메뉴 건너뛰기




Volumn 5 AUG, Issue , 2014, Pages

Understanding transporter specificity and the discrete appearance of channel-like gating domains in transporters

Author keywords

Aspergillus nidulans; Atypical kinetics; Crystal structure; Drug transporters; Endocytosis turnover; Genetic; Model systems

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ALLOPURINOL; AMINO ACID TRANSPORTER; ANTIDEPRESSANT AGENT; ANTIFUNGAL AGENT; ANTINEOPLASTIC AGENT; ANTIPROTOZOAL AGENT; CARRIER PROTEIN; CATECHOLAMINE TRANSPORTER; DIURETIC AGENT; DOPAMINE TRANSPORTER; G PROTEIN COUPLED RECEPTOR; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; MULTIDRUG RESISTANCE PROTEIN; PURINE TRANSPORTER; SEROTONIN TRANSPORTER; SODIUM POTASSIUM CHLORIDE COTRANSPORTER; UNCLASSIFIED DRUG; CARDIAC GLYCOSIDE; GLUCOSE TRANSPORTER; MULTIDRUG RESISTANCE PROTEIN 1; PEPTIDE TRANSPORTER 1; PERMEASE; PROTON PUMP INHIBITOR; SODIUM GLUCOSE COTRANSPORTER 1; SODIUM GLUCOSE COTRANSPORTER 2; SODIUM GLUCOSE COTRANSPORTER 3; URACIL PERMEASE;

EID: 84906512759     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2014.00207     Document Type: Review
Times cited : (53)

References (154)
  • 1
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnov, I., Kasho, V., Verner, G., Kaback, H.R., and Iwata, S. (2003). Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615.
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnov, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 2
    • 4444328639 scopus 로고    scopus 로고
    • Lactose permease as a paradigm for membrane transport proteins
    • Abramson, J., Iwata, S., and Kaback, H.R. (2004) Lactose permease as a paradigm for membrane transport proteins. Mol. Membr. Biol. 21, 227-233.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 227-233
    • Abramson, J.1    Iwata, S.2    Kaback, H.R.3
  • 3
    • 81355128964 scopus 로고    scopus 로고
    • Transporters are an under-developed therapeutic target
    • Alexander, S. (2011). Transporters are an under-developed therapeutic target. Discuss. Br. J. Pharmacol. 164, 1751-1752
    • (2011) Discuss. Br. J. Pharmacol. , vol.164 , pp. 1751-1752
    • Alexander, S.1
  • 4
    • 0037379670 scopus 로고    scopus 로고
    • A Leishmania major nucleobase transporter responsible for allopurinol uptake is a functional homolog of the Trypanosoma brucei H2 transporter
    • Al-Salabi, M.I., L.J. Wallace, and De Koning, H.P. (2003) A Leishmania major nucleobase transporter responsible for allopurinol uptake is a functional homolog of the Trypanosoma brucei H2 transporter. Mol. Pharmacol. 63, 814-820.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 814-820
    • Al-Salabi, M.I.1    Wallace, L.J.2    De Koning, H.P.3
  • 5
    • 24144459588 scopus 로고    scopus 로고
    • Purine nucleobase transport in amastigotes of Leishmania mexicana: involvement in allopurinol uptake
    • Al-Salabi, M.I., and de Koning, H.P. (2005) Purine nucleobase transport in amastigotes of Leishmania mexicana: involvement in allopurinol uptake. Antimicrob. Agents Chemother. 49, 3682-3689.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3682-3689
    • Al-Salabi, M.I.1    de Koning, H.P.2
  • 7
    • 79960915923 scopus 로고    scopus 로고
    • Mutational analysis and modeling reveal functionally critical residues in transmembrane segments 1 and 3 of the UapA transporter
    • Amillis, S., Kosti, V., Pantazopoulou, A., Mikros, E., and Diallinas, G. (2011). Mutational analysis and modeling reveal functionally critical residues in transmembrane segments 1 and 3 of the UapA transporter. J. Mol. Biol. 411, 567-580.
    • (2011) J. Mol. Biol. , vol.411 , pp. 567-580
    • Amillis, S.1    Kosti, V.2    Pantazopoulou, A.3    Mikros, E.4    Diallinas, G.5
  • 8
    • 0035798405 scopus 로고    scopus 로고
    • Substitution F569S converts UapA, a specific uric acid-xanthine transporter, into a broad specificity transporter for purine-related solutes
    • Amillis, S., Koukaki, M., and Diallinas, G. (2001). Substitution F569S converts UapA, a specific uric acid-xanthine transporter, into a broad specificity transporter for purine-related solutes. J. Mol. Biol. 313, 765-774.
    • (2001) J. Mol. Biol. , vol.313 , pp. 765-774
    • Amillis, S.1    Koukaki, M.2    Diallinas, G.3
  • 9
    • 1942487886 scopus 로고    scopus 로고
    • Transcription of purine transporter genes is activated during the isotropic growth phase of Aspergillus nidulans conidia
    • Amillis, S., Cecchetto, G., Sophianopoulou, V., Koukaki, M., Scazzocchio, C., and Diallinas, G. (2004). Transcription of purine transporter genes is activated during the isotropic growth phase of Aspergillus nidulans conidia. Mol. Microbiol. 52, 205-216.
    • (2004) Mol. Microbiol. , vol.52 , pp. 205-216
    • Amillis, S.1    Cecchetto, G.2    Sophianopoulou, V.3    Koukaki, M.4    Scazzocchio, C.5    Diallinas, G.6
  • 10
    • 0016608664 scopus 로고
    • Initiator constitutive mutation with an 'uppromoter' effect in Aspergillus nidulans
    • Arst H.N. Jr., and Scazzocchio, C. (1975) Initiator constitutive mutation with an 'uppromoter' effect in Aspergillus nidulans. Nature 254, 31-34.
    • (1975) Nature , vol.254 , pp. 31-34
    • Arst Jr., H.N.1    Scazzocchio, C.2
  • 11
    • 77954919918 scopus 로고    scopus 로고
    • Targeting drug transporters - combining in silico and in vitro approaches to predict in vivo
    • Bahadduri, P.M., Polli, J.E., Swaan P.W., and Ekins, S. (2010). Targeting drug transporters - combining in silico and in vitro approaches to predict in vivo. Methods Mol. Biol. 637, 65-103.
    • (2010) Methods Mol. Biol. , vol.637 , pp. 65-103
    • Bahadduri, P.M.1    Polli, J.E.2    Swaan, P.W.3    Ekins, S.4
  • 12
    • 77956189075 scopus 로고    scopus 로고
    • Structural perspectives on secondary active transporters
    • Boudker, O., and Verdon, G. (2010). Structural perspectives on secondary active transporters. Trends Pharmacol. Sci. 31, 418-426.
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 418-426
    • Boudker, O.1    Verdon, G.2
  • 13
    • 0035365996 scopus 로고    scopus 로고
    • + with thiodigalactoside
    • + with thiodigalactoside. J. Membr. Biol. 181, 215-224.
    • (2001) J. Membr. Biol. , vol.181 , pp. 215-224
    • Brooker, R.J.1
  • 14
    • 0037593443 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and in situ characterization of the first high affinity nucleobase transporter from a protozoan
    • Burchmore, R.J., Wallace, L.J., Candlish, D., Al-Salabi, M.I., Beal, P.R., Barrett, M.P., Baldwin, S.A., and de Koning, H.P. (2003) Cloning, heterologous expression, and in situ characterization of the first high affinity nucleobase transporter from a protozoan. J. Biol. Chem. 278, 23502-23507.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23502-23507
    • Burchmore, R.J.1    Wallace, L.J.2    Candlish, D.3    Al-Salabi, M.I.4    Beal, P.R.5    Barrett, M.P.6    Baldwin, S.A.7    de Koning, H.P.8
  • 15
    • 79957597366 scopus 로고    scopus 로고
    • Transport activity-dependent intracellular sorting of the yeast general amino acid permease
    • Cain, N.E., and Kaiser, C.A. (2011) Transport activity-dependent intracellular sorting of the yeast general amino acid permease. Mol. Biol. Cell 22, 1919-1929.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1919-1929
    • Cain, N.E.1    Kaiser, C.A.2
  • 16
    • 0033855955 scopus 로고    scopus 로고
    • The conserved motif in hydrophilic loop 2/3 and loop 8/9 of the lactose permease of Escherichia coli Analysis of suppressor mutations
    • Cain, S.M., Matzke, E.A., and Brooker, R.J. (2000). The conserved motif in hydrophilic loop 2/3 and loop 8/9 of the lactose permease of Escherichia coli. Analysis of suppressor mutations. J. Membr Biol. 176, 159-168
    • (2000) J. Membr Biol. , vol.176 , pp. 159-168
    • Cain, S.M.1    Matzke, E.A.2    Brooker, R.J.3
  • 17
    • 41449093586 scopus 로고    scopus 로고
    • Substrate binding and formation of an occluded state in the leucine transporter
    • Celik, L., Schiøtt, B., and Tajkhorshid, E. (2008). Substrate binding and formation of an occluded state in the leucine transporter. Biophys J. 94, 1600-1612.
    • (2008) Biophys J , vol.94 , pp. 1600-1612
    • Celik, L.1    Schiøtt, B.2    Tajkhorshid, E.3
  • 18
    • 0142148146 scopus 로고    scopus 로고
    • Substrate-induced trafficking of the dopamine transporter in heterologously expressing cells and in rat striatal synaptosomal preparations
    • Chi L., and Reith, M.E. (2003). Substrate-induced trafficking of the dopamine transporter in heterologously expressing cells and in rat striatal synaptosomal preparations. J. Pharmacol. Exp. Ther. 307, 729-736.
    • (2003) J. Pharmacol. Exp. Ther. , vol.307 , pp. 729-736
    • Chi, L.1    Reith, M.E.2
  • 19
    • 84895114924 scopus 로고    scopus 로고
    • ABC transporters in multidrug resistance and pharmacokinetics, and strategies for drug development
    • Choi, Y.H., and Yu, A.M. (2014). ABC transporters in multidrug resistance and pharmacokinetics, and strategies for drug development. Curr. Pharm Des. 20, 793-807.
    • (2014) Curr. Pharm Des. , vol.20 , pp. 793-807
    • Choi, Y.H.1    Yu, A.M.2
  • 21
    • 77953024005 scopus 로고    scopus 로고
    • Transporters, channels, or simple diffusion? Dogmas, atypical roles and complexity in transport systems
    • Conde, A., Diallinas, G., Chaumont, F., Chaves, M., and Gerós, H. (2010). Transporters, channels, or simple diffusion? Dogmas, atypical roles and complexity in transport systems. Int. J. Biochem. Cell Biol. 42, 857-868.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 857-868
    • Conde, A.1    Diallinas, G.2    Chaumont, F.3    Chaves, M.4    Gerós, H.5
  • 22
    • 73949133608 scopus 로고    scopus 로고
    • Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats
    • Crisman, T.J,. Qu, S., Kanner, B.I., and Forrest, L.R. (2009). Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats. Proc. Natl. Acad. Sci. U S A. 106, 20752-20757.
    • (2009) Proc. Natl. Acad. Sci. U S A. , vol.106 , pp. 20752-20757
    • Crisman, T.J.1    Qu, S.2    Kanner, B.I.3    Forrest, L.R.4
  • 23
    • 84879420063 scopus 로고    scopus 로고
    • Implications of aberrant temperaturesensitive glucose transport via the glucose transporter deficiency mutant (GLUT1DS) T295M for the alternate-access and fixed-site transport models
    • Cunningham, P., and Naftalin, R.J. (2013). Implications of aberrant temperaturesensitive glucose transport via the glucose transporter deficiency mutant (GLUT1DS) T295M for the alternate-access and fixed-site transport models. J. Membr. Biol. 246, 495-511.
    • (2013) J. Membr. Biol. , vol.246 , pp. 495-511
    • Cunningham, P.1    Naftalin, R.J.2
  • 24
    • 33646836322 scopus 로고    scopus 로고
    • Docking studies show that D-glucose and quercetin slide through the transporter GLUT1
    • Cunningham, P., Afzal-Ahmed, I., and Naftalin, R.J. (2006). Docking studies show that D-glucose and quercetin slide through the transporter GLUT1. J. Biol. Chem. 281, 5797-5780
    • (2006) J. Biol. Chem. , vol.281 , pp. 5780-5797
    • Cunningham, P.1    Afzal-Ahmed, I.2    Naftalin, R.J.3
  • 25
    • 0014064310 scopus 로고
    • Use of analogues and the substratesensitivity of mutants in analysis of purine uptake and breakdown in Aspergillus nidulans
    • Darlington, A.J., and Scazzocchio, C. (1976). Use of analogues and the substratesensitivity of mutants in analysis of purine uptake and breakdown in Aspergillus nidulans. J. Bacteriol. 93(3):937-940.
    • (1976) J. Bacteriol. , vol.93 , Issue.3 , pp. 937-940
    • Darlington, A.J.1    Scazzocchio, C.2
  • 26
    • 0030849192 scopus 로고    scopus 로고
    • Hypoxanthine uptake through a purineselective nucleobase transporter in Trypanosoma brucei brucei procyclic cells is driven by proton motive force
    • de Koning, H.P., and Jarvis, S.M. (1997). Hypoxanthine uptake through a purineselective nucleobase transporter in Trypanosoma brucei brucei procyclic cells is driven by proton motive force, Eur. J. Biochem. 247 1102-1110.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1102-1110
    • de Koning, H.P.1    Jarvis, S.M.2
  • 27
    • 2142660741 scopus 로고    scopus 로고
    • The trypanocide diminazene aceturate is accumulated predominantly through the TbAT1 purine transporter: additional insights on diamidine resistance in african trypanosomes
    • de Koning, H.P., Anderson L.F., Stewart, M., Burchmore, R.J., Wallace, L.J., and Barrett, M.P. (2004). The trypanocide diminazene aceturate is accumulated predominantly through the TbAT1 purine transporter: additional insights on diamidine resistance in african trypanosomes. Antimicrob. Agents Chemother. 48, 1515-1519.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1515-1519
    • de Koning, H.P.1    Anderson, L.F.2    Stewart, M.3    Burchmore, R.J.4    Wallace, L.J.5    Barrett, M.P.6
  • 28
    • 67649437020 scopus 로고    scopus 로고
    • Structure-function relationships in the nucleobase-ascorbate transporter (NAT) family: lessons from model microbial genetic systems
    • Diallinas, G., and Gournas, C. (2008) Structure-function relationships in the nucleobase-ascorbate transporter (NAT) family: lessons from model microbial genetic systems. Channels 2, 363-372.
    • (2008) Channels , vol.2 , pp. 363-372
    • Diallinas, G.1    Gournas, C.2
  • 29
    • 0024676807 scopus 로고
    • A gene coding for the uric acid-xanthine permease of Aspergillus nidulans: inactivational cloning, characterization, and sequence of a cis-acting mutation
    • Diallinas, G., and Scazzocchio, C. (1989). A gene coding for the uric acid-xanthine permease of Aspergillus nidulans: inactivational cloning, characterization, and sequence of a cis-acting mutation. Genetics 122, 341-350.
    • (1989) Genetics , vol.122 , pp. 341-350
    • Diallinas, G.1    Scazzocchio, C.2
  • 30
    • 84881166424 scopus 로고    scopus 로고
    • Allopurinol and xanthine use different translocation mechanisms and trajectories in the fungal UapA transporter
    • Diallinas, G. (2013). Allopurinol and xanthine use different translocation mechanisms and trajectories in the fungal UapA transporter. Biochimie 95, 1755-1764.
    • (2013) Biochimie , vol.95 , pp. 1755-1764
    • Diallinas, G.1
  • 31
    • 58149230945 scopus 로고    scopus 로고
    • Biochemistry. An almost-complete movie
    • Diallinas, G. (2008). Biochemistry. An almost-complete movie. Science 2008 322, 1644-1645.
    • (2008) Science 2008 , vol.322 , pp. 1644-1645
    • Diallinas, G.1
  • 32
    • 77957790538 scopus 로고    scopus 로고
    • Diallinas, G. (2007). Aspergillus transporters. In "The Aspergilli: Genomics, Medicine, Biotechnology and Research Methods", eds. G. Goldman and S. Osmani, CRC press.
    • (2007)
    • Diallinas, G.1
  • 34
    • 69249220125 scopus 로고    scopus 로고
    • Structure of a prokaryotic virtual proton pump at 3.2 A resolution
    • Fang, Y., JayaraL., Wu, F, Williams, C, Xiong Y, and Miller, C. (2009). Structure of a prokaryotic virtual proton pump at 3.2 A resolution. Nature 460, 1040-1043.
    • (2009) Nature , vol.460 , pp. 1040-1043
    • Fang, Y.1    Jayara, L.2    Wu, F.3    Williams, C.4    Xiong, Y.5    Miller, C.6
  • 35
    • 73949083478 scopus 로고    scopus 로고
    • The rocking bundle: a mechanism for ioncoupled solute flux by symmetrical transporters
    • Forrest, L.R., and Rudnick, G. (2009). The rocking bundle: a mechanism for ioncoupled solute flux by symmetrical transporters. Physiology 24, 377-386
    • (2009) Physiology , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 36
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • Forrest, L.R., Krämer, R., and Ziegler, C. (2011). The structural basis of secondary active transport mechanisms. Biochim. Biophys. Acta 1807, 167-188.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Krämer, R.2    Ziegler, C.3
  • 37
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins
    • Frillingos, S., Sahin-Tóth M., Wu, J., and Kaback, H.R. (1998). Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins. FASEB J. 12, 1281-1299.
    • (1998) FASEB J , vol.12 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Tóth, M.2    Wu, J.3    Kaback, H.R.4
  • 38
    • 84867547605 scopus 로고    scopus 로고
    • Insights to the evolution of Nucleobase-Ascorbate Transporters (NAT/NCS2 family) from the Cys-scanning analysis of xanthine permease XanQ
    • Frillingos, S. (2012) Insights to the evolution of Nucleobase-Ascorbate Transporters (NAT/NCS2 family) from the Cys-scanning analysis of xanthine permease XanQ. Int J. Biochem. Mol. Biol. 3, 250-272.
    • (2012) Int J. Biochem. Mol. Biol. , vol.3 , pp. 250-272
    • Frillingos, S.1
  • 40
    • 67649200539 scopus 로고    scopus 로고
    • Structure and mechanism of an amino acid antiporter
    • Gao, X., Lu, F., Zhou, L., Dang, S., Sun, L., Li, X., Wang, J., and Shi, Y. (2009). Structure and mechanism of an amino acid antiporter. Science 324, 1565-1568.
    • (2009) Science , vol.324 , pp. 1565-1568
    • Gao, X.1    Lu, F.2    Zhou, L.3    Dang, S.4    Sun, L.5    Li, X.6    Wang, J.7    Shi, Y.8
  • 41
    • 77953482526 scopus 로고    scopus 로고
    • Purine substrate recognition by the nucleobase-ascorbate transporter signature motif in the YgfO xanthine permease: ASN-325 binds and ALA-323 senses substrate
    • Georgopoulou, E., Mermelekas, G., Karena, E., and Frillingos, S. (2010) Purine substrate recognition by the nucleobase-ascorbate transporter signature motif in the YgfO xanthine permease: ASN-325 binds and ALA-323 senses substrate. J. Biol. Chem. 285, 19422-19433.
    • (2010) J. Biol. Chem. , vol.285 , pp. 19422-19433
    • Georgopoulou, E.1    Mermelekas, G.2    Karena, E.3    Frillingos, S.4
  • 44
    • 0027490676 scopus 로고
    • Sequence and regulation of the uapA gene encoding a uric acid-xanthine permease in the fungus Aspergillus nidulans
    • Gorfinkiel, L, Diallinas G, and Scazzocchio, C. (1993). Sequence and regulation of the uapA gene encoding a uric acid-xanthine permease in the fungus Aspergillus nidulans. J. Biol. Chem. 268, 23376-23381.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23376-23381
    • Gorfinkiel, L.1    Diallinas, G.2    Scazzocchio, C.3
  • 45
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • Gouaux, E., and Mackinnon, R. (2005). Principles of selective ion transport in channels and pumps. Science 310, 1461-1465.
    • (2005) Science , vol.310 , pp. 1461-1465
    • Gouaux, E.1    Mackinnon, R.2
  • 46
    • 39749203097 scopus 로고    scopus 로고
    • Characterization and kinetics of the major purine transporters in Aspergillus fumigatus
    • Goudela, S., Reichard, U., Amillis, S., and Diallinas, G. (2008). Characterization and kinetics of the major purine transporters in Aspergillus fumigatus. Fungal Genet. Biol. 45, 459-472.
    • (2008) Fungal Genet. Biol. , vol.45 , pp. 459-472
    • Goudela, S.1    Reichard, U.2    Amillis, S.3    Diallinas, G.4
  • 47
    • 33750475581 scopus 로고    scopus 로고
    • Comparative kinetic analysis of AzgA and Fcy21p, prototypes of the two major fungal hypoxanthine-adenineguanine transporter families
    • Goudela, S, Tsilivi, H, and Diallinas, G. (2006). Comparative kinetic analysis of AzgA and Fcy21p, prototypes of the two major fungal hypoxanthine-adenineguanine transporter families. Mol. Membr. Biol. 23, 291-303.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 291-303
    • Goudela, S.1    Tsilivi, H.2    Diallinas, G.3
  • 48
    • 20444437463 scopus 로고    scopus 로고
    • Comparative substrate recognition by bacterial and fungal purine transporters of the NAT/NCS2 family
    • Goudela, S., Karatza P., Koukaki, M., Frillingos, S., and Diallinas, G. (2005). Comparative substrate recognition by bacterial and fungal purine transporters of the NAT/NCS2 family. Mol. Membr. Biol. 22, 263-275.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 263-275
    • Goudela, S.1    Karatza, P.2    Koukaki, M.3    Frillingos, S.4    Diallinas, G.5
  • 49
    • 42149085549 scopus 로고    scopus 로고
    • The nucleobase-ascorbate transporter (NAT) family: genomics, evolution, structure-function relationships and physiological role
    • Gournas, C., Papageorgiou I., and Diallinas, G. (2008). The nucleobase-ascorbate transporter (NAT) family: genomics, evolution, structure-function relationships and physiological role. Mol. Biosyst. 4, 404-416.
    • (2008) Mol. Biosyst. , vol.4 , pp. 404-416
    • Gournas, C.1    Papageorgiou, I.2    Diallinas, G.3
  • 50
    • 72949088410 scopus 로고    scopus 로고
    • Transport-dependent endocytosis and turnover of a uric acid-xanthine permease
    • Gournas, C., Amillis, S., Vlanti, A., and Diallinas, G. (2010). Transport-dependent endocytosis and turnover of a uric acid-xanthine permease. Mol. Microbiol. 75, 246-260.
    • (2010) Mol. Microbiol. , vol.75 , pp. 246-260
    • Gournas, C.1    Amillis, S.2    Vlanti, A.3    Diallinas, G.4
  • 51
    • 0141456376 scopus 로고    scopus 로고
    • Evidence for structural symmetry and functional asymmetry in the lactose permease of Escherichia coli
    • Green, A.L., Hrodey, H.A., and Brooker, R.J. (2003). Evidence for structural symmetry and functional asymmetry in the lactose permease of Escherichia coli. Biochemistry 42, 11226-11233.
    • (2003) Biochemistry , vol.42 , pp. 11226-11233
    • Green, A.L.1    Hrodey, H.A.2    Brooker, R.J.3
  • 52
    • 72649091578 scopus 로고    scopus 로고
    • Targeting receptors, transporters and site of absorption to improve oral drug delivery
    • Hamman, J.H., Demana, P.H., and Olivier, E. (2007). Targeting receptors, transporters and site of absorption to improve oral drug delivery. Drug Target Insights. 2, 71-81.
    • (2007) Drug Target Insights , vol.2 , pp. 71-81
    • Hamman, J.H.1    Demana, P.H.2    Olivier, E.3
  • 53
    • 65249139907 scopus 로고    scopus 로고
    • Analysis and update of the human solute carrier (SLC) gene superfamily
    • He, L., Vasiliou, K., and Nebert, D.W. (2009). Analysis and update of the human solute carrier (SLC) gene superfamily. Hum. Genomics 3, 195-206.
    • (2009) Hum. Genomics , vol.3 , pp. 195-206
    • He, L.1    Vasiliou, K.2    Nebert, D.W.3
  • 54
    • 72849115627 scopus 로고    scopus 로고
    • The International Transporter Consortium: a collaborative group of scientists from academia, industry, and the FDA
    • Huang, S.M., Zhang, L., and Giacomini, K.M. (2010). The International Transporter Consortium: a collaborative group of scientists from academia, industry, and the FDA. Clin. Pharmacol. Ther. 87, 32-36.
    • (2010) Clin. Pharmacol. Ther. , vol.87 , pp. 32-36
    • Huang, S.M.1    Zhang, L.2    Giacomini, K.M.3
  • 55
    • 84867600078 scopus 로고    scopus 로고
    • Borrelia burgdorferi harbors a transport system essential for purine salvage and mammalian infection
    • Jain, S., Sutchu, S., Rosa, P.A., Byram, R., and Jewett, M.W. (2012). Borrelia burgdorferi harbors a transport system essential for purine salvage and mammalian infection. Infect. Immun. 80, 3086-3093.
    • (2012) Infect. Immun. , vol.80 , pp. 3086-3093
    • Jain, S.1    Sutchu, S.2    Rosa, P.A.3    Byram, R.4    Jewett, M.W.5
  • 57
    • 77953657278 scopus 로고    scopus 로고
    • Trivalent arsenicals and glucose use different translocation pathways in mammalian GLUT1
    • Jiang, X., McDermott, J.R., Ajees, A.A., Rosen, B.P., and Liu, Z. (2010). Trivalent arsenicals and glucose use different translocation pathways in mammalian GLUT1. Metallomics 2, 211-219.
    • (2010) Metallomics , vol.2 , pp. 211-219
    • Jiang, X.1    McDermott, J.R.2    Ajees, A.A.3    Rosen, B.P.4    Liu, Z.5
  • 60
    • 0031398840 scopus 로고    scopus 로고
    • From membrane to molecule to the third amino acid from the left with a membrane transport protein
    • Kaback, HR, and Wu, J. (1997). From membrane to molecule to the third amino acid from the left with a membrane transport protein. Q. Rev. Biophys. 30, 333-364.
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 333-364
    • Kaback, H.R.1    Wu, J.2
  • 63
    • 79955662093 scopus 로고    scopus 로고
    • The alternating access transport mechanism in LacY
    • Kaback, H.R., Smirnova, I., Kasho, V., Nie, Y., and Zhou, Y. (2011). The alternating access transport mechanism in LacY. Membr. Biol. 239, 85-93.
    • (2011) Membr. Biol. , vol.239 , pp. 85-93
    • Kaback, H.R.1    Smirnova, I.2    Kasho, V.3    Nie, Y.4    Zhou, Y.5
  • 64
    • 0030769787 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: the lactose permease of Escherichia coli
    • Kaback, H.R., Voss, J., and Wu, J. (1997). Helix packing in polytopic membrane proteins: the lactose permease of Escherichia coli. Curr. Opin. Struct. Biol. 7, 537-542.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 537-542
    • Kaback, H.R.1    Voss, J.2    Wu, J.3
  • 65
    • 84876165804 scopus 로고    scopus 로고
    • The arrestin-like protein ArtA is essential for ubiquitination and endocytosis of the UapA transporter in response to both broad-range and specific signals
    • Karachaliou, M., Amillis, S., Evangelinos, M., Kokotos, A.C., Yalelis V., and Diallinas, G. (2013). The arrestin-like protein ArtA is essential for ubiquitination and endocytosis of the UapA transporter in response to both broad-range and specific signals. Mol. Microbiol. 88, 301-317.
    • (2013) Mol. Microbiol. , vol.88 , pp. 301-317
    • Karachaliou, M.1    Amillis, S.2    Evangelinos, M.3    Kokotos, A.C.4    Yalelis, V.5    Diallinas, G.6
  • 66
    • 33845966781 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential, and Ile-329-Val-339 form an alpha-helix
    • Karatza P., Panos, P., Georgopoulou, E., and Frillingos, S. (2006). Cysteine-scanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential, and Ile-329-Val-339 form an alpha-helix. J. Biol. Chem. 281, 39881-39890.
    • (2006) J. Biol. Chem. , vol.281 , pp. 39881-39890
    • Karatza, P.1    Panos, P.2    Georgopoulou, E.3    Frillingos, S.4
  • 67
    • 80655144745 scopus 로고    scopus 로고
    • The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli
    • Karena, E., Frillingos, S. (2011). The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli. J. Biol. Chem. 286, 39595-39605.
    • (2011) J. Biol. Chem. , vol.286 , pp. 39595-39605
    • Karena, E.1    Frillingos, S.2
  • 68
    • 69949131591 scopus 로고    scopus 로고
    • Role of intramembrane polar residues in the YgfO xanthine permease: HIS-31 and ASN-93 are crucial for affinity and specificity, and ASP-304 and GLU-272 are irreplaceable
    • Karena E., and Frillingos, S. (2009). Role of intramembrane polar residues in the YgfO xanthine permease: HIS-31 and ASN-93 are crucial for affinity and specificity, and ASP-304 and GLU-272 are irreplaceable. J. Biol. Chem. 284, 24257-24268.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24257-24268
    • Karena, E.1    Frillingos, S.2
  • 69
    • 84874688353 scopus 로고    scopus 로고
    • The promiscuous binding of pharmaceutical drugs and their transporter-mediated uptake into cells: what we (need to) know and how we can do so
    • Kell, D.B., Dobson, P.D., Bilsland, E., and Oliver, S.G. (2013). The promiscuous binding of pharmaceutical drugs and their transporter-mediated uptake into cells: what we (need to) know and how we can do so. Drug Discov. Today. 18, 218-239.
    • (2013) Drug Discov. Today. , vol.18 , pp. 218-239
    • Kell, D.B.1    Dobson, P.D.2    Bilsland, E.3    Oliver, S.G.4
  • 70
    • 80051666394 scopus 로고    scopus 로고
    • Pharmaceutical drug transport: the issues and the implications that it is essentially carrier-mediated only
    • Kell, D.B., Dobson, P.D., and Oliver, S.G. (2011). Pharmaceutical drug transport: the issues and the implications that it is essentially carrier-mediated only. Drug Discov. Today. 16, 704-714.
    • (2011) Drug Discov. Today. , vol.16 , pp. 704-714
    • Kell, D.B.1    Dobson, P.D.2    Oliver, S.G.3
  • 72
    • 84876086941 scopus 로고    scopus 로고
    • Heterologous expression of Candida albicans Pma1p in Saccharomyces cerevisiae
    • Keniya, M.V., Cannon, R.D., Nguyễn, Â., Tyndall, J.D., and Monk, B.C. (2013). Heterologous expression of Candida albicans Pma1p in Saccharomyces cerevisiae. FEMS Yeast Res. 13, 302-311.
    • (2013) FEMS Yeast Res , vol.13 , pp. 302-311
    • Keniya, M.V.1    Cannon, R.D.2    Nguyễn, Â.3    Tyndall, J.D.4    Monk, B.C.5
  • 73
    • 84864353522 scopus 로고    scopus 로고
    • Identification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) family
    • Kosti, V., Lambrinidis, G., Myrianthopoulos, V., Diallinas, G., and Mikros, E. (2012). Identification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) family. PLoS One 7, e41939.
    • (2012) PLoS One , vol.7
    • Kosti, V.1    Lambrinidis, G.2    Myrianthopoulos, V.3    Diallinas, G.4    Mikros, E.5
  • 74
    • 77950519435 scopus 로고    scopus 로고
    • Dynamic elements at both cytoplasmically and extracellularly facing sides of the UapA transporter selectively control the accessibility of substrates to their translocation pathway
    • Kosti, V., Papageorgiou I., and Diallinas, G. (2010). Dynamic elements at both cytoplasmically and extracellularly facing sides of the UapA transporter selectively control the accessibility of substrates to their translocation pathway. J. Mol. Biol. 397, 1132-1143.
    • (2010) J. Mol. Biol. , vol.397 , pp. 1132-1143
    • Kosti, V.1    Papageorgiou, I.2    Diallinas, G.3
  • 75
    • 20444448199 scopus 로고    scopus 로고
    • The nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway
    • Koukaki, M., Vlanti A., Goudela, S., Pantazopoulou, A., Gioule, H., Tournaviti, S., and Diallinas, G. (2005). The nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway. J. Mol. Biol. 350, 499-513.
    • (2005) J. Mol. Biol. , vol.350 , pp. 499-513
    • Koukaki, M.1    Vlanti, A.2    Goudela, S.3    Pantazopoulou, A.4    Gioule, H.5    Tournaviti, S.6    Diallinas, G.7
  • 76
    • 66249098083 scopus 로고    scopus 로고
    • Unlocking the molecular secrets of sodium-coupled transporters
    • Krishnamurthy, H., Piscitelli, C.L., and Gouaux, E. (2009). Unlocking the molecular secrets of sodium-coupled transporters. Nature 459, 347-355.
    • (2009) Nature , vol.459 , pp. 347-355
    • Krishnamurthy, H.1    Piscitelli, C.L.2    Gouaux, E.3
  • 77
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • Krishnamurthy, H., and Gouaux, E. (2012). X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481, 469-744.
    • (2012) Nature , vol.481 , pp. 469-744
    • Krishnamurthy, H.1    Gouaux, E.2
  • 78
    • 84892484643 scopus 로고    scopus 로고
    • Transport assays in filamentous fungi: kinetic characterization of the UapC purine transporter of Aspergillus nidulans
    • Krypotou, E., and Diallinas, G. (2014). Transport assays in filamentous fungi: kinetic characterization of the UapC purine transporter of Aspergillus nidulans. Fungal Genet. Biol. 63, 1-8.
    • (2014) Fungal Genet. Biol. , vol.63 , pp. 1-8
    • Krypotou, E.1    Diallinas, G.2
  • 79
    • 84903380425 scopus 로고    scopus 로고
    • Modelling, substrate docking and mutational analysis identify residues essential for function and specificity of the major fungal purine transporter AzgA
    • In press, doi:10.1111/mmi.12646
    • Krypotou, E., Lambrinidis, G., Evangelidis, T., Mikros, E., and Diallinas, G.(2014). Modelling, substrate docking and mutational analysis identify residues essential for function and specificity of the major fungal purine transporter AzgA. Mol. Microbiol. In press, doi: 10.1111/mmi.12646.
    • (2014) Mol. Microbiol.
    • Krypotou, E.1    Lambrinidis, G.2    Evangelidis, T.3    Mikros, E.4    Diallinas, G.5
  • 81
    • 80054813491 scopus 로고    scopus 로고
    • Genome-wide assessment of the carriers involved in the cellular uptake of drugs: a model system in yeast
    • Lanthaler, K., Bilsland, E., Dobson P.D., Moss, H.J., Pir, P., Kell, D.B., and Oliver, S.G. (2011). Genome-wide assessment of the carriers involved in the cellular uptake of drugs: a model system in yeast. BMC Biol. 9, 70.
    • (2011) BMC Biol , vol.9 , pp. 70
    • Lanthaler, K.1    Bilsland, E.2    Dobson, P.D.3    Moss, H.J.4    Pir, P.5    Kell, D.B.6    Oliver, S.G.7
  • 82
    • 0018070089 scopus 로고
    • The genetic control of the molybdoflavoproteins in Aspergillus nidulans IV. A comparison between purine hydroxylase I and II
    • Lewis, N.J, Hurt, P., Sealy-Lewis, H.M., Scazzocchio, C. (1978). The genetic control of the molybdoflavoproteins in Aspergillus nidulans. IV. A comparison between purine hydroxylase I and II. Eur. J. Biochem. 91, 311-316.
    • (1978) Eur. J. Biochem. , vol.91 , pp. 311-316
    • Lewis, N.J.1    Hurt, P.2    Sealy-Lewis, H.M.3    Scazzocchio, C.4
  • 83
    • 55549102963 scopus 로고    scopus 로고
    • Arrestinrelated ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • Lin, C.H., MacGurn, J.A., Chu, T., Stefan, C.J., and Emr, S.D. (2008). Arrestinrelated ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135, 714-725
    • (2008) Cell , vol.135 , pp. 714-725
    • Lin, C.H.1    MacGurn, J.A.2    Chu, T.3    Stefan, C.J.4    Emr, S.D.5
  • 84
    • 84860836541 scopus 로고    scopus 로고
    • Regulation of uric acid excretion by the kidney
    • Lipkowitz, M.S. (2012). Regulation of uric acid excretion by the kidney. Curr. Rheumatol. Rep. 14, 179-188.
    • (2012) Curr. Rheumatol. Rep. , vol.14 , pp. 179-188
    • Lipkowitz, M.S.1
  • 85
    • 34548546480 scopus 로고    scopus 로고
    • Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase
    • Liu, J., Sitaram, A., and Burd, C.G. (2007). Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase Traffic 8, 1375-1384.
    • (2007) Traffic , vol.8 , pp. 1375-1384
    • Liu, J.1    Sitaram, A.2    Burd, C.G.3
  • 87
    • 84868095500 scopus 로고    scopus 로고
    • Apo-intermediate in the transport cycle of lactose permease (LacY)
    • Madej, M.G., Soro, S.N., and Kaback, H.R. (2012). Apo-intermediate in the transport cycle of lactose permease (LacY). Proc. Natl. Acad. Sci. USA 109, E2970- E2978.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Madej, M.G.1    Soro, S.N.2    Kaback, H.R.3
  • 89
    • 0034105567 scopus 로고    scopus 로고
    • Amino acid residues N450 and Q449 are critical for the uptake capacity and specificity of UapA, a prototype of a nucleobase-ascorbate transporter family
    • Meintanis, C., Karagouni, A.D., and Diallinas, G. (2000). Amino acid residues N450 and Q449 are critical for the uptake capacity and specificity of UapA, a prototype of a nucleobase-ascorbate transporter family. Mol. Membr. Biol. 17, 47-57.
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 47-57
    • Meintanis, C.1    Karagouni, A.D.2    Diallinas, G.3
  • 90
    • 6944247728 scopus 로고    scopus 로고
    • Neurotransmitter transporter trafficking: endocytosis, recycling, and regulation
    • Melikian, H.E. (2004). Neurotransmitter transporter trafficking: endocytosis, recycling, and regulation. Pharmacol. Ther. 104, 17-27
    • (2004) Pharmacol. Ther. , vol.104 , pp. 17-27
    • Melikian, H.E.1
  • 91
    • 78049395093 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of helices TM8, TM9a, and TM9b and intervening loops in the YgfO xanthine permease: a carboxyl group is essential at ASP-276
    • Mermelekas, G., Georgopoulou, E., Kallis, A., Botou, M., Vlantos, V., and Frillingos, S. (2010). Cysteine-scanning analysis of helices TM8, TM9a, and TM9b and intervening loops in the YgfO xanthine permease: a carboxyl group is essential at ASP-276. J. Biol. Chem. 285, 35011-35020.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35011-35020
    • Mermelekas, G.1    Georgopoulou, E.2    Kallis, A.3    Botou, M.4    Vlantos, V.5    Frillingos, S.6
  • 92
    • 34347401218 scopus 로고    scopus 로고
    • Regulation of receptors and transporters by ubiquitination: new insights into surprisingly similar mechanisms
    • Miranda, M., and Sorkin, A. (2007). Regulation of receptors and transporters by ubiquitination: new insights into surprisingly similar mechanisms. Mol. Interv. 7, 157-167.
    • (2007) Mol. Interv. , vol.7 , pp. 157-167
    • Miranda, M.1    Sorkin, A.2
  • 93
    • 34247579197 scopus 로고    scopus 로고
    • Chemotherapy of leishmaniasis: past, present and future
    • Mishra, J., Saxena, A., and Singh, S. (2007). Chemotherapy of leishmaniasis: past, present and future. Curr. Med. Chem. 14, 1153-1169.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1153-1169
    • Mishra, J.1    Saxena, A.2    Singh, S.3
  • 94
    • 0042468096 scopus 로고    scopus 로고
    • Impact of drug transporter studies on drug discovery and development
    • Mizuno, N., Niwa, T., Yotsumoto, Y., Sugiyama, Y. (2003). Impact of drug transporter studies on drug discovery and development. Pharmacol. Rev. 55, 425-461.
    • (2003) Pharmacol. Rev. , vol.55 , pp. 425-461
    • Mizuno, N.1    Niwa, T.2    Yotsumoto, Y.3    Sugiyama, Y.4
  • 95
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami, S., Nakashima, R., Yamashita, E., Yamaguchi, A. (2002). Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419, 587-593.
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 96
    • 77952243804 scopus 로고    scopus 로고
    • Reassessment of models of facilitated transport and cotransport
    • Naftalin, R.J. (2010). Reassessment of models of facilitated transport and cotransport. J. Membr. Biol. 234, 75-112.
    • (2010) J. Membr. Biol. , vol.234 , pp. 75-112
    • Naftalin, R.J.1
  • 97
    • 57649114095 scopus 로고    scopus 로고
    • Alternating carrier models of asymmetric glucose transport violate the energy conservation laws
    • Naftalin, R.J. (2008). Alternating carrier models of asymmetric glucose transport violate the energy conservation laws. Biophys. J. 95, 4300-4314.
    • (2008) Biophys. J. , vol.95 , pp. 4300-4314
    • Naftalin, R.J.1
  • 98
    • 0030805221 scopus 로고    scopus 로고
    • Carrier-mediated transport of oligopeptides in the human fibrosarcoma cell line HT1080
    • Nakanishi, T., Tamai, I., Sai, Y., Sasaki, T., and Tsuji, A. (1997). Carrier-mediated transport of oligopeptides in the human fibrosarcoma cell line HT1080. Cancer Res. 57, 4118-4122.
    • (1997) Cancer Res , vol.57 , pp. 4118-4122
    • Nakanishi, T.1    Tamai, I.2    Sai, Y.3    Sasaki, T.4    Tsuji, A.5
  • 99
    • 0033813664 scopus 로고    scopus 로고
    • Cancer cell-targeted drug delivery utilizing oligopeptide transport activity
    • Nakanishi, T., Tamai, I., Takaki, A., and Tsuji, A. (2000). Cancer cell-targeted drug delivery utilizing oligopeptide transport activity. Int. J. Cancer 88, 274-280.
    • (2000) Int. J. Cancer , vol.88 , pp. 274-280
    • Nakanishi, T.1    Tamai, I.2    Takaki, A.3    Tsuji, A.4
  • 100
    • 14744270896 scopus 로고    scopus 로고
    • Trypanosoma brucei: expression of multiple purine transporters prevents the development of allopurinol resistance
    • Natto, M.J., Wallace, L.J., Candlish, D., Al-Salabi, M.I., Coutts, S.E., and de Koning, H.P. (2005) Trypanosoma brucei: expression of multiple purine transporters prevents the development of allopurinol resistance. Exp. Parasitol. 109 80-86.
    • (2005) Exp. Parasitol. , vol.109 , pp. 80-86
    • Natto, M.J.1    Wallace, L.J.2    Candlish, D.3    Al-Salabi, M.I.4    Coutts, S.E.5    de Koning, H.P.6
  • 103
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • Nikko, E., and Pelham, H.R. (2009). Arrestin-mediated endocytosis of yeast plasma membrane transporters. Traffic 10, 1856-1867.
    • (2009) Traffic , vol.10 , pp. 1856-1867
    • Nikko, E.1    Pelham, H.R.2
  • 104
    • 57049101734 scopus 로고    scopus 로고
    • Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
    • Nikko, E, Sullivan, JA, and Pelham, H.R. (2008). Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1. EMBO Rep. 9, 1216-1221.
    • (2008) EMBO Rep , vol.9 , pp. 1216-1221
    • Nikko, E.1    Sullivan, J.A.2    Pelham, H.R.3
  • 106
    • 80054771982 scopus 로고    scopus 로고
    • Substrate-induced internalization of the high-affinity choline transporter
    • Okuda, T., Konishi, A., Misawa H., and Haga, T. (2011). Substrate-induced internalization of the high-affinity choline transporter. J. Neurosci. 31, 14989-14997.
    • (2011) J. Neurosci. , vol.31 , pp. 14989-14997
    • Okuda, T.1    Konishi, A.2    Misawa, H.3    Haga, T.4
  • 107
    • 84871313471 scopus 로고    scopus 로고
    • Functional consequences of sulfhydryl modification of the γ-aminobutyric acid transporter 1 at a single solvent-exposed cysteine residue
    • Omoto, J.J., Maestas, M.J., Rahnama-Vaghef, A., Choi, Y.E., Salto, G. Jr., Sanchez, R.V., Anderson, C.M., and Eskandari, S. (2012). Functional consequences of sulfhydryl modification of the γ-aminobutyric acid transporter 1 at a single solvent-exposed cysteine residue. J. Membr. Biol. 245, 841-857.
    • (2012) J. Membr. Biol. , vol.245 , pp. 841-857
    • Omoto, J.J.1    Maestas, M.J.2    Rahnama-Vaghef, A.3    Choi, Y.E.4    Salto Jr., G.5    Sanchez, R.V.6    Anderson, C.M.7    Eskandari, S.8
  • 109
    • 33644631485 scopus 로고    scopus 로고
    • Therapeutic effects of xanthine oxidase inhibitors: renaissance half a century after the discovery of allopurinol
    • Pacher, P., Nivorozhkin, A., and Szabó, C. (2006). Therapeutic effects of xanthine oxidase inhibitors: renaissance half a century after the discovery of allopurinol. Pharmacol. Rev. 58, 87-114.
    • (2006) Pharmacol. Rev. , vol.58 , pp. 87-114
    • Pacher, P.1    Nivorozhkin, A.2    Szabó, C.3
  • 111
    • 51349162011 scopus 로고    scopus 로고
    • Specific interdomain synergy in the UapA transporter determines its unique specificity for uric acid among NAT carriers
    • Papageorgiou, I., Gournas, C., Vlanti, A., Amillis, S., Pantazopoulou, A., and Diallinas, G. (2008a). Specific interdomain synergy in the UapA transporter determines its unique specificity for uric acid among NAT carriers. J. Mol Biol. 382, 1121-1135.
    • (2008) J. Mol Biol. , vol.382 , pp. 1121-1135
    • Papageorgiou, I.1    Gournas, C.2    Vlanti, A.3    Amillis, S.4    Pantazopoulou, A.5    Diallinas, G.6
  • 112
    • 41549100692 scopus 로고    scopus 로고
    • Kinetic and mutational analysis of the Trypanosoma brucei NBT1 nucleobase transporter expressed in Saccharomyces cerevisiae reveals structural similarities between ENT and MFS transporters
    • Papageorgiou, I., De Koning, H.P., Soteriadou, K., and Diallinas, G. (2008b). Kinetic and mutational analysis of the Trypanosoma brucei NBT1 nucleobase transporter expressed in Saccharomyces cerevisiae reveals structural similarities between ENT and MFS transporters. Int. J. Parasitol. 38, 641-653.
    • (2008) Int. J. Parasitol. , vol.38 , pp. 641-653
    • Papageorgiou, I.1    De Koning, H.P.2    Soteriadou, K.3    Diallinas, G.4
  • 113
    • 46649112362 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: ILE-432 and ASN-430 are important
    • Papakostas, K., Georgopoulou, E., and Frillingos, S. (2008). Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: ILE-432 and ASN-430 are important. J. Biol. Chem. 283, 13666-13678.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13666-13678
    • Papakostas, K.1    Georgopoulou, E.2    Frillingos, S.3
  • 114
    • 84901064632 scopus 로고    scopus 로고
    • Multidrug resistance in fungi: regulation of transporter-encoding gene expression
    • Paul, S., and Moye-Rowley, W.S. (2014). Multidrug resistance in fungi: regulation of transporter-encoding gene expression. Front Physiol. 5, 143.
    • (2014) Front Physiol , vol.5 , pp. 143
    • Paul, S.1    Moye-Rowley, W.S.2
  • 115
    • 84894830041 scopus 로고    scopus 로고
    • How LeuT shapes our understanding of the mechanisms of sodium-coupled neurotransmitter transporters
    • Penmatsa, A., and Gouaux, E. (2014). How LeuT shapes our understanding of the mechanisms of sodium-coupled neurotransmitter transporters. J. Physiol. 592, 863-869.
    • (2014) J. Physiol , vol.592 , pp. 863-869
    • Penmatsa, A.1    Gouaux, E.2
  • 116
    • 78650817193 scopus 로고    scopus 로고
    • Neurotransmitter/sodium symporter orthologue LeuT has a single high-affinity substrate site
    • Piscitelli, C.L., Krishnamurthy, H., and Gouaux, E. (2010). Neurotransmitter/sodium symporter orthologue LeuT has a single high-affinity substrate site. Nature 468, 1129-11232.
    • (2010) Nature , vol.468 , pp. 1129-11232
    • Piscitelli, C.L.1    Krishnamurthy, H.2    Gouaux, E.3
  • 117
    • 84891751622 scopus 로고    scopus 로고
    • The druggable genome: Evaluation of drug targets in clinical trials suggests major shifts in molecular class and indication
    • Rask-Andersen, M., Masuram, S., and Schiöth, H.B. (2014). The druggable genome: Evaluation of drug targets in clinical trials suggests major shifts in molecular class and indication. Annu. Rev. Pharmacol. Toxicol. 54, 9-26.
    • (2014) Annu. Rev. Pharmacol. Toxicol. , vol.54 , pp. 9-26
    • Rask-Andersen, M.1    Masuram, S.2    Schiöth, H.B.3
  • 118
    • 84870165698 scopus 로고    scopus 로고
    • SLC5 and SLC2 transporters in epithelia-cellular role and molecular mechanisms
    • Raja, M., Puntheeranurak, T., Hinterdorfer, P., and Kinne, R. (2012). SLC5 and SLC2 transporters in epithelia-cellular role and molecular mechanisms. Curr. Top. Membr. 70, 29-76.
    • (2012) Curr. Top. Membr. , vol.70 , pp. 29-76
    • Raja, M.1    Puntheeranurak, T.2    Hinterdorfer, P.3    Kinne, R.4
  • 119
    • 0346494926 scopus 로고    scopus 로고
    • TransportDB: A Relational Database of Cellular Membrane Transport Systems
    • Ren, Q., Chen K., and Paulsen, I.T. (2004). TransportDB: A Relational Database of Cellular Membrane Transport Systems. Nucl. Acids Res. 32, D284-D288.
    • (2004) Nucl. Acids Res , vol.32
    • Ren, Q.1    Chen, K.2    Paulsen, I.T.3
  • 120
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • Reyes, N., Ginter, C., and 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
  • 121
    • 51349159616 scopus 로고    scopus 로고
    • Different ubiquitin signals act at the Golgi and plasma membrane to direct GAP1 trafficking
    • Risinger, A.L., and Kaiser, C.A. (2008). Different ubiquitin signals act at the Golgi and plasma membrane to direct GAP1 trafficking. Mol. Biol. Cell. 19, 2962-2972.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 2962-2972
    • Risinger, A.L.1    Kaiser, C.A.2
  • 124
    • 84890736388 scopus 로고    scopus 로고
    • Advances in Pglycoprotein-based approaches for delivering anticancer drugs: pharmacokinetic perspective and clinical relevance
    • Saneja, A., Khare, V., Alam, N., Dubey, R.D. and Gupta, P.N. (2014). Advances in Pglycoprotein-based approaches for delivering anticancer drugs: pharmacokinetic perspective and clinical relevance. Expert Opin. Drug Deliv. 11, 121-138.
    • (2014) Expert Opin. Drug Deliv. , vol.11 , pp. 121-138
    • Saneja, A.1    Khare, V.2    Alam, N.3    Dubey, R.D.4    Gupta, P.N.5
  • 126
    • 0015800425 scopus 로고
    • The genetic control of molybdoflavoproteins in Aspergillus nidulans Allopurinol-resistant mutants constitutive for xanthine-dehydrogenase
    • Scazzocchio, C., Holl, F.B., and Foguelman, A.I. (1973). The genetic control of molybdoflavoproteins in Aspergillus nidulans, Allopurinol-resistant mutants constitutive for xanthine-dehydrogenase. Eur. J. Biochem. 36 428-445.
    • (1973) Eur. J. Biochem. , vol.36 , pp. 428-445
    • Scazzocchio, C.1    Holl, F.B.2    Foguelman, A.I.3
  • 128
    • 84865298889 scopus 로고    scopus 로고
    • Highlights from recently determined structures of membrane proteins: a focus on channels and transporters
    • Sciara, G., and Mancia, F. (2012). Highlights from recently determined structures of membrane proteins: a focus on channels and transporters. Curr. Opin. Struct. Biol. 22, 476-481.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 476-481
    • Sciara, G.1    Mancia, F.2
  • 130
  • 131
    • 44949086583 scopus 로고    scopus 로고
    • The mechanism of a neurotransmitter:sodium symporter--inward release of Na+ and substrate is triggered by substrate in a second binding site
    • Shi, L., Quick, M., Zhao, Y., Weinstein, H., and Javitch, J.A. (2008). The mechanism of a neurotransmitter:sodium symporter--inward release of Na+ and substrate is triggered by substrate in a second binding site. Mol. Cell 30, 667-677.
    • (2008) Mol. Cell , vol.30 , pp. 667-677
    • Shi, L.1    Quick, M.2    Zhao, Y.3    Weinstein, H.4    Javitch, J.A.5
  • 132
    • 84874249804 scopus 로고    scopus 로고
    • Common folds and transport mechanisms of secondary active transporters
    • Shi, Y. (2013). Common folds and transport mechanisms of secondary active transporters. Annu. Rev. Biophys. 42, 51-72.
    • (2013) Annu. Rev. Biophys. , vol.42 , pp. 51-72
    • Shi, Y.1
  • 133
    • 58149233796 scopus 로고    scopus 로고
    • A competitive inhibitor traps LeuT in an open-to-out conformation
    • Singh, S.K., Piscitelli, C.L., Yamashita, A., and Gouaux, E. (2008). A competitive inhibitor traps LeuT in an open-to-out conformation. Science 322, 1655-1661.
    • (2008) Science , vol.322 , pp. 1655-1661
    • Singh, S.K.1    Piscitelli, C.L.2    Yamashita, A.3    Gouaux, E.4
  • 136
    • 84892518651 scopus 로고    scopus 로고
    • Flexible gates generate occluded intermediates in the transport cycle of LacY
    • Stelzl, L.S., Fowler, P.W., Sansom, M.S., and Beckstein, O. (2014). Flexible gates generate occluded intermediates in the transport cycle of LacY. J. Mol. Biol. 426, 735-751.
    • (2014) J. Mol. Biol. , vol.426 , pp. 735-751
    • Stelzl, L.S.1    Fowler, P.W.2    Sansom, M.S.3    Beckstein, O.4
  • 137
    • 34347379169 scopus 로고    scopus 로고
    • Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase rsp5 to membrane proteins in vivo and in vitro
    • Sullivan, J.A., Lewis, M.J., Nikko, E., Pelham, H.R. (2007). Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase rsp5 to membrane proteins in vivo and in vitro. Mol. Biol. Cell, 18, 2429-2440.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2429-2440
    • Sullivan, J.A.1    Lewis, M.J.2    Nikko, E.3    Pelham, H.R.4
  • 138
    • 84908457716 scopus 로고    scopus 로고
    • Bacterial Multidrug Efflux Pumps: Mechanisms, Physiology and Pharmacological Exploitations
    • In press, doi:10.1016/j.bbrc.2014.05.090
    • Sun, J., Deng, Z., and Yan, A. (2014). Bacterial Multidrug Efflux Pumps: Mechanisms, Physiology and Pharmacological Exploitations. Biochem. Biophys Res. Commun. In press, doi: 10.1016/j.bbrc.2014.05.090.
    • (2014) Biochem. Biophys Res. Commun.
    • Sun, J.1    Deng, Z.2    Yan, A.3
  • 140
    • 84937713700 scopus 로고    scopus 로고
    • Structural dynamics of the monoamine transporter homolog LeuT from accelerated conformational sampling and channel analysis
    • In press, doi:10.1002/prot.24588
    • Thomas, J.R., Gedeon, P.C., and Madura, J.D. (2014). Structural dynamics of the monoamine transporter homolog LeuT from accelerated conformational sampling and channel analysis. Proteins 2014. In press, doi: 10.1002/prot.24588.
    • (2014) Proteins , pp. 2014
    • Thomas, J.R.1    Gedeon, P.C.2    Madura, J.D.3
  • 141
    • 84897388135 scopus 로고    scopus 로고
    • Identification of the intracellular gate for a member of the equilibrative nucleoside transporter (ENT) family
    • Valdés, R., Elferich, J., Shinde, U., and Landfear, S.M. (2014). Identification of the intracellular gate for a member of the equilibrative nucleoside transporter (ENT) family. J. Biol. Chem. 289, 8799-8809.
    • (2014) J. Biol. Chem. , vol.289 , pp. 8799-8809
    • Valdés, R.1    Elferich, J.2    Shinde, U.3    Landfear, S.M.4
  • 142
    • 0344873602 scopus 로고    scopus 로고
    • Ammonium-induced internalization of UapC, the general purine permease from Aspergillus nidulans
    • Valdez-Taubas, J., Harispe,.L, Scazzocchio, C., Gorfinkiel, L., Rosa, A.L. (2004). Ammonium-induced internalization of UapC, the general purine permease from Aspergillus nidulans. Fungal Genet. Biol. 41, 42-51.
    • (2004) Fungal Genet. Biol. , vol.41 , pp. 42-51
    • Valdez-Taubas, J.1    Harispe, L.2    Scazzocchio, C.3    Gorfinkiel, L.4    Rosa, A.L.5
  • 143
    • 57749119180 scopus 로고    scopus 로고
    • Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor
    • Van Zeebroeck, G., Bonini, B.M., Versele, M., and Thevelein, J.M. (2009). Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor. Nat. Chem. Biol. 5, 45-52.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 45-52
    • Van Zeebroeck, G.1    Bonini, B.M.2    Versele, M.3    Thevelein, J.M.4
  • 144
    • 84904057061 scopus 로고    scopus 로고
    • Specific analogs uncouple transport, signaling, oligo-ubiquitination and endocytosis in the yeast Gap1 amino acid transceptor
    • In press, doi:10.1111/mmi.12654
    • Van Zeebroeck, G., Rubio-Texeira, M., Schothorst, J., and Thevelein, J.M. (2014). Specific analogs uncouple transport, signaling, oligo-ubiquitination and endocytosis in the yeast Gap1 amino acid transceptor. Mol. Microbiol. In press, doi: 10.1111/mmi.12654
    • (2014) Mol. Microbiol
    • Van Zeebroeck, G.1    Rubio-Texeira, M.2    Schothorst, J.3    Thevelein, J.M.4
  • 145
    • 33644947026 scopus 로고    scopus 로고
    • A novel-type substrateselectivity filter and ER-exit determinants in the UapA purine transporter
    • Vlanti, A., Amillis, S., Koukaki, M., and Diallinas, G. (2006). A novel-type substrateselectivity filter and ER-exit determinants in the UapA purine transporter. J. Mol. Biol. 357, 808-819.
    • (2006) J. Mol. Biol. , vol.357 , pp. 808-819
    • Vlanti, A.1    Amillis, S.2    Koukaki, M.3    Diallinas, G.4
  • 146
    • 84887403382 scopus 로고    scopus 로고
    • Structural basis for action by diverse antidepressants on biogenic amine transporters
    • Wang, H., Goehring, A., Wang, K.H., Penmatsa, A., Ressler, R., and Gouaux, E. (2013). Structural basis for action by diverse antidepressants on biogenic amine transporters. Nature 503, 141-145.
    • (2013) Nature , vol.503 , pp. 141-145
    • Wang, H.1    Goehring, A.2    Wang, K.H.3    Penmatsa, A.4    Ressler, R.5    Gouaux, E.6
  • 148
    • 0035900674 scopus 로고    scopus 로고
    • Substrate-induced regulation of gammaaminobutyric acid transporter trafficking requires tyrosine phosphorylation
    • Whitworth, T.L., and Quick, M.W. (2001). Substrate-induced regulation of gammaaminobutyric acid transporter trafficking requires tyrosine phosphorylation. J. Biol. Chem. 276, 42932-42937.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42932-42937
    • Whitworth, T.L.1    Quick, M.W.2
  • 149
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters
    • Yamashita, A., Singh, S.K., Kawate, T., Jin, Y., and 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
  • 150
    • 67649252642 scopus 로고    scopus 로고
    • Trafficking of dopamine transporters in psychostimulant actions
    • Zahniser, N.R., and Sorkin, A. (2009). Trafficking of dopamine transporters in psychostimulant actions. Semin. Cell Dev. Biol. 20, 411-417.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 411-417
    • Zahniser, N.R.1    Sorkin, A.2
  • 151
    • 84882393631 scopus 로고    scopus 로고
    • Prodrug design targeting intestinal PepT1 for improved oral absorption: design and performance
    • Zhang, Y., Sun, J., Sun, Y., Wang, Y., and He, Z. (2013). Prodrug design targeting intestinal PepT1 for improved oral absorption: design and performance. Curr. Drug Metab. 14, 675-687.
    • (2013) Curr. Drug Metab. , vol.14 , pp. 675-687
    • Zhang, Y.1    Sun, J.2    Sun, Y.3    Wang, Y.4    He, Z.5
  • 152
    • 84887884596 scopus 로고    scopus 로고
    • Combating P-glycoprotein-mediated multidrug resistance using therapeutic nanoparticles
    • Zhang, Q., and Li, F. (2013). Combating P-glycoprotein-mediated multidrug resistance using therapeutic nanoparticles. Curr. Pharm. Des. 19, 6655-6666.
    • (2013) Curr. Pharm. Des , vol.19 , pp. 6655-6666
    • Zhang, Q.1    Li, F.2
  • 153
    • 79952811744 scopus 로고    scopus 로고
    • The role of local hydration and hydrogen-bonding dynamics in ion and solute release from ion-coupled secondary transporters
    • Zhao, C., Noskov, S.Y. (2011). The role of local hydration and hydrogen-bonding dynamics in ion and solute release from ion-coupled secondary transporters. Biochemistry 50, 1848-1856.
    • (2011) Biochemistry , vol.50 , pp. 1848-1856
    • Zhao, C.1    Noskov, S.Y.2
  • 154
    • 84884237765 scopus 로고    scopus 로고
    • Hit identification and optimization in virtual screening: practical recommendations based on a critical literature analysis
    • Zhu, T., Cao, S., Su, P.C., Patel, R., Shah, D., Chokshi, H.B., Szukala, R., Johnson, M.E., Hevener, K.E. (2013). Hit identification and optimization in virtual screening: practical recommendations based on a critical literature analysis. J. Med. Chem. 56, 6560-6572.
    • (2013) J. Med. Chem. , vol.56 , pp. 6560-6572
    • Zhu, T.1    Cao, S.2    Su, P.C.3    Patel, R.4    Shah, D.5    Chokshi, H.B.6    Szukala, R.7    Johnson, M.E.8    Hevener, K.E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.