메뉴 건너뛰기




Volumn 11, Issue 7, 2016, Pages 1908-1916

Inhibitor Discovery for the Human GLUT1 from Homology Modeling and Virtual Screening

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE TRANSPORTER 1; LIGAND; XYLOSE; SLC2A1 PROTEIN, HUMAN;

EID: 84978656625     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00304     Document Type: Article
Times cited : (49)

References (61)
  • 1
    • 0027970863 scopus 로고
    • Glucose transporter proteins in brain
    • Maher, F., Vannucci, S. J., and Simpson, I. A. (1994) Glucose transporter proteins in brain FASEB J. 8, 1003-1011
    • (1994) FASEB J. , vol.8 , pp. 1003-1011
    • Maher, F.1    Vannucci, S.J.2    Simpson, I.A.3
  • 2
    • 0017688926 scopus 로고
    • Reconstitution and purification of the D-glucose transporter from human erythrocytes
    • Kasahara, M. and Hinkle, P. C. (1977) Reconstitution and purification of the D-glucose transporter from human erythrocytes J. Biol. Chem. 252, 7384-7390
    • (1977) J. Biol. Chem. , vol.252 , pp. 7384-7390
    • Kasahara, M.1    Hinkle, P.C.2
  • 3
    • 74949118966 scopus 로고    scopus 로고
    • Glucose transporters in the 21st Century
    • Thorens, B. and Mueckler, M. (2010) Glucose transporters in the 21st Century Am. J. Physiol. Endocrinol. Metab. 298, E141-145 10.1152/ajpendo.00712.2009
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.298 , pp. E141-145
    • Thorens, B.1    Mueckler, M.2
  • 4
    • 84875135352 scopus 로고    scopus 로고
    • The SLC2 (GLUT) family of membrane transporters
    • Mueckler, M. and Thorens, B. (2013) The SLC2 (GLUT) family of membrane transporters Mol. Aspects Med. 34, 121-138 10.1016/j.mam.2012.07.001
    • (2013) Mol. Aspects Med. , vol.34 , pp. 121-138
    • Mueckler, M.1    Thorens, B.2
  • 7
    • 79952216550 scopus 로고    scopus 로고
    • Potential role of sugar transporters in cancer and their relationship with anticancer therapy
    • Calvo, M. B., Figueroa, A., Pulido, E. G., Campelo, R. G., and Aparicio, L. A. (2010) Potential role of sugar transporters in cancer and their relationship with anticancer therapy Int. J. Endocrinol. 2010, 1 10.1155/2010/205357
    • (2010) Int. J. Endocrinol. , vol.2010 , pp. 1
    • Calvo, M.B.1    Figueroa, A.2    Pulido, E.G.3    Campelo, R.G.4    Aparicio, L.A.5
  • 9
    • 85006768050 scopus 로고
    • The metabolism of tumors in the body
    • Warburg, O., Wind, F., and Negelein, E. (1927) The metabolism of tumors in the body J. Gen. Physiol. 8, 519-530 10.1085/jgp.8.6.519
    • (1927) J. Gen. Physiol. , vol.8 , pp. 519-530
    • Warburg, O.1    Wind, F.2    Negelein, E.3
  • 10
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: The metabolic requirements of cell proliferation
    • Vander Heiden, M. G., Cantley, L. C., and Thompson, C. B. (2009) Understanding the Warburg effect: the metabolic requirements of cell proliferation Science 324, 1029-1033 10.1126/science.1160809
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 11
    • 33746078149 scopus 로고    scopus 로고
    • 18F-FDG PET as a candidate for "qualified biomarker": Functional assessment of treatment response in oncology
    • Larson, S. M. and Schwartz, L. H. (2006) 18F-FDG PET as a candidate for "qualified biomarker": functional assessment of treatment response in oncology J. Nucl. Med. 47, 901-903
    • (2006) J. Nucl. Med. , vol.47 , pp. 901-903
    • Larson, S.M.1    Schwartz, L.H.2
  • 12
    • 35148870732 scopus 로고    scopus 로고
    • Glut-1 antibodies induce growth arrest and apoptosis in human cancer cell lines
    • Rastogi, S., Banerjee, S., Chellappan, S., and Simon, G. R. (2007) Glut-1 antibodies induce growth arrest and apoptosis in human cancer cell lines Cancer Lett. 257, 244-251 10.1016/j.canlet.2007.07.021
    • (2007) Cancer Lett. , vol.257 , pp. 244-251
    • Rastogi, S.1    Banerjee, S.2    Chellappan, S.3    Simon, G.R.4
  • 14
    • 84864875404 scopus 로고    scopus 로고
    • A small-molecule inhibitor of glucose transporter 1 downregulates glycolysis, induces cell-cycle arrest, and inhibits cancer cell growth in vitro and in vivo
    • Liu, Y., Cao, Y., Zhang, W., Bergmeier, S., Qian, Y., Akbar, H., Colvin, R., Ding, J., Tong, L., Wu, S., Hines, J., and Chen, X. (2012) A small-molecule inhibitor of glucose transporter 1 downregulates glycolysis, induces cell-cycle arrest, and inhibits cancer cell growth in vitro and in vivo Mol. Cancer Ther. 11, 1672-1682 10.1158/1535-7163.MCT-12-0131
    • (2012) Mol. Cancer Ther. , vol.11 , pp. 1672-1682
    • Liu, Y.1    Cao, Y.2    Zhang, W.3    Bergmeier, S.4    Qian, Y.5    Akbar, H.6    Colvin, R.7    Ding, J.8    Tong, L.9    Wu, S.10    Hines, J.11    Chen, X.12
  • 15
    • 0030839797 scopus 로고    scopus 로고
    • Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid
    • Rumsey, S. C., Kwon, O., Xu, G. W., Burant, C. F., Simpson, I., and Levine, M. (1997) Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid J. Biol. Chem. 272, 18982-18989 10.1074/jbc.272.30.18982
    • (1997) J. Biol. Chem. , vol.272 , pp. 18982-18989
    • Rumsey, S.C.1    Kwon, O.2    Xu, G.W.3    Burant, C.F.4    Simpson, I.5    Levine, M.6
  • 16
    • 0002383467 scopus 로고
    • Sugar transport in the red blood cell: Structure-activity relationships in substrates and antagonists
    • Lefevre, P. G. (1961) Sugar transport in the red blood cell: structure-activity relationships in substrates and antagonists Pharmacol. Rev. 13, 39-70
    • (1961) Pharmacol. Rev. , vol.13 , pp. 39-70
    • Lefevre, P.G.1
  • 17
    • 84930899862 scopus 로고    scopus 로고
    • Caffeine inhibits glucose transport by binding at the GLUT1 nucleotide-binding site
    • Sage, J. M., Cura, A. J., Lloyd, K. P., and Carruthers, A. (2015) Caffeine inhibits glucose transport by binding at the GLUT1 nucleotide-binding site Am. J. Physiol. Cell Physiol. 308, C827-834 10.1152/ajpcell.00001.2015
    • (2015) Am. J. Physiol. Cell Physiol. , vol.308 , pp. C827-834
    • Sage, J.M.1    Cura, A.J.2    Lloyd, K.P.3    Carruthers, A.4
  • 18
    • 0142153877 scopus 로고    scopus 로고
    • Interactions of androgens, green tea catechins and the antiandrogen flutamide with the external glucose-binding site of the human erythrocyte glucose transporter GLUT1
    • Naftalin, R. J., Afzal, I., Cunningham, P., Halai, M., Ross, C., Salleh, N., and Milligan, S. R. (2003) Interactions of androgens, green tea catechins and the antiandrogen flutamide with the external glucose-binding site of the human erythrocyte glucose transporter GLUT1 Br. J. Pharmacol. 140, 487-499 10.1038/sj.bjp.0705460
    • (2003) Br. J. Pharmacol. , vol.140 , pp. 487-499
    • Naftalin, R.J.1    Afzal, I.2    Cunningham, P.3    Halai, M.4    Ross, C.5    Salleh, N.6    Milligan, S.R.7
  • 19
    • 33947484536 scopus 로고
    • Studies on the metabolism of adipose tissue. Xvi. Inhibition by phlorizin and phloretin of the insulin-stimulated uptake of glucose
    • Frerichs, H. and Ball, E. G. (1964) Studies on the metabolism of adipose tissue. xvi. inhibition by phlorizin and phloretin of the insulin-stimulated uptake of glucose Biochemistry 3, 981-985 10.1021/bi00895a024
    • (1964) Biochemistry , vol.3 , pp. 981-985
    • Frerichs, H.1    Ball, E.G.2
  • 20
    • 0030871885 scopus 로고    scopus 로고
    • D-Glucose, forskolin and cytochalasin B affinities for the glucose transporter Glut1. Study of pH and reconstitution effects by biomembrane affinity chromatography
    • Lu, L., Lundqvist, A., Zeng, C. M., Lagerquist, C., and Lundahl, P. (1997) D-Glucose, forskolin and cytochalasin B affinities for the glucose transporter Glut1. Study of pH and reconstitution effects by biomembrane affinity chromatography J. Chromatogr. A 776, 81-86 10.1016/S0021-9673(97)00151-9
    • (1997) J. Chromatogr. A , vol.776 , pp. 81-86
    • Lu, L.1    Lundqvist, A.2    Zeng, C.M.3    Lagerquist, C.4    Lundahl, P.5
  • 22
    • 84905448179 scopus 로고    scopus 로고
    • Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE
    • Wisedchaisri, G., Park, M. S., Iadanza, M. G., Zheng, H., and Gonen, T. (2014) Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE Nat. Commun. 5, 4521 10.1038/ncomms5521
    • (2014) Nat. Commun. , vol.5 , pp. 4521
    • Wisedchaisri, G.1    Park, M.S.2    Iadanza, M.G.3    Zheng, H.4    Gonen, T.5
  • 23
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. (1966) Simple allosteric model for membrane pumps Nature 211, 969-970 10.1038/211969a0
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 24
    • 79952738070 scopus 로고    scopus 로고
    • The alternating-access mechanism of MFS transporters arises from inverted-topology repeats
    • Radestock, S. and Forrest, L. R. (2011) The alternating-access mechanism of MFS transporters arises from inverted-topology repeats J. Mol. Biol. 407, 698-715 10.1016/j.jmb.2011.02.008
    • (2011) J. Mol. Biol. , vol.407 , pp. 698-715
    • Radestock, S.1    Forrest, L.R.2
  • 26
    • 80755122853 scopus 로고    scopus 로고
    • Lactose permease and the alternating access mechanism
    • Smirnova, I., Kasho, V., and Kaback, H. R. (2011) Lactose permease and the alternating access mechanism Biochemistry 50, 9684-9693 10.1021/bi2014294
    • (2011) Biochemistry , vol.50 , pp. 9684-9693
    • Smirnova, I.1    Kasho, V.2    Kaback, H.R.3
  • 27
    • 84902002905 scopus 로고    scopus 로고
    • Crystal structure of the human glucose transporter GLUT1
    • Deng, D., Xu, C., Sun, P., Wu, J., Yan, C., Hu, M., and Yan, N. (2014) Crystal structure of the human glucose transporter GLUT1 Nature 510, 121-125 10.1038/nature13306
    • (2014) Nature , vol.510 , pp. 121-125
    • Deng, D.1    Xu, C.2    Sun, P.3    Wu, J.4    Yan, C.5    Hu, M.6    Yan, N.7
  • 31
    • 84878896166 scopus 로고    scopus 로고
    • Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters
    • Quistgaard, E. M., Low, C., Moberg, P., Tresaugues, L., and Nordlund, P. (2013) Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters Nat. Struct. Mol. Biol. 20, 766-768 10.1038/nsmb.2569
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 766-768
    • Quistgaard, E.M.1    Low, C.2    Moberg, P.3    Tresaugues, L.4    Nordlund, P.5
  • 32
    • 84867657593 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of glucose transporters GLUT1-4
    • Sun, L., Zeng, X., Yan, C., Sun, X., Gong, X., Rao, Y., and Yan, N. (2012) Crystal structure of a bacterial homologue of glucose transporters GLUT1-4 Nature 490, 361-366 10.1038/nature11524
    • (2012) Nature , vol.490 , pp. 361-366
    • Sun, L.1    Zeng, X.2    Yan, C.3    Sun, X.4    Gong, X.5    Rao, Y.6    Yan, N.7
  • 33
    • 11144323163 scopus 로고    scopus 로고
    • Virtual screening of chemical libraries
    • Shoichet, B. K. (2004) Virtual screening of chemical libraries Nature 432, 862-865 10.1038/nature03197
    • (2004) Nature , vol.432 , pp. 862-865
    • Shoichet, B.K.1
  • 34
    • 38549097071 scopus 로고    scopus 로고
    • The universal protein resource (UniProt)
    • UniProt Consortium (2008) The universal protein resource (UniProt) Nucleic Acids Res. 36, D190-195
    • (2008) Nucleic Acids Res. , vol.36 , pp. D190-195
    • Consortium, U.1
  • 35
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput Nucleic Acids Res. 32, 1792-1797 10.1093/nar/gkh340
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 36
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234, 779-815 10.1006/jmbi.1993.1626
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 37
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen, M. Y. and Sali, A. (2006) Statistical potential for assessment and prediction of protein structures Protein Sci. 15, 2507-2524 10.1110/ps.062416606
    • (2006) Protein Sci. , vol.15 , pp. 2507-2524
    • Shen, M.Y.1    Sali, A.2
  • 38
    • 84909619181 scopus 로고    scopus 로고
    • POVME 2.0: An enhanced tool for determining pocket shape and volume characteristics
    • Durrant, J. D., Votapka, L., Sorensen, J., and Amaro, R. E. (2014) POVME 2.0: an enhanced tool for determining pocket shape and volume characteristics J. Chem. Theory Comput. 10, 5047-5056 10.1021/ct500381c
    • (2014) J. Chem. Theory Comput. , vol.10 , pp. 5047-5056
    • Durrant, J.D.1    Votapka, L.2    Sorensen, J.3    Amaro, R.E.4
  • 39
    • 84978667188 scopus 로고    scopus 로고
    • Schrödinger Release, -2: Maestro, 10.2, Schrödinger, LLC. New York, NY, USA
    • Schrödinger Release 2015, -2: Maestro, 10.2, Schrödinger, LLC., New York, NY, USA. http://www.schrodinger.com.
    • (2015)
  • 40
    • 13844312649 scopus 로고    scopus 로고
    • ZINC - A free database of commercially available compounds for virtual screening
    • Irwin, J. J. and Shoichet, B. K. (2005) ZINC - a free database of commercially available compounds for virtual screening J. Chem. Inf. Model. 45, 177-182 10.1021/ci049714+
    • (2005) J. Chem. Inf. Model. , vol.45 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 41
    • 77951986384 scopus 로고    scopus 로고
    • Conformer generation with OMEGA: Algorithm and validation using high quality structures from the Protein Databank and Cambridge Structural Database
    • Hawkins, P. C., Skillman, A. G., Warren, G. L., Ellingson, B. A., and Stahl, M. T. (2010) Conformer generation with OMEGA: algorithm and validation using high quality structures from the Protein Databank and Cambridge Structural Database J. Chem. Inf. Model. 50, 572-584 10.1021/ci100031x
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 572-584
    • Hawkins, P.C.1    Skillman, A.G.2    Warren, G.L.3    Ellingson, B.A.4    Stahl, M.T.5
  • 42
    • 84978772692 scopus 로고    scopus 로고
    • OEDocking, 3.0.1; OMEGA, 2.5.1.4, OpenEye Scientific Software. Santa Fe, NM, USA
    • OEDocking, 3.0.1; OMEGA, 2.5.1.4, OpenEye Scientific Software., Santa Fe, NM, USA. http://www.eyesopen.com.
  • 43
    • 84867328344 scopus 로고    scopus 로고
    • FRED and HYBRID docking performance on standardized datasets
    • McGann, M. (2012) FRED and HYBRID docking performance on standardized datasets J. Comput.-Aided Mol. Des. 26, 897-906 10.1007/s10822-012-9584-8
    • (2012) J. Comput.-Aided Mol. Des. , vol.26 , pp. 897-906
    • McGann, M.1
  • 45
    • 0033580489 scopus 로고    scopus 로고
    • Caffeine alters A2A adenosine receptors and their function in human platelets
    • Varani, K., Portaluppi, F., Merighi, S., Ongini, E., Belardinelli, L., and Borea, P. A. (1999) Caffeine alters A2A adenosine receptors and their function in human platelets Circulation 99, 2499-2502 10.1161/01.CIR.99.19.2499
    • (1999) Circulation , vol.99 , pp. 2499-2502
    • Varani, K.1    Portaluppi, F.2    Merighi, S.3    Ongini, E.4    Belardinelli, L.5    Borea, P.A.6
  • 46
    • 77950571108 scopus 로고    scopus 로고
    • New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays
    • Baell, J. B. and Holloway, G. A. (2010) New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays J. Med. Chem. 53, 2719-2740 10.1021/jm901137j
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 47
    • 33645511221 scopus 로고    scopus 로고
    • Structural model for gamma-aminobutyric acid receptor noncompetitive antagonist binding: Widely diverse structures fit the same site
    • Chen, L., Durkin, K. A., and Casida, J. E. (2006) Structural model for gamma-aminobutyric acid receptor noncompetitive antagonist binding: widely diverse structures fit the same site Proc. Natl. Acad. Sci. U. S. A. 103, 5185-5190 10.1073/pnas.0600370103
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 5185-5190
    • Chen, L.1    Durkin, K.A.2    Casida, J.E.3
  • 49
    • 84868313349 scopus 로고    scopus 로고
    • High selectivity of the gamma-aminobutyric acid transporter 2 (GAT-2, SLC6A13) revealed by structure-based approach
    • Schlessinger, A., Wittwer, M. B., Dahlin, A., Khuri, N., Bonomi, M., Fan, H., Giacomini, K. M., and Sali, A. (2012) High selectivity of the gamma-aminobutyric acid transporter 2 (GAT-2, SLC6A13) revealed by structure-based approach J. Biol. Chem. 287, 37745-37756 10.1074/jbc.M112.388157
    • (2012) J. Biol. Chem. , vol.287 , pp. 37745-37756
    • Schlessinger, A.1    Wittwer, M.B.2    Dahlin, A.3    Khuri, N.4    Bonomi, M.5    Fan, H.6    Giacomini, K.M.7    Sali, A.8
  • 50
    • 84894374374 scopus 로고    scopus 로고
    • Functional architecture of MFS D-glucose transporters
    • Madej, M. G., Sun, L., Yan, N., and Kaback, H. R. (2014) Functional architecture of MFS D-glucose transporters Proc. Natl. Acad. Sci. U. S. A. 111, E719-727 10.1073/pnas.1400336111
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. E719-727
    • Madej, M.G.1    Sun, L.2    Yan, N.3    Kaback, H.R.4
  • 51
    • 55549141879 scopus 로고    scopus 로고
    • How well can the accuracy of comparative protein structure models be predicted?
    • Eramian, D., Eswar, N., Shen, M. Y., and Sali, A. (2008) How well can the accuracy of comparative protein structure models be predicted? Protein Sci. 17, 1881-1893 10.1110/ps.036061.108
    • (2008) Protein Sci. , vol.17 , pp. 1881-1893
    • Eramian, D.1    Eswar, N.2    Shen, M.Y.3    Sali, A.4
  • 52
    • 0033747337 scopus 로고    scopus 로고
    • Serine and threonine residues bend alpha-helices in the chi(1) = g(-) conformation
    • Ballesteros, J. A., Deupi, X., Olivella, M., Haaksma, E. E., and Pardo, L. (2000) Serine and threonine residues bend alpha-helices in the chi(1) = g(-) conformation Biophys. J. 79, 2754-2760 10.1016/S0006-3495(00)76514-3
    • (2000) Biophys. J. , vol.79 , pp. 2754-2760
    • Ballesteros, J.A.1    Deupi, X.2    Olivella, M.3    Haaksma, E.E.4    Pardo, L.5
  • 53
    • 0025950411 scopus 로고
    • Differentiation of erythrocyte-(GLUT1), liver-(GLUT2), and adipocyte-type (GLUT4) glucose transporters by binding of the inhibitory ligands cytochalasin B, forskolin, dipyridamole, and isobutylmethylxanthine
    • Hellwig, B. and Joost, H. G. (1991) Differentiation of erythrocyte-(GLUT1), liver-(GLUT2), and adipocyte-type (GLUT4) glucose transporters by binding of the inhibitory ligands cytochalasin B, forskolin, dipyridamole, and isobutylmethylxanthine Mol. Pharmacol. 40, 383-389
    • (1991) Mol. Pharmacol. , vol.40 , pp. 383-389
    • Hellwig, B.1    Joost, H.G.2
  • 54
    • 0013971330 scopus 로고
    • Competitive inhibition of intestinal glucose transport by phlorizin analogs
    • Diedrich, D. F. (1966) Competitive inhibition of intestinal glucose transport by phlorizin analogs Arch. Biochem. Biophys. 117, 248-256 10.1016/0003-9861(66)90409-7
    • (1966) Arch. Biochem. Biophys. , vol.117 , pp. 248-256
    • Diedrich, D.F.1
  • 55
    • 77954242599 scopus 로고    scopus 로고
    • SGLT2 inhibition - A novel strategy for diabetes treatment
    • Chao, E. C. and Henry, R. R. (2010) SGLT2 inhibition - a novel strategy for diabetes treatment Nat. Rev. Drug Discovery 9, 551-559 10.1038/nrd3180
    • (2010) Nat. Rev. Drug Discovery , vol.9 , pp. 551-559
    • Chao, E.C.1    Henry, R.R.2
  • 56
    • 0029913703 scopus 로고    scopus 로고
    • Expression of the rat GLUT1 glucose transporter in the yeast Saccharomyces cerevisiae
    • Kasahara, T. and Kasahara, M. (1996) Expression of the rat GLUT1 glucose transporter in the yeast Saccharomyces cerevisiae Biochem. J. 315 (Pt 1) 177-182 10.1042/bj3150177
    • (1996) Biochem. J. , vol.315 , pp. 177-182
    • Kasahara, T.1    Kasahara, M.2
  • 59
    • 84946045408 scopus 로고    scopus 로고
    • Ligand Discovery for the Alanine-Serine-Cysteine Transporter (ASCT2, SLC1A5) from Homology Modeling and Virtual Screening
    • Colas, C., Grewer, C., Otte, N. J., Gameiro, A., Albers, T., Singh, K., Shere, H., Bonomi, M., Holst, J., and Schlessinger, A. (2015) Ligand Discovery for the Alanine-Serine-Cysteine Transporter (ASCT2, SLC1A5) from Homology Modeling and Virtual Screening PLoS Comput. Biol. 11, e1004477 10.1371/journal.pcbi.1004477
    • (2015) PLoS Comput. Biol. , vol.11 , pp. e1004477
    • Colas, C.1    Grewer, C.2    Otte, N.J.3    Gameiro, A.4    Albers, T.5    Singh, K.6    Shere, H.7    Bonomi, M.8    Holst, J.9    Schlessinger, A.10
  • 60
    • 84938703009 scopus 로고    scopus 로고
    • Structure-based identification of inhibitors for the SLC13 family of Na(+)/dicarboxylate cotransporters
    • Colas, C., Pajor, A. M., and Schlessinger, A. (2015) Structure-based identification of inhibitors for the SLC13 family of Na(+)/dicarboxylate cotransporters Biochemistry 54, 4900-4908 10.1021/acs.biochem.5b00388
    • (2015) Biochemistry , vol.54 , pp. 4900-4908
    • Colas, C.1    Pajor, A.M.2    Schlessinger, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.