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Volumn 55, Issue 1, 2007, Pages 1-15

A primer on the mechanics of P-glycoprotein the multidrug transporter

Author keywords

ABC transporter; Drug transport; Multidrug resistance; P glycoprotein

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALDOSTERONE; AMPRENAVIR; COLCHICINE; CYCLOSPORIN A; DACTINOMYCIN; DAUNORUBICIN; DEXAMETHASONE; DIGOXIN; DOMPERIDONE; DOXORUBICIN; ELACRIDAR; ETOPOSIDE; GLYCOPROTEIN P; HYDROCORTISONE; INDINAVIR; LOPERAMIDE; MEVINOLIN; MIFEPRISTONE; NELFINAVIR; OC 144 09; ONDANSETRON; PACLITAXEL; QUINIDINE; RITONAVIR; SAQUINAVIR; TACROLIMUS; TARIQUIDAR; TENIPOSIDE; TERFENADINE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALSPODAR; VERAPAMIL; VINBLASTINE; VINCRISTINE; ZOSUQUIDAR;

EID: 33846215616     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2006.10.007     Document Type: Review
Times cited : (185)

References (200)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: from microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Annu Rev Cell Biol 8 (1992) 67-113
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 0027458116 scopus 로고
    • ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance
    • Doige C.A., and Ames G.F.L. ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance. Annu Rev Microbiol 47 (1993) 291-319
    • (1993) Annu Rev Microbiol , vol.47 , pp. 291-319
    • Doige, C.A.1    Ames, G.F.L.2
  • 3
    • 0034953105 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • Dean M., Hamon Y., and Chimini G. The human ATP-binding cassette (ABC) transporter superfamily. J Lipid Res 42 (2001) 1007-1017
    • (2001) J Lipid Res , vol.42 , pp. 1007-1017
    • Dean, M.1    Hamon, Y.2    Chimini, G.3
  • 4
    • 0023638508 scopus 로고
    • Localisation of the human multiple drug resistance gene, MDR1, to 7q21.1
    • Callen D.F., Baker E., Simmers R.N., Seshadri R., and Roninson I.B. Localisation of the human multiple drug resistance gene, MDR1, to 7q21.1. Hum Genet 77 (1987) 142-144
    • (1987) Hum Genet , vol.77 , pp. 142-144
    • Callen, D.F.1    Baker, E.2    Simmers, R.N.3    Seshadri, R.4    Roninson, I.B.5
  • 5
    • 0024414605 scopus 로고
    • Structure and expression of the human MDR (P-glycoprotein) gene family
    • Chin J.E., Soffir R., Noonan K.E., Choi K., and Roninson I.B. Structure and expression of the human MDR (P-glycoprotein) gene family. Mol Cell Biol 9 (1989) 3808-3820
    • (1989) Mol Cell Biol , vol.9 , pp. 3808-3820
    • Chin, J.E.1    Soffir, R.2    Noonan, K.E.3    Choi, K.4    Roninson, I.B.5
  • 6
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: a physiological role for the mdr2 gene
    • Ruetz S., and Gros P. Phosphatidylcholine translocase: a physiological role for the mdr2 gene. Cell 77 (1994) 1071-1081
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 7
    • 0027363563 scopus 로고
    • Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absences of phospholipid from bile and to liver disease
    • Smit J.J.M., Schinkel A.H., Oude Elferink R.P., Groen A.K., Wagenaar E., van Deemter L., et al. Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absences of phospholipid from bile and to liver disease. Cell 75 (1993) 451-462
    • (1993) Cell , vol.75 , pp. 451-462
    • Smit, J.J.M.1    Schinkel, A.H.2    Oude Elferink, R.P.3    Groen, A.K.4    Wagenaar, E.5    van Deemter, L.6
  • 8
    • 0034604707 scopus 로고    scopus 로고
    • MDR3 glycoprotein, a phosphatidylcholine translocase, transports several cytotoxic drugs and directly interacts with drugs as judged by interference with nucleotide trapping
    • Smith A.J., van Helvoort A., van Meer G., Szabo K., Welker E., Szakacs G., et al. MDR3 glycoprotein, a phosphatidylcholine translocase, transports several cytotoxic drugs and directly interacts with drugs as judged by interference with nucleotide trapping. J Biol Chem 275 (2000) 23530-23539
    • (2000) J Biol Chem , vol.275 , pp. 23530-23539
    • Smith, A.J.1    van Helvoort, A.2    van Meer, G.3    Szabo, K.4    Welker, E.5    Szakacs, G.6
  • 9
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano R.L., and Ling V. A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim Biophys Acta 455 (1976) 152-162
    • (1976) Biochim Biophys Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 10
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells
    • Chen C.J., Chin J.E., Ueda K., Clark D.P., Pastan I., Gottesman M.M., et al. Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell 47 (1986) 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
  • 11
    • 0034212332 scopus 로고    scopus 로고
    • The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
    • van Veen H.W., Margolles A., Muller M., Higgins C.F., and Konings W.N. The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism. EMBO J 19 (2000) 2503-2514
    • (2000) EMBO J , vol.19 , pp. 2503-2514
    • van Veen, H.W.1    Margolles, A.2    Muller, M.3    Higgins, C.F.4    Konings, W.N.5
  • 12
    • 0032601621 scopus 로고    scopus 로고
    • Merck Frosst Award Lecture 1998. Molecular dissection of the human multidrug resistance P-glycoprotein
    • Loo T.W., and Clarke D.M. Merck Frosst Award Lecture 1998. Molecular dissection of the human multidrug resistance P-glycoprotein. Biochem Cell Biol 77 (1999) 11-23
    • (1999) Biochem Cell Biol , vol.77 , pp. 11-23
    • Loo, T.W.1    Clarke, D.M.2
  • 13
    • 0027408359 scopus 로고
    • N-glycosylation and deletion mutants of the human MDR-1 P-glycoprotein
    • Schinkel A.H., Kemp S., Dolle M., Rudenko G., and Wagenaar E. N-glycosylation and deletion mutants of the human MDR-1 P-glycoprotein. J Biol Chem 268 (1993) 7474-7481
    • (1993) J Biol Chem , vol.268 , pp. 7474-7481
    • Schinkel, A.H.1    Kemp, S.2    Dolle, M.3    Rudenko, G.4    Wagenaar, E.5
  • 14
    • 0022534951 scopus 로고
    • A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria
    • Higgins C.F., Hiles I.D., Salmond G.P.C., Gill D.R., Downie J.A., Evans I.J., et al. A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria. Nature 323 (1986) 448-450
    • (1986) Nature , vol.323 , pp. 448-450
    • Higgins, C.F.1    Hiles, I.D.2    Salmond, G.P.C.3    Gill, D.R.4    Downie, J.A.5    Evans, I.J.6
  • 15
    • 0025374695 scopus 로고
    • Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport
    • Hyde S.C., Emsley P., Hartshorn M.J., Mimmack M.M., Gileadi U., Pearce S.R., et al. Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport. Nature 346 (1990) 362-365
    • (1990) Nature , vol.346 , pp. 362-365
    • Hyde, S.C.1    Emsley, P.2    Hartshorn, M.J.3    Mimmack, M.M.4    Gileadi, U.5    Pearce, S.R.6
  • 16
    • 0024779132 scopus 로고
    • P-glycoprotein: multi-drug-resistance and a superfamily of membrane-associated transport proteins
    • Juranka P.F., Zastawny R.L., and Ling V. P-glycoprotein: multi-drug-resistance and a superfamily of membrane-associated transport proteins. FASEB J 3 (1989) 2583-2592
    • (1989) FASEB J , vol.3 , pp. 2583-2592
    • Juranka, P.F.1    Zastawny, R.L.2    Ling, V.3
  • 17
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo T.W., and Clarke D.M. Membrane topology of a cysteine-less mutant of human P-glycoprotein. J Biol Chem 270 (1995) 843-848
    • (1995) J Biol Chem , vol.270 , pp. 843-848
    • Loo, T.W.1    Clarke, D.M.2
  • 18
    • 0028950653 scopus 로고
    • Membrane topology of P-glycoprotein as determined by epitope insertion: transmembrane organization of the N-terminal domain of mdr3
    • Kast C., Canfield V., Levenson R., and Gros P. Membrane topology of P-glycoprotein as determined by epitope insertion: transmembrane organization of the N-terminal domain of mdr3. Biochemistry 34 (1995) 4402-4411
    • (1995) Biochemistry , vol.34 , pp. 4402-4411
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 19
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., and Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1 (1982) 945-951
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 20
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton K.J., and Higgins C.F. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol Microbiol 28 (1998) 5-13
    • (1998) Mol Microbiol , vol.28 , pp. 5-13
    • Linton, K.J.1    Higgins, C.F.2
  • 22
    • 33745174833 scopus 로고    scopus 로고
    • The conserved tyrosine residues 401 and 1044 in ATP sites of human P-glycoprotein are critical for ATP binding and hydrolysis: evidence for a conserved subdomain, the A-loop in the ATP-binding cassette
    • Kim I.W., Peng X.H., Sauna Z.E., FitzGerald P.C., Xia D., Muller M., et al. The conserved tyrosine residues 401 and 1044 in ATP sites of human P-glycoprotein are critical for ATP binding and hydrolysis: evidence for a conserved subdomain, the A-loop in the ATP-binding cassette. Biochemistry 45 (2006) 7605-7616
    • (2006) Biochemistry , vol.45 , pp. 7605-7616
    • Kim, I.W.1    Peng, X.H.2    Sauna, Z.E.3    FitzGerald, P.C.4    Xia, D.5    Muller, M.6
  • 23
    • 0036829647 scopus 로고    scopus 로고
    • The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing Walker A sequence
    • Loo T.W., Bartlett M.C., and Clarke D.M. The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing Walker A sequence. J Biol Chem 277 (2002) 41303-41306
    • (2002) J Biol Chem , vol.277 , pp. 41303-41306
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 24
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., Thomas P.J., et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10 (2002) 139-149
    • (2002) Mol Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6
  • 25
    • 31844443618 scopus 로고    scopus 로고
    • The A-loop a conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding
    • Ambudkar S.V., Kim I.W., Xia D., and Sauna Z.E. The A-loop a conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding. FEBS Lett 580 (2006) 1049-1055
    • (2006) FEBS Lett , vol.580 , pp. 1049-1055
    • Ambudkar, S.V.1    Kim, I.W.2    Xia, D.3    Sauna, Z.E.4
  • 27
    • 0024307162 scopus 로고
    • Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance
    • Azzaria M., Schurr E., and Gros P. Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance. Mol Cell Biol 9 (1989) 5289-5297
    • (1989) Mol Cell Biol , vol.9 , pp. 5289-5297
    • Azzaria, M.1    Schurr, E.2    Gros, P.3
  • 28
    • 0034700265 scopus 로고    scopus 로고
    • Mutational analysis of conserved carboxylate residues in the nucleotide binding sites of P-glycoprotein
    • Urbatsch I.L., Julien M., Carrier I., Rousseau M.E., Cayrol R., and Gros P. Mutational analysis of conserved carboxylate residues in the nucleotide binding sites of P-glycoprotein. Biochemistry 39 (2000) 14138-14149
    • (2000) Biochemistry , vol.39 , pp. 14138-14149
    • Urbatsch, I.L.1    Julien, M.2    Carrier, I.3    Rousseau, M.E.4    Cayrol, R.5    Gros, P.6
  • 29
    • 21844451868 scopus 로고    scopus 로고
    • The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment
    • Rothnie A., Storm J., McMahon R., Taylor A., Kerr I.D., and Callaghan R. The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment. FEBS Lett 579 (2005) 3984-3990
    • (2005) FEBS Lett , vol.579 , pp. 3984-3990
    • Rothnie, A.1    Storm, J.2    McMahon, R.3    Taylor, A.4    Kerr, I.D.5    Callaghan, R.6
  • 30
    • 0034601811 scopus 로고    scopus 로고
    • Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein
    • Urbatsch I.L., Gimi K., Wilke-Mounts S., and Senior A.E. Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein. Biochemistry 39 (2000) 11921-11927
    • (2000) Biochemistry , vol.39 , pp. 11921-11927
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 31
    • 0029784872 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted P-glycoprotein. A fourier transform attenuated total reflection infrared spectroscopy analysis
    • Sonveaux N., Shapiro A.B., Goormaghtigh E., Ling V., and Ruysschaert J.-M. Secondary and tertiary structure changes of reconstituted P-glycoprotein. A fourier transform attenuated total reflection infrared spectroscopy analysis. J Biol Chem 271 (1996) 24617-24624
    • (1996) J Biol Chem , vol.271 , pp. 24617-24624
    • Sonveaux, N.1    Shapiro, A.B.2    Goormaghtigh, E.3    Ling, V.4    Ruysschaert, J.-M.5
  • 32
    • 0032574948 scopus 로고    scopus 로고
    • Secondary structure of P-glycoprotein investigated by circular dichroism and amino acid sequence analysis
    • Dong M., Ladaviere L., Penin F., Deleage G., and Baggetto L.G. Secondary structure of P-glycoprotein investigated by circular dichroism and amino acid sequence analysis. Biochim Biophys Acta 1371 (1998) 317-334
    • (1998) Biochim Biophys Acta , vol.1371 , pp. 317-334
    • Dong, M.1    Ladaviere, L.2    Penin, F.3    Deleage, G.4    Baggetto, L.G.5
  • 33
    • 0029896988 scopus 로고    scopus 로고
    • Mutational analysis of the predicted first transmembrane segment of each homologous half of human P-glycoprotein suggests that they are symmetrically arranged in the membrane
    • Loo T.W., and Clark D.P. Mutational analysis of the predicted first transmembrane segment of each homologous half of human P-glycoprotein suggests that they are symmetrically arranged in the membrane. J Biol Chem 271 (1996) 15414-15419
    • (1996) J Biol Chem , vol.271 , pp. 15414-15419
    • Loo, T.W.1    Clark, D.P.2
  • 34
    • 0029909604 scopus 로고    scopus 로고
    • Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates
    • Loo T.W., and Clark D.P. Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates. J Biol Chem 271 (1996) 27482-27487
    • (1996) J Biol Chem , vol.271 , pp. 27482-27487
    • Loo, T.W.1    Clark, D.P.2
  • 35
    • 0032700184 scopus 로고    scopus 로고
    • Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques
    • Loo T.W., and Clarke D.M. Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques. Biochim Biophys Acta 1461 (1999) 315-325
    • (1999) Biochim Biophys Acta , vol.1461 , pp. 315-325
    • Loo, T.W.1    Clarke, D.M.2
  • 36
    • 0642272487 scopus 로고    scopus 로고
    • An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulphide cross-linking and homology modelling
    • Stenham D.R., Campbell J.D., Sansom M.S.P., Higgins C.F., Kerr I.D., and Linton K.J. An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulphide cross-linking and homology modelling. FASEB J 17 (2003) 2287-2289
    • (2003) FASEB J , vol.17 , pp. 2287-2289
    • Stenham, D.R.1    Campbell, J.D.2    Sansom, M.S.P.3    Higgins, C.F.4    Kerr, I.D.5    Linton, K.J.6
  • 37
    • 1542320036 scopus 로고    scopus 로고
    • Disulphide cross-linking analysis shows that transmembrane segments 5 and 8 of human P-glycoprotein are close together on the cytoplasmic side of the membrane
    • Loo T.W., Bartlett M.C., and Clarke D.M. Disulphide cross-linking analysis shows that transmembrane segments 5 and 8 of human P-glycoprotein are close together on the cytoplasmic side of the membrane. J Biol Chem 279 (2004) 7692-7697
    • (2004) J Biol Chem , vol.279 , pp. 7692-7697
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 38
    • 2442597224 scopus 로고    scopus 로고
    • Val133 and Cys137 in transmembrane segment 2 are close to Arg935 and Gly939 in transmembrane segment 11 of human P-glycoprotein
    • Loo T.W., Bartlett M.C., and Clarke D.M. Val133 and Cys137 in transmembrane segment 2 are close to Arg935 and Gly939 in transmembrane segment 11 of human P-glycoprotein. J Biol Chem 279 (2004) 18232-18238
    • (2004) J Biol Chem , vol.279 , pp. 18232-18238
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 39
    • 0031786405 scopus 로고    scopus 로고
    • A new structural model for P-glycoprotein
    • Jones P.M., and George A.M. A new structural model for P-glycoprotein. J Membr Biol 166 (1998) 133-147
    • (1998) J Membr Biol , vol.166 , pp. 133-147
    • Jones, P.M.1    George, A.M.2
  • 40
    • 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., et al. 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 (2005) 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
  • 41
    • 13244292479 scopus 로고    scopus 로고
    • Three-dimensional structure of P-glycoprotein. The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state
    • Rosenberg M.F., Callaghan R., Modok S., Higgins C.F., and Ford R.C. Three-dimensional structure of P-glycoprotein. The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state. J Biol Chem 280 (2005) 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
  • 42
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang G., and Roth C.B. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293 (2001) 1793-1800
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 43
    • 18644363550 scopus 로고    scopus 로고
    • Structure of the ABC transporter MsbA in complex with ADP, vanadate and lipopolysaccharide
    • Reyes C.L., and Chang G. Structure of the ABC transporter MsbA in complex with ADP, vanadate and lipopolysaccharide. Science 308 (2005) 1028-1031
    • (2005) Science , vol.308 , pp. 1028-1031
    • Reyes, C.L.1    Chang, G.2
  • 44
    • 0030971840 scopus 로고    scopus 로고
    • Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis
    • Rosenberg M.F., Callaghan R., Ford R.C., and Higgins C.F. Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J Biol Chem 272 (1997) 10685-10694
    • (1997) J Biol Chem , vol.272 , pp. 10685-10694
    • Rosenberg, M.F.1    Callaghan, R.2    Ford, R.C.3    Higgins, C.F.4
  • 45
    • 17944370228 scopus 로고    scopus 로고
    • Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle
    • Rosenberg M.F., Velarde G., Ford R.C., Martin C., Berridge G., Kerr I.D., et al. Repacking of the transmembrane domains of P-glycoprotein during the transport ATPase cycle. EMBO J 20 (2001) 5615-5625
    • (2001) EMBO J , vol.20 , pp. 5615-5625
    • Rosenberg, M.F.1    Velarde, G.2    Ford, R.C.3    Martin, C.4    Berridge, G.5    Kerr, I.D.6
  • 46
    • 0037131184 scopus 로고    scopus 로고
    • Projection structure of P-glycoprotein by electron microscopy. Evidence for a closed conformation of the nucleotide binding domains
    • Lee J.-Y., Urbatsch I.L., Senior A.E., and Wilkens S. Projection structure of P-glycoprotein by electron microscopy. Evidence for a closed conformation of the nucleotide binding domains. J Biol Chem 277 (2002) 40125-40131
    • (2002) J Biol Chem , vol.277 , pp. 40125-40131
    • Lee, J.-Y.1    Urbatsch, I.L.2    Senior, A.E.3    Wilkens, S.4
  • 47
    • 0031455482 scopus 로고    scopus 로고
    • The P-glycoprotein efflux pump: how does it transport drugs?
    • Sharom F.J. The P-glycoprotein efflux pump: how does it transport drugs?. J Membr Biol 160 (1997) 161-175
    • (1997) J Membr Biol , vol.160 , pp. 161-175
    • Sharom, F.J.1
  • 48
    • 0032518394 scopus 로고    scopus 로고
    • A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene
    • van Veen H.W., Callaghan R., Soceneantu L., Sardini A., Konings W.N., and Higgins C.F. A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene. Nature 391 (1998) 291-295
    • (1998) Nature , vol.391 , pp. 291-295
    • van Veen, H.W.1    Callaghan, R.2    Soceneantu, L.3    Sardini, A.4    Konings, W.N.5    Higgins, C.F.6
  • 49
    • 0027432409 scopus 로고
    • Fluorescent cellular indicators are extruded by the multidrug resistance protein
    • Homolya L., Hollo Z., Germann U.A., Pastan I., Gottesman M.M., and Sarkadi B. Fluorescent cellular indicators are extruded by the multidrug resistance protein. J Biol Chem 268 (1993) 21493-21496
    • (1993) J Biol Chem , vol.268 , pp. 21493-21496
    • Homolya, L.1    Hollo, Z.2    Germann, U.A.3    Pastan, I.4    Gottesman, M.M.5    Sarkadi, B.6
  • 50
    • 0025193531 scopus 로고
    • Photosensitised labelling of a functional multidrug transporter in living drug-resistant tumour cells
    • Raviv Y., Pollard H.B., Bruggemann E.P., Pastan I., and Gottesman M.M. Photosensitised labelling of a functional multidrug transporter in living drug-resistant tumour cells. J Biol Chem 265 (1990) 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
  • 51
    • 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. 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 (1999) 24759-24765
    • (1999) J Biol Chem , vol.274 , pp. 24759-24765
    • Loo, T.W.1    Clarke, D.M.2
  • 52
    • 0033083015 scopus 로고    scopus 로고
    • Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site
    • Shapiro A.B., Fox K., Lam P., and Ling V. Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site. Eur J Biochem 259 (1999) 841-850
    • (1999) Eur J Biochem , vol.259 , pp. 841-850
    • Shapiro, A.B.1    Fox, K.2    Lam, P.3    Ling, V.4
  • 54
    • 0347379911 scopus 로고    scopus 로고
    • Methanethiosulphonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites
    • Loo T.W., Bartlett M.C., and Clarke D.M. Methanethiosulphonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites. J Biol Chem 278 (2003) 50136-50141
    • (2003) J Biol Chem , vol.278 , pp. 50136-50141
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 55
    • 27144451192 scopus 로고    scopus 로고
    • Interaction of LDS-751 and rhodamine 123 with P-glycoprotein: evidence for simultaneous binding of both drugs
    • Lugo M.R., and Sharom F.J. Interaction of LDS-751 and rhodamine 123 with P-glycoprotein: evidence for simultaneous binding of both drugs. Biochemistry 44 (2005) 14020-14029
    • (2005) Biochemistry , vol.44 , pp. 14020-14029
    • Lugo, M.R.1    Sharom, F.J.2
  • 57
    • 0030004763 scopus 로고    scopus 로고
    • Co-operative, competitive and non-competitive interactions between modulators of P-glycoprotein
    • Ayesh S., Shao Y.-M., and Stein W.D. Co-operative, competitive and non-competitive interactions between modulators of P-glycoprotein. Biochim Biophys Acta 316 (1996) 8-18
    • (1996) Biochim Biophys Acta , vol.316 , pp. 8-18
    • Ayesh, S.1    Shao, Y.-M.2    Stein, W.D.3
  • 59
    • 0030062653 scopus 로고    scopus 로고
    • Competition of hydrophobic peptides, cytotoxic drugs, and chemosensitizers on a common P-glycoprotein pharmacophore as revealed by its ATPase activity
    • Borgnia M.J., Eytan G.D., and Assarak Y.G. Competition of hydrophobic peptides, cytotoxic drugs, and chemosensitizers on a common P-glycoprotein pharmacophore as revealed by its ATPase activity. J Biol Chem 271 (1996) 3163-3171
    • (1996) J Biol Chem , vol.271 , pp. 3163-3171
    • Borgnia, M.J.1    Eytan, G.D.2    Assarak, Y.G.3
  • 60
    • 0038480045 scopus 로고    scopus 로고
    • Structure-activity relationship: analysis of P-glycoprotein substrates and inhibitors
    • Wang R.B., Kuo C.L., Lien L.L., and Lien E.J. Structure-activity relationship: analysis of P-glycoprotein substrates and inhibitors. J Clin Pharm Ther 28 (2003) 203-228
    • (2003) J Clin Pharm Ther , vol.28 , pp. 203-228
    • Wang, R.B.1    Kuo, C.L.2    Lien, L.L.3    Lien, E.J.4
  • 61
    • 0028128286 scopus 로고
    • Localisation of the forskolin labelling sites to both halves of P-glycoprotein: similarity of the sites labelled by forskolin and prazosin
    • Morris D.I., Greenberger L.M., Bruggemann E.P., Cardarelli C., Gottesman M.M., Pastan I., et al. Localisation of the forskolin labelling sites to both halves of P-glycoprotein: similarity of the sites labelled by forskolin and prazosin. Mol Pharmacol 46 (1994) 329-337
    • (1994) Mol Pharmacol , vol.46 , pp. 329-337
    • Morris, D.I.1    Greenberger, L.M.2    Bruggemann, E.P.3    Cardarelli, C.4    Gottesman, M.M.5    Pastan, I.6
  • 62
    • 0026669363 scopus 로고
    • Characterisation of the azidopine and vinblastine binding site of P-glycoprotein
    • Bruggemann E.P., Currier S.J., Gottesman M.M., and Pastan I. Characterisation of the azidopine and vinblastine binding site of P-glycoprotein. J Biol Chem 267 (1992) 21020-21026
    • (1992) J Biol Chem , vol.267 , pp. 21020-21026
    • Bruggemann, E.P.1    Currier, S.J.2    Gottesman, M.M.3    Pastan, I.4
  • 63
    • 0029954843 scopus 로고    scopus 로고
    • P-glycoprotein-a mediator of multidrug resistance in tumour cells
    • Germann U.A. P-glycoprotein-a mediator of multidrug resistance in tumour cells. Eur J Cancer 32A (1996) 927-944
    • (1996) Eur J Cancer , vol.32 A , pp. 927-944
    • Germann, U.A.1
  • 64
    • 0031434236 scopus 로고    scopus 로고
    • Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate
    • Loo T.W., and Clarke D.M. Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate. J Biol Chem 272 (1997) 31945-31948
    • (1997) J Biol Chem , vol.272 , pp. 31945-31948
    • Loo, T.W.1    Clarke, D.M.2
  • 65
    • 0035805573 scopus 로고    scopus 로고
    • Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analogue of verapamil, MTS-verapamil
    • Loo T.W., and Clarke D.M. Defining the drug-binding site in the human multidrug resistance P-glycoprotein using a methanethiosulfonate analogue of verapamil, MTS-verapamil. J Biol Chem 276 (2001) 14972-14979
    • (2001) J Biol Chem , vol.276 , pp. 14972-14979
    • Loo, T.W.1    Clarke, D.M.2
  • 66
    • 33745008903 scopus 로고    scopus 로고
    • Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket
    • Loo T.W., Bartlett M.C., and Clarke D.M. Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket. Biochem J 396 (2006) 537-545
    • (2006) Biochem J , vol.396 , pp. 537-545
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 67
    • 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. Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein. J Biol Chem 277 (2002) 44332-44338
    • (2002) J Biol Chem , vol.277 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 68
    • 0036176213 scopus 로고    scopus 로고
    • Identification of ligand-binding regions of P-glycoprotein by activated-pharmacophore photoaffinity labeling and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry
    • Ecker G.F., Csaszar E., Kopp S., Plagens B., Holzer W., Ernst W., et al. Identification of ligand-binding regions of P-glycoprotein by activated-pharmacophore photoaffinity labeling and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry. Mol Pharmacol 61 (2002) 637-648
    • (2002) Mol Pharmacol , vol.61 , pp. 637-648
    • Ecker, G.F.1    Csaszar, E.2    Kopp, S.3    Plagens, B.4    Holzer, W.5    Ernst, W.6
  • 69
    • 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. Identification and localization of three photobinding sites of iodoarylazidoprazosin in hamster P-glycoprotein. Eur J Biochem 268 (2001) 2629-2634
    • (2001) Eur J Biochem , vol.268 , pp. 2629-2634
    • Isenberg, B.1    Thole, H.2    Tummler, B.3    Demmer, A.4
  • 71
    • 31844452412 scopus 로고    scopus 로고
    • Insight in eukaryotic ABC transporter function by mutation analysis
    • Frelet A., and Klein M. Insight in eukaryotic ABC transporter function by mutation analysis. FEBS Lett 580 (2006) 1064-1084
    • (2006) FEBS Lett , vol.580 , pp. 1064-1084
    • Frelet, A.1    Klein, M.2
  • 73
    • 0027215242 scopus 로고
    • Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain 11 as a putative drug binding site
    • Kajiji S., Talbot F., Grizzuti K., Van Dyke-Phillips V., Agresti M., Safa A.R., et al. Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain 11 as a putative drug binding site. Biochemistry 32 (1993) 4185-4194
    • (1993) Biochemistry , vol.32 , pp. 4185-4194
    • Kajiji, S.1    Talbot, F.2    Grizzuti, K.3    Van Dyke-Phillips, V.4    Agresti, M.5    Safa, A.R.6
  • 74
    • 0027260959 scopus 로고
    • Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein
    • Loo T.W., and Clark D.P. Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein. J Biol Chem 268 (1993) 19965-19972
    • (1993) J Biol Chem , vol.268 , pp. 19965-19972
    • Loo, T.W.1    Clark, D.P.2
  • 75
    • 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. Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers. J Biol Chem 276 (2001) 36877-36880
    • (2001) J Biol Chem , vol.276 , pp. 36877-36880
    • Loo, T.W.1    Clarke, D.M.2
  • 76
    • 4644265234 scopus 로고    scopus 로고
    • The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium
    • Loo T.W., Bartlett M.C., and Clarke D.M. The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium. Biochemistry 43 (2004) 12081-12089
    • (2004) Biochemistry , vol.43 , pp. 12081-12089
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 77
    • 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. Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"?. Biochem Biophys Res Commun 329 (2005) 419-422
    • (2005) Biochem Biophys Res Commun , vol.329 , pp. 419-422
    • Loo, T.W.1    Clarke, D.M.2
  • 78
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang G., and Roth C.B. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293 (2001) 1793-1800
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 79
    • 0037687304 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding
    • Loo T.W., Bartlett M.C., and Clarke D.M. Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein. Direct evidence for the substrate-induced fit mechanism for drug binding. J Biol Chem 278 (2003) 13603-13606
    • (2003) J Biol Chem , vol.278 , pp. 13603-13606
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 80
    • 33744902318 scopus 로고    scopus 로고
    • Interaction of transported drugs with the lipid bilayer and P-glycoprotein through a solvation exchange mechanism
    • Omote H., and Al-Shawi M.K. Interaction of transported drugs with the lipid bilayer and P-glycoprotein through a solvation exchange mechanism. Biophys J 90 (2006) 4046-4059
    • (2006) Biophys J , vol.90 , pp. 4046-4059
    • Omote, H.1    Al-Shawi, M.K.2
  • 81
    • 0027937143 scopus 로고
    • ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells
    • Shapiro A.B., and Ling V. ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells. J Biol Chem 269 (1994) 3745-3754
    • (1994) J Biol Chem , vol.269 , pp. 3745-3754
    • Shapiro, A.B.1    Ling, V.2
  • 82
    • 0029027674 scopus 로고
    • Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Sharom F.J., Yu X., Chu J.W.K., and Doige C.A. Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochem J 308 (1995) 381-390
    • (1995) Biochem J , vol.308 , pp. 381-390
    • Sharom, F.J.1    Yu, X.2    Chu, J.W.K.3    Doige, C.A.4
  • 83
    • 0028362501 scopus 로고
    • Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch I.L., Al-Shawi M.K., and Senior A.E. Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein. Biochemistry 33 (1994) 7069-7076
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Urbatsch, I.L.1    Al-Shawi, M.K.2    Senior, A.E.3
  • 84
    • 0346732289 scopus 로고    scopus 로고
    • Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein
    • Al-Shawi M.K., Polar M.K., Omote H., and Figler R.A. Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein. J Biol Chem 278 (2003) 52629-52640
    • (2003) J Biol Chem , vol.278 , pp. 52629-52640
    • Al-Shawi, M.K.1    Polar, M.K.2    Omote, H.3    Figler, R.A.4
  • 85
    • 0038419822 scopus 로고    scopus 로고
    • Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site
    • Loo T.W., Bartlett M.C., and Clarke D.M. Permanent activation of the human P-glycoprotein by covalent modification of a residue in the drug-binding site. J Biol Chem 278 (2003) 20449-20452
    • (2003) J Biol Chem , vol.278 , pp. 20449-20452
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 87
    • 0030697879 scopus 로고    scopus 로고
    • The multidrug resistance reversal agents SR33557 modulates vinca alkaloid binding to P-glycoprotein by an allosteric interaction
    • Martin C., Berridge G., Higgins C.F., and Callaghan R. The multidrug resistance reversal agents SR33557 modulates vinca alkaloid binding to P-glycoprotein by an allosteric interaction. Br J Pharmacol 122 (1997) 765-771
    • (1997) Br J Pharmacol , vol.122 , pp. 765-771
    • Martin, C.1    Berridge, G.2    Higgins, C.F.3    Callaghan, R.4
  • 88
    • 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. Partial purification and reconstitution of the human multidrug-resistance pump: characterization of the drug-stimulatable ATP hydrolysis. Proc Natl Acad Sci USA 89 (1992) 8472-8476
    • (1992) Proc Natl Acad Sci USA , 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
  • 90
    • 0027509809 scopus 로고
    • Effects of lipids and detergents on ATPase-active P-glycoprotein
    • Doige C.A., Yu X.H., and Sharom F.J. Effects of lipids and detergents on ATPase-active P-glycoprotein. Biochim Biophys Acta 1146 (1993) 65-72
    • (1993) Biochim Biophys Acta , vol.1146 , pp. 65-72
    • Doige, C.A.1    Yu, X.H.2    Sharom, F.J.3
  • 91
    • 27144464932 scopus 로고    scopus 로고
    • Effect of the modulation of the membrane lipid composition on the localization and function of P-glycoprotein in MDR1-MDCK cells
    • Kamau S.W., Kramer S.D., Gunthert M., and Wunderli-Allenapach H. Effect of the modulation of the membrane lipid composition on the localization and function of P-glycoprotein in MDR1-MDCK cells. In Vitro Cell Dev Biol Anim 41 (2005) 207-216
    • (2005) In Vitro Cell Dev Biol Anim , vol.41 , pp. 207-216
    • Kamau, S.W.1    Kramer, S.D.2    Gunthert, M.3    Wunderli-Allenapach, H.4
  • 92
    • 0029121417 scopus 로고
    • Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity
    • Loo T.W., and Clarke D.M. Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity. J Biol Chem 270 (1995) 22957-22961
    • (1995) J Biol Chem , vol.270 , pp. 22957-22961
    • Loo, T.W.1    Clarke, D.M.2
  • 93
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch I.L., Sankaran B., Bhagat S., and Senior A.E. Both P-glycoprotein nucleotide-binding sites are catalytically active. J Biol Chem 270 (1995) 26956-26961
    • (1995) J Biol Chem , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 94
    • 0027482461 scopus 로고
    • Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein
    • Sharom F.J., Yu X., and Doige C.A. Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein. J Biol Chem 268 (1993) 24197-24202
    • (1993) J Biol Chem , vol.268 , pp. 24197-24202
    • Sharom, F.J.1    Yu, X.2    Doige, C.A.3
  • 95
    • 0030065776 scopus 로고    scopus 로고
    • Functional reconstitution of P-glycoprotein reveals an apparent near stoichiometric drug transport to ATP hydrolysis
    • Eytan G.D., Regev R., and Assaraf Y.G. Functional reconstitution of P-glycoprotein reveals an apparent near stoichiometric drug transport to ATP hydrolysis. J Biol Chem 271 (1996) 3172-3178
    • (1996) J Biol Chem , vol.271 , pp. 3172-3178
    • Eytan, G.D.1    Regev, R.2    Assaraf, Y.G.3
  • 96
    • 0032523818 scopus 로고    scopus 로고
    • Stoichiometry of coupling of rhodamine 123 transport to ATP hydrolysis by P-glycoprotein
    • Shapiro A.B., and Ling V. Stoichiometry of coupling of rhodamine 123 transport to ATP hydrolysis by P-glycoprotein. Eur J Biochem 254 (1998) 189-193
    • (1998) Eur J Biochem , vol.254 , pp. 189-193
    • Shapiro, A.B.1    Ling, V.2
  • 97
    • 0030868612 scopus 로고    scopus 로고
    • Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein
    • Ambudkar S.V., Cardarelli C.O., Pashinsky I., and Stein W.D. Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein. J Biol Chem 272 (1997) 21260-21266
    • (1997) J Biol Chem , vol.272 , pp. 21260-21266
    • Ambudkar, S.V.1    Cardarelli, C.O.2    Pashinsky, I.3    Stein, W.D.4
  • 98
    • 27144547163 scopus 로고    scopus 로고
    • Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy
    • Delannoy S., Urbatsch I.L., Tombline G., Senior A.E., and Volberding P.A. Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy. Biochemistry 44 (2005) 14010-14019
    • (2005) Biochemistry , vol.44 , pp. 14010-14019
    • Delannoy, S.1    Urbatsch, I.L.2    Tombline, G.3    Senior, A.E.4    Volberding, P.A.5
  • 99
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch I.L., Sankaran B., Weber J., and Senior A.E. P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J Biol Chem 270 (1995) 19383-19390
    • (1995) J Biol Chem , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 100
    • 0032584289 scopus 로고    scopus 로고
    • Mutations in either nucleotide-binding site of P-glycoprotein (Mdr3) prevent vanadate trapping of nucleotide at both sites
    • Urbatsch I.L., Beaudet L., Carrier I., and Gros P. Mutations in either nucleotide-binding site of P-glycoprotein (Mdr3) prevent vanadate trapping of nucleotide at both sites. Biochemistry 37 (1998) 4592-4602
    • (1998) Biochemistry , vol.37 , pp. 4592-4602
    • Urbatsch, I.L.1    Beaudet, L.2    Carrier, I.3    Gros, P.4
  • 101
    • 0037417765 scopus 로고    scopus 로고
    • Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle
    • Qu Q., Russell P.L., and Sharom F.J. Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle. Biochemistry 42 (2003) 1170-1177
    • (2003) Biochemistry , vol.42 , pp. 1170-1177
    • Qu, Q.1    Russell, P.L.2    Sharom, F.J.3
  • 102
    • 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 M.F., Kamis A.B., Callaghan R., Higgins C.F., and Ford R.C. Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding. J Biol Chem 278 (2003) 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
  • 103
    • 23044503311 scopus 로고    scopus 로고
    • ATP hydrolysis promotes interaction between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein
    • Loo T.W., Bartlett D.M., and Clarke D.M. ATP hydrolysis promotes interaction between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein. Biochemistry 44 (2005) 10250-10258
    • (2005) Biochemistry , vol.44 , pp. 10250-10258
    • Loo, T.W.1    Bartlett, D.M.2    Clarke, D.M.3
  • 104
    • 0035951073 scopus 로고    scopus 로고
    • The vinblastine binding site adopts high- and low-affinity conformations during a transport cycle of P-glycoprotein
    • Martin C., Higgins C.F., and Callaghan R. The vinblastine binding site adopts high- and low-affinity conformations during a transport cycle of P-glycoprotein. Biochemistry 40 (2001) 15733-15742
    • (2001) Biochemistry , vol.40 , pp. 15733-15742
    • Martin, C.1    Higgins, C.F.2    Callaghan, R.3
  • 105
    • 0026053770 scopus 로고
    • Structural model of the nucleotide-binding conserved component of periplasmic permeases
    • Mimura C.S., Holbrook S.R., and Ames G.F. Structural model of the nucleotide-binding conserved component of periplasmic permeases. Proc Natl Acad Sci USA 88 (1991) 84-88
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 84-88
    • Mimura, C.S.1    Holbrook, S.R.2    Ames, G.F.3
  • 106
    • 0035943691 scopus 로고    scopus 로고
    • Cross-linking of human multidrug resistance P-glycoprotein by the substrate, Tris-(2-maleimidoethyl) amine, is altered by ATP hydrolysis. Evidence for rotation of a transmembrane helix
    • Loo T.W., and Clarke D.M. Cross-linking of human multidrug resistance P-glycoprotein by the substrate, Tris-(2-maleimidoethyl) amine, is altered by ATP hydrolysis. Evidence for rotation of a transmembrane helix. J Biol Chem 276 (2001) 31800-31805
    • (2001) J Biol Chem , vol.276 , pp. 31800-31805
    • Loo, T.W.1    Clarke, D.M.2
  • 107
    • 0035836495 scopus 로고    scopus 로고
    • Coordinate changes in drug resistance and drug-induced conformational transitions in altered-function mutants of the multidrug transporter P-glycoprotein
    • Ruth A., Stein W.D., Rose E., and Roninson I.B. Coordinate changes in drug resistance and drug-induced conformational transitions in altered-function mutants of the multidrug transporter P-glycoprotein. Biochemistry 40 (2001) 4332-4339
    • (2001) Biochemistry , vol.40 , pp. 4332-4339
    • Ruth, A.1    Stein, W.D.2    Rose, E.3    Roninson, I.B.4
  • 108
    • 0035836477 scopus 로고    scopus 로고
    • Analysis of MDR1 P-glycoprotein conformational changes in permeabilized cells using differential immunoreactivity
    • Druley T.E., Stein W.D., and Roninson I.B. Analysis of MDR1 P-glycoprotein conformational changes in permeabilized cells using differential immunoreactivity. Biochemistry 40 (2001) 4312-4322
    • (2001) Biochemistry , vol.40 , pp. 4312-4322
    • Druley, T.E.1    Stein, W.D.2    Roninson, I.B.3
  • 109
    • 0034681959 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity
    • Julien M., and Gros P. Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity. Biochemistry 39 (2000) 4559-4568
    • (2000) Biochemistry , vol.39 , pp. 4559-4568
    • Julien, M.1    Gros, P.2
  • 110
    • 0032528075 scopus 로고    scopus 로고
    • Dissection of drug-binding-induced conformational changes in P-glycoprotein
    • Wang G.C., Pincheira R., and Zhang J.T. Dissection of drug-binding-induced conformational changes in P-glycoprotein. Eur J Biochem 255 (1998) 383-390
    • (1998) Eur J Biochem , vol.255 , pp. 383-390
    • Wang, G.C.1    Pincheira, R.2    Zhang, J.T.3
  • 111
    • 0029840320 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains
    • Liu R., and Sharom F.J. Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains. Biochemistry 35 (1996) 11865-11873
    • (1996) Biochemistry , vol.35 , pp. 11865-11873
    • Liu, R.1    Sharom, F.J.2
  • 112
    • 0037449746 scopus 로고    scopus 로고
    • Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains
    • Loo T.W., Bartlett M.C., and Clarke D.M. Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains. J Biol Chem 278 (2003) 1575-1578
    • (2003) J Biol Chem , vol.278 , pp. 1575-1578
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 113
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins C.F., and Linton K.J. The ATP switch model for ABC transporters. Nat Struct Mol Biol 11 (2005) 918-926
    • (2005) Nat Struct Mol Biol , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 114
    • 33846236802 scopus 로고    scopus 로고
    • Linton KJ, Higgins CF. Structure and function of ABC transporters: the ATP switch provides flexible control. Pflug Arch Eur J Phys [Epub ahead of print].
  • 115
    • 33644840984 scopus 로고    scopus 로고
    • The power of the pump: mechanisms of action of P-glycoprotein (ABCB1)
    • Ambudkar S.V., Kim I.W., and Sauna Z.E. The power of the pump: mechanisms of action of P-glycoprotein (ABCB1). Eur J Pharma Sci 27 (2006) 392-400
    • (2006) Eur J Pharma Sci , vol.27 , pp. 392-400
    • Ambudkar, S.V.1    Kim, I.W.2    Sauna, Z.E.3
  • 116
    • 85163560788 scopus 로고    scopus 로고
    • Substrate-binding sites in ABC transporters
    • Holland I.B., Cole S.P.C., Kuchler K., and Higgins C.F. (Eds), Elsevier, London
    • van Veen H.W., and Callaghan R. Substrate-binding sites in ABC transporters. In: Holland I.B., Cole S.P.C., Kuchler K., and Higgins C.F. (Eds). ABC proteins: from bacteria to man (2003), Elsevier, London 81-106
    • (2003) ABC proteins: from bacteria to man , pp. 81-106
    • van Veen, H.W.1    Callaghan, R.2
  • 117
    • 0032716822 scopus 로고    scopus 로고
    • Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR antiporters
    • Krupka R.M. Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR antiporters. J Membr Biol 172 (1999) 129-143
    • (1999) J Membr Biol , vol.172 , pp. 129-143
    • Krupka, R.M.1
  • 118
    • 0023898749 scopus 로고
    • Physical-chemical properties shared by compounds that modulate multidrug resistance in human leukemic cells
    • Zamora J.M., Pearce H.L., and Beck W.T. Physical-chemical properties shared by compounds that modulate multidrug resistance in human leukemic cells. Mol Pharmacol 33 (1988) 454-462
    • (1988) Mol Pharmacol , vol.33 , pp. 454-462
    • Zamora, J.M.1    Pearce, H.L.2    Beck, W.T.3
  • 119
    • 0031156390 scopus 로고    scopus 로고
    • How does P-glycoprotein recognise its substrates?
    • Ueda K., Taguchi Y., and Morishima M. How does P-glycoprotein recognise its substrates?. Semin Cancer Biol 8 (1997) 151-159
    • (1997) Semin Cancer Biol , vol.8 , pp. 151-159
    • Ueda, K.1    Taguchi, Y.2    Morishima, M.3
  • 120
    • 0037204543 scopus 로고    scopus 로고
    • Progress in understanding the structure-activity relationships of P-glycoprotein
    • Stouch T.R., and Gudmundsson O. Progress in understanding the structure-activity relationships of P-glycoprotein. Adv Drug Deliv Rev 54 (2002) 315-328
    • (2002) Adv Drug Deliv Rev , vol.54 , pp. 315-328
    • Stouch, T.R.1    Gudmundsson, O.2
  • 121
    • 0032518454 scopus 로고    scopus 로고
    • A general pattern for substrate recognition by P-glycoprotein
    • Seelig A. A general pattern for substrate recognition by P-glycoprotein. Eur J Biochem 251 (1998) 252-261
    • (1998) Eur J Biochem , vol.251 , pp. 252-261
    • Seelig, A.1
  • 122
    • 0031962285 scopus 로고    scopus 로고
    • How does P-glycoprotein recognise its substrates?
    • Seelig A. How does P-glycoprotein recognise its substrates?. Int J Clin Pharmacol Ther 36 (1998) 50-54
    • (1998) Int J Clin Pharmacol Ther , vol.36 , pp. 50-54
    • Seelig, A.1
  • 123
    • 0033739115 scopus 로고    scopus 로고
    • Structure-activity relationship of P-glycoprotein substrates and modifiers
    • Seelig A., and Landwojtowicz E. Structure-activity relationship of P-glycoprotein substrates and modifiers. Eur J Pharm Sci 12 (2000) 31-40
    • (2000) Eur J Pharm Sci , vol.12 , pp. 31-40
    • Seelig, A.1    Landwojtowicz, E.2
  • 124
    • 17444419056 scopus 로고    scopus 로고
    • A pharmacophore hypothesis for P-glycoprotein substrate recognition using GRIND-based 3D-QSAR
    • Cianchetta G., Singleton R.W., Zhang M., Wildgoose M., Giesing D., Fravolini A., et al. A pharmacophore hypothesis for P-glycoprotein substrate recognition using GRIND-based 3D-QSAR. J Med Chem 48 (2005) 2927-2935
    • (2005) J Med Chem , vol.48 , pp. 2927-2935
    • Cianchetta, G.1    Singleton, R.W.2    Zhang, M.3    Wildgoose, M.4    Giesing, D.5    Fravolini, A.6
  • 125
    • 0034055630 scopus 로고    scopus 로고
    • Substrate recognition by P-glycoprotein and the multidrug resistance-associated protein MRP1: a comparison
    • Seelig A., Li Blatter X., and Wohnsland F. Substrate recognition by P-glycoprotein and the multidrug resistance-associated protein MRP1: a comparison. Int J Clin Pharmacol Ther 38 (2000) 111-121
    • (2000) Int J Clin Pharmacol Ther , vol.38 , pp. 111-121
    • Seelig, A.1    Li Blatter, X.2    Wohnsland, F.3
  • 126
    • 0037171818 scopus 로고    scopus 로고
    • A computational ensemble pharmacophore model for identifying substrates of P-glycoprotein
    • Penzotti J.E., Lamb M.L., Evensen E., and Grootenhuis P.D.J. A computational ensemble pharmacophore model for identifying substrates of P-glycoprotein. J Med Chem 45 (2002) 1737-1740
    • (2002) J Med Chem , vol.45 , pp. 1737-1740
    • Penzotti, J.E.1    Lamb, M.L.2    Evensen, E.3    Grootenhuis, P.D.J.4
  • 127
    • 20444403742 scopus 로고    scopus 로고
    • Classification of substrates and inhibitors of P-glycoprotein using unsupervised machine learning approach
    • Wang Y.H., Li Y., Yang S.L., and Yang L. Classification of substrates and inhibitors of P-glycoprotein using unsupervised machine learning approach. J Chem Inf Model 45 (2005) 750-757
    • (2005) J Chem Inf Model , vol.45 , pp. 750-757
    • Wang, Y.H.1    Li, Y.2    Yang, S.L.3    Yang, L.4
  • 128
    • 33645357793 scopus 로고    scopus 로고
    • A topological substructural approach for the prediction of P-glycoprotein substrates
    • Cabrera M.A., Gonzalez I., Fernandez C., Navarro C., and Bermejo M. A topological substructural approach for the prediction of P-glycoprotein substrates. J Pharm Sci 95 (2006) 589-606
    • (2006) J Pharm Sci , vol.95 , pp. 589-606
    • Cabrera, M.A.1    Gonzalez, I.2    Fernandez, C.3    Navarro, C.4    Bermejo, M.5
  • 129
    • 0037457796 scopus 로고    scopus 로고
    • Considerations in the design and development of transport inhibitors as adjuncts to drug therapy
    • Dantzig A.H., de Alwis D.P., and Burgess M. Considerations in the design and development of transport inhibitors as adjuncts to drug therapy. Adv Drug Deliv Rev 55 (2003) 133-150
    • (2003) Adv Drug Deliv Rev , vol.55 , pp. 133-150
    • Dantzig, A.H.1    de Alwis, D.P.2    Burgess, M.3
  • 130
    • 0042167430 scopus 로고    scopus 로고
    • P-glycoprotein inhibitors and their screening: a perspective from bioavailability enhancement
    • Varma M.V.S., Ashokraj Y., Dey C.D., and Panchagnula R. P-glycoprotein inhibitors and their screening: a perspective from bioavailability enhancement. Pharmacol Res 48 (2003) 347-359
    • (2003) Pharmacol Res , vol.48 , pp. 347-359
    • Varma, M.V.S.1    Ashokraj, Y.2    Dey, C.D.3    Panchagnula, R.4
  • 131
    • 0035253714 scopus 로고    scopus 로고
    • Phase I study of infusional paclitaxel in combination with the P-glycoprotein antagonist PSC 833
    • Chico I., Kang M.H., Bergan R., Abraham J., Bakke S., Meadows B., et al. Phase I study of infusional paclitaxel in combination with the P-glycoprotein antagonist PSC 833. J Clin Oncol 19 (2001) 832-842
    • (2001) J Clin Oncol , vol.19 , pp. 832-842
    • Chico, I.1    Kang, M.H.2    Bergan, R.3    Abraham, J.4    Bakke, S.5    Meadows, B.6
  • 132
    • 0035863315 scopus 로고    scopus 로고
    • In vitro and in vivo reversal of P-glycoprotein mediated multidrug resistance by a novel potent modulator, XR9576
    • Mistry P., Stewart A.J., Dangerfield W., Okiji S., Liddle C., Bootle D., et al. In vitro and in vivo reversal of P-glycoprotein mediated multidrug resistance by a novel potent modulator, XR9576. Cancer Res 61 (2001) 749-758
    • (2001) Cancer Res , vol.61 , pp. 749-758
    • Mistry, P.1    Stewart, A.J.2    Dangerfield, W.3    Okiji, S.4    Liddle, C.5    Bootle, D.6
  • 133
    • 0034214366 scopus 로고    scopus 로고
    • Discovery and characterization of OC144-093, a novel inhibitor of P-glycoprotein-mediated multidrug resistance
    • Newman M.J., Rodart J.C., Benbatoul K.D., Romano S.J., Zhang C., Krane S., et al. Discovery and characterization of OC144-093, a novel inhibitor of P-glycoprotein-mediated multidrug resistance. Cancer Res 60 (2000) 2964-2972
    • (2000) Cancer Res , vol.60 , pp. 2964-2972
    • Newman, M.J.1    Rodart, J.C.2    Benbatoul, K.D.3    Romano, S.J.4    Zhang, C.5    Krane, S.6
  • 134
    • 0032763895 scopus 로고    scopus 로고
    • Selectivity of the multidrug resistance modulator, LY335979, for P-glycoprotein and effect on cytochrome P450 activities
    • Dantzig A.H., Shepard R.L., Law K.L., Tabas L., Pratt S., Gillespie J.S., et al. Selectivity of the multidrug resistance modulator, LY335979, for P-glycoprotein and effect on cytochrome P450 activities. J Pharmacol Exp Ther 290 (1999) 854-890
    • (1999) J Pharmacol Exp Ther , vol.290 , pp. 854-890
    • Dantzig, A.H.1    Shepard, R.L.2    Law, K.L.3    Tabas, L.4    Pratt, S.5    Gillespie, J.S.6
  • 135
    • 0037211554 scopus 로고    scopus 로고
    • Modulation of P-glycoprotein but not MRP1- or BCRP-mediated drug resistance by LY335979
    • Shepard R.L., Cao J., Starling J.J., and Dantzig A.H. Modulation of P-glycoprotein but not MRP1- or BCRP-mediated drug resistance by LY335979. Int J Cancer 103 (2003) 121-125
    • (2003) Int J Cancer , vol.103 , pp. 121-125
    • Shepard, R.L.1    Cao, J.2    Starling, J.J.3    Dantzig, A.H.4
  • 136
    • 0033179095 scopus 로고    scopus 로고
    • Frequency and clinical significance of the expression of the multidrug resistance proteins MDR-1/P-glycoprotein, MRP1, and LRP in acute myeloid leukemia: a Southwest Oncology Group Study
    • Leith C.P., Kopecky K.J., Chen I.M., Eijdems L., Slovak M.L., McConnell T.S., et al. Frequency and clinical significance of the expression of the multidrug resistance proteins MDR-1/P-glycoprotein, MRP1, and LRP in acute myeloid leukemia: a Southwest Oncology Group Study. Blood 94 (1999) 1086-1099
    • (1999) Blood , vol.94 , pp. 1086-1099
    • Leith, C.P.1    Kopecky, K.J.2    Chen, I.M.3    Eijdems, L.4    Slovak, M.L.5    McConnell, T.S.6
  • 137
    • 20044362282 scopus 로고    scopus 로고
    • The implications of P-glycoprotein in HIV: friend or foe?
    • Owen A., Chandler B., and Back D.J. The implications of P-glycoprotein in HIV: friend or foe?. Fundam Clin Pharmacol 19 (2005) 283-296
    • (2005) Fundam Clin Pharmacol , vol.19 , pp. 283-296
    • Owen, A.1    Chandler, B.2    Back, D.J.3
  • 138
    • 0032900953 scopus 로고    scopus 로고
    • Biochemical, cellular and pharmacological aspects of the multidrug transporter
    • Ambudkar S.V. Biochemical, cellular and pharmacological aspects of the multidrug transporter. Annu Rev Pharmacol Toxicol 39 (1999) 361-398
    • (1999) Annu Rev Pharmacol Toxicol , vol.39 , pp. 361-398
    • Ambudkar, S.V.1
  • 139
    • 0028818393 scopus 로고
    • Partial inhibition of multidrug resistance by safingol is independent of modulation of P-glycoprotein substrate activities and correlated with inhibition of protein kinase C
    • Sachs C.W., Safa A.R., Harrison S.D., and Fine R.L. Partial inhibition of multidrug resistance by safingol is independent of modulation of P-glycoprotein substrate activities and correlated with inhibition of protein kinase C. J Biol Chem 270 (1995) 26639-26648
    • (1995) J Biol Chem , vol.270 , pp. 26639-26648
    • Sachs, C.W.1    Safa, A.R.2    Harrison, S.D.3    Fine, R.L.4
  • 140
    • 0030067789 scopus 로고    scopus 로고
    • Characterisation of phosphorylation-defective mutants of human P-glycoprotein expressed in mammalian cells
    • Germann U.A., Chambers T.C., Ambudkar S.V., Licht T., Cardarelli C.O., Pastan I., et al. Characterisation of phosphorylation-defective mutants of human P-glycoprotein expressed in mammalian cells. J Biol Chem 271 (1996) 1708-1716
    • (1996) J Biol Chem , vol.271 , pp. 1708-1716
    • Germann, U.A.1    Chambers, T.C.2    Ambudkar, S.V.3    Licht, T.4    Cardarelli, C.O.5    Pastan, I.6
  • 141
    • 0028342805 scopus 로고
    • Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: evidence against direct drug extrusion from the plasma membrane
    • Altenberg G.A., Vanoye C.G., Horton J.K., and Reuss L. Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: evidence against direct drug extrusion from the plasma membrane. Proc Natl Acad Sci USA 91 (1994) 4654-4657
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4654-4657
    • Altenberg, G.A.1    Vanoye, C.G.2    Horton, J.K.3    Reuss, L.4
  • 142
    • 17544365536 scopus 로고    scopus 로고
    • The role of passive transbilayer drug movement in multidrug resistance and its modulation
    • Eytan G.D., Regev R., Oren R., and Assaraf Y.G. The role of passive transbilayer drug movement in multidrug resistance and its modulation. J Biol Chem 271 (1996) 12897-12902
    • (1996) J Biol Chem , vol.271 , pp. 12897-12902
    • Eytan, G.D.1    Regev, R.2    Oren, R.3    Assaraf, Y.G.4
  • 143
    • 0030701599 scopus 로고    scopus 로고
    • Flip-flop of doxorubicin across erythrocyte and lipid membranes
    • Regev R., and Eytan G.D. Flip-flop of doxorubicin across erythrocyte and lipid membranes. Biochem Pharmacol 54 (1997) 1151-1158
    • (1997) Biochem Pharmacol , vol.54 , pp. 1151-1158
    • Regev, R.1    Eytan, G.D.2
  • 144
    • 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. P-glycoprotein confers methotrexate resistance in 3T6 cells with deficient carrier-mediated methotrexate uptake. Proc Natl Acad Sci USA 93 (1996) 1238-1242
    • (1996) Proc Natl Acad Sci USA , 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
  • 145
    • 0030785799 scopus 로고    scopus 로고
    • Efficiency of P-glycoprotein-mediated exclusion of rhodamine dyes from multidrug-resistant cells is determined by their passive transmembrane movement rate
    • Eytan G.D., Regev R., Oren G., Hurwitz C.D., and Assaraf Y.G. Efficiency of P-glycoprotein-mediated exclusion of rhodamine dyes from multidrug-resistant cells is determined by their passive transmembrane movement rate. Eur J Biochem 248 (1997) 104-112
    • (1997) Eur J Biochem , vol.248 , pp. 104-112
    • Eytan, G.D.1    Regev, R.2    Oren, G.3    Hurwitz, C.D.4    Assaraf, Y.G.5
  • 146
    • 0033864507 scopus 로고    scopus 로고
    • Symmetry and structure in P-glycoprotein and ABC transporters what goes around comes around
    • Jones P.M., and George A.M. Symmetry and structure in P-glycoprotein and ABC transporters what goes around comes around. Eur J Biochem 267 (2000) 5298-5305
    • (2000) Eur J Biochem , vol.267 , pp. 5298-5305
    • Jones, P.M.1    George, A.M.2
  • 147
    • 0029781640 scopus 로고    scopus 로고
    • Multidrug resistance in Lactococcus lactis: evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane
    • Bolhuis H., van Veen H.W., Molenaar D., Poolman B., Driessen A.J.M., and Konings W.N. Multidrug resistance in Lactococcus lactis: evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane. EMBO J 15 (1996) 4239-4245
    • (1996) EMBO J , vol.15 , pp. 4239-4245
    • Bolhuis, H.1    van Veen, H.W.2    Molenaar, D.3    Poolman, B.4    Driessen, A.J.M.5    Konings, W.N.6
  • 148
    • 0030784559 scopus 로고    scopus 로고
    • Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membrane by P-glycoprotein
    • Shapiro A.B., and Ling V. Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membrane by P-glycoprotein. Eur J Biochem 250 (1997) 122-129
    • (1997) Eur J Biochem , vol.250 , pp. 122-129
    • Shapiro, A.B.1    Ling, V.2
  • 149
    • 0030822996 scopus 로고    scopus 로고
    • P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer
    • Shapiro A.B., Corder A.B., and Ling V. P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer. Eur J Biochem 250 (1997) 115-121
    • (1997) Eur J Biochem , vol.250 , pp. 115-121
    • Shapiro, A.B.1    Corder, A.B.2    Ling, V.3
  • 150
    • 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. 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 (1998) 181-188
    • (1998) Eur J Biochem , vol.254 , pp. 181-188
    • Shapiro, A.B.1    Ling, V.2
  • 151
    • 0035503608 scopus 로고    scopus 로고
    • P-glycoprotein does not reduce substrate concentration from the extracellular leaflet of the plasma membrane in living cells
    • Chen Y., Pant A.C., and Simon S.M. P-glycoprotein does not reduce substrate concentration from the extracellular leaflet of the plasma membrane in living cells. Cancer Res 61 (2001) 7763-7769
    • (2001) Cancer Res , vol.61 , pp. 7763-7769
    • Chen, Y.1    Pant, A.C.2    Simon, S.M.3
  • 152
    • 0026580336 scopus 로고
    • Is the multidrug transporter a flippase?
    • Higgins C.F., and Gottesman M.M. Is the multidrug transporter a flippase?. Trends Biochem Sci 17 (1992) 18-21
    • (1992) Trends Biochem Sci , vol.17 , pp. 18-21
    • Higgins, C.F.1    Gottesman, M.M.2
  • 153
    • 0028332661 scopus 로고
    • Calcein accumulation as a fluorometric functional assay of the multidrug transporter
    • Hollo Z., Homolya L., Davis C.W., and Sarkadi B. Calcein accumulation as a fluorometric functional assay of the multidrug transporter. Biochim Biophys Acta 1191 (1994) 384-388
    • (1994) Biochim Biophys Acta , vol.1191 , pp. 384-388
    • Hollo, Z.1    Homolya, L.2    Davis, C.W.3    Sarkadi, B.4
  • 154
    • 0028285002 scopus 로고
    • Kinetic evidence suggesting that the multidrug transporter differentially handles influx and efflux of its substrates
    • Stein W.D., Cardarelli C., Pastan I., and Gottesman M.M. Kinetic evidence suggesting that the multidrug transporter differentially handles influx and efflux of its substrates. Mol Pharmacol 45 (1994) 763-772
    • (1994) Mol Pharmacol , vol.45 , pp. 763-772
    • Stein, W.D.1    Cardarelli, C.2    Pastan, I.3    Gottesman, M.M.4
  • 155
    • 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. A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein. J Biol Chem 277 (2002) 45688-45694
    • (2002) J Biol Chem , vol.277 , pp. 45688-45694
    • Omote, H.1    Al-Shawi, M.K.2
  • 156
    • 0035849506 scopus 로고    scopus 로고
    • Phospholipid flippase activity of the reconstituted P-glycoprotein multidrug transporter
    • Romsicki Y., and Sharom F.J. Phospholipid flippase activity of the reconstituted P-glycoprotein multidrug transporter. Biochemistry 40 (2001) 6937-6947
    • (2001) Biochemistry , vol.40 , pp. 6937-6947
    • Romsicki, Y.1    Sharom, F.J.2
  • 157
    • 22544457473 scopus 로고    scopus 로고
    • The reconstituted P-glycoprotein multidrug transporter is a flippase for glucosylceramide and other simple glycosphingolipids
    • Eckford P.D.W., and Sharom F.J. The reconstituted P-glycoprotein multidrug transporter is a flippase for glucosylceramide and other simple glycosphingolipids. Biochem J 389 (2005) 517-526
    • (2005) Biochem J , vol.389 , pp. 517-526
    • Eckford, P.D.W.1    Sharom, F.J.2
  • 158
    • 0025060257 scopus 로고
    • Heat shock and arsenite increase expression of the multidrug resistance (MDR1) gene in human renal carcinoma cells
    • Chin K.V., Tanaka S., Darlington G., Pastan I., and Gottesman M.M. Heat shock and arsenite increase expression of the multidrug resistance (MDR1) gene in human renal carcinoma cells. J Biol Chem 265 (1990) 221-226
    • (1990) J Biol Chem , vol.265 , pp. 221-226
    • Chin, K.V.1    Tanaka, S.2    Darlington, G.3    Pastan, I.4    Gottesman, M.M.5
  • 159
  • 160
    • 0031014915 scopus 로고    scopus 로고
    • Involvement of the transcription factor NF-IL6 in phorbol ester induction of P-glycoprotein in U937 cells
    • Combates N.J., Kwon P.O., Rzepka R.W., and Cohen D. Involvement of the transcription factor NF-IL6 in phorbol ester induction of P-glycoprotein in U937 cells. Cell Growth Differ 8 (1997) 213-219
    • (1997) Cell Growth Differ , vol.8 , pp. 213-219
    • Combates, N.J.1    Kwon, P.O.2    Rzepka, R.W.3    Cohen, D.4
  • 161
    • 0027506202 scopus 로고
    • Induction of multidrug resistance in human cells by transient exposure to different chemotherapeutic drugs
    • Chaudhary P.M., and Roninson I.B. Induction of multidrug resistance in human cells by transient exposure to different chemotherapeutic drugs. J Natl Cancer Inst 85 (1993) 632-639
    • (1993) J Natl Cancer Inst , vol.85 , pp. 632-639
    • Chaudhary, P.M.1    Roninson, I.B.2
  • 162
    • 0025477701 scopus 로고
    • Regulation of mdr RNA levels in response to cytotoxic drugs in rodent cells
    • Chin K.V., Chauhan S.S., Pastan I., and Gottesman M.M. Regulation of mdr RNA levels in response to cytotoxic drugs in rodent cells. Cell Growth Differ 1 (1990) 361-365
    • (1990) Cell Growth Differ , vol.1 , pp. 361-365
    • Chin, K.V.1    Chauhan, S.S.2    Pastan, I.3    Gottesman, M.M.4
  • 163
    • 0034723353 scopus 로고    scopus 로고
    • Transcriptional activation of the MDR1 gene by UV irradiation
    • Hu Z., Jin S., and Scotto K.W. Transcriptional activation of the MDR1 gene by UV irradiation. J Biol Chem 275 (2000) 2979-2985
    • (2000) J Biol Chem , vol.275 , pp. 2979-2985
    • Hu, Z.1    Jin, S.2    Scotto, K.W.3
  • 164
    • 0030984112 scopus 로고    scopus 로고
    • p53-dependent regulation of MDR1 gene expression causes selective resistance to chemotherapeutic agents
    • Thottassery J.V., Zambett G.P., Arimeri K., Schuetz E.G., and Schuetz J.D. p53-dependent regulation of MDR1 gene expression causes selective resistance to chemotherapeutic agents. Proc Natl Acad Sci USA 94 (1997) 11037-11042
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11037-11042
    • Thottassery, J.V.1    Zambett, G.P.2    Arimeri, K.3    Schuetz, E.G.4    Schuetz, J.D.5
  • 165
    • 0027191153 scopus 로고
    • The core promoter region of the P-glycoprotein gene is sufficient to confer differential responsiveness to wild-type and mutant p53
    • Zastawny R.L., Salvino R., Chen J., Benchimol S., and Ling V. The core promoter region of the P-glycoprotein gene is sufficient to confer differential responsiveness to wild-type and mutant p53. Oncogene 8 (1993) 1529-1535
    • (1993) Oncogene , vol.8 , pp. 1529-1535
    • Zastawny, R.L.1    Salvino, R.2    Chen, J.3    Benchimol, S.4    Ling, V.5
  • 166
    • 23644453292 scopus 로고    scopus 로고
    • Reactive oxygen species-linked regulation of the multidrug resistance transporter P-glycoprotein in Nox-1 overexpressing prostate tumour spheroids
    • Wartenberg M., Hoffmann E., Schwindt H., Grunheck F., Petros J., Arnold J.R.S., et al. Reactive oxygen species-linked regulation of the multidrug resistance transporter P-glycoprotein in Nox-1 overexpressing prostate tumour spheroids. FEBS Lett 579 (2005) 4541-4549
    • (2005) FEBS Lett , vol.579 , pp. 4541-4549
    • Wartenberg, M.1    Hoffmann, E.2    Schwindt, H.3    Grunheck, F.4    Petros, J.5    Arnold, J.R.S.6
  • 167
    • 0023179571 scopus 로고
    • Expression of the multidrug-resistant gene in hepatocarcinogenesis and regenerating rat liver
    • Thorgeirsson S.S., Huber B.E., Sorrell S., Fojo A.T., Pastan I., and Gottesman M.M. Expression of the multidrug-resistant gene in hepatocarcinogenesis and regenerating rat liver. Science 236 (1987) 1120-1122
    • (1987) Science , vol.236 , pp. 1120-1122
    • Thorgeirsson, S.S.1    Huber, B.E.2    Sorrell, S.3    Fojo, A.T.4    Pastan, I.5    Gottesman, M.M.6
  • 168
    • 0025386379 scopus 로고
    • Regulation of the multidrug resistance gene in regenerating rat liver
    • Marino P.A., Gottesman M.M., and Pastan I. Regulation of the multidrug resistance gene in regenerating rat liver. Cell Growth Differ 1 (1990) 57-62
    • (1990) Cell Growth Differ , vol.1 , pp. 57-62
    • Marino, P.A.1    Gottesman, M.M.2    Pastan, I.3
  • 169
    • 0032713821 scopus 로고    scopus 로고
    • Rapid activation of MDR1 gene expression in human metastatic sarcoma after in vivo exposure to doxorubicin
    • Abolhoda A., Wilson A.E., Ross H., Danenberg P.V., Burt M., and Scotto K.W. Rapid activation of MDR1 gene expression in human metastatic sarcoma after in vivo exposure to doxorubicin. Clin Cancer Res 5 (1999) 3352-3356
    • (1999) Clin Cancer Res , vol.5 , pp. 3352-3356
    • Abolhoda, A.1    Wilson, A.E.2    Ross, H.3    Danenberg, P.V.4    Burt, M.5    Scotto, K.W.6
  • 171
    • 0032403478 scopus 로고    scopus 로고
    • Hypomethylation status of CpG sites at the promoter region and overexpression of the human MDR1 gene in acute myeloid leukaemias
    • Nakayama M., Wada M., Harada T., Nagayama J., Kusaba H., Ohshima K., et al. Hypomethylation status of CpG sites at the promoter region and overexpression of the human MDR1 gene in acute myeloid leukaemias. Blood 92 (1998) 4296-4307
    • (1998) Blood , vol.92 , pp. 4296-4307
    • Nakayama, M.1    Wada, M.2    Harada, T.3    Nagayama, J.4    Kusaba, H.5    Ohshima, K.6
  • 172
    • 0034637516 scopus 로고    scopus 로고
    • Regulation of multidrug resistance 1 (MDR1)/P-glycoprotein gene expression and activity by heat-shock transcription factor 1 (HSF1)
    • Vilsboa N.E., Galan A., Troyano A., de Blas E., and Aller P. Regulation of multidrug resistance 1 (MDR1)/P-glycoprotein gene expression and activity by heat-shock transcription factor 1 (HSF1). J Biol Chem 275 (2000) 24970-24976
    • (2000) J Biol Chem , vol.275 , pp. 24970-24976
    • Vilsboa, N.E.1    Galan, A.2    Troyano, A.3    de Blas, E.4    Aller, P.5
  • 173
    • 0027290898 scopus 로고
    • Sp1 activates the MDR1 promoter through one of two distinct G-rich regions that modulate promoter activity
    • Cornwell M.M., and Smith D.E. Sp1 activates the MDR1 promoter through one of two distinct G-rich regions that modulate promoter activity. J Biol Chem 268 (1993) 19505-19511
    • (1993) J Biol Chem , vol.268 , pp. 19505-19511
    • Cornwell, M.M.1    Smith, D.E.2
  • 174
    • 0031932166 scopus 로고    scopus 로고
    • Regulation of the MDR1 promoter by cyclic AMP-dependent protein kinase and transcription factor Sp1
    • Rohlff C., and Glazer R.I. Regulation of the MDR1 promoter by cyclic AMP-dependent protein kinase and transcription factor Sp1. Int J Oncol 12 (1998) 383-386
    • (1998) Int J Oncol , vol.12 , pp. 383-386
    • Rohlff, C.1    Glazer, R.I.2
  • 175
    • 0032920661 scopus 로고    scopus 로고
    • Increased AP-1 activity in drug resistant human breast cancer MCF-7 cells
    • Daschner P.J., Ciolino H.P., Plonzek C.A., and Yeh G.C. Increased AP-1 activity in drug resistant human breast cancer MCF-7 cells. Breast Cancer Res Tr 53 (1999) 229-240
    • (1999) Breast Cancer Res Tr , vol.53 , pp. 229-240
    • Daschner, P.J.1    Ciolino, H.P.2    Plonzek, C.A.3    Yeh, G.C.4
  • 176
    • 0028149768 scopus 로고
    • NF-IL6 a member of the C/EBP family of transcription factors binds and trans-activates the human MDR1 gene promoter
    • Combates N.J., Rzepka R.W., Chen Y.N., and Cohen D. NF-IL6 a member of the C/EBP family of transcription factors binds and trans-activates the human MDR1 gene promoter. J Biol Chem 269 (1994) 29715-29719
    • (1994) J Biol Chem , vol.269 , pp. 29715-29719
    • Combates, N.J.1    Rzepka, R.W.2    Chen, Y.N.3    Cohen, D.4
  • 177
    • 0031861729 scopus 로고    scopus 로고
    • Transcriptional regulation of the MDR1 gene by histone acetyltransferase/deacetylase is mediated by NF-Y
    • Jin S., and Scotto K.W. Transcriptional regulation of the MDR1 gene by histone acetyltransferase/deacetylase is mediated by NF-Y. Mol Cell Biol 18 (1998) 4377-4384
    • (1998) Mol Cell Biol , vol.18 , pp. 4377-4384
    • Jin, S.1    Scotto, K.W.2
  • 178
    • 0028820126 scopus 로고
    • 12-O-Tetradecanoylphorbol-13-acetate activation of the MDR1 promoter is mediated by EGR1
    • McCoy C., Smith D.E., and Cornwell M.M. 12-O-Tetradecanoylphorbol-13-acetate activation of the MDR1 promoter is mediated by EGR1. Mol Cell Biol 15 (1995) 6100-6108
    • (1995) Mol Cell Biol , vol.15 , pp. 6100-6108
    • McCoy, C.1    Smith, D.E.2    Cornwell, M.M.3
  • 179
    • 0032513246 scopus 로고    scopus 로고
    • Direct involvement of the Y-box binding protein YB-1 in genotoxic stress-induced activation of the human multidrug resistance 1 gene
    • Ohga T., Uchiumi T., Makino Y., Wada M., Kuwano M., and Kohno K. Direct involvement of the Y-box binding protein YB-1 in genotoxic stress-induced activation of the human multidrug resistance 1 gene. J Biol Chem 273 (1998) 5997-6000
    • (1998) J Biol Chem , vol.273 , pp. 5997-6000
    • Ohga, T.1    Uchiumi, T.2    Makino, Y.3    Wada, M.4    Kuwano, M.5    Kohno, K.6
  • 180
    • 0034635186 scopus 로고    scopus 로고
    • Identification and characterisation of the MDR1 promoter-enhancing factor 1 (MEF1) in the multidrug resistant HL60/VCR human acute myeloid leukaemia cell line
    • Ogretmen B., and Safa A.R. Identification and characterisation of the MDR1 promoter-enhancing factor 1 (MEF1) in the multidrug resistant HL60/VCR human acute myeloid leukaemia cell line. Biochemistry 39 (2000) 194-204
    • (2000) Biochemistry , vol.39 , pp. 194-204
    • Ogretmen, B.1    Safa, A.R.2
  • 181
    • 0033573850 scopus 로고    scopus 로고
    • Negative regulation of MDR1 promoter activity in MCF-7, but not multidrug resistant MCF-7/Adr, cells by cross-coupled NF-kappa B/p65 and c-Fos transcription factors and their interaction with a CAAT region
    • Ogretmen B., and Safa A.R. Negative regulation of MDR1 promoter activity in MCF-7, but not multidrug resistant MCF-7/Adr, cells by cross-coupled NF-kappa B/p65 and c-Fos transcription factors and their interaction with a CAAT region. Biochemistry 38 (1999) 2189-2199
    • (1999) Biochemistry , vol.38 , pp. 2189-2199
    • Ogretmen, B.1    Safa, A.R.2
  • 182
    • 0030662414 scopus 로고    scopus 로고
    • Wild-type p53 gene increases MDR1 gene expression but decreases drug resistance in an MDR cell line KBV200
    • Li Z.H., Zhu Y.J., and Lit X.T. Wild-type p53 gene increases MDR1 gene expression but decreases drug resistance in an MDR cell line KBV200. Cancer Lett 119 (1997) 177-184
    • (1997) Cancer Lett , vol.119 , pp. 177-184
    • Li, Z.H.1    Zhu, Y.J.2    Lit, X.T.3
  • 183
    • 0038193551 scopus 로고    scopus 로고
    • P-glycoprotein (MDR1) expression in leukaemic cells is regulated at two distinct steps, mRNA stabilisation and translational initiation
    • Yague E., Armesilla A.L., Harrison G., Elliott J., Sardini A., Higgins C.F., et al. P-glycoprotein (MDR1) expression in leukaemic cells is regulated at two distinct steps, mRNA stabilisation and translational initiation. J Biol Chem 278 (2003) 10344-10352
    • (2003) J Biol Chem , vol.278 , pp. 10344-10352
    • Yague, E.1    Armesilla, A.L.2    Harrison, G.3    Elliott, J.4    Sardini, A.5    Higgins, C.F.6
  • 184
    • 30644477941 scopus 로고    scopus 로고
    • Heat shock-independent induction of multidrug resistance by heat shock factor 1
    • Tchenio T., Havard M., Martinez L.A., and Dautry F. Heat shock-independent induction of multidrug resistance by heat shock factor 1. Mol Cell Biol 26 (2006) 580-591
    • (2006) Mol Cell Biol , vol.26 , pp. 580-591
    • Tchenio, T.1    Havard, M.2    Martinez, L.A.3    Dautry, F.4
  • 185
    • 0005582691 scopus 로고    scopus 로고
    • Transcription of the multidrug resistance gene MDR1: a therapeutic target
    • Scotto K.W., and Johnson R.A. Transcription of the multidrug resistance gene MDR1: a therapeutic target. Mol Interv 1 (2001) 117-125
    • (2001) Mol Interv , vol.1 , pp. 117-125
    • Scotto, K.W.1    Johnson, R.A.2
  • 186
    • 0037648903 scopus 로고    scopus 로고
    • The basic and clinical implications of ABC transporters, Y-box binding protein-1 (YB-1) and angiogenesis-related factors in human malignancies
    • Kuwano M., Uchiumi T., Hayakawa H., Ono M., Wada M., Izumi H., et al. The basic and clinical implications of ABC transporters, Y-box binding protein-1 (YB-1) and angiogenesis-related factors in human malignancies. Cancer Sci 94 (2003) 9-14
    • (2003) Cancer Sci , vol.94 , pp. 9-14
    • Kuwano, M.1    Uchiumi, T.2    Hayakawa, H.3    Ono, M.4    Wada, M.5    Izumi, H.6
  • 187
    • 0027483327 scopus 로고
    • Identification of 5′ and 3′ sequences involved in the regulation of transcription of the human mdr1 gene in vivo
    • Madden M.J., Morrow C.S., Nakagawa M., Goldsmith M.E., Fairchild C.R., and Cowan K.H. Identification of 5′ and 3′ sequences involved in the regulation of transcription of the human mdr1 gene in vivo. J Biol Chem 268 (1993) 8290-8297
    • (1993) J Biol Chem , vol.268 , pp. 8290-8297
    • Madden, M.J.1    Morrow, C.S.2    Nakagawa, M.3    Goldsmith, M.E.4    Fairchild, C.R.5    Cowan, K.H.6
  • 188
    • 0345688182 scopus 로고    scopus 로고
    • Transcriptional regulation of ABC drug transporters
    • Scotto K.W. Transcriptional regulation of ABC drug transporters. Oncogene 22 (2003) 7496-7511
    • (2003) Oncogene , vol.22 , pp. 7496-7511
    • Scotto, K.W.1
  • 189
    • 0035038919 scopus 로고    scopus 로고
    • The orphan nuclear receptor SXR coordinately regulates drug metabolism and efflux
    • Synold T.W., Dussault I., and Forman B.M. The orphan nuclear receptor SXR coordinately regulates drug metabolism and efflux. Nat Med 7 (2001) 584-590
    • (2001) Nat Med , vol.7 , pp. 584-590
    • Synold, T.W.1    Dussault, I.2    Forman, B.M.3
  • 190
    • 0035805536 scopus 로고    scopus 로고
    • Nuclear receptor response elements mediate induction of intestinal MDR1 by rifampicin
    • Geick A., Eichelbaum M., and Burk O. Nuclear receptor response elements mediate induction of intestinal MDR1 by rifampicin. J Biol Chem 276 (2001) 14581-14587
    • (2001) J Biol Chem , vol.276 , pp. 14581-14587
    • Geick, A.1    Eichelbaum, M.2    Burk, O.3
  • 191
    • 0035857453 scopus 로고    scopus 로고
    • The expression of pregnane X receptor and its target gene, cytochrome P450 3A1, in perinatal mouse
    • Masuyama H., Hirsch-Ernst K.I., Mizutani H., Inoshita H., and Kudo T. The expression of pregnane X receptor and its target gene, cytochrome P450 3A1, in perinatal mouse. Mol Cell Endocrinol 172 (2001) 47-56
    • (2001) Mol Cell Endocrinol , vol.172 , pp. 47-56
    • Masuyama, H.1    Hirsch-Ernst, K.I.2    Mizutani, H.3    Inoshita, H.4    Kudo, T.5
  • 192
    • 17844366538 scopus 로고    scopus 로고
    • The pregnane X receptor regulates gene expression in a ligand- and promoter-selective fashion
    • Masuyama H., Suwaki N., Tateishi Y., Nakatsukasa H., Segawa T., and Hiramatsu Y. The pregnane X receptor regulates gene expression in a ligand- and promoter-selective fashion. Mol Endocrinol 19 (2005) 1170-1180
    • (2005) Mol Endocrinol , vol.19 , pp. 1170-1180
    • Masuyama, H.1    Suwaki, N.2    Tateishi, Y.3    Nakatsukasa, H.4    Segawa, T.5    Hiramatsu, Y.6
  • 193
    • 26844549175 scopus 로고    scopus 로고
    • A role for constitutive androstane receptor in the regulation of human intestinal MDR1 expression
    • Burk O., Arnold K.A., Geick A., Tegude H., and Eichelbaum M. A role for constitutive androstane receptor in the regulation of human intestinal MDR1 expression. Biol Chem 386 (2005) 503-513
    • (2005) Biol Chem , vol.386 , pp. 503-513
    • Burk, O.1    Arnold, K.A.2    Geick, A.3    Tegude, H.4    Eichelbaum, M.5
  • 194
    • 29244438188 scopus 로고    scopus 로고
    • Aberrant transcription from an unrelated promoter can result in MDR-1 expression following drug selection in vitro and in relapsed lymphoma samples
    • Huff L.M., Wang Z., Iglesias A., Fojo T., and Lee J.S. Aberrant transcription from an unrelated promoter can result in MDR-1 expression following drug selection in vitro and in relapsed lymphoma samples. Cancer Res 65 (2005) 11694-11703
    • (2005) Cancer Res , vol.65 , pp. 11694-11703
    • Huff, L.M.1    Wang, Z.2    Iglesias, A.3    Fojo, T.4    Lee, J.S.5
  • 196
    • 28544432478 scopus 로고    scopus 로고
    • Epigenetic changes to the MDR-1 locus in response to chemotherapeutic drugs
    • Baker E.K., Johnstone R.W., Zalcberg J.R., and El-Osta A. Epigenetic changes to the MDR-1 locus in response to chemotherapeutic drugs. Oncogene 24 (2005) 8061-8075
    • (2005) Oncogene , vol.24 , pp. 8061-8075
    • Baker, E.K.1    Johnstone, R.W.2    Zalcberg, J.R.3    El-Osta, A.4
  • 197
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman M.M., and Pastan I. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu Rev Biochem 62 (1993) 385-427
    • (1993) Annu Rev Biochem , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 198
    • 31844448665 scopus 로고    scopus 로고
    • The translocation mechanism of P-glycoprotein
    • Callaghan R., Ford R.C., and Kerr I.D. The translocation mechanism of P-glycoprotein. FEBS Lett 580 (2006) 1056-1063
    • (2006) FEBS Lett , vol.580 , pp. 1056-1063
    • Callaghan, R.1    Ford, R.C.2    Kerr, I.D.3
  • 199
    • 0033958086 scopus 로고    scopus 로고
    • Multiple physiological functions for multidrug transporter P-glycoprotein?
    • Johnstone R.W., Ruefli A.A., and Smyth M.J. Multiple physiological functions for multidrug transporter P-glycoprotein?. Trends Biochem Sci 25 (2000) 1-6
    • (2000) Trends Biochem Sci , vol.25 , pp. 1-6
    • Johnstone, R.W.1    Ruefli, A.A.2    Smyth, M.J.3
  • 200
    • 0036710923 scopus 로고    scopus 로고
    • Transcriptional regulators of the human multidrug resistance 1 gene: recent views
    • Labialle S., Gayet L., Marthinet E., Rigal D., and Baggetto L.G. Transcriptional regulators of the human multidrug resistance 1 gene: recent views. Biochem Pharmacol 64 (2002) 943-948
    • (2002) Biochem Pharmacol , vol.64 , pp. 943-948
    • Labialle, S.1    Gayet, L.2    Marthinet, E.3    Rigal, D.4    Baggetto, L.G.5


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