메뉴 건너뛰기




Volumn 16, Issue 15, 2010, Pages 1742-1752

Pharmacoinformatic approaches to design natural product type ligands of ABC-transporters

Author keywords

ABC transporter; In silico methods; Natural products; P glycoprotein

Indexed keywords

ABC TRANSPORTER; ALDOSTERONE; ANDROSTANOLONE; ANDROSTENEDIONE; ANTINEOPLASTIC AGENT; BREAST CANCER RESISTANCE PROTEIN; CHALCONE DERIVATIVE; CORTICOSTERONE; CORTODOXONE; CYCLOSPORIN DERIVATIVE; DEXAMETHASONE; FLAVANONE DERIVATIVE; FLAVONE DERIVATIVE; FLAVONOL DERIVATIVE; HYDROCORTISONE; HYDROXYPROGESTERONE; ISOFLAVONE; MEDROXYPROGESTERONE ACETATE; MULTIDRUG RESISTANCE PROTEIN 1; PHENOTHIAZINE DERIVATIVE; PRASTERONE; PREGNENOLONE; PROGESTERONE; PROPAFENONE; PROTEIN INHIBITOR; TESTOSTERONE; THIOXANTHENE DERIVATIVE; TRIAZINE DERIVATIVE; UNINDEXED DRUG; VERAPAMIL DERIVATIVE; BIOLOGICAL PRODUCT; FLAVONOID; GLYCOPROTEIN P; LIGAND; MULTIDRUG RESISTANCE PROTEIN; SESQUITERPENE; STEROID; TUMOR PROTEIN;

EID: 77957975632     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161210791163992     Document Type: Article
Times cited : (18)

References (71)
  • 1
    • 31844444140 scopus 로고    scopus 로고
    • The molecular basis of multidrug resistance in cancer: The early years of P-glycoprotein research
    • Gottesman MM, Ling V. The molecular basis of multidrug resistance in cancer: the early years of P-glycoprotein research. FEBS Lett 2006; 580: 998-1009.
    • (2006) FEBS Lett , vol.580 , pp. 998-1009
    • Gottesman, M.M.1    Ling, V.2
  • 3
    • 0019430432 scopus 로고
    • Overcoming of vincristine resistance in P388 leukemia in vivo and in vitro through enhanced cytotoxicity of vincristine and vinblastine by verapamil
    • Tsuruo T, Iida H, Tsukagoshi S, Sakurai Y. Overcoming of vincristine resistance in P388 leukemia in vivo and in vitro through enhanced cytotoxicity of vincristine and vinblastine by verapamil. Cancer Res 1981; 41: 1967-1972.
    • (1981) Cancer Res , vol.41 , pp. 1967-1972
    • Tsuruo, T.1    Iida, H.2    Tsukagoshi, S.3    Sakurai, Y.4
  • 4
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano RL, Ling V. A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim Biophys Acta 1976; 455: 152-162.
    • (1976) Biochim Biophys Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 5
    • 0034953105 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • Dean M, Hamon Y, Chimini G. The human ATP-binding cassette (ABC) transporter superfamily. J Lipid Res 2001; 42: 1007-1017.
    • (2001) J Lipid Res , vol.42 , pp. 1007-1017
    • Dean, M.1    Hamon, Y.2    Chimini, G.3
  • 6
    • 43149118341 scopus 로고    scopus 로고
    • The role of ABC transporters in drug absorption, distribution, metabolism, excretion and toxicity (ADME-Tox)
    • Szakacs G, Varadi A, Ozvegy-Laczka C, Sarkadi B. The role of ABC transporters in drug absorption, distribution, metabolism, excretion and toxicity (ADME-Tox). Drug Discov Today 2008; 13: 379-393.
    • (2008) Drug Discov Today , vol.13 , pp. 379-393
    • Szakacs, G.1    Varadi, A.2    Ozvegy-Laczka, C.3    Sarkadi, B.4
  • 7
    • 33644692007 scopus 로고    scopus 로고
    • P-glycoprotein recognition of substrates and circumvention through rational drug design
    • Raub TJ. P-glycoprotein recognition of substrates and circumvention through rational drug design. Mol Pharm 2006; 3: 3-25.
    • (2006) Mol Pharm , vol.3 , pp. 3-25
    • Raub, T.J.1
  • 8
    • 14544287387 scopus 로고    scopus 로고
    • Inhibitors of p-glycoprotein--lead identification and optimisation
    • Pleban K, Ecker GF. Inhibitors of p-glycoprotein--lead identification and optimisation. Mini Rev Med Chem 2005; 5: 153-163.
    • (2005) Mini Rev Med Chem , vol.5 , pp. 153-163
    • Pleban, K.1    Ecker, G.F.2
  • 9
    • 22144481699 scopus 로고    scopus 로고
    • Structure activity relationships and quantitative structure activity relationships for the flavonoid-mediated inhibition of breast cancer resistance protein
    • Zhang S, Yang X, Coburn RA, Morris ME. Structure activity relationships and quantitative structure activity relationships for the flavonoid-mediated inhibition of breast cancer resistance protein. Biochem Pharmacol 2005; 70: 627-639.
    • (2005) Biochem Pharmacol , vol.70 , pp. 627-639
    • Zhang, S.1    Yang, X.2    Coburn, R.A.3    Morris, M.E.4
  • 10
    • 2142711101 scopus 로고    scopus 로고
    • Flavonoids are inhibitors of breast cancer resistance protein (ABCG2)-mediated transport
    • Zhang S, Yang X, Morris ME. Flavonoids are inhibitors of breast cancer resistance protein (ABCG2)-mediated transport. Mol Pharmacol 2004; 65: 1208-1216.
    • (2004) Mol Pharmacol , vol.65 , pp. 1208-1216
    • Zhang, S.1    Yang, X.2    Morris, M.E.3
  • 11
    • 69949106198 scopus 로고    scopus 로고
    • Emerging significance of flavonoids as P-glycoprotein inhibitors in cancer chemotherapy
    • Bansal T, Jaggi M, Khar RK, Talegaonkar S. Emerging significance of flavonoids as P-glycoprotein inhibitors in cancer chemotherapy. J Pharm Pharm Sci 2009; 12: 46-78.
    • (2009) J Pharm Pharm Sci , vol.12 , pp. 46-78
    • Bansal, T.1    Jaggi, M.2    Khar, R.K.3    Talegaonkar, S.4
  • 12
    • 0032544087 scopus 로고    scopus 로고
    • Flavonoids: A class of modulators with bifunctional interactions at vicinal ATP- and steroid-binding sites on mouse P-glycoprotein
    • Conseil G, Baubichon-Cortay H, Dayan G, Jault JM, Barron D, Di Pietro A. Flavonoids: a class of modulators with bifunctional interactions at vicinal ATP- and steroid-binding sites on mouse P-glycoprotein. Proc Natl Acad Sci USA 1998; 95: 9831-9836.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9831-9836
    • Conseil, G.1    Baubichon-Cortay, H.2    Dayan, G.3    Jault, J.M.4    Barron, D.5    Di Pietro, A.6
  • 13
    • 41549159003 scopus 로고    scopus 로고
    • Multispecificity of drug transporters: Probing inhibitor selectivity for the human drug efflux transporters ABCB1 and ABCG2
    • Cramer J, Kopp S, Bates SE, Chiba P, Ecker GF. Multispecificity of drug transporters: probing inhibitor selectivity for the human drug efflux transporters ABCB1 and ABCG2. ChemMedChem 2007; 2: 1783-1788.
    • (2007) ChemMedChem , vol.2 , pp. 1783-1788
    • Cramer, J.1    Kopp, S.2    Bates, S.E.3    Chiba, P.4    Ecker, G.F.5
  • 14
    • 33947485697 scopus 로고
    • A Mathematical contribution to structure-activity studies
    • Free SM, Jr., Wilson JW. A Mathematical contribution to structure-activity studies. J Med Chem 1964; 7: 395-399.
    • (1964) J Med Chem , vol.7 , pp. 395-399
    • Free Jr., S.M.1    Wilson, J.W.2
  • 15
    • 50349103259 scopus 로고    scopus 로고
    • Structure-activity relationships of new inhibitors of breast cancer resistance protein (ABCG2)
    • Pick A, Muller H, Wiese M. Structure-activity relationships of new inhibitors of breast cancer resistance protein (ABCG2). Bioorg Med Chem 2008; 16: 8224-8236.
    • (2008) Bioorg Med Chem , vol.16 , pp. 8224-8236
    • Pick, A.1    Muller, H.2    Wiese, M.3
  • 16
    • 0028708076 scopus 로고
    • Human P-glycoprotein as a multi-drug transporter analyzed by using transepithelial transport system
    • Ueda K, Saeki T, Hirai M, Tanigawara Y, Tanaka K, Okamura M, et al. Human P-glycoprotein as a multi-drug transporter analyzed by using transepithelial transport system. Jpn J Physiol 1994; 44 (Suppl 2): S67-S71.
    • (1994) Jpn J Physiol , vol.44 , Issue.SUPPL. 2
    • Ueda, K.1    Saeki, T.2    Hirai, M.3    Tanigawara, Y.4    Tanaka, K.5    Okamura, M.6
  • 17
    • 0024501045 scopus 로고
    • Progesterone interacts with P-glycoprotein in multidrug-resistant cells and in the endometrium of gravid uterus
    • Yang CP, DePinho SG, Greenberger LM, Arceci RJ, Horwitz SB. Progesterone interacts with P-glycoprotein in multidrug-resistant cells and in the endometrium of gravid uterus. J Biol Chem 1989; 264: 782-788.
    • (1989) J Biol Chem , vol.264 , pp. 782-788
    • Yang, C.P.1    Depinho, S.G.2    Greenberger, L.M.3    Arceci, R.J.4    Horwitz, S.B.5
  • 18
    • 0035834190 scopus 로고    scopus 로고
    • Modulation of P-glycoprotein activity in Calu-3 cells using steroids and beta-ligands
    • Hamilton KO, Yazdanian MA, Audus KL. Modulation of P-glycoprotein activity in Calu-3 cells using steroids and beta-ligands. Int J Pharm 2001; 228: 171-179.
    • (2001) Int J Pharm , vol.228 , pp. 171-179
    • Hamilton, K.O.1    Yazdanian, M.A.2    Audus, K.L.3
  • 19
    • 8144230162 scopus 로고    scopus 로고
    • Comparison of steroid substrates and inhibitors of P-glycoprotein by 3D-QSAR analysis
    • Li Y, Wang YH, Yang L, Zhang SW, Liu CH, Yang SL. Comparison of steroid substrates and inhibitors of P-glycoprotein by 3D-QSAR analysis. J Mol Structure 2005; 733: 111-118.
    • (2005) J Mol Structure , vol.733 , pp. 111-118
    • Li, Y.1    Wang, Y.H.2    Yang, L.3    Zhang, S.W.4    Liu, C.H.5    Yang, S.L.6
  • 20
    • 0030589989 scopus 로고    scopus 로고
    • Steroid treatment, accumulation, and antagonism of P-glycoprotein in multidrug-resistant cells
    • Barnes KM, Dickstein B, Cutler GB, Jr., Fojo T, Bates SE. Steroid treatment, accumulation, and antagonism of P-glycoprotein in multidrug-resistant cells. Biochemistry 1996; 35: 4820-4827.
    • (1996) Biochemistry , vol.35 , pp. 4820-4827
    • Barnes, K.M.1    Dickstein, B.2    Cutler Jr., G.B.3    Fojo, T.4    Bates, S.E.5
  • 22
    • 34948839413 scopus 로고    scopus 로고
    • Biological evaluation, structure-activity relationships, and three-dimensional quantitative structure-activity relationship studies of dihydro-beta-agarofuran sesquiter-penes as modulators of P-glycoprotein-dependent multidrug resistance
    • Reyes CP, Munoz-Martinez F, Torrecillas IR, Mendoza CR, Gamarro F, Bazzocchi IL, et al. Biological evaluation, structure-activity relationships, and three-dimensional quantitative structure-activity relationship studies of dihydro-beta-agarofuran sesquiter-penes as modulators of P-glycoprotein-dependent multidrug resistance. J Med Chem 2007; 50: 4808-4817.
    • (2007) J Med Chem , vol.50 , pp. 4808-4817
    • Reyes, C.P.1    Munoz-Martinez, F.2    Torrecillas, I.R.3    Mendoza, C.R.4    Gamarro, F.5    Bazzocchi, I.L.6
  • 24
    • 0037050736 scopus 로고    scopus 로고
    • Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization
    • Kage K, Tsukahara S, Sugiyama T, Asada S, Ishikawa E, Tsuruo T, et al. Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization. Int J Cancer 2002; 97: 626-630.
    • (2002) Int J Cancer , vol.97 , pp. 626-630
    • Kage, K.1    Tsukahara, S.2    Sugiyama, T.3    Asada, S.4    Ishikawa, E.5    Tsuruo, T.6
  • 25
    • 0032404092 scopus 로고    scopus 로고
    • A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance
    • Allikmets R, Schriml LM, Hutchinson A, Romano-Spica V, Dean M. A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance. Cancer Res 1998; 58: 5337-5339.
    • (1998) Cancer Res , vol.58 , pp. 5337-5339
    • Allikmets, R.1    Schriml, L.M.2    Hutchinson, A.3    Romano-Spica, V.4    Dean, M.5
  • 26
    • 64649090980 scopus 로고    scopus 로고
    • Molecular basis of multidrug transport by ABC transporters
    • Seeger MA, van Veen HW. Molecular basis of multidrug transport by ABC transporters. Biochim Biophys Acta 2009; 1794: 725-737.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 725-737
    • Seeger, M.A.1    van Veen, H.W.2
  • 27
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson RJ, Locher KP. Structure of a bacterial multidrug ABC transporter. Nature 2006; 443: 180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 29
    • 47049126229 scopus 로고    scopus 로고
    • Identification of putative binding sites of P-glycoprotein based on its homology model
    • Globisch C, Pajeva IK, Wiese M. Identification of putative binding sites of P-glycoprotein based on its homology model. Chem Med Chem 2008; 3: 280-295.
    • (2008) Chem Med Chem , vol.3 , pp. 280-295
    • Globisch, C.1    Pajeva, I.K.2    Wiese, M.3
  • 30
    • 58849086773 scopus 로고    scopus 로고
    • Data-driven homology modelling of P-glycoprotein in the ATP-bound state indicates flexibility of the transmembrane domains
    • Stockner T, de Vries SJ, Bonvin AM, Ecker GF, Chiba P. Data-driven homology modelling of P-glycoprotein in the ATP-bound state indicates flexibility of the transmembrane domains. FEBS J 2009; 276: 964-972.
    • (2009) FEBS J , vol.276 , pp. 964-972
    • Stockner, T.1    de Vries, S.J.2    Bonvin, A.M.3    Ecker, G.F.4    Chiba, P.5
  • 32
    • 41649122089 scopus 로고    scopus 로고
    • Homology modeling of breast cancer resistance protein (ABCG2)
    • Hazai E, Bikadi Z. Homology modeling of breast cancer resistance protein (ABCG2). J Struct Biol 2008; 162: 63-74.
    • (2008) J Struct Biol , vol.162 , pp. 63-74
    • Hazai, E.1    Bikadi, Z.2
  • 33
    • 34548133239 scopus 로고    scopus 로고
    • P-glycoprotein models of the apo and ATP-bound states based on homology with Sav1866 and MalK
    • O'Mara ML, Tieleman DP. P-glycoprotein models of the apo and ATP-bound states based on homology with Sav1866 and MalK. FEBS Lett 2007; 581: 4217-4222.
    • (2007) FEBS Lett , vol.581 , pp. 4217-4222
    • O'Mara, M.L.1    Tieleman, D.P.2
  • 34
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson RJ, Locher KP. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett 2007; 581: 935-938.
    • (2007) FEBS Lett , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 35
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward A, Reyes CL, Yu J, Roth CB, Chang G. Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc Natl Acad Sci USA 2007; 104: 19005-19010.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 36
    • 63449139456 scopus 로고    scopus 로고
    • Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding
    • Aller SG, Yu J, Ward A, Weng Y, Chittaboina S, Zhuo R, et al. Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding. Science 2009; 323: 1718-1722.
    • (2009) Science , vol.323 , pp. 1718-1722
    • Aller, S.G.1    Yu, J.2    Ward, A.3    Weng, Y.4    Chittaboina, S.5    Zhuo, R.6
  • 37
    • 70449714688 scopus 로고    scopus 로고
    • Combined pharmacophore modeling, Docking, and 3D QSAR studies of ABCB1 and ABCC1 transporter inhibitors
    • Pajeva IK, Globisch C, Wiese M. Combined pharmacophore modeling, Docking, and 3D QSAR studies of ABCB1 and ABCC1 transporter inhibitors. Chem Med Chem 2009; 4(11): 1883-1896.
    • (2009) Chem Med Chem , vol.4 , Issue.11 , pp. 1883-1896
    • Pajeva, I.K.1    Globisch, C.2    Wiese, M.3
  • 38
    • 0033609856 scopus 로고    scopus 로고
    • The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface
    • Loo TW, Clarke DM. The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface. J Biol Chem 1999; 274: 24759-24765.
    • (1999) J Biol Chem , vol.274 , pp. 24759-24765
    • Loo, T.W.1    Clarke, D.M.2
  • 39
    • 47049101437 scopus 로고    scopus 로고
    • Mutational analysis of ABC proteins
    • Loo TW, Clarke DM. Mutational analysis of ABC proteins. Arch Biochem Biophys 2008; 476: 51-64.
    • (2008) Arch Biochem Biophys , vol.476 , pp. 51-64
    • Loo, T.W.1    Clarke, D.M.2
  • 41
    • 0037113961 scopus 로고    scopus 로고
    • Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein
    • Loo TW, Clarke DM. Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein. J Biol Chem 2002; 277: 44332-44338.
    • (2002) J Biol Chem , vol.277 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 42
    • 0037046150 scopus 로고    scopus 로고
    • Proximity of bound Hoechst 33342 to the ATPase catalytic sites places the drug binding site of P-glycoprotein within the cytoplasmic membrane leaflet
    • Qu Q, Sharom FJ. Proximity of bound Hoechst 33342 to the ATPase catalytic sites places the drug binding site of P-glycoprotein within the cytoplasmic membrane leaflet. Biochemistry 2002; 41: 4744-4752.
    • (2002) Biochemistry , vol.41 , pp. 4744-4752
    • Qu, Q.1    Sharom, F.J.2
  • 44
    • 0033083015 scopus 로고    scopus 로고
    • Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site
    • Shapiro AB, Fox K, Lam P, Ling V. Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site. Eur J Biochem 1999; 259: 841-850.
    • (1999) Eur J Biochem , vol.259 , pp. 841-850
    • Shapiro, A.B.1    Fox, K.2    Lam, P.3    Ling, V.4
  • 45
    • 33749985062 scopus 로고    scopus 로고
    • Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket
    • Loo TW, Bartlett MC, Clarke DM. Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket. Biochem J 2006; 399: 351-359.
    • (2006) Biochem J , vol.399 , pp. 351-359
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 46
    • 0031434236 scopus 로고    scopus 로고
    • Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate
    • Loo TW, Clarke DM. Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate. J Biol Chem 1997; 272: 31945-31948.
    • (1997) J Biol Chem , vol.272 , pp. 31945-31948
    • Loo, T.W.1    Clarke, D.M.2
  • 47
    • 33750478648 scopus 로고    scopus 로고
    • Multiple drugbinding sites on the R482G isoform of the ABCG2 transporter
    • Clark R, Kerr ID, Callaghan R. Multiple drugbinding sites on the R482G isoform of the ABCG2 transporter. Br J Pharmacol 2006; 149: 506-515.
    • (2006) Br J Pharmacol , vol.149 , pp. 506-515
    • Clark, R.1    Kerr, I.D.2    Callaghan, R.3
  • 48
    • 31844455959 scopus 로고    scopus 로고
    • Substrate recognition and transport by multidrug resistance protein 1 (ABCC1)
    • Deeley RG, Cole SP. Substrate recognition and transport by multidrug resistance protein 1 (ABCC1). FEBS Lett 2006; 580: 1103-1111.
    • (2006) FEBS Lett , vol.580 , pp. 1103-1111
    • Deeley, R.G.1    Cole, S.P.2
  • 49
    • 67650084777 scopus 로고    scopus 로고
    • Identification of novel specific and general inhibitors of the three major human ATP-binding cassette transporters P-gp, BCRP and MRP2 among registered drugs
    • Matsson P, Pedersen JM, Norinder U, Bergstrom CA, Artursson P. Identification of novel specific and general inhibitors of the three major human ATP-binding cassette transporters P-gp, BCRP and MRP2 among registered drugs. Pharm Res 2009; 26: 1816-1831.
    • (2009) Pharm Res , vol.26 , pp. 1816-1831
    • Matsson, P.1    Pedersen, J.M.2    Norinder, U.3    Bergstrom, C.A.4    Artursson, P.5
  • 50
    • 33744791529 scopus 로고    scopus 로고
    • Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a nonproductive catalytic site
    • Ramaen O, Leulliot N, Sizun C, Ulryck N, Pamlard O, Lallemand JY, et al. Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a nonproductive catalytic site. J Mol Biol 2006; 359: 940-949.
    • (2006) J Mol Biol , vol.359 , pp. 940-949
    • Ramaen, O.1    Leulliot, N.2    Sizun, C.3    Ulryck, N.4    Pamlard, O.5    Lallemand, J.Y.6
  • 51
    • 67650448010 scopus 로고    scopus 로고
    • Identification of putative steroid-binding sites in human ABCB1 and ABCG2
    • Mares-Samano S, Badhan R, Penny J. Identification of putative steroid-binding sites in human ABCB1 and ABCG2. Eur J Med Chem 2009; 44: 3601-3611.
    • (2009) Eur J Med Chem , vol.44 , pp. 3601-3611
    • Mares-Samano, S.1    Badhan, R.2    Penny, J.3
  • 52
    • 33645972931 scopus 로고    scopus 로고
    • In silico modelling of the interaction of flavonoids with human P-glycoprotein nucleotide-binding domain
    • Badhan R, Penny J. In silico modelling of the interaction of flavonoids with human P-glycoprotein nucleotide-binding domain. Eur J Med Chem 2006; 41: 285-295.
    • (2006) Eur J Med Chem , vol.41 , pp. 285-295
    • Badhan, R.1    Penny, J.2
  • 53
    • 62749188875 scopus 로고    scopus 로고
    • Role of ATP-binding cassette (ABC) transporters in interactions between natural products and drugs
    • Aszalos A. Role of ATP-binding cassette (ABC) transporters in interactions between natural products and drugs. Curr Drug Metab 2008; 9: 1010-1018.
    • (2008) Curr Drug Metab , vol.9 , pp. 1010-1018
    • Aszalos, A.1
  • 54
    • 61549086853 scopus 로고    scopus 로고
    • Grapefruit juice and its constituents augment colchicine intestinal absorption: Potential hazardous interaction and the role of p-glycoprotein
    • Dahan A, Amidon GL. Grapefruit juice and its constituents augment colchicine intestinal absorption: potential hazardous interaction and the role of p-glycoprotein. Pharm Res 2009; 26: 883-892.
    • (2009) Pharm Res , vol.26 , pp. 883-892
    • Dahan, A.1    Amidon, G.L.2
  • 55
    • 57349143594 scopus 로고    scopus 로고
    • Interaction of white and pink grapefruit juice with acetaminophen (paracetamol) in vivo in mice
    • Dasgupta A, Reyes MA, Risin SA, Actor JK. Interaction of white and pink grapefruit juice with acetaminophen (paracetamol) in vivo in mice. J Med Food 2008; 11: 795-798.
    • (2008) J Med Food , vol.11 , pp. 795-798
    • Dasgupta, A.1    Reyes, M.A.2    Risin, S.A.3    Actor, J.K.4
  • 56
    • 42249088111 scopus 로고    scopus 로고
    • Further characterization of a furanocoumarin-free grapefruit juice on drug disposition: Studies with cyclosporine
    • Paine MF, Widmer WW, Pusek SN, Beavers KL, Criss AB, Snyder J, et al. Further characterization of a furanocoumarin-free grapefruit juice on drug disposition: studies with cyclosporine. Am J Clin Nutr 2008; 87: 863-871.
    • (2008) Am J Clin Nutr , vol.87 , pp. 863-871
    • Paine, M.F.1    Widmer, W.W.2    Pusek, S.N.3    Beavers, K.L.4    Criss, A.B.5    Snyder, J.6
  • 57
    • 17644380257 scopus 로고    scopus 로고
    • Predicting drug disposition via application of BCS: Transport/absorption/ elimination interplay and development of a biopharmaceutics drug disposition classification system
    • Wu CY, Benet LZ. Predicting drug disposition via application of BCS: transport/absorption/ elimination interplay and development of a biopharmaceutics drug disposition classification system. Pharm Res 2005; 22: 11-23.
    • (2005) Pharm Res , vol.22 , pp. 11-23
    • Wu, C.Y.1    Benet, L.Z.2
  • 58
    • 39149115065 scopus 로고    scopus 로고
    • Predicting drug disposition, absorption/elimination/transporter interplay and the role of food on drug absorption
    • Custodio JM, Wu CY, Benet LZ. Predicting drug disposition, absorption/elimination/transporter interplay and the role of food on drug absorption. Adv Drug Deliv Rev 2008; 60: 717-733.
    • (2008) Adv Drug Deliv Rev , vol.60 , pp. 717-733
    • Custodio, J.M.1    Wu, C.Y.2    Benet, L.Z.3
  • 59
    • 0026760889 scopus 로고
    • P-glycoprotein as the drug efflux pump in primary cultured bovine brain capillary endothelial cells
    • Tsuji A, Terasaki T, Takabatake Y, Tenda Y, Tamai I, Yamashima T, et al. P-glycoprotein as the drug efflux pump in primary cultured bovine brain capillary endothelial cells. Life Sci 1992; 51: 1427-1437.
    • (1992) Life Sci , vol.51 , pp. 1427-1437
    • Tsuji, A.1    Terasaki, T.2    Takabatake, Y.3    Tenda, Y.4    Tamai, I.5    Yamashima, T.6
  • 61
    • 0346728729 scopus 로고    scopus 로고
    • The ABCs of drug transport in intestine and liver: Efflux proteins limiting drug absorption and bioavailability
    • Chan LM, Lowes S, Hirst BH. The ABCs of drug transport in intestine and liver: efflux proteins limiting drug absorption and bioavailability. Eur J Pharm Sci 2004; 21: 25-51.
    • (2004) Eur J Pharm Sci , vol.21 , pp. 25-51
    • Chan, L.M.1    Lowes, S.2    Hirst, B.H.3
  • 64
    • 0034351504 scopus 로고    scopus 로고
    • A widely applicable set of descriptors
    • Labute P. A widely applicable set of descriptors. J Mol Graph Model 2000; 18: 464-477.
    • (2000) J Mol Graph Model , vol.18 , pp. 464-477
    • Labute, P.1
  • 65
    • 34147159665 scopus 로고    scopus 로고
    • Self-organizing maps for identification of new inhibitors of P-glycoprotein
    • Kaiser D, Terfloth L, Kopp S, Schulz J, de Laet R, Chiba P, et al. Self-organizing maps for identification of new inhibitors of P-glycoprotein. J Med Chem 2007; 50: 1698-1702.
    • (2007) J Med Chem , vol.50 , pp. 1698-1702
    • Kaiser, D.1    Terfloth, L.2    Kopp, S.3    Schulz, J.4    de Laet, R.5    Chiba, P.6
  • 67
    • 34347363131 scopus 로고    scopus 로고
    • Quantitative structure--activity relationship analysis and molecular dynamics simulation to functionally validate nonsy-nonymous polymorphisms of human ABC transporter ABCB1 (P-glycoprotein/MDR1)
    • Sakurai A, Onishi Y, Hirano H, Seigneuret M, Obanayama K, Kim G, et al. Quantitative structure--activity relationship analysis and molecular dynamics simulation to functionally validate nonsy-nonymous polymorphisms of human ABC transporter ABCB1 (P-glycoprotein/MDR1). Biochemistry 2007; 46: 7678-7693.
    • (2007) Biochemistry , vol.46 , pp. 7678-7693
    • Sakurai, A.1    Onishi, Y.2    Hirano, H.3    Seigneuret, M.4    Obanayama, K.5    Kim, G.6
  • 68
    • 0037424343 scopus 로고    scopus 로고
    • Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding
    • Rosenberg MF, Kamis AB, Callaghan R, Higgins CF, Ford RC. Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding. J Biol Chem 2003; 278: 8294-8299.
    • (2003) J Biol Chem , vol.278 , pp. 8294-8299
    • Rosenberg, M.F.1    Kamis, A.B.2    Callaghan, R.3    Higgins, C.F.4    Ford, R.C.5
  • 69
    • 13244292479 scopus 로고    scopus 로고
    • Three-dimensional structure of P-glycoprotein: The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state
    • Rosenberg MF, Callaghan R, Modok S, Higgins CF, Ford RC. Three-dimensional structure of P-glycoprotein: the transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state. J Biol Chem 2005; 280: 2857-2862.
    • (2005) J Biol Chem , vol.280 , pp. 2857-2862
    • Rosenberg, M.F.1    Callaghan, R.2    Modok, S.3    Higgins, C.F.4    Ford, R.C.5
  • 70
    • 0035844237 scopus 로고    scopus 로고
    • The structure of the multidrug resistance protein 1 (MRP1/ABCC1). crystallization and single-particle analysis
    • Rosenberg MF, Mao Q, Holzenburg A, Ford RC, Deeley RG, Cole SP. The structure of the multidrug resistance protein 1 (MRP1/ABCC1). crystallization and single-particle analysis. J Biol Chem 2001; 276: 16076-16082.
    • (2001) J Biol Chem , vol.276 , pp. 16076-16082
    • Rosenberg, M.F.1    Mao, Q.2    Holzenburg, A.3    Ford, R.C.4    Deeley, R.G.5    Cole, S.P.6
  • 71
    • 33750446035 scopus 로고    scopus 로고
    • Purification and 3D structural analysis of oligomeric human multidrug transporter ABCG2
    • McDevitt CA, Collins RF, Conway M, Modok S, Storm J, Kerr ID, et al. Purification and 3D structural analysis of oligomeric human multidrug transporter ABCG2. Structure 2006; 14: 1623-1632.
    • (2006) Structure , vol.14 , pp. 1623-1632
    • McDevitt, C.A.1    Collins, R.F.2    Conway, M.3    Modok, S.4    Storm, J.5    Kerr, I.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.