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Volumn 51, Issue 13, 2012, Pages 2852-2866

Evidence for modulatory sites at the lipid-protein interface of the human multidrug transporter P-glycoprotein

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC MODULATORS; ALLOSTERIC SITE; ATP HYDROLYSIS; ATPASE DOMAIN; COOH-TERMINAL; CYCLOSPORIN A; DRUG BINDING; DRUG MOLECULES; FUNCTIONAL DOMAINS; HIGHLY SENSITIVE; HOMOLOGY MODELING; INDEPENDENT MODE; MULTIDRUG TRANSPORTERS; P-GLYCOPROTEIN; POTENTIAL SITES; PROTEIN INTERFACES; RATIONAL DESIGN; SUBSTRATE BINDING; TRANSMEMBRANES; VERAPAMIL;

EID: 84859396429     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201479k     Document Type: Article
Times cited : (16)

References (72)
  • 1
    • 0024279163 scopus 로고
    • The multidrug-transporter: A double-edged sword
    • Gottesman, M. M. and Pastan, I. (1988) The multidrug-transporter: A double-edged sword J. Biol. Chem. 263, 12163-12166
    • (1988) J. Biol. Chem. , vol.263 , pp. 12163-12166
    • Gottesman, M.M.1    Pastan, I.2
  • 3
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr 1 (P-glycoprotein) gene from multidrug-resistant human cells
    • Chen, C.-j., Chin, J. E., Ueda, K., Clark, D. P., Pastan, I., Gottesman, M. M., and Roninson, I. B. (1986) Internal duplication and homology with bacterial transport proteins in the mdr 1 (P-glycoprotein) gene from multidrug-resistant human cells Cell 47, 381-389
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.-J.1    Chin, J.E.2    Ueda, K.3    Clark, D.P.4    Pastan, I.5    Gottesman, M.M.6    Roninson, I.B.7
  • 4
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman, M. M. and Pastan, I. (1993) Biochemistry of multidrug resistance mediated by the multidrug transporter Annu. Rev. Biochem. 62, 385-427
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 5
    • 36849079744 scopus 로고    scopus 로고
    • Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein
    • Zolnerciks, J. K., Wooding, C., and Linton, K. J. (2007) Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein FASEB J. 21, 3937-3948
    • (2007) FASEB J. , vol.21 , pp. 3937-3948
    • Zolnerciks, J.K.1    Wooding, C.2    Linton, K.J.3
  • 8
    • 0035805573 scopus 로고    scopus 로고
    • Defining the drug-binding site in the human multidrug resistance P- glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil
    • Loo, T. W. and Clarke, D. M. (2001) Defining the drug-binding site in the human multidrug resistance P- glycoprotein using a methanethiosulfonate analog of verapamil, MTS-verapamil J. Biol. Chem. 276, 14972-14979
    • (2001) J. Biol. Chem. , vol.276 , pp. 14972-14979
    • Loo, T.W.1    Clarke, D.M.2
  • 9
    • 0035813143 scopus 로고    scopus 로고
    • Determining the dimensions of the drug-binding domain of human P- glycoprotein using thiol cross-linking compounds as molecular rulers
    • Loo, T. W. and Clarke, D. M. (2001) Determining the dimensions of the drug-binding domain of human P- glycoprotein using thiol cross-linking compounds as molecular rulers J. Biol. Chem. 276, 36877-36880
    • (2001) J. Biol. Chem. , vol.276 , pp. 36877-36880
    • Loo, T.W.1    Clarke, D.M.2
  • 10
    • 0028229881 scopus 로고
    • Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides
    • Loo, T. W. and Clarke, D. M. (1994) Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides J. Biol. Chem. 269, 7750-7755
    • (1994) J. Biol. Chem. , vol.269 , pp. 7750-7755
    • Loo, T.W.1    Clarke, D.M.2
  • 11
    • 0007630205 scopus 로고
    • ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells
    • Horio, M., Gottesman, M. M., and Pastan, I. (1988) ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells Proc. Natl. Acad. Sci. U.S.A. 85, 3580-3584
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3580-3584
    • Horio, M.1    Gottesman, M.M.2    Pastan, I.3
  • 12
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • Ramachandra, M., Ambudkar, S. V., Chen, D., Hrycyna, C. A., Dey, S., Gottesman, M. M., and Pastan, I. (1998) Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state Biochemistry 37, 5010-5019
    • (1998) Biochemistry , vol.37 , pp. 5010-5019
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6    Pastan, I.7
  • 14
    • 0025059269 scopus 로고
    • Structural characteristics of compounds that modulate P-glycoprotein-associated multidrug resistance
    • Pearce, H. L., Winter, M. A., and Beck, W. T. (1990) Structural characteristics of compounds that modulate P-glycoprotein-associated multidrug resistance Adv. Enzyme Regul. 30, 357-373
    • (1990) Adv. Enzyme Regul. , vol.30 , pp. 357-373
    • Pearce, H.L.1    Winter, M.A.2    Beck, W.T.3
  • 15
    • 0026512425 scopus 로고
    • Rational design and pre-clinical pharmacology of drugs for reversing multidrug resistance
    • Hait, W. N. and Aftab, D. T. (1992) Rational design and pre-clinical pharmacology of drugs for reversing multidrug resistance Biochem. Pharmacol. 43, 103-107
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 103-107
    • Hait, W.N.1    Aftab, D.T.2
  • 16
    • 0026739494 scopus 로고
    • Structure-activity study and design of multidrug-resistant reversal compounds by a computer automated structure evaluation methodology
    • Klopman, G., Srivastava, S., Kolossvary, I., Epand, R. F., Ahmed, N., and Epand, R. M. (1992) Structure-activity study and design of multidrug-resistant reversal compounds by a computer automated structure evaluation methodology Cancer Res. 52, 4121-4129
    • (1992) Cancer Res. , vol.52 , pp. 4121-4129
    • Klopman, G.1    Srivastava, S.2    Kolossvary, I.3    Epand, R.F.4    Ahmed, N.5    Epand, R.M.6
  • 17
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Raviv, Y., Pollard, H. B., Bruggemann, E. P., Pastan, I., and Gottesman, M. M. (1990) Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells J. Biol. Chem. 265, 3975-3980
    • (1990) J. Biol. Chem. , vol.265 , pp. 3975-3980
    • Raviv, Y.1    Pollard, H.B.2    Bruggemann, E.P.3    Pastan, I.4    Gottesman, M.M.5
  • 18
    • 0030052748 scopus 로고    scopus 로고
    • P-glycoprotein confers methotrexate resistance in 3T6 cells with deficient carrier-mediated methotrexate uptake
    • de Graaf, D., Sharma, R. C., Mechetner, E. B., Schimke, R. T., and Roninson, I. B. (1996) P-glycoprotein confers methotrexate resistance in 3T6 cells with deficient carrier-mediated methotrexate uptake Proc. Natl. Acad. Sci. U.S.A. 93, 1238-1242
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1238-1242
    • De Graaf, D.1    Sharma, R.C.2    Mechetner, E.B.3    Schimke, R.T.4    Roninson, I.B.5
  • 19
    • 0030784559 scopus 로고    scopus 로고
    • Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membranes by P-glycoprotein
    • Shapiro, A. B. and Ling, V. (1997) Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membranes by P-glycoprotein Eur. J. Biochem. 250, 122-129
    • (1997) Eur. J. Biochem. , vol.250 , pp. 122-129
    • Shapiro, A.B.1    Ling, V.2
  • 20
    • 0032523929 scopus 로고    scopus 로고
    • Transport of LDS-751 from the cytoplasmic leaflet of the plasma membrane by the rhodamine-123-selective site of P-glycoprotein
    • Shapiro, A. B. and Ling, V. (1998) Transport of LDS-751 from the cytoplasmic leaflet of the plasma membrane by the rhodamine-123-selective site of P-glycoprotein Eur. J. Biochem. 254, 181-188
    • (1998) Eur. J. Biochem. , vol.254 , pp. 181-188
    • Shapiro, A.B.1    Ling, V.2
  • 21
    • 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, T. W. and Clarke, D. M. (1999) 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. 274, 24759-24765
    • (1999) J. Biol. Chem. , vol.274 , pp. 24759-24765
    • Loo, T.W.1    Clarke, D.M.2
  • 22
    • 47049101437 scopus 로고    scopus 로고
    • Mutational analysis of ABC proteins
    • Loo, T. W. and Clarke, D. M. (2008) Mutational analysis of ABC proteins Arch. Biochem. Biophys. 476, 51-64
    • (2008) Arch. Biochem. Biophys. , vol.476 , pp. 51-64
    • Loo, T.W.1    Clarke, D.M.2
  • 24
    • 13444266621 scopus 로고    scopus 로고
    • P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: A combined photoaffinity labeling-protein homology modeling approach
    • Pleban, K., Kopp, S., Csaszar, E., Peer, M., Hrebicek, T., Rizzi, A., Ecker, G. F., and Chiba, P. (2005) P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: A combined photoaffinity labeling-protein homology modeling approach Mol. Pharmacol. 67, 365-374
    • (2005) Mol. Pharmacol. , vol.67 , pp. 365-374
    • Pleban, K.1    Kopp, S.2    Csaszar, E.3    Peer, M.4    Hrebicek, T.5    Rizzi, A.6    Ecker, G.F.7    Chiba, P.8
  • 25
    • 75149147634 scopus 로고    scopus 로고
    • Multidrug efflux pumps: Drug binding - Gates or cavity?
    • Crowley, E. and Callaghan, R. (2010) Multidrug efflux pumps: Drug binding - gates or cavity? FEBS J. 277, 530-539
    • (2010) FEBS J. , vol.277 , pp. 530-539
    • Crowley, E.1    Callaghan, R.2
  • 27
    • 0032528254 scopus 로고    scopus 로고
    • Multidrug resistance transporter P-glycoprotein has distinct but interacting binding sites for cytotoxic drugs and reversing agents
    • Pascaud, C., Garrigos, M., and Orlowski, S. (1998) Multidrug resistance transporter P-glycoprotein has distinct but interacting binding sites for cytotoxic drugs and reversing agents Biochem. J. 333, 351-358
    • (1998) Biochem. J. , vol.333 , pp. 351-358
    • Pascaud, C.1    Garrigos, M.2    Orlowski, S.3
  • 29
    • 0038043182 scopus 로고    scopus 로고
    • Allosteric modulation of human P-glycoprotein. Inhibition of transport by preventing substrate translocation and dissociation
    • Maki, N., Hafkemeyer, P., and Dey, S. (2003) Allosteric modulation of human P-glycoprotein. Inhibition of transport by preventing substrate translocation and dissociation J. Biol. Chem. 278, 18132-18139
    • (2003) J. Biol. Chem. , vol.278 , pp. 18132-18139
    • Maki, N.1    Hafkemeyer, P.2    Dey, S.3
  • 30
    • 0029797074 scopus 로고    scopus 로고
    • Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a Vaccinia -based transient expression system
    • Ramachandra, M., Ambudkar, S. V., Gottesman, M. M., Pastan, I., and Hrycyna, C. A. (1996) Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a Vaccinia -based transient expression system Mol. Biol. Cell 7, 1485-1498
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1485-1498
    • Ramachandra, M.1    Ambudkar, S.V.2    Gottesman, M.M.3    Pastan, I.4    Hrycyna, C.A.5
  • 34
    • 0026722467 scopus 로고
    • Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase
    • Sarkadi, B., Price, E. M., Boucher, R. C., Germann, U. A., and Scarborough, G. A. (1992) Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase J. Biol. Chem. 267, 4854-4858
    • (1992) J. Biol. Chem. , vol.267 , pp. 4854-4858
    • Sarkadi, B.1    Price, E.M.2    Boucher, R.C.3    Germann, U.A.4    Scarborough, G.A.5
  • 35
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • Hirokawa, T., Boon-Chieng, S., and Mitaku, S. (1998) SOSUI: Classification and secondary structure prediction system for membrane proteins Bioinformatics 14, 378-379
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 36
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • Rost, B. (1996) PHD: Predicting one-dimensional protein structure by profile-based neural networks Methods Enzymol. 266, 525-539
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 37
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady, G. E. and Simon, I. (2001) The HMMTOP transmembrane topology prediction server Bioinformatics 17, 849-850
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 38
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 39
    • 0027264995 scopus 로고
    • Predicting the topology of eukaryotic membrane proteins
    • Sipos, L. and von Heijne, G. (1993) Predicting the topology of eukaryotic membrane proteins Eur. J. Biochem. 213, 1333-1340
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1333-1340
    • Sipos, L.1    Von Heijne, G.2
  • 40
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne, G. (1994) Membrane proteins: From sequence to structure Annu. Rev. Biophys. Biomol. Struct. 23, 167-192
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 167-192
    • Von Heijne, G.1
  • 42
    • 33747184794 scopus 로고    scopus 로고
    • Prediction of transmembrane helix orientation in polytopic membrane proteins
    • Adamian, L. and Liang, J. (2006) Prediction of transmembrane helix orientation in polytopic membrane proteins BMC Struct. Biol. 6, 13
    • (2006) BMC Struct. Biol. , vol.6 , pp. 13
    • Adamian, L.1    Liang, J.2
  • 43
    • 33744942933 scopus 로고    scopus 로고
    • Biochemical and pharmacological properties of an allosteric modulator site of the human P-glycoprotein (ABCB1)
    • Maki, N. and Dey, S. (2006) Biochemical and pharmacological properties of an allosteric modulator site of the human P-glycoprotein (ABCB1) Biochem. Pharmacol. 72, 145-155
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 145-155
    • Maki, N.1    Dey, S.2
  • 44
    • 0030791978 scopus 로고    scopus 로고
    • Structure-activity relationships of P-glycoprotein interacting drugs: Kinetic characterization of their effects on ATPase activity
    • Litman, T., Zeuthen, T., Skovsgaard, T., and Stein, W. D. (1997) Structure-activity relationships of P-glycoprotein interacting drugs: Kinetic characterization of their effects on ATPase activity Biochim. Biophys. Acta 1361, 159-168
    • (1997) Biochim. Biophys. Acta , vol.1361 , pp. 159-168
    • Litman, T.1    Zeuthen, T.2    Skovsgaard, T.3    Stein, W.D.4
  • 45
    • 0026662530 scopus 로고
    • Partial purification and reconstitution of the human multidrug-resistance pump: Characterization of the drug-stimulatable ATP hydrolysis
    • Ambudkar, S. V., Lelong, I. H., Zhang, J., Cardarelli, C. O., Gottesman, M. M., and Pastan, I. (1992) Partial purification and reconstitution of the human multidrug-resistance pump: Characterization of the drug-stimulatable ATP hydrolysis Proc. Natl. Acad. Sci. U.S.A. 89, 8472-8476
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8472-8476
    • Ambudkar, S.V.1    Lelong, I.H.2    Zhang, J.3    Cardarelli, C.O.4    Gottesman, M.M.5    Pastan, I.6
  • 46
    • 0032562795 scopus 로고    scopus 로고
    • Drug-stimulated nucleotide trapping in the human multidrug transporter MDR1. Cooperation of the nucleotide binding domains
    • Szabó, K., Welker, E., Bakos, Müller, M., Roninson, I., Váradi, A., and Sarkadi, B. (1998) Drug-stimulated nucleotide trapping in the human multidrug transporter MDR1. Cooperation of the nucleotide binding domains J. Biol. Chem. 273, 10132-10138
    • (1998) J. Biol. Chem. , vol.273 , pp. 10132-10138
    • Szabó, K.1    Welker, E.2    Bakos3    Müller, M.4    Roninson, I.5    Váradi, A.6    Sarkadi, B.7
  • 47
    • 0033580634 scopus 로고    scopus 로고
    • A single amino acid residue contributes to distinct mechanisms of inhibition of the human multidrug transporter by stereoisomers of the dopamine receptor antagonist flupentixol
    • Dey, S., Hafkemeyer, P., Pastan, I., and Gottesman, M. M. (1999) A single amino acid residue contributes to distinct mechanisms of inhibition of the human multidrug transporter by stereoisomers of the dopamine receptor antagonist flupentixol Biochemistry 38, 6630-6639
    • (1999) Biochemistry , vol.38 , pp. 6630-6639
    • Dey, S.1    Hafkemeyer, P.2    Pastan, I.3    Gottesman, M.M.4
  • 48
    • 33644538904 scopus 로고    scopus 로고
    • Modulator-Induced Interference in Functional Cross Talk between the Substrate and the ATP Sites of Human P-glycoprotein
    • Maki, N., Moitra, K., Silver, C., Ghosh, P., Chattopadhyay, A., and Dey, S. (2006) Modulator-Induced Interference in Functional Cross Talk between the Substrate and the ATP Sites of Human P-glycoprotein Biochemistry 45, 2739-2751
    • (2006) Biochemistry , vol.45 , pp. 2739-2751
    • Maki, N.1    Moitra, K.2    Silver, C.3    Ghosh, P.4    Chattopadhyay, A.5    Dey, S.6
  • 49
    • 0024421664 scopus 로고
    • Reversal mechanism of multidrug resistance by verapamil: Direct binding of verapamil to P-glycoprotein on specific sites and transport of verapamil outward across the plasma membrane of K562/ADM cells
    • Yusa, K. and Tsuruo, T. (1989) Reversal mechanism of multidrug resistance by verapamil: Direct binding of verapamil to P-glycoprotein on specific sites and transport of verapamil outward across the plasma membrane of K562/ADM cells Cancer Res. 49, 5002-5006
    • (1989) Cancer Res. , vol.49 , pp. 5002-5006
    • Yusa, K.1    Tsuruo, T.2
  • 50
    • 0037160075 scopus 로고    scopus 로고
    • A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein
    • Omote, H. and Al-Shawi, M. K. (2002) A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein J. Biol. Chem. 277, 45688-45694
    • (2002) J. Biol. Chem. , vol.277 , pp. 45688-45694
    • Omote, H.1    Al-Shawi, M.K.2
  • 51
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson, R. J. and Locher, K. P. (2007) Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP FEBS Lett. 581, 935-938
    • (2007) FEBS Lett. , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 52
    • 14644425991 scopus 로고    scopus 로고
    • Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"?
    • Loo, T. W. and Clarke, D. M. (2005) Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"? Biochem. Biophys. Res. Commun. 329, 419-422
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 419-422
    • Loo, T.W.1    Clarke, D.M.2
  • 53
    • 32044453808 scopus 로고    scopus 로고
    • Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux
    • Loo, T. W. and Clarke, D. M. (2005) Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux J. Membr. Biol. 206, 173-185
    • (2005) J. Membr. Biol. , vol.206 , pp. 173-185
    • Loo, T.W.1    Clarke, D.M.2
  • 54
    • 33646855552 scopus 로고    scopus 로고
    • Allosteric modulation of the human P-glycoprotein involves conformational changes mimicking catalytic transition intermediates
    • Ghosh, P., Moitra, K., Maki, N., and Dey, S. (2006) Allosteric modulation of the human P-glycoprotein involves conformational changes mimicking catalytic transition intermediates Arch. Biochem. Biophys. 450, 100-112
    • (2006) Arch. Biochem. Biophys. , vol.450 , pp. 100-112
    • Ghosh, P.1    Moitra, K.2    Maki, N.3    Dey, S.4
  • 55
    • 33744964346 scopus 로고    scopus 로고
    • Allosteric modulation bypasses the requirement for ATP hydrolysis in regenerating low affinity transition state conformation of human P-glycoprotein
    • Maki, N., Moitra, K., Ghosh, P., and Dey, S. (2006) Allosteric modulation bypasses the requirement for ATP hydrolysis in regenerating low affinity transition state conformation of human P-glycoprotein J. Biol. Chem. 281, 10769-10777
    • (2006) J. Biol. Chem. , vol.281 , pp. 10769-10777
    • Maki, N.1    Moitra, K.2    Ghosh, P.3    Dey, S.4
  • 56
    • 0027418815 scopus 로고
    • Human P-Glycoprotein transports Cyclosporin-A and FK506
    • Saeki, T., Ueda, K., Tanigawara, Y., Hori, R., and Komano, T. (1993) Human P-Glycoprotein transports Cyclosporin-A and FK506 J. Biol. Chem. 268, 6077-6080
    • (1993) J. Biol. Chem. , vol.268 , pp. 6077-6080
    • Saeki, T.1    Ueda, K.2    Tanigawara, Y.3    Hori, R.4    Komano, T.5
  • 57
    • 0034858151 scopus 로고    scopus 로고
    • Identification and localization of three photobinding sites of iodoarylazidoprazosin in hamster P-glycoprotein
    • Isenberg, B., Thole, H., Tummler, B., and Demmer, A. (2001) Identification and localization of three photobinding sites of iodoarylazidoprazosin in hamster P-glycoprotein Eur. J. Biochem. 268, 2629-2634
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2629-2634
    • Isenberg, B.1    Thole, H.2    Tummler, B.3    Demmer, A.4
  • 58
    • 0031041385 scopus 로고    scopus 로고
    • Multidrug-resistant human sarcoma cells with a mutant P-glycoprotein, altered phenotype, and resistance to cyclosporins
    • Chen, G., Duran, G. E., Steger, K. A., Lacayo, N. J., Jaffrezou, J. P., Dumontet, C., and Sikic, B. I. (1997) Multidrug-resistant human sarcoma cells with a mutant P-glycoprotein, altered phenotype, and resistance to cyclosporins J. Biol. Chem. 272, 5974-5982
    • (1997) J. Biol. Chem. , vol.272 , pp. 5974-5982
    • Chen, G.1    Duran, G.E.2    Steger, K.A.3    Lacayo, N.J.4    Jaffrezou, J.P.5    Dumontet, C.6    Sikic, B.I.7
  • 59
    • 0032559001 scopus 로고    scopus 로고
    • Identification of the cyclosporin-binding site in P-glycoprotein
    • Demeule, M., Laplante, A., Murphy, G. F., Wenger, R. M., and Beliveau, R. (1998) Identification of the cyclosporin-binding site in P-glycoprotein Biochemistry 37, 18110-18118
    • (1998) Biochemistry , vol.37 , pp. 18110-18118
    • Demeule, M.1    Laplante, A.2    Murphy, G.F.3    Wenger, R.M.4    Beliveau, R.5
  • 60
    • 0347379911 scopus 로고    scopus 로고
    • Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2003) Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites J. Biol. Chem. 278, 50136-50141
    • (2003) J. Biol. Chem. , vol.278 , pp. 50136-50141
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 61
    • 0037113961 scopus 로고    scopus 로고
    • Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein
    • Loo, T. W. and Clarke, D. M. (2002) Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein J. Biol. Chem. 277, 44332-44338
    • (2002) J. Biol. Chem. , vol.277 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 62
    • 77951905043 scopus 로고    scopus 로고
    • Determinants of specificity at the protein-lipid interface in membranes
    • Ernst, A. M., Contreras, F. X., Brugger, B., and Wieland, F. (2010) Determinants of specificity at the protein-lipid interface in membranes FEBS Lett. 584, 1713-1720
    • (2010) FEBS Lett. , vol.584 , pp. 1713-1720
    • Ernst, A.M.1    Contreras, F.X.2    Brugger, B.3    Wieland, F.4
  • 63
    • 0035834626 scopus 로고    scopus 로고
    • The lipid/protein interface as xenobiotic target site: Kinetic analysis of the nicotinic acetylcholine receptor
    • Walcher, S., Altschuh, J., and Sandermann, H., Jr. (2001) The lipid/protein interface as xenobiotic target site: Kinetic analysis of the nicotinic acetylcholine receptor J. Biol. Chem. 276, 42191-42195
    • (2001) J. Biol. Chem. , vol.276 , pp. 42191-42195
    • Walcher, S.1    Altschuh, J.2    Sandermann Jr., H.3
  • 64
    • 9644294471 scopus 로고    scopus 로고
    • Structural basis for lipid modulation of nicotinic acetylcholine receptor function
    • Barrantes, F. J. (2004) Structural basis for lipid modulation of nicotinic acetylcholine receptor function Brain Res. Brain Res. Rev. 47, 71-95
    • (2004) Brain Res. Brain Res. Rev. , vol.47 , pp. 71-95
    • Barrantes, F.J.1
  • 65
    • 0027230908 scopus 로고
    • Quinacrine and ethidium bind to different loci on the Torpedo acetylcholine receptor
    • Arias, H. R., Valenzuela, C. F., and Johnson, D. A. (1993) Quinacrine and ethidium bind to different loci on the Torpedo acetylcholine receptor Biochemistry 32, 6237-6242
    • (1993) Biochemistry , vol.32 , pp. 6237-6242
    • Arias, H.R.1    Valenzuela, C.F.2    Johnson, D.A.3
  • 66
    • 0026704565 scopus 로고
    • Site-specific mutations of nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating
    • Li, L., Lee, Y. H., Pappone, P., Palma, A., and McNamee, M. G. (1992) Site-specific mutations of nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating Biophys. J. 62, 61-63
    • (1992) Biophys. J. , vol.62 , pp. 61-63
    • Li, L.1    Lee, Y.H.2    Pappone, P.3    Palma, A.4    McNamee, M.G.5
  • 67
    • 0031595748 scopus 로고    scopus 로고
    • Mutations at lipid-exposed residues of the acetylcholine receptor affect its gating kinetics
    • Bouzat, C., Roccamo, A. M., Garbus, I., and Barrantes, F. J. (1998) Mutations at lipid-exposed residues of the acetylcholine receptor affect its gating kinetics Mol. Pharmacol. 54, 146-153
    • (1998) Mol. Pharmacol. , vol.54 , pp. 146-153
    • Bouzat, C.1    Roccamo, A.M.2    Garbus, I.3    Barrantes, F.J.4
  • 68
    • 0026733435 scopus 로고
    • Quinacrine binds to the lipid-protein interface of the Torpedo acetylcholine receptor: A fluorescence study
    • Valenzuela, C. F., Kerr, J. A., and Johnson, D. A. (1992) Quinacrine binds to the lipid-protein interface of the Torpedo acetylcholine receptor: A fluorescence study J. Biol. Chem. 267, 8238-8244
    • (1992) J. Biol. Chem. , vol.267 , pp. 8238-8244
    • Valenzuela, C.F.1    Kerr, J.A.2    Johnson, D.A.3
  • 70
    • 58149170576 scopus 로고    scopus 로고
    • Interaction of the P-glycoprotein multidrug efflux pump with cholesterol: Effects on ATPase activity, drug binding and transport
    • Eckford, P. D. and Sharom, F. J. (2008) Interaction of the P-glycoprotein multidrug efflux pump with cholesterol: Effects on ATPase activity, drug binding and transport Biochemistry 47, 13686-13698
    • (2008) Biochemistry , vol.47 , pp. 13686-13698
    • Eckford, P.D.1    Sharom, F.J.2
  • 71
    • 13844315498 scopus 로고    scopus 로고
    • Homology modeling of a human glycine α1 receptor reveals a plausible anesthetic binding site
    • Bertaccini, E. J., Shapiro, J., Brutlag, D. L., and Trudell, J. R. (2005) Homology modeling of a human glycine α1 receptor reveals a plausible anesthetic binding site J. Chem. Inf. Model. 45, 128-135
    • (2005) J. Chem. Inf. Model. , vol.45 , pp. 128-135
    • Bertaccini, E.J.1    Shapiro, J.2    Brutlag, D.L.3    Trudell, J.R.4
  • 72
    • 0035027558 scopus 로고    scopus 로고
    • Characterization of the dizocilpine binding site on the nicotinic acetylcholine receptor
    • Arias, H. R., McCardy, E. A., and Blanton, M. P. (2001) Characterization of the dizocilpine binding site on the nicotinic acetylcholine receptor Mol. Pharmacol. 59, 1051-1060
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1051-1060
    • Arias, H.R.1    McCardy, E.A.2    Blanton, M.P.3


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