메뉴 건너뛰기




Volumn 70, Issue 4, 2005, Pages 500-510

Interactions of mefloquine with ABC proteins, MRP1 (ABCC1) and MRP4 (ABCC4) that are present in human red cell membranes

Author keywords

ATP hydrolysis; Erythrocyte membranes; Mefloquine; MK 571; Multidrug resistance associated proteins 1 and 4

Indexed keywords

2,4 DINITROPHENOL; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMODIAQUINE; ANTIMALARIAL AGENT; CALCEIN; CHLOROQUINE; CYCLIC GMP; GLUTATHIONE DERIVATIVE; GLUTATHIONE DISULFIDE; MEFLOQUINE; MULTIDRUG RESISTANCE PROTEIN 1; MULTIDRUG RESISTANCE PROTEIN 4; MULTIDRUG RESISTANCE PROTEIN 5; PRIMAQUINE; PROSTAGLANDIN E1; QUERCETIN; QUINIDINE; QUININE; QUINOLINE DERIVATIVE; VERLUKAST;

EID: 22144455747     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2005.05.022     Document Type: Article
Times cited : (61)

References (47)
  • 1
    • 0029912351 scopus 로고    scopus 로고
    • ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pump
    • I. Leier, G. Jedlitschky, U. Buchholz, M. Center, S.P.C. Cole, and R.G. Deeley ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pump Biochem J 314 1996 433 437
    • (1996) Biochem J , vol.314 , pp. 433-437
    • Leier, I.1    Jedlitschky, G.2    Buchholz, U.3    Center, M.4    Cole, S.P.C.5    Deeley, R.G.6
  • 2
    • 0029958285 scopus 로고    scopus 로고
    • Identification of the multidrug-resistance protein (MRP) as the glutathione-S-conjugate export pump of erythrocytes
    • L. Pulaski, G. Jedlitschky, I. Leier, U. Buchholz, and D. Keppler Identification of the multidrug-resistance protein (MRP) as the glutathione-S-conjugate export pump of erythrocytes Eur J Biochem 241 1996 644 648
    • (1996) Eur J Biochem , vol.241 , pp. 644-648
    • Pulaski, L.1    Jedlitschky, G.2    Leier, I.3    Buchholz, U.4    Keppler, D.5
  • 3
    • 20244386956 scopus 로고    scopus 로고
    • Increased sensitivity to anticancer drugs and decreased inflammatory response in mice lacking the multidrug resistance-associated protein
    • J. Wijnholds, R. Evers, L.M.R. Van, C.A.A.M. Mol, G.J.R. Zaman, and U. Mayer Increased sensitivity to anticancer drugs and decreased inflammatory response in mice lacking the multidrug resistance-associated protein Nat Med 3 1997 1275 1279
    • (1997) Nat Med , vol.3 , pp. 1275-1279
    • Wijnholds, J.1    Evers, R.2    Van, L.M.R.3    Mol, C.A.A.M.4    Zaman, G.J.R.5    Mayer, U.6
  • 4
    • 0141447401 scopus 로고    scopus 로고
    • CGMP and glutathione-conjugate transport in human erythrocytes - The roles of the multidrug resistance-associated proteins, MRP1, MRP4 and MRP5
    • A. Klokouzas, C.P. Wu, H.W. Van Veen, M.A. Barrand, and S.B. Hladky cGMP and glutathione-conjugate transport in human erythrocytes - the roles of the multidrug resistance-associated proteins, MRP1, MRP4 and MRP5 Eur J Biochem 270 2003 3696 3708
    • (2003) Eur J Biochem , vol.270 , pp. 3696-3708
    • Klokouzas, A.1    Wu, C.P.2    Van Veen, H.W.3    Barrand, M.A.4    Hladky, S.B.5
  • 5
    • 0032530924 scopus 로고    scopus 로고
    • Direct binding of chloroquine to the multidrug resistance protein (MRP). Possible role for MRP in chloroquine drug transport and resistance in tumor cells
    • M. Vezmar, and E. Georges Direct binding of chloroquine to the multidrug resistance protein (MRP). Possible role for MRP in chloroquine drug transport and resistance in tumor cells Biochem Pharmacol 56 1998 733 742
    • (1998) Biochem Pharmacol , vol.56 , pp. 733-742
    • Vezmar, M.1    Georges, E.2
  • 6
    • 0030598403 scopus 로고    scopus 로고
    • Modulation of the function of human MDR1 P-glycoprotein by the antimalarial drug mefloquine
    • C.D. Riffkin, R. Chung, D.M. Wall, J.R. Zalcberg, A.F. Cowman, and M. Foley Modulation of the function of human MDR1 P-glycoprotein by the antimalarial drug mefloquine Biochem Pharmacol 52 1996 1545 1552
    • (1996) Biochem Pharmacol , vol.52 , pp. 1545-1552
    • Riffkin, C.D.1    Chung, R.2    Wall, D.M.3    Zalcberg, J.R.4    Cowman, A.F.5    Foley, M.6
  • 7
    • 0031049609 scopus 로고    scopus 로고
    • Mutually co-operative interactions between modulators of p-glycoprotein
    • Y.M. Shao, S. Ayesh, and W.D. Stein Mutually co-operative interactions between modulators of p-glycoprotein Biochim Biophys Acta: Mol Basis Dis 1360 1997 30 38
    • (1997) Biochim Biophys Acta: Mol Basis Dis , vol.1360 , pp. 30-38
    • Shao, Y.M.1    Ayesh, S.2    Stein, W.D.3
  • 8
    • 0035054299 scopus 로고    scopus 로고
    • Cellular and biophysical evidence for interactions between adenosine triphosphate and P-glycoprotein substrates: Functional implications for adenosine triphosphate/drug cotransport in P-glycoprotein overexpressing tumor cells and in P-glycoprotein low-level expressing erythrocytes
    • E.H. Abraham, B. Shrivastav, A.Y. Salikhova, K.M. Sterling, N. Johnston, and G. Guidotti Cellular and biophysical evidence for interactions between adenosine triphosphate and P-glycoprotein substrates: functional implications for adenosine triphosphate/drug cotransport in P-glycoprotein overexpressing tumor cells and in P-glycoprotein low-level expressing erythrocytes Blood Cells Mol Dis 27 2001 181 200
    • (2001) Blood Cells Mol Dis , vol.27 , pp. 181-200
    • Abraham, E.H.1    Shrivastav, B.2    Salikhova, A.Y.3    Sterling, K.M.4    Johnston, N.5    Guidotti, G.6
  • 9
    • 0022599437 scopus 로고
    • Derivation and preliminary characterization of adriamycin resistant lines of human-lung cancer-cells
    • P.R. Twentyman, N.E. Fox, K.A. Wright, and N.M. Bleehen Derivation and preliminary characterization of adriamycin resistant lines of human-lung cancer-cells Br J Cancer 53 1986 529 537
    • (1986) Br J Cancer , vol.53 , pp. 529-537
    • Twentyman, P.R.1    Fox, N.E.2    Wright, K.A.3    Bleehen, N.M.4
  • 10
    • 0028155964 scopus 로고
    • A 190 k protein overexpressed in non-P-glycoprotein containing MDR cells and its relation to the MRP gene
    • M.A. Barrand, A.C. Heppell-Parton, K.A. Wright, P.H. Rabbitts, and P.R. Twentyman A 190 k protein overexpressed in non-P-glycoprotein containing MDR cells and its relation to the MRP gene J Natl Cancer Inst 86 1994 110 117
    • (1994) J Natl Cancer Inst , vol.86 , pp. 110-117
    • Barrand, M.A.1    Heppell-Parton, A.C.2    Wright, K.A.3    Rabbitts, P.H.4    Twentyman, P.R.5
  • 11
    • 0036893815 scopus 로고    scopus 로고
    • Thiopurine metabolism and identification of the thiopurine metabolites transported by MRP4 and MRP5 overexpressed in human embryonic kidney cells
    • P.R. Wielinga, G. Reid, E.E. Challa, I. van der Heijden, L. Van Deemter, and M. De Haas Thiopurine metabolism and identification of the thiopurine metabolites transported by MRP4 and MRP5 overexpressed in human embryonic kidney cells Mol Pharmacol 62 2002 1321 1331
    • (2002) Mol Pharmacol , vol.62 , pp. 1321-1331
    • Wielinga, P.R.1    Reid, G.2    Challa, E.E.3    Van Der Heijden, I.4    Van Deemter, L.5    De Haas, M.6
  • 12
    • 0038752694 scopus 로고    scopus 로고
    • Characterization of the transport of nucleoside analog drugs by the human multidrug resistance proteins MRP4 and MRP5
    • G. Reid, P. Wielinga, N. Zelcer, M. De Haas, L. Van Deemter, and J. Wijnholds Characterization of the transport of nucleoside analog drugs by the human multidrug resistance proteins MRP4 and MRP5 Mol Pharmacol 63 2003 1094 1103
    • (2003) Mol Pharmacol , vol.63 , pp. 1094-1103
    • Reid, G.1    Wielinga, P.2    Zelcer, N.3    De Haas, M.4    Van Deemter, L.5    Wijnholds, J.6
  • 13
    • 0020003969 scopus 로고
    • + channel in one-step inside-out vesicles from human red cell membranes
    • + channel in one-step inside-out vesicles from human red cell membranes Nature 296 1982 742 744
    • (1982) Nature , vol.296 , pp. 742-744
    • Lew, V.L.1    Muallem, S.2    Seymour, C.A.3
  • 14
    • 0023722545 scopus 로고    scopus 로고
    • Mechanism of spontaneous inside-out vesiculation of red cell membranes
    • V.L. Lew, A. Hockaday, C.J. Freeman, and R.M. Bookchin Mechanism of spontaneous inside-out vesiculation of red cell membranes J Cell Biol 106 1998 1893 1901
    • (1998) J Cell Biol , vol.106 , pp. 1893-1901
    • Lew, V.L.1    Hockaday, A.2    Freeman, C.J.3    Bookchin, R.M.4
  • 15
    • 0028006733 scopus 로고
    • GS-X pump is functionally overexpressed in cis- diamminedichloroplatinum(ii)-resistant human leukemia HL-60 cells and down-regulated by cell-differentiation
    • T. Ishikawa, C.D. Wright, and H. Ishizuka GS-X pump is functionally overexpressed in cis-diamminedichloroplatinum(ii)-resistant human leukemia HL-60 cells and down-regulated by cell-differentiation J Biol Chem 269 1994 29085 29093
    • (1994) J Biol Chem , vol.269 , pp. 29085-29093
    • Ishikawa, T.1    Wright, C.D.2    Ishizuka, H.3
  • 16
    • 0029805368 scopus 로고    scopus 로고
    • + exchange by soluble and particulate guanylate cyclase
    • + exchange by soluble and particulate guanylate cyclase Am J Physiol-Cell Physiol 271 1996 C1556 C1564
    • (1996) Am J Physiol-Cell Physiol , vol.271
    • Petrov, V.1    Lijnen, P.2
  • 17
    • 0031878165 scopus 로고    scopus 로고
    • 2+, calmodulin-dependent cyclic nucleotide phosphodiesterase which is involved in the hydrolysis of cGMP
    • 2+, calmodulin-dependent cyclic nucleotide phosphodiesterase which is involved in the hydrolysis of cGMP Meth Find Exp Clin Pharmacol 20 1998 387 393
    • (1998) Meth Find Exp Clin Pharmacol , vol.20 , pp. 387-393
    • Petrov, V.1    Fagard, R.2    Lijnen, P.3
  • 18
    • 0029618288 scopus 로고
    • Effect of probenecid, verapamil and progesterone on the concentration-dependent and temperature-sensitive human erythrocyte uptake and export of guanosine 3′,5′ cyclic monophosphate (cGMP)
    • K. Flo, M. Hansen, A. Orbo, K.E. Kjorstad, J.M. Maltau, and G. Sager Effect of probenecid, verapamil and progesterone on the concentration-dependent and temperature-sensitive human erythrocyte uptake and export of guanosine 3′,5′ cyclic monophosphate (cGMP) Scand J Clin Lab Invest 55 1995 715 721
    • (1995) Scand J Clin Lab Invest , vol.55 , pp. 715-721
    • Flo, K.1    Hansen, M.2    Orbo, A.3    Kjorstad, K.E.4    Maltau, J.M.5    Sager, G.6
  • 19
    • 0035879951 scopus 로고    scopus 로고
    • Influences of glutathione on anionic substrate efflux in tumour cells expressing the multidrug resistance-associated protein, MRP1
    • T. Bagrij, A. Klokouzas, S.B. Hladky, and M.A. Barrand Influences of glutathione on anionic substrate efflux in tumour cells expressing the multidrug resistance-associated protein, MRP1 Biochem Pharmacol 62 2001 199 206
    • (2001) Biochem Pharmacol , vol.62 , pp. 199-206
    • Bagrij, T.1    Klokouzas, A.2    Hladky, S.B.3    Barrand, M.A.4
  • 20
    • 0034614112 scopus 로고    scopus 로고
    • Analysis of the MRP4 drug resistance profile in transfected NIH3T3 cells
    • K. Lee, A.J.P. Klein-Szanto, and G.D. Kruh Analysis of the MRP4 drug resistance profile in transfected NIH3T3 cells J Natl Cancer Inst 92 2000 1934 1940
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1934-1940
    • Lee, K.1    Klein-Szanto, A.J.P.2    Kruh, G.D.3
  • 21
    • 0035937707 scopus 로고    scopus 로고
    • Correlation between steady-state ATP hydrolysis and vanadate-induced ADP trapping in human P-glycoprotein - Evidence for ADP release as the rate-limiting step in the catalytic cycle and its modulation by substrates
    • K.M. Kerr, Z.E. Sauna, and S.V. Ambudkar Correlation between steady-state ATP hydrolysis and vanadate-induced ADP trapping in human P-glycoprotein - evidence for ADP release as the rate-limiting step in the catalytic cycle and its modulation by substrates J Biol Chem 276 2001 8657 8664
    • (2001) J Biol Chem , vol.276 , pp. 8657-8664
    • Kerr, K.M.1    Sauna, Z.E.2    Ambudkar, S.V.3
  • 22
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • W. Schaffner, and C. Weissmann A rapid, sensitive, and specific method for the determination of protein in dilute solution Anal Biochem 56 1973 502 514
    • (1973) Anal Biochem , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 23
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • M. Ramachandra, S.V. Ambudkar, D. Chen, C.A. Hrycyna, S. Dey, and M.M. Gottesman Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state Biochemistry 37 1998 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
  • 24
    • 0035877703 scopus 로고    scopus 로고
    • Functionally similar vanadate-induced 8-azidoadenosine 5′-alpha-P-32 diphosphate-trapped transition state intermediates of human P-glycoprotein are generated in the absence and presence of ATP hydrolysis
    • Z.E. Sauna, M.M. Smith, M. Muller, and S.V. Ambudkar Functionally similar vanadate-induced 8-azidoadenosine 5′-alpha-P-32 diphosphate-trapped transition state intermediates of human P-glycoprotein are generated in the absence and presence of ATP hydrolysis J Biol Chem 276 2001 21199 21208
    • (2001) J Biol Chem , vol.276 , pp. 21199-21208
    • Sauna, Z.E.1    Smith, M.M.2    Muller, M.3    Ambudkar, S.V.4
  • 25
    • 0032321894 scopus 로고    scopus 로고
    • Drug-stimulatable ATPase activity in crude membranes of human MDR1-transfected mammalian cells
    • S.V. Ambudkar Drug-stimulatable ATPase activity in crude membranes of human MDR1-transfected mammalian cells Meth Enzymol 292 1998 504 514
    • (1998) Meth Enzymol , vol.292 , pp. 504-514
    • Ambudkar, S.V.1
  • 26
    • 0035853686 scopus 로고    scopus 로고
    • Characterization of the catalytic cycle of ATP hydrolysis by human P-glycoprotein - The two ATP hydrolysis events in a single catalytic cycle are kinetically similar but affect different functional outcomes
    • Z.E. Sauna, and S.V. Ambudkar Characterization of the catalytic cycle of ATP hydrolysis by human P-glycoprotein - the two ATP hydrolysis events in a single catalytic cycle are kinetically similar but affect different functional outcomes J Biol Chem 276 2001 11653 11661
    • (2001) J Biol Chem , vol.276 , pp. 11653-11661
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 27
    • 4243636993 scopus 로고    scopus 로고
    • MRP1-mediated transport of 2,4-dinitrophenyl-S-glutathione (DNP-SG) in membrane vesicles prepared from human erythrocytes and COR-L23/R lung tumour cells
    • A. Klokouzas, M.A. Barrand, and S.B. Hladky MRP1-mediated transport of 2,4-dinitrophenyl-S-glutathione (DNP-SG) in membrane vesicles prepared from human erythrocytes and COR-L23/R lung tumour cells Br J Pharmacol 131 2000 161P
    • (2000) Br J Pharmacol , vol.131
    • Klokouzas, A.1    Barrand, M.A.2    Hladky, S.B.3
  • 28
    • 0024472768 scopus 로고
    • 2+-dependent cardiac transport system for glutathione S-conjugates. a study using rat heart sarcolemma vesicles
    • 2+-dependent cardiac transport system for glutathione S-conjugates. A study using rat heart sarcolemma vesicles J Biol Chem 264 1989 17343 17348
    • (1989) J Biol Chem , vol.264 , pp. 17343-17348
    • Ishikawa, T.1
  • 29
    • 0019470706 scopus 로고
    • Enzymatic conjugation of erythrocyte glutathione with 1-chloro-2,4-dintrobenzene: The fate of glutathione conjugate in ertythrocytes and the effect of glutathione depletion on hemoglobin
    • Y.C. Awasthi, H.S. Garg, D.D. Dao, C.A. Partridge, and S.K. Srivastava Enzymatic conjugation of erythrocyte glutathione with 1-chloro-2,4- dintrobenzene: the fate of glutathione conjugate in ertythrocytes and the effect of glutathione depletion on hemoglobin Blood 58 1981 733 738
    • (1981) Blood , vol.58 , pp. 733-738
    • Awasthi, Y.C.1    Garg, H.S.2    Dao, D.D.3    Partridge, C.A.4    Srivastava, S.K.5
  • 30
    • 0016291269 scopus 로고
    • Statistical quality control and routine data processing for radioimmunoassays and immunoradiometric assays
    • D. Rodbard Statistical quality control and routine data processing for radioimmunoassays and immunoradiometric assays Clin Chem 20 1974 1255 1270
    • (1974) Clin Chem , vol.20 , pp. 1255-1270
    • Rodbard, D.1
  • 31
    • 0035660407 scopus 로고    scopus 로고
    • Effects of clotrimazole on transport mediated by multidrug resistance associated protein 1 (MRP1) in human erythrocytes and tumour cells
    • A. Klokouzas, M.A. Barrand, and S.B. Hladky Effects of clotrimazole on transport mediated by multidrug resistance associated protein 1 (MRP1) in human erythrocytes and tumour cells Eur J Biochem 268 2001 6569 6577
    • (2001) Eur J Biochem , vol.268 , pp. 6569-6577
    • Klokouzas, A.1    Barrand, M.A.2    Hladky, S.B.3
  • 32
    • 0030841332 scopus 로고    scopus 로고
    • Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines
    • M. Kool, M. De Haas, G.L. Scheffer, R.J. Scheper, M.J.T. Van Eijk, and J.A. Juijn Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines Cancer Res 57 1997 3537 3547
    • (1997) Cancer Res , vol.57 , pp. 3537-3547
    • Kool, M.1    De Haas, M.2    Scheffer, G.L.3    Scheper, R.J.4    Van Eijk, M.J.T.5    Juijn, J.A.6
  • 33
    • 0032893268 scopus 로고    scopus 로고
    • Expression of human MRP6, a homologue of the multidrug resistance protein gene MRP1, in tissues and cancer cells
    • M. Kool, M. van der Linden, M. De Haas, F. Baas, and P. Borst Expression of human MRP6, a homologue of the multidrug resistance protein gene MRP1, in tissues and cancer cells Cancer Res 59 1999 175 182
    • (1999) Cancer Res , vol.59 , pp. 175-182
    • Kool, M.1    Van Der Linden, M.2    De Haas, M.3    Baas, F.4    Borst, P.5
  • 34
    • 0037705377 scopus 로고    scopus 로고
    • Characterization of the MRP4- and MRP5-mediated transport of cyclic nucleotides from intact cells
    • P.R. Wielinga, I. van der Heijden, G. Reid, J.H. Beijnen, J. Wijnholds, and P. Borst Characterization of the MRP4- and MRP5-mediated transport of cyclic nucleotides from intact cells J Biol Chem 278 2003 17664 17671
    • (2003) J Biol Chem , vol.278 , pp. 17664-17671
    • Wielinga, P.R.1    Van Der Heijden, I.2    Reid, G.3    Beijnen, J.H.4    Wijnholds, J.5    Borst, P.6
  • 36
    • 10344227755 scopus 로고    scopus 로고
    • Multidrug resistance protein 4 (MRP4/ABCC4)-mediated ATP hydrolysis: Effect of transporty substrates and characterization of the post-hydrolysis transition state
    • Z.E. Sauna, K. Nandigama, and S.V. Ambudkar Multidrug resistance protein 4 (MRP4/ABCC4)-mediated ATP hydrolysis: Effect of transporty substrates and characterization of the post-hydrolysis transition state J Biol Chem 279 2004 48855 48864
    • (2004) J Biol Chem , vol.279 , pp. 48855-48864
    • Sauna, Z.E.1    Nandigama, K.2    Ambudkar, S.V.3
  • 37
    • 0028940488 scopus 로고
    • ATP hydrolysis by multidrug-resistance protein from Chinese hamster ovary cells
    • A.E. Senior, M.K. Al-Shawi, and I.L. Urbatsch ATP hydrolysis by multidrug-resistance protein from Chinese hamster ovary cells J Bioenerg Biomemb 27 1995 31 36
    • (1995) J Bioenerg Biomemb , vol.27 , pp. 31-36
    • Senior, A.E.1    Al-Shawi, M.K.2    Urbatsch, I.L.3
  • 38
    • 0030868612 scopus 로고    scopus 로고
    • Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein
    • S.V. Ambudkar, C.O. Cardarelli, I. Pashinsky, and W.D. Stein Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein J Biol Chem 272 1997 21160 21166
    • (1997) J Biol Chem , vol.272 , pp. 21160-21166
    • Ambudkar, S.V.1    Cardarelli, C.O.2    Pashinsky, I.3    Stein, W.D.4
  • 39
    • 0030689692 scopus 로고    scopus 로고
    • ATPase activity of purified multidrug resistance-associated protein
    • X.B. Chang, Y.X. Hou, and J.R. Riordan ATPase activity of purified multidrug resistance-associated protein J Biol Chem 272 1997 30962 30968
    • (1997) J Biol Chem , vol.272 , pp. 30962-30968
    • Chang, X.B.1    Hou, Y.X.2    Riordan, J.R.3
  • 40
    • 0033370596 scopus 로고    scopus 로고
    • ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells
    • Q. Mao, E.M. Leslie, R.G. Deeley, and S.P.C. Cole ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells Biochim Biophys Acta: Biomembr 1461 1999 69 82
    • (1999) Biochim Biophys Acta: Biomembr , vol.1461 , pp. 69-82
    • Mao, Q.1    Leslie, E.M.2    Deeley, R.G.3    Cole, S.P.C.4
  • 41
    • 0035033774 scopus 로고    scopus 로고
    • Modulation of multidrug resistance protein 1 (MRP1/ABCC1) transport and ATPase activities by interaction with dietary flavonoids
    • E.M. Leslie, Q.C. Mao, C.J. Oleschuk, R.G. Deeley, and S.P.C. Cole Modulation of multidrug resistance protein 1 (MRP1/ABCC1) transport and ATPase activities by interaction with dietary flavonoids Mol Pharmacol 59 2001 1171 1180
    • (2001) Mol Pharmacol , vol.59 , pp. 1171-1180
    • Leslie, E.M.1    Mao, Q.C.2    Oleschuk, C.J.3    Deeley, R.G.4    Cole, S.P.C.5
  • 43
    • 0031574219 scopus 로고    scopus 로고
    • The malaria parasite supplies glutathione to its host cell - Investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum
    • H. Atamna, and H. Ginsburg The malaria parasite supplies glutathione to its host cell - investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum Eur J Biochem 250 1997 670 679
    • (1997) Eur J Biochem , vol.250 , pp. 670-679
    • Atamna, H.1    Ginsburg, H.2
  • 45
    • 0027253435 scopus 로고
    • Organic anions exhibit distinct inhibition patterns on the low-K(m) and high-K(m) transport of S-(2,4-dinitrophenyl)glutathione through the human erythrocyte membrane
    • G. Bartosz, H. Sies, and T.P.M. Akerboom Organic anions exhibit distinct inhibition patterns on the low-K(m) and high-K(m) transport of S-(2,4-dinitrophenyl)glutathione through the human erythrocyte membrane Biochem J 292 1993 171 174
    • (1993) Biochem J , vol.292 , pp. 171-174
    • Bartosz, G.1    Sies, H.2    Akerboom, T.P.M.3
  • 46
    • 0029930665 scopus 로고    scopus 로고
    • Export of guanosine 3′,5′-cyclic monophosphate (cGMP) from human erythrocytes characterized by inside-out membrane vesicles
    • G. Sager, A. Orbo, R.H. Pettersen, and K.E. Kjorstad Export of guanosine 3′,5′-cyclic monophosphate (cGMP) from human erythrocytes characterized by inside-out membrane vesicles Scand J Clin Lab Invest 56 1996 289 293
    • (1996) Scand J Clin Lab Invest , vol.56 , pp. 289-293
    • Sager, G.1    Orbo, A.2    Pettersen, R.H.3    Kjorstad, K.E.4
  • 47
    • 0034730755 scopus 로고    scopus 로고
    • The multidrug resistance protein 5 functions as an ATP-dependent export pump for cyclic nucleotides
    • G. Jedlitschky, B. Burchell, and D. Keppler The multidrug resistance protein 5 functions as an ATP-dependent export pump for cyclic nucleotides J Biol Chem 275 2000 30069 30074
    • (2000) J Biol Chem , vol.275 , pp. 30069-30074
    • Jedlitschky, G.1    Burchell, B.2    Keppler, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.