Norregaard, D. Frederiksen, E.O. Nielsen, and U. Gether Delineation of an endogenous zinc-binding site in the human dopamine transporter EMBO J. 17 1998 4266 4273
    • (1998) EMBO J. , vol.17 , pp. 4266-4273
    • Norregaard, L.1    Frederiksen, D.2    Nielsen, E.O.3    Gether, U.4
  • 43
    • 0042232503 scopus 로고    scopus 로고
    • Evidence for distinct sodium-, dopamine-, and cocaine-dependent conformational changes in transmembrane segments 7 and 8 of the dopamine transporter
    • L. Norregaard, C.J. Loland, and U. Gether Evidence for distinct sodium-, dopamine-, and cocaine-dependent conformational changes in transmembrane segments 7 and 8 of the dopamine transporter J. Biol. Chem. 278 2003 30587 30596
    • (2003) J. Biol. Chem. , vol.278 , pp. 30587-30596
    • Norregaard, L.1    Loland, C.J.2    Gether, U.3
  • 44
    • 41149130280 scopus 로고    scopus 로고
    • Labeling of dopamine transporter transmembrane domain 1 with the tropane ligand N-[4-(4-azido-3-[125I]iodophenyl)butyl]-2beta-carbomethoxy-3beta-(4- chloro phenyl)tropane implicates proximity of cocaine and substrate active sites
    • M.L. Parnas, J.D. Gaffaney, M.F. Zou, J.R. Lever, A.H. Newman, and R.A. Vaughan Labeling of dopamine transporter transmembrane domain 1 with the tropane ligand N-[4-(4-azido-3-[125I]iodophenyl)butyl]-2beta-carbomethoxy-3beta-(4- chloro phenyl)tropane implicates proximity of cocaine and substrate active sites Mol. Pharmacol. 73 2008 1141 1150
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1141-1150
    • Parnas, M.L.1    Gaffaney, J.D.2    Zou, M.F.3    Lever, J.R.4    Newman, A.H.5    Vaughan, R.A.6
  • 45
    • 84887404259 scopus 로고    scopus 로고
    • X-ray structure of dopamine transporter elucidates antidepressant mechanism
    • A. Penmatsa, K.H. Wang, and E. Gouaux X-ray structure of dopamine transporter elucidates antidepressant mechanism Nature 503 2013 85 90
    • (2013) Nature , vol.503 , pp. 85-90
    • Penmatsa, A.1    Wang, K.H.2    Gouaux, E.3
  • 46
    • 78650817193 scopus 로고    scopus 로고
    • Neurotransmitter/sodium symporter orthologue LeuT has a single high-affinity substrate site
    • C.L. Piscitelli, H. Krishnamurthy, and E. Gouaux Neurotransmitter/sodium symporter orthologue LeuT has a single high-affinity substrate site Nature 468 2010 1129 1132
    • (2010) Nature , vol.468 , pp. 1129-1132
    • Piscitelli, C.L.1    Krishnamurthy, H.2    Gouaux, E.3
  • 47
    • 84873952800 scopus 로고    scopus 로고
    • Steric hindrance mutagenesis in the conserved extracellular vestibule impedes allosteric binding of antidepressants to the serotonin transporter
    • P. Plenge, L. Shi, T. Beuming, J. Te, A.H. Newman, H. Weinstein, U. Gether, and C.J. Loland Steric hindrance mutagenesis in the conserved extracellular vestibule impedes allosteric binding of antidepressants to the serotonin transporter J. Biol. Chem. 287 2012 39316 39326
    • (2012) J. Biol. Chem. , vol.287 , pp. 39316-39326
    • Plenge, P.1    Shi, L.2    Beuming, T.3    Te, J.4    Newman, A.H.5    Weinstein, H.6    Gether, U.7    Loland, C.J.8
  • 48
    • 20444413791 scopus 로고    scopus 로고
    • High- and low-affinity binding of S-citalopram to the human serotonin transporter mutated at 20 putatively important amino acid positions
    • P. Plenge, and O. Wiborg High- and low-affinity binding of S-citalopram to the human serotonin transporter mutated at 20 putatively important amino acid positions Neurosci. Lett. 383 2005 203 208
    • (2005) Neurosci. Lett. , vol.383 , pp. 203-208
    • Plenge, P.1    Wiborg, O.2
  • 49
    • 84875126075 scopus 로고    scopus 로고
    • SLC6 transporters: Structure, function, regulation, disease association and therapeutics
    • A.B. Pramod, J. Foster, L. Carvelli, and L.K. Henry SLC6 transporters: structure, function, regulation, disease association and therapeutics Mol. Aspects Med. 34 2013 197 219
    • (2013) Mol. Aspects Med. , vol.34 , pp. 197-219
    • Pramod, A.B.1    Foster, J.2    Carvelli, L.3    Henry, L.K.4
  • 51
    • 52049114697 scopus 로고    scopus 로고
    • The conserved salt bridge in human alpha-defensin 5 is required for its precursor processing and proteolytic stability
    • M. Rajabi, E. de Leeuw, M. Pazgier, J. Li, J. Lubkowski, and W. Lu The conserved salt bridge in human alpha-defensin 5 is required for its precursor processing and proteolytic stability J. Biol. Chem. 283 2008 21509 21518
    • (2008) J. Biol. Chem. , vol.283 , pp. 21509-21518
    • Rajabi, M.1    De Leeuw, E.2    Pazgier, M.3    Li, J.4    Lubkowski, J.5    Lu, W.6
  • 52
    • 0035800785 scopus 로고    scopus 로고
    • The uptake inhibitors cocaine and benztropine differentially alter the conformation of the human dopamine transporter
    • M.E. Reith, J.L. Berfield, L.C. Wang, J.V. Ferrer, and J.A. Javitch The uptake inhibitors cocaine and benztropine differentially alter the conformation of the human dopamine transporter J. Biol. Chem. 276 2001 29012 29018
    • (2001) J. Biol. Chem. , vol.276 , pp. 29012-29018
    • Reith, M.E.1    Berfield, J.L.2    Wang, L.C.3    Ferrer, J.V.4    Javitch, J.A.5
  • 53
    • 0030575913 scopus 로고    scopus 로고
    • Binding domains for blockers and substrates on the cloned human dopamine transporter studied by protection against N-ethylmaleimide-induced reduction of 2 beta-carbomethoxy-3 beta-(4-fluorophenyl)[3H]tropane ([3H]WIN 35,428) binding
    • M.E. Reith, C. Xu, and L.L. Coffey Binding domains for blockers and substrates on the cloned human dopamine transporter studied by protection against N-ethylmaleimide-induced reduction of 2 beta-carbomethoxy-3 beta-(4-fluorophenyl)[3H]tropane ([3H]WIN 35,428) binding Biochem. Pharmacol. 52 1996 1435 1446
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 1435-1446
    • Reith, M.E.1    Xu, C.2    Coffey, L.L.3
  • 54
    • 77949281313 scopus 로고    scopus 로고
    • Regulation of the dopamine transporter: Aspects relevant to psychostimulant drugs of abuse
    • K.C. Schmitt, and M.E. Reith Regulation of the dopamine transporter: aspects relevant to psychostimulant drugs of abuse Ann. N.Y. Acad. Sci. 1187 2010 316 340
    • (2010) Ann. N.Y. Acad. Sci. , vol.1187 , pp. 316-340
    • Schmitt, K.C.1    Reith, M.E.2
  • 56
    • 58149233796 scopus 로고    scopus 로고
    • A competitive inhibitor traps LeuT in an open-to-out conformation
    • S.K. Singh, C.L. Piscitelli, A. Yamashita, and E. Gouaux A competitive inhibitor traps LeuT in an open-to-out conformation Science 322 2008 1655 1661
    • (2008) Science , vol.322 , pp. 1655-1661
    • Singh, S.K.1    Piscitelli, C.L.2    Yamashita, A.3    Gouaux, E.4
  • 57
    • 34548178234 scopus 로고    scopus 로고
    • Antidepressant binding site in a bacterial homologue of neurotransmitter transporters
    • S.K. Singh, A. Yamashita, and E. Gouaux Antidepressant binding site in a bacterial homologue of neurotransmitter transporters Nature 448 2007 952 956
    • (2007) Nature , vol.448 , pp. 952-956
    • Singh, S.K.1    Yamashita, A.2    Gouaux, E.3
  • 58
    • 45649084560 scopus 로고    scopus 로고
    • Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction
    • C.A. Smith, and T. Kortemme Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction J. Mol. Biol. 380 2008 742 756
    • (2008) J. Mol. Biol. , vol.380 , pp. 742-756
    • Smith, C.A.1    Kortemme, T.2
  • 60
    • 79951702177 scopus 로고    scopus 로고
    • How addictive drugs disrupt presynaptic dopamine neurotransmission
    • D. Sulzer How addictive drugs disrupt presynaptic dopamine neurotransmission Neuron 69 2011 628 649
    • (2011) Neuron , vol.69 , pp. 628-649
    • Sulzer, D.1
  • 61
    • 77953163443 scopus 로고    scopus 로고
    • Discovery of drugs to treat cocaine dependence: Behavioral and neurochemical effects of atypical dopamine transport inhibitors
    • G. Tanda, A.H. Newman, and J.L. Katz Discovery of drugs to treat cocaine dependence: behavioral and neurochemical effects of atypical dopamine transport inhibitors Adv. Pharmacol. 57 2009 253 289
    • (2009) Adv. Pharmacol. , vol.57 , pp. 253-289
    • Tanda, G.1    Newman, A.H.2    Katz, J.L.3
  • 62
    • 0029072718 scopus 로고
    • Photoaffinity-labeled ligand binding domains on dopamine transporters identified by peptide mapping
    • R.A. Vaughan Photoaffinity-labeled ligand binding domains on dopamine transporters identified by peptide mapping Mol. Pharmacol. 47 1995 956 964
    • (1995) Mol. Pharmacol. , vol.47 , pp. 956-964
    • Vaughan, R.A.1
  • 63
    • 84883766007 scopus 로고    scopus 로고
    • Mechanisms of dopamine transporter regulation in normal and disease states
    • R.A. Vaughan, and J.D. Foster Mechanisms of dopamine transporter regulation in normal and disease states Trends Pharm. Sci. 34 2013 489 496
    • (2013) Trends Pharm. Sci. , vol.34 , pp. 489-496
    • Vaughan, R.A.1    Foster, J.D.2
  • 64
    • 0030972751 scopus 로고    scopus 로고
    • Protein kinase C-mediated phosphorylation and functional regulation of dopamine transporters in striatal synaptosomes
    • R.A. Vaughan, R.A. Huff, G.R. Uhl, and M.J. Kuhar Protein kinase C-mediated phosphorylation and functional regulation of dopamine transporters in striatal synaptosomes J. Biol. Chem. 272 1997 15541 15546
    • (1997) J. Biol. Chem. , vol.272 , pp. 15541-15546
    • Vaughan, R.A.1    Huff, R.A.2    Uhl, G.R.3    Kuhar, M.J.4
  • 65
    • 0029816108 scopus 로고    scopus 로고
    • Dopamine transporter ligand binding domains. Structural and functional properties revealed by limited proteolysis
    • R.A. Vaughan, and M.J. Kuhar Dopamine transporter ligand binding domains. Structural and functional properties revealed by limited proteolysis J. Biol. Chem. 271 1996 21672 21680
    • (1996) J. Biol. Chem. , vol.271 , pp. 21672-21680
    • Vaughan, R.A.1    Kuhar, M.J.2
  • 67
    • 84862790971 scopus 로고    scopus 로고
    • Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context
    • H. Wang, J. Elferich, and E. Gouaux Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context Nat. Struct. Mol. Biol. 19 2012 212 219
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 212-219
    • Wang, H.1    Elferich, J.2    Gouaux, E.3
  • 70
    • 84878850253 scopus 로고    scopus 로고
    • The role of cysteines and histidins of the norepinephrine transporter
    • B. Wenge, and H. Bonisch The role of cysteines and histidins of the norepinephrine transporter Neurochem. Res. 38 2013 1303 1314
    • (2013) Neurochem. Res. , vol.38 , pp. 1303-1314
    • Wenge, B.1    Bonisch, H.2
  • 71
    • 0031022680 scopus 로고    scopus 로고
    • Binding domains for blockers and substrates on the dopamine transporter in rat striatal membranes studied by protection against N-ethylmaleimide-induced reduction of [3H]WIN 35,428 binding
    • C. Xu, L.L. Coffey, and M.E. Reith Binding domains for blockers and substrates on the dopamine transporter in rat striatal membranes studied by protection against N-ethylmaleimide-induced reduction of [3H]WIN 35,428 binding Naunyn-Schmiedeberg's Arch. Pharmacol. 355 1997 64 73
    • (1997) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.355 , pp. 64-73
    • Xu, C.1    Coffey, L.L.2    Reith, M.E.3
  • 73
    • 67349282342 scopus 로고    scopus 로고
    • Antidepressant specificity of serotonin transporter suggested by three LeuT-SSRI structures
    • Z. Zhou, J. Zhen, N.K. Karpowich, C.J. Law, M.E. Reith, and D.N. Wang Antidepressant specificity of serotonin transporter suggested by three LeuT-SSRI structures Nat. Struct. Mol. Biol. 16 2009 652 657
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 652-657
    • Zhou, Z.1    Zhen, J.2    Karpowich, N.K.3    Law, C.J.4    Reith, M.E.5    Wang, D.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.