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Volumn 27, Issue 1-3, 1998, Pages 31-60

Molecular analysis of the multidrug transporter, P-glycoprotein

Author keywords

ATP binding cassette; ATPase; Drug transport; Multidrug resistance; P glycoprotein; Phosphorylation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BIOSYNTHESIS; CANCER; CHOLESTEROL; DRUG TRANSPORT; GLYCOPROTEIN P; ION CHANNEL; MAMMAL CELL; MOLECULAR ANALYSIS; MULTIDRUG RESISTANCE; PLASMA PROTEIN; PROTEIN PHOSPHORYLATION; TUMOR CELL;

EID: 0032439160     PISSN: 09209069     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-94-017-2374-9_2     Document Type: Article
Times cited : (34)

References (271)
  • 2
    • 0028033393 scopus 로고
    • Functional role of phosphorylation of the multidrug transporter (P-glycoprotein) by protein kinase C in multidrug-resistant MCF-7 cells
    • Aftab DT, Yang JM and Hait WN (1994) Functional role of phosphorylation of the multidrug transporter (P-glycoprotein) by protein kinase C in multidrug-resistant MCF-7 cells. Oncol Res 6: 59-70.
    • (1994) Oncol Res , vol.6 , pp. 59-70
    • Yang Jm, A.D.T.1    Hait, W.N.2
  • 3
    • 0027256373 scopus 로고
    • Expression of the antisense cDNA for protein kinase-C-alpha attenuates resistance in doxorubicinresistant MCF-7 breast carcinoma cells
    • Ahmad S and Glazer RI (1993) Expression of the antisense cDNA for protein kinase-C-alpha attenuates resistance in doxorubicinresistant MCF-7 breast carcinoma cells. Mol Pharmacol 43: 858-862.
    • (1993) Mol Pharmacol , vol.43 , pp. 858-862
    • Ahmad, S.1    Glazer, R.I.2
  • 4
    • 0028107948 scopus 로고
    • Modulation of P-glycoprotein by protein kinase C alpha in a baculovirus expression system
    • Ahmad S, Safa AR and Glazer RI (1994) Modulation of P-glycoprotein by protein kinase C alpha in a baculovirus expression system. Biochemistry 33: 10313-10318.
    • (1994) Biochemistry , vol.33 , pp. 10313-10318
    • Safa Ar, A.S.1    Glazer, R.I.2
  • 5
    • 0023836456 scopus 로고
    • Most drugs that reverse multidrug resistance also inhibit photoaffinity labeling of P-glycoprotein by a vinblastine analog
    • Akiyama S-i, Cornwell MM, Kuwano M, Pastan I and Gottesman MM (1988) Most drugs that reverse multidrug resistance also inhibit photoaffinity labeling of P-glycoprotein by a vinblastine analog. Mol. Pharmacol. 33: 144-147.
    • (1988) Mol. Pharmacol. , vol.33 , pp. 144-147
    • S-i, A.1    Cornwell, M.M.2    Kuwano, M.3    Pastan, I.4    Gottesman, M.M.5
  • 6
    • 0027417398 scopus 로고
    • Characterization of the adenosine triphosphatase activity of Chinese hamster P-glycoprotein
    • Al-Shawi MK and Senior AE (1993) Characterization of the adenosine triphosphatase activity of Chinese hamster P-glycoprotein. J Biol Chem 268: 4197-4206.
    • (1993) J Biol Chem , vol.268 , pp. 4197-4206
    • Al-Shawi, M.K.1    Senior, A.E.2
  • 7
    • 0028307625 scopus 로고
    • Covalent inhibitors of P-glycoprotein ATPase activity
    • Al-Shawi MK, Urbatsch IL and Senior AE (1994) Covalent inhibitors of P-glycoprotein ATPase activity. J Biol Chem 269: 8986-8992.
    • (1994) J Biol Chem , vol.269 , pp. 8986-8992
    • Urbatsch Il, A.M.K.1    Senior, A.E.2
  • 8
    • 0028342805 scopus 로고
    • Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: Evidence against direct drug extrusion from the plasma membrane
    • Altenberg GA, Vanoye CG, Horton JK and Reuss L (1994) Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: evidence against direct drug extrusion from the plasma membrane. Proc Natl Acad Sci USA 91: 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
  • 9
    • 0026662530 scopus 로고
    • Partial purification and reconstitution of the human multidrug resistance pump - Characterization of the drug-stimulatable ATP hydrolysis
    • Ambudkar SV, Lelong IH, Zhang JP, Cardarelli CO, Gottesman MM and Pastan I (1992) Partial purification and reconstitution of the human multidrug resistance pump - characterization of the drug-stimulatable ATP hydrolysis. Proc Natl Acad Sci. USA 89: 8472-8476.
    • (1992) Proc Natl Acad Sci. USA , vol.89 , pp. 8472-8476
    • Ambudkar, S.V.1    Lelong, I.H.2    Zhang, J.P.3    Cardarelli, C.O.4    Gottesman, M.M.5    Pastan, I.6
  • 10
    • 0028915094 scopus 로고
    • Purification and reconstitution of functional human P-glycoprotein
    • Ambudkar SV (1995) Purification and reconstitution of functional human P-glycoprotein. J Bioenerg Biomembr 27: 23-29.
    • (1995) J Bioenerg Biomembr , vol.27 , pp. 23-29
    • Ambudkar, S.V.1
  • 11
    • 0030868612 scopus 로고    scopus 로고
    • Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein
    • Ambudkar SV, Cardarelli CO, Pashinsky I and Stein WD (1997) Relation between the turnover number for vinblastine transport and for vinblastine-stimulated ATP hydrolysis by human P-glycoprotein. J Biol Chem 272: 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
  • 12
    • 0026472873 scopus 로고
    • Traffic ATPases: A superfamily of transport proteins operating from Escherichia coli to humans
    • Ames GF-L, Mimura CS, Holbrook SR and Shyamala V (1992) Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv Enzymol 65: 1-47.
    • (1992) Adv Enzymol , vol.65 , pp. 1-47
    • Ames, G.F.-L.1    Mimura, C.S.2    Holbrook, S.R.3    Shyamala, V.4
  • 14
    • 0027230003 scopus 로고
    • Is the multidrug resistance an ATP channel
    • Arias IM (1993) Is the multidrug resistance an ATP channel. Hepatology 18:216-217.
    • (1993) Hepatology , vol.18 , pp. 216-217
    • Arias, I.M.1
  • 15
    • 0024290913 scopus 로고
    • Altered plasma membrane ultrastructure in multidrug-resistant cells
    • Arsenault AL, Ling V and Kartner N (1988) Altered plasma membrane ultrastructure in multidrug-resistant cells. Biochim Biophys Acta 938: 315-321.
    • (1988) Biochim Biophys Acta , vol.938 , pp. 315-321
    • Arsenault, A.L.1    Ling, V.2    Kartner, N.3
  • 16
    • 0030004763 scopus 로고    scopus 로고
    • Co-operative, competitive and non-competitive interactions between modulators of P-glycoprotein
    • Ayesh S, Shao YM and Stein WD (1996) Co-operative, competitive and non-competitive interactions between modulators of P-glycoprotein. Biochim Biophys Acta 1316: 8-18.
    • (1996) Biochim Biophys Acta , vol.1316 , pp. 8-18
    • Shao Ym, A.S.1    Stein, W.D.2
  • 17
    • 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 (1989) Discrete mutations introduced in the predicted nucleotide-binding sites of the mdr1 gene abolish its ability to confer multidrug resistance. Mol Cell Biol 9: 5289-5297.
    • (1989) Mol Cell Biol , vol.9 , pp. 5289-5297
    • Schurr E, A.M.1    Gros, P.2
  • 18
    • 0026716259 scopus 로고
    • Modulation of P-glycoprotein phosphorylation and drug transport by sodium butyrate
    • Bates SE, Currier SJ, Alvarez M and Fojo AT (1992) Modulation of P-glycoprotein phosphorylation and drug transport by sodium butyrate. Biochemistry 31: 6366-6372.
    • (1992) Biochemistry , vol.31 , pp. 6366-6372
    • Bates, S.E.1    Currier, S.J.2    Alvarez, M.3    Fojo, A.T.4
  • 19
    • 0027853682 scopus 로고
    • Differential modulation of P-glycoprotein transport by protein kinase inhibition
    • Bates SE, Lee JS, Dickstein B, Spolyar M and Fojo AT (1993) Differential modulation of P-glycoprotein transport by protein kinase inhibition. Biochemistry 32: 9156-9164.
    • (1993) Biochemistry , vol.32 , pp. 9156-9164
    • Bates, S.E.1    Lee, J.S.2    Dickstein, B.3    Spolyar, M.4    Fojo, A.T.5
  • 20
    • 0028059144 scopus 로고
    • Overexpression and purification of the carboxyl-terminal nucleotide-binding domain from mouse P-glycoprotein
    • Baubichon-Cortay H, Baggetto LG, Dayan G and Di Pietro A (1994) Overexpression and purification of the carboxyl-terminal nucleotide-binding domain from mouse P-glycoprotein. J Biol Chem 269: 22983-22989.
    • (1994) J Biol Chem , vol.269 , pp. 22983-22989
    • Baubichon-Cortay, H.1    Baggetto, L.G.2    Dayan, G.3    Di Pietro, A.4
  • 21
    • 0028982951 scopus 로고
    • Functional dissection of P-glycoprotein nucleotide binding domains in chimeric and mutant proteins
    • Beaudet L and Gros P (1995) Functional dissection of P-glycoprotein nucleotide binding domains in chimeric and mutant proteins. J Biol Chem 270: 17159-17170.
    • (1995) J Biol Chem , vol.270 , pp. 17159-17170
    • Beaudet, L.1    Gros, P.2
  • 22
    • 0002113054 scopus 로고
    • Characteristics of multidrug resistance in human tumor cells
    • Roninson, IB (ed) Plenum Publishing Corporation: New York
    • Beck WT and Danks MK (1991) Characteristics of multidrug resistance in human tumor cells. In: Roninson, IB (ed) Molecular and cellular biology of multidrug resistance in tumor cells (pp. 3-46. Plenum Publishing Corporation: New York.
    • (1991) Molecular and Cellular Biology of Multidrug Resistance in Tumor Cells , pp. 3-46
    • Beck, W.T.1    Danks, M.K.2
  • 23
    • 0026501892 scopus 로고
    • Photoaffinity substrates for Pglycoprotein
    • Beck WT and Qian X-D (1992) Photoaffinity substrates for Pglycoprotein. Biochem Pharmacol 43: 89-93.
    • (1992) Biochem Pharmacol , vol.43 , pp. 89-93
    • Beck, W.T.1    Qian, X.-D.2
  • 24
    • 0029048812 scopus 로고
    • Multidrug resistance protein (Mdr)alkaline phosphatase hybrids in Escherichia coli suggest a major revision in the topology of the C-terminal half of Mdr
    • Béja O and Bibi E (1995) Multidrug resistance protein (Mdr)alkaline phosphatase hybrids in Escherichia coli suggest a major revision in the topology of the C-terminal half of Mdr. J Biol Chem 270: 12351-12354.
    • (1995) J Biol Chem , vol.270 , pp. 12351-12354
    • Béja, O.1    Bibi, E.2
  • 25
    • 0030001378 scopus 로고    scopus 로고
    • P-glycoproteins and multidrug resistance
    • Bellamy WT (1996) P-glycoproteins and multidrug resistance. Annu Rev Pharmacol Toxicol 36: 161-183.
    • (1996) Annu Rev Pharmacol Toxicol , vol.36 , pp. 161-183
    • Bellamy, W.T.1
  • 26
    • 0028098714 scopus 로고
    • Membrane topology of multidrug resistance protein expressed in Escherichia coli
    • Bibi E and Béja O (1994) Membrane topology of multidrug resistance protein expressed in Escherichia coli. J Biol Chem 269: 19910-19915.
    • (1994) J Biol Chem , vol.269 , pp. 19910-19915
    • Bibi, E.1    Béja, O.2
  • 27
    • 0014767029 scopus 로고
    • Cellular resistance to actinomycin D in Chinese hamster cells in vitro: Cross-resistance, radioautographic, and cytogenetic studies
    • Biedler JL and Riehm H (1970) Cellular resistance to actinomycin D in Chinese hamster cells in vitro: Cross-resistance, radioautographic, and cytogenetic studies. Cancer Res. 30: 1174-1184.
    • (1970) Cancer Res. , vol.30 , pp. 1174-1184
    • Biedler, J.L.1    Riehm, H.2
  • 28
    • 0030069428 scopus 로고    scopus 로고
    • Reversible labeling of a chemosensitizer binding domain of P- Glycoprotein with a novel 1,4-dihydropyridine drug transport inhibitor
    • Boer R, Dichtl M, Borchers C, Ulrich WR, Marecek JF, Prestwich GD, Glossmann H and Striessnig J (1996a) Reversible labeling of a chemosensitizer binding domain of P- glycoprotein with a novel 1,4-dihydropyridine drug transport inhibitor. Biochemistry 35: 1387-1396.
    • (1996) Biochemistry , vol.35 , pp. 1387-1396
    • Boer, R.1    Dichtl, M.2    Borchers, C.3    Ulrich, W.R.4    Marecek, J.F.5    Prestwich, G.D.6    Glossmann, H.7    Striessnig, J.8
  • 31
    • 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 MJ, Eytan GD and Assaraf YG (1996) Competition of hydrophobic peptides, cytotoxic drugs, and chemosensitizers on a common P-glycoprotein pharmacophore as revealed by its ATPase activity. J Biol Chem 271: 3163-3171.
    • (1996) J Biol Chem , vol.271 , pp. 3163-3171
    • Eytan Gd, B.M.J.1    Assaraf, Y.G.2
  • 32
    • 0029945113 scopus 로고    scopus 로고
    • What have we learnt thus far from mice with disrupted P-glycoprotein genes?
    • Borst P and Schinkel AH (1996) What have we learnt thus far from mice with disrupted P-glycoprotein genes? Eur J Cancer 32A: 985-990.
    • (1996) Eur J Cancer , vol.32 A , pp. 985-990
    • Borst, P.1    Schinkel, A.H.2
  • 33
    • 0030975889 scopus 로고    scopus 로고
    • Genetic dissection of the function of mammalian P-glycoproteins
    • Borst P and Schinkel AH (1997) Genetic dissection of the function of mammalian P-glycoproteins. Trends Genet 13: 217-222.
    • (1997) Trends Genet , vol.13 , pp. 217-222
    • Borst, P.1    Schinkel, A.H.2
  • 35
    • 0023762744 scopus 로고
    • Mechanism of multidrug resistance
    • Bradley G, Juranka PF and Ling V (1988) Mechanism of multidrug resistance. Biochim Biophys Acta 948: 87-128.
    • (1988) Biochim Biophys Acta , vol.948 , pp. 87-128
    • Juranka Pf, B.G.1    Ling, V.2
  • 36
    • 0028931885 scopus 로고
    • Sequential coexpression of the multidrug resistance genes MRP and mdr1 and their products in VP-16 (etoposide)-selected H69 small cell lung cancer cells
    • Brock I, Hipfner DR, Nielsen BS, Jensen PB, Deeley RG, Cole SP and Sehested M (1995) Sequential coexpression of the multidrug resistance genes MRP and mdr1 and their products in VP-16 (etoposide)-selected H69 small cell lung cancer cells. Cancer Res 55:459-462.
    • (1995) Cancer Res , vol.55 , pp. 459-462
    • Brock, I.1    Hipfner, D.R.2    Nielsen, B.S.3    Jensen, P.B.4    Deeley, R.G.5    Cole, S.P.6    Sehested, M.7
  • 38
    • 0024971222 scopus 로고
    • Two different regions of P-glycoprotein are photoaffinity labeled by azidopine
    • Bruggemann EP, Germann UA, Gottesman MM and Pastan I (1989) Two different regions of P-glycoprotein are photoaffinity labeled by azidopine. J Biol Chem 264: 15483-15488.
    • (1989) J Biol Chem , vol.264 , pp. 15483-15488
    • Bruggemann, E.P.1    Germann, U.A.2    Gottesman, M.M.3    Pastan, I.4
  • 39
    • 0026669363 scopus 로고
    • Characterization of the azidopine and vinblastine binding site of P-glycoprotein
    • Bruggemann EP, Currier SJ, Gottesman MM and Pastan I (1992) Characterization of the azidopine and vinblastine binding site of P-glycoprotein. J Biol Chem 267: 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
  • 40
    • 0024556196 scopus 로고
    • Preparation and utility of a radioiodinated analogue of daunomycin in the study of multidrug resistance
    • Busche R, Tummler B, Riordan JR and Cano-Gauci DE (1989) Preparation and utility of a radioiodinated analogue of daunomycin in the study of multidrug resistance. Mol Pharmacol 35: 414-421.
    • (1989) Mol Pharmacol , vol.35 , pp. 414-421
    • Busche, R.1    Tummler, B.2    Riordan, J.R.3    De Cano-Gauci4
  • 41
    • 0026068740 scopus 로고
    • Functional analysis of chimeric genes obtained by exchanging homologous domains of the mouse mdr1 and mdr2 genes
    • Buschman E and Gros P (1991) Functional analysis of chimeric genes obtained by exchanging homologous domains of the mouse mdr1 and mdr2 genes. Mol Cell Biol 11: 595-603.
    • (1991) Mol Cell Biol , vol.11 , pp. 595-603
    • Buschman, E.1    Gros, P.2
  • 42
    • 0026640274 scopus 로고
    • Mdr2 encodes P-glycoprotein expressed in the bile canalicular membrane as determined by isoform-specific antibodies
    • Buschman E, Arceci RJ, Croop JM, Che M, Arias IM, Housman DE and Gros P (1992) mdr2 encodes P-glycoprotein expressed in the bile canalicular membrane as determined by isoform-specific antibodies. J Biol Chem 267: 18093-18099.
    • (1992) J Biol Chem , vol.267 , pp. 18093-18099
    • Buschman, E.1    Arceci, R.J.2    Croop, J.M.3    Che, M.4    Arias, I.M.5    De Housman6    Gros, P.7
  • 43
    • 0028964955 scopus 로고
    • Differential effects of P-glycoprotein inhibitors on NIH3T3 cells transfected with wild-type (G185) or mutant (VI85) multidrug transporters
    • Cardarelli CO, Aksentijevich I, Pastan I and Gottesman MM (1995) Differential effects of P-glycoprotein inhibitors on NIH3T3 cells transfected with wild-type (G185) or mutant (VI85) multidrug transporters. Cancer Res 55: 1086-1091.
    • (1995) Cancer Res , vol.55 , pp. 1086-1091
    • Cardarelli, C.O.1    Aksentijevich, I.2    Pastan, I.3    Gottesman, M.M.4
  • 44
    • 0025318529 scopus 로고
    • Protein kinase C phosphorylates P-glycoprotein in multidrug resistant human KB carcinoma cells
    • Chambers TC, McAvoy EM, Jacobs JW and Eilon G (1990) Protein kinase C phosphorylates P-glycoprotein in multidrug resistant human KB carcinoma cells. J Biol Chem 265: 7679-7686.
    • (1990) J Biol Chem , vol.265 , pp. 7679-7686
    • Chambers, T.C.1    McAvoy, E.M.2    Jacobs, J.W.3    Eilon, G.4
  • 45
    • 0027076780 scopus 로고
    • Regulation by phorbol ester and protein kinase-C inhibitors, and by a protein phosphatase inhibitor (okadaic acid), of P-glycoprotein phosphorylation and relationship to drug accumulation in multidrug-resistant human-KB cells
    • Chambers TC, Zheng B and Kuo JF (1992) Regulation by phorbol ester and protein kinase-C inhibitors, and by a protein phosphatase inhibitor (okadaic acid), of P-glycoprotein phosphorylation and relationship to drug accumulation in multidrug-resistant human-KB cells. Mol Pharmacol 41: 1008-1015.
    • (1992) Mol Pharmacol , vol.41 , pp. 1008-1015
    • Zheng B, C.T.C.1    Kuo, J.F.2
  • 46
    • 6544271594 scopus 로고
    • Phosphorylation and regulation of P-glycoprotein by protein kinase C
    • Miyazaki, T., Takaku, F. and Sakurada, K. (eds) Elsevier Science Publishers: Amsterdam
    • Chambers TC and Kuo JF (1993) Phosphorylation and regulation of P-glycoprotein by protein kinase C. In: Miyazaki, T., Takaku, F. and Sakurada, K. (eds) The mechanism and new approach on drug resistance of cancer cells (pp. 159-166). Elsevier Science Publishers: Amsterdam.
    • (1993) The Mechanism and New Approach on Drug Resistance of Cancer Cells , pp. 159-166
    • Chambers, T.C.1    Kuo, J.F.2
  • 47
    • 0027460274 scopus 로고
    • Identification of specific sites in human P-glycoprotein phosphorylated by protein kinase-C
    • Chambers TC, Pohl J, Raynor RL and Kuo JF (1993) Identification of specific sites in human P-glycoprotein phosphorylated by protein kinase-C. J Biol Chem 268: 4592-4595.
    • (1993) J Biol Chem , vol.268 , pp. 4592-4595
    • Chambers, T.C.1    Pohl, J.2    Raynor, R.L.3    Kuo, J.F.4
  • 48
    • 0028213201 scopus 로고
    • Phosphorylation by protein kinase C and cyclic AMP-dependent protein kinase of synthetic peptides derived from the linker region of human P-glycoprotein
    • Chambers TC, Pohl J, Glass DB and Kuo JF (1994) Phosphorylation by protein kinase C and cyclic AMP-dependent protein kinase of synthetic peptides derived from the linker region of human P-glycoprotein. Biochem J 299: 309-315.
    • (1994) Biochem J , vol.299 , pp. 309-315
    • Chambers, T.C.1    Pohl, J.2    Glass, D.B.3    Kuo, J.F.4
  • 49
    • 0028846607 scopus 로고
    • Bacterial expression of the linker region of human MDR1 P-glycoprotein and mutational analysis of phosphorylation sites
    • Chambers TC, Germann UA, Gottesman MM, Pastan I, Kuo JF and Ambudkar SV (1995) Bacterial expression of the linker region of human MDR1 P-glycoprotein and mutational analysis of phosphorylation sites. Biochemistry: 14156-14162.
    • (1995) Biochemistry , pp. 14156-14162
    • Chambers, T.C.1    Germann, U.A.2    Gottesman, M.M.3    Pastan, I.4    Kuo, J.F.5    Ambudkar, S.V.6
  • 50
    • 0041459803 scopus 로고    scopus 로고
    • Phosphorylation of proteins involved in multidrug resistance
    • Gupta, S. and Tsuruo, T. (eds) John Wiley & Sons: Chichester, U.K.
    • Chambers TC (1996) Phosphorylation of proteins involved in multidrug resistance. In: Gupta, S. and Tsuruo, T. (eds) Multidrug resistance in cancer cells (pp. 303-318). John Wiley & Sons: Chichester, U.K.
    • (1996) Multidrug Resistance in Cancer Cells , pp. 303-318
    • Chambers, T.C.1
  • 51
    • 0027005480 scopus 로고
    • Activation of MDR1 (P-glycoprotein) gene expression in human cells by protein kinase C agonists
    • Chaudhary P and Roninson IB (1992) Activation of MDR1 (P-glycoprotein) gene expression in human cells by protein kinase C agonists. Oncol Res 4: 281-290.
    • (1992) Oncol Res , vol.4 , pp. 281-290
    • Chaudhary, P.1    Roninson, I.B.2
  • 52
    • 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 JE, Ueda K, Clark DP, Pastan I, Gottesman MM and Roninson IB (1986) Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell 47: 381-389.
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.-J.1    Chin, J.E.2    Ueda, K.3    Clark, D.P.4    Pastan, I.5    Gottesman, M.M.6    Roninson, I.B.7
  • 53
    • 0031041385 scopus 로고    scopus 로고
    • Multidrug-resistant human sarcoma cells with a mutant P-glycoprotein, altered phenotype, and resistance to cyclosporins
    • Chen G, Duran GE, Steger KA, Lacayo NJ, Jaffrezou JP, Dumontet C and Sikic BI (1997) Multidrug-resistant human sarcoma cells with a mutant P-glycoprotein, altered phenotype, and resistance to cyclosporins. J Biol Chem 272: 5974-5982.
    • (1997) J Biol Chem , vol.272 , pp. 5974-5982
    • Chen, G.1    Duran, G.E.2    Steger, K.A.3    Lacayo, N.J.4    Jaffrezou, J.P.5    Dumontet, C.6    Sikic, B.I.7
  • 54
    • 0028249115 scopus 로고
    • The MDR superfamily of genes and its biological implications
    • Childs S and Ling V (1994) The MDR superfamily of genes and its biological implications. Important Adv Oncol 1994: 21-36.
    • (1994) Important Adv Oncol , vol.1994 , pp. 21-36
    • Childs, S.1    Ling, V.2
  • 55
    • 0024292717 scopus 로고
    • An altered pattern of cross-resistance in multidrug-resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene
    • Choi K, Chen C-J, Kriegler M and Roninson IB (1989) An altered pattern of cross-resistance in multidrug-resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene. Cell 53: 519-529.
    • (1989) Cell , vol.53 , pp. 519-529
    • Choi, K.1    Chen, C.-J.2    Kriegler, M.3    Roninson, I.B.4
  • 56
    • 0028177656 scopus 로고
    • P-glycoprotein epitope mapping. I. Identification of a linear human-specific epitope in the fourth loop of the P-glycoprotein extracellular domain by MM4.17 murine monoclonal antibody to human multi-drug-resistant cells
    • Cianfriglia M, Willingham MC, Tombesi M, Scagliotti GV, Frasca G and Chersi A (1994) P-glycoprotein epitope mapping. I. Identification of a linear human-specific epitope in the fourth loop of the P-glycoprotein extracellular domain by MM4.17 murine monoclonal antibody to human multi-drug-resistant cells. Int J Cancer 56: 153-160.
    • (1994) Int J Cancer , vol.56 , pp. 153-160
    • Cianfriglia, M.1    Willingham, M.C.2    Tombesi, M.3    Scagliotti, G.V.4    Frasca, G.5    Chersi, A.6
  • 57
    • 0029832410 scopus 로고    scopus 로고
    • Topology of MDR1-P-glycoprotein as indicated by epitope mapping of monoclonal antibodies to human MDR cells
    • Cianfriglia M, Poloni F, Signoretti C, Romagnoli G, Tombesi M and Felici F (1996) Topology of MDR1-P-glycoprotein as indicated by epitope mapping of monoclonal antibodies to human MDR cells. Cytotechnology 19: 247-251.
    • (1996) Cytotechnology , vol.19 , pp. 247-251
    • Cianfriglia, M.1    Poloni, F.2    Signoretti, C.3    Romagnoli, G.4    Tombesi, M.5    Felici, F.6
  • 59
    • 0009480826 scopus 로고    scopus 로고
    • Regulation of MDR genes
    • Gupta S and Tsuruo T (eds) John Wiley & Sons, Chichester, U.K.
    • Cornwell MM (1996) Regulation of MDR genes. In: Gupta S and Tsuruo T (eds) Multidrug resistance in cancer cells (pp. 39-48) John Wiley & Sons, Chichester, U.K.
    • (1996) Multidrug Resistance in Cancer Cells , pp. 39-48
    • Cornwell, M.M.1
  • 60
    • 0023033333 scopus 로고
    • Increased vinblastine binding to membrane vesicles from multidrug resistant KB cells
    • Cornwell MM, Gottesman MM and Pastan I (1986a) Increased vinblastine binding to membrane vesicles from multidrug resistant KB cells. J Biol Chem 262: 7921-7928.
    • (1986) J Biol Chem , vol.262 , pp. 7921-7928
    • Gottesman Mm, C.M.M.1    Pastan, I.2
  • 61
    • 0001463656 scopus 로고
    • Membrane vesicles from multidrug-resistant human cancer cells contain a specific 150-170 kDa protein detected by photoaffinity labeling
    • Cornwell MM, Safa AR, Felsted RL, Gottesman MM and Pastan I (1986b) Membrane vesicles from multidrug-resistant human cancer cells contain a specific 150-170 kDa protein detected by photoaffinity labeling. Proc Natl Acad Sci USA 83: 3847-3850.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3847-3850
    • Cornwell, M.M.1    Safa, A.R.2    Felsted, R.L.3    Gottesman, M.M.4    Pastan, I.5
  • 62
    • 0023553574 scopus 로고
    • ATP-binding properties of P-glycoprotein from multidrug resistant KB cells
    • Cornwell MM, Tsuruo T, Gottesman MM and Pastan I (1987) ATP-binding properties of P-glycoprotein from multidrug resistant KB cells. FASEB J 1: 51-54.
    • (1987) FASEB J , vol.1 , pp. 51-54
    • Cornwell, M.M.1    Tsuruo, T.2    Gottesman, M.M.3    Pastan, I.4
  • 63
    • 0041459791 scopus 로고
    • Binding of drugs and ATP by P-glycoprotein and transport of drugs by vesicles from human multidrug-resistant cells
    • Roninson, I.B. (ed) Plenum Publishing Corporation: New York
    • Cornwell MM, Pastan I and Gottesman MM (1991) Binding of drugs and ATP by P-glycoprotein and transport of drugs by vesicles from human multidrug-resistant cells. In: Roninson, I.B. (ed) Molecular and cellular biology of multidrug resistance in tumor cells (pp. 229-242). Plenum Publishing Corporation: New York.
    • (1991) Molecular and Cellular Biology of Multidrug Resistance in Tumor Cells , pp. 229-242
    • Cornwell, M.M.1    Pastan, I.2    Gottesman, M.M.3
  • 65
    • 0026473238 scopus 로고
    • Identification of residues in the first cytoplasmic loop of P-glycoprotein involved in the function of chimeric human MDR1-MDR2 transporters
    • Currier SJ, Kane SE, Willingham MC, Cardarelli CO, Pastan I and Gottesman MM (1992) Identification of residues in the first cytoplasmic loop of P-glycoprotein involved in the function of chimeric human MDR1-MDR2 transporters. J Biol Chem 267: 25153-25159.
    • (1992) J Biol Chem , vol.267 , pp. 25153-25159
    • Currier, S.J.1    Kane, S.E.2    Willingham, M.C.3    Cardarelli, C.O.4    Pastan, I.5    Gottesman, M.M.6
  • 66
    • 0015893137 scopus 로고
    • Active outward transport of daunomycin in resistant Ehrlich ascites tumor cells
    • Danø K (1973) Active outward transport of daunomycin in resistant Ehrlich ascites tumor cells. Biochem Biophys Acta 323: 466-483.
    • (1973) Biochem Biophys Acta , vol.323 , pp. 466-483
    • Danø, K.1
  • 67
    • 0023085877 scopus 로고
    • Dynamics of membrane lipid metabolism and turnover
    • Dawidowicz EA (1987) Dynamics of membrane lipid metabolism and turnover. Annu Rev Biochem 56: 43-61.
    • (1987) Annu Rev Biochem , vol.56 , pp. 43-61
    • Dawidowicz, E.A.1
  • 68
    • 0029948519 scopus 로고    scopus 로고
    • Recombinant N-terminal nucleotide-binding domain from mouse P-glycoprotein. Overexpression, purification, and role of cysteine 430
    • Dayan G, Baubichon-Cortay H, Jault JM, Cortay JC, Deleage G and Di Pietro A (1996) Recombinant N-terminal nucleotide-binding domain from mouse P-glycoprotein. Overexpression, purification, and role of cysteine 430. J Biol Chem 271: 11652-11658.
    • (1996) J Biol Chem , vol.271 , pp. 11652-11658
    • Dayan, G.1    Baubichon-Cortay, H.2    Jault, J.M.3    Cortay, J.C.4    Deleage, G.5    Di Pietro, A.6
  • 69
    • 0031013536 scopus 로고    scopus 로고
    • Role of multidrug resistance P-glycoproteins in cholesterol esterification
    • Debry P, Nash EA, Neklason DW and Metherall JE (1997) Role of multidrug resistance P-glycoproteins in cholesterol esterification. J Biol Chem 272: 1026-1031.
    • (1997) J Biol Chem , vol.272 , pp. 1026-1031
    • Debry, P.1    Nash, E.A.2    Neklason, D.W.3    Metherall, J.E.4
  • 70
    • 0030889916 scopus 로고    scopus 로고
    • Molecular interactions of cyclosporin A with P-glycoprotein. Photolabeling with cyclosporin derivatives
    • Demeule M, Wenger RM and Beliveau R (1997) Molecular interactions of cyclosporin A with P-glycoprotein. Photolabeling with cyclosporin derivatives. J Biol Chem 272: 6647-6652.
    • (1997) J Biol Chem , vol.272 , pp. 6647-6652
    • Wenger Rm, D.M.1    Beliveau, R.2
  • 71
    • 0030597326 scopus 로고    scopus 로고
    • Competitive inhibition of photoaffinity labelling of P-glycoprotein by anticancer drugs and modulators including S9788
    • Demmer A, Dunn T, Hoof T, Kubesch P and Tummler B (1996) Competitive inhibition of photoaffinity labelling of P-glycoprotein by anticancer drugs and modulators including S9788. Eur J Pharmacol 315: 339-343.
    • (1996) Eur J Pharmacol , vol.315 , pp. 339-343
    • Demmer, A.1    Dunn, T.2    Hoof, T.3    Kubesch, P.4    Tummler, B.5
  • 72
    • 0026561813 scopus 로고
    • Identification of distinct P-glycoprotein gene sequences in rat
    • Deuchars KL, Duthie M and Ling V (1992) Identification of distinct P-glycoprotein gene sequences in rat. Biochim Biophys Acta 1130: 157-165.
    • (1992) Biochim Biophys Acta , vol.1130 , pp. 157-165
    • Duthie M, D.K.L.1    Ling, V.2
  • 73
    • 0025253133 scopus 로고
    • Two members of the mouse mdr gene family confer multidrug resistance with overlapping but distinct drug specificities
    • Devault A and Gros P (1990) Two members of the mouse mdr gene family confer multidrug resistance with overlapping but distinct drug specificities. Mol Cell Biol 10: 1652-1663.
    • (1990) Mol Cell Biol , vol.10 , pp. 1652-1663
    • Devault, A.1    Gros, P.2
  • 74
    • 0026556302 scopus 로고
    • Amino acid substitutions in the 6th transmembrane domain of P-glycoprotein alter multidrug resistance
    • Devine SE, Ling V and Melera PW (1992) Amino acid substitutions in the 6th transmembrane domain of P-glycoprotein alter multidrug resistance. Proc Natl Acad Sci USA 89: 4564-4568.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4564-4568
    • Devine, S.E.1    Ling, V.2    Melera, P.W.3
  • 75
    • 0028106003 scopus 로고
    • Diversity of multidrug resistance in mammalian cells
    • Devine SE and Melera PW (1994) Diversity of multidrug resistance in mammalian cells. J Biol Chem 269: 6133-6139.
    • (1994) J Biol Chem , vol.269 , pp. 6133-6139
    • Devine, S.E.1    Melera, P.W.2
  • 76
    • 0026755153 scopus 로고
    • Functional analysis of chimeric proteins constructed by exchanging homologous domains of two P-glycoproteins conferring distinct drug resistance profiles
    • Dhir R and Gros P (1992) Functional analysis of chimeric proteins constructed by exchanging homologous domains of two P-glycoproteins conferring distinct drug resistance profiles. Biochemistry 31: 6103-6110.
    • (1992) Biochemistry , vol.31 , pp. 6103-6110
    • Dhir, R.1    Gros, P.2
  • 77
    • 0026672405 scopus 로고
    • ATPase activity of partially purified P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Doige CA, Yu XH and Sharom FJ (1992) ATPase activity of partially purified P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochim Biophys Acta 1109: 149-160.
    • (1992) Biochim Biophys Acta , vol.1109 , pp. 149-160
    • Yu Xh, D.C.A.1    Sharom, F.J.2
  • 78
    • 0027509809 scopus 로고
    • The effects of lipids and detergents on ATPase-active P-glycoprotein
    • Doige CA, Yu XH and Sharom FJ (1993) The effects of lipids and detergents on ATPase-active P-glycoprotein. Biochim Biophys Acta 1146: 65-72.
    • (1993) Biochim Biophys Acta , vol.1146 , pp. 65-72
    • Yu Xh, D.C.A.1    Sharom, F.J.2
  • 79
    • 0029804316 scopus 로고    scopus 로고
    • Efficient purification and reconstitution of P-glycoprotein for functional and structural studies
    • Dong M, Penin F and Baggetto LG (1996) Efficient purification and reconstitution of P-glycoprotein for functional and structural studies. J Biol Chem 271: 28875-28883.
    • (1996) J Biol Chem , vol.271 , pp. 28875-28883
    • Penin F, D.M.1    Baggetto, L.G.2
  • 80
    • 0023608484 scopus 로고
    • Simultaneous expression of two P-glycoprotein genes in drug-sensitive Chinese hamster ovary cells
    • Endicott JA, Juranka PF, Sarangi F, Gerlach JH, Deuchars KL and Ling V (1987) Simultaneous expression of two P-glycoprotein genes in drug-sensitive Chinese hamster ovary cells. Mol Cell Biol 7: 4075-4081.
    • (1987) Mol Cell Biol , vol.7 , pp. 4075-4081
    • Endicott, J.A.1    Juranka, P.F.2    Sarangi, F.3    Gerlach, J.H.4    Deuchars, K.L.5    Ling, V.6
  • 81
    • 0024329881 scopus 로고
    • The biochemistry of P-glycoproteinmediated multidrug resistance
    • Endicott JA and Ling V (1989) The biochemistry of P-glycoproteinmediated multidrug resistance. Annu Rev Biochem 58: 137-171.
    • (1989) Annu Rev Biochem , vol.58 , pp. 137-171
    • Endicott, J.A.1    Ling, V.2
  • 82
    • 0026270018 scopus 로고
    • Complete cDNA sequences encoding the Chinese hamster P-glycoprotein gene family
    • Endicott JA, Sarangi F and Ling V (1991) Complete cDNA sequences encoding the Chinese hamster P-glycoprotein gene family. DNA Seq. 2: 89-101.
    • (1991) DNA Seq. , vol.2 , pp. 89-101
    • Sarangi F, E.J.A.1    Ling, V.2
  • 83
    • 0028020549 scopus 로고
    • Transport of polypeptide ionophores into proteoliposomes reconstituted with rat liver P-glycoprotein
    • Eytan GD, Borgnia MJ, Regev R and Assaraf YG (1994) Transport of polypeptide ionophores into proteoliposomes reconstituted with rat liver P-glycoprotein. J Biol Chem 269: 26058-26065.
    • (1994) J Biol Chem , vol.269 , pp. 26058-26065
    • Eytan, G.D.1    Borgnia, M.J.2    Regev, R.3    Assaraf, Y.G.4
  • 84
    • 0030065776 scopus 로고    scopus 로고
    • Functional reconstitution of P-glycoprotein reveals an apparent near stoichiometric drug transport to ATP hydrolysis
    • Eytan GD, Regev R and Assaraf YG (1996) Functional reconstitution of P-glycoprotein reveals an apparent near stoichiometric drug transport to ATP hydrolysis. J Biol Chem 271: 3172-3178.
    • (1996) J Biol Chem , vol.271 , pp. 3172-3178
    • Regev R, E.G.D.1    Assaraf, Y.G.2
  • 85
    • 0026475310 scopus 로고
    • P-glycoprotein possesses a 1,4 - Dihydropyridine-selective drug acceptor site which is allosterically coupled to a vinca-alkaloid-selective binding site
    • Ferry DR, Russell MA and Cullen MH (1992) P-glycoprotein possesses a 1,4 - dihydropyridine-selective drug acceptor site which is allosterically coupled to a vinca-alkaloid-selective binding site. Biochem Biophys Res Commun 188: 440-445.
    • (1992) Biochem Biophys Res Commun , vol.188 , pp. 440-445
    • Ferry, D.R.1    Russell, M.A.A.2    Cullen, M.H.3
  • 86
    • 0028978838 scopus 로고
    • Allosteric regulation of [3H]vinblastine binding to P-glycoprotein of MCF-7 ADR cells by dexniguldipine
    • Ferry DR, Malkhandi PJ, Russell MA and Kerr DJ (1995) Allosteric regulation of [3H]vinblastine binding to P-glycoprotein of MCF-7 ADR cells by dexniguldipine. Biochem Pharmacol 49: 1851-1861.
    • (1995) Biochem Pharmacol , vol.49 , pp. 1851-1861
    • Ferry, D.R.1    Malkhandi, P.J.2    Russell, M.A.A.3    Kerr, D.J.4
  • 87
    • 1842387251 scopus 로고
    • Phorbol esters induce multidrug resistance in human breast cancer cells
    • Fine RL, Patel J and Chabner BA (1988) Phorbol esters induce multidrug resistance in human breast cancer cells. Proc Natl Acad Sci USA 85: 582-586.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 582-586
    • Patel J, F.R.L.1    Chabner, B.A.2
  • 88
    • 0030052091 scopus 로고    scopus 로고
    • P-glycoprotein, multidrug resistance and protein kinase C
    • Fine RL, Chambers TC and Sachs CW (1996) P-glycoprotein, multidrug resistance and protein kinase C. Stem Cells 14: 47-55.
    • (1996) Stem Cells , vol.14 , pp. 47-55
    • Chambers Tc, F.R.L.1    Sachs, C.W.2
  • 89
    • 0021856764 scopus 로고
    • Reduced drug accumulation in multiply drug-resistant human KB carcinoma cell lines
    • Fojo A, Akiyama S-I, Gottesman MM and Pastan I (1985) Reduced drug accumulation in multiply drug-resistant human KB carcinoma cell lines. Cancer Res 45: 3002-3007.
    • (1985) Cancer Res , vol.45 , pp. 3002-3007
    • Fojo, A.1    Akiyama, S.-I.2    Gottesman, M.M.3    Pastan, I.4
  • 90
    • 0029939665 scopus 로고    scopus 로고
    • Experimental reversal of P-glycoprotein-mediated multidrug resistance by pharmacological chemosensitisers
    • Ford JM (1996) Experimental reversal of P-glycoprotein-mediated multidrug resistance by pharmacological chemosensitisers. Eur J Cancer 32A: 991-1001.
    • (1996) Eur J Cancer , vol.32 A , pp. 991-1001
    • Ford, J.M.1
  • 91
    • 0027971693 scopus 로고
    • Isolation of rat pgp3 cDNA: Evidence for gender and zonal regulation of expression in the liver
    • Furuya KN, Gebhardt R, Schuetz EG and Schuetz JD (1994) Isolation of rat pgp3 cDNA: evidence for gender and zonal regulation of expression in the liver. Biochim Biophys Acta 1219: 636-644.
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 636-644
    • Furuya, K.N.1    Gebhardt, R.2    Schuetz, E.G.3    Schuetz, J.D.4
  • 92
    • 0031039693 scopus 로고    scopus 로고
    • Competitive and non-competitive inhibition of the multidrug-resistance- Associated P-glycoprotein ATPase-further experimental evidence for a multisite model
    • Garrigos M, Mir LM and Orlowski S (1997) Competitive and non-competitive inhibition of the multidrug-resistance- associated P-glycoprotein ATPase-further experimental evidence for a multisite model. Eur J Biochem 244: 664-673.
    • (1997) Eur J Biochem , vol.244 , pp. 664-673
    • Mir Lm, G.M.1    Orlowski, S.2
  • 93
    • 0025141784 scopus 로고
    • Detection of P-glycoprotein isoforms by gene-specific monoclonal antibodies
    • Georges E, Bradley G, Gariepy J and Ling V (1990) Detection of P-glycoprotein isoforms by gene-specific monoclonal antibodies. Proc Natl Acad Sci USA 87: 152-156.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 152-156
    • Georges, E.1    Bradley, G.2    Gariepy, J.3    Ling, V.4
  • 94
    • 0027391633 scopus 로고
    • Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody
    • Georges E, Tsuruo T and Ling V (1993) Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody. J Biol Chem 268: 1792-1798.
    • (1993) J Biol Chem , vol.268 , pp. 1792-1798
    • Tsuruo T, G.E.1    Ling, V.2
  • 95
    • 0027748455 scopus 로고
    • Molecular analysis of the multidrug transporter
    • Germann UA (1993) Molecular analysis of the multidrug transporter. Cytotechnology 12: 33-62.
    • (1993) Cytotechnology , vol.12 , pp. 33-62
    • Germann, U.A.1
  • 97
    • 0029954843 scopus 로고    scopus 로고
    • P-glycoprotein-a mediator of multidrug resistance in tumour cells
    • Germann UA (1996) P-glycoprotein-a mediator of multidrug resistance in tumour cells. Eur J Cancer 32A: 927-944.
    • (1996) Eur J Cancer , vol.32 A , pp. 927-944
    • Germann, U.A.1
  • 100
    • 0026775053 scopus 로고
    • Separation of drug transport and chloride channel functions of the human multidrug resistance P-glycoprotein
    • Gill DR, Hyde SC, Higgins CF, Valverde MA, Mintenig GM and Sepúlveda FV (1992) Separation of drug transport and chloride channel functions of the human multidrug resistance P-glycoprotein. Cell 71: 23-32.
    • (1992) Cell , vol.71 , pp. 23-32
    • Gill, D.R.1    Hyde, S.C.2    Higgins, C.F.3    Valverde, Ma.4    Mintenig, G.M.5    Sepúlveda, F.V.6
  • 101
    • 0031041323 scopus 로고    scopus 로고
    • Identification of the in vivo phosphorylation sites for acidic-directed kinases in murine mdr1b P-glycoprotein
    • Glavy JS, Horwitz SB and Orr GA (1997) Identification of the in vivo phosphorylation sites for acidic-directed kinases in murine mdr1b P-glycoprotein. J Biol Chem 272: 5909-5914.
    • (1997) J Biol Chem , vol.272 , pp. 5909-5914
    • Horwitz Sb, G.J.S.1    Orr, G.A.2
  • 102
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL and Brown MS (1990) Regulation of the mevalonate pathway. Nature 343: 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 103
    • 0029889967 scopus 로고    scopus 로고
    • Protein kinase C-mediated phosphorylation does not regulate drug transport by the human multidrug resistance P-glycoprotein
    • Goodfellow HR, Sordini A, Ruetz S, Callaghan R, Gros P, McNaughton PA and Higgins CF (1996) Protein kinase C-mediated phosphorylation does not regulate drug transport by the human multidrug resistance P-glycoprotein. J Biol Chem 271: 13668-13674.
    • (1996) J Biol Chem , vol.271 , pp. 13668-13674
    • Goodfellow, H.R.1    Sordini, A.2    Ruetz, S.3    Callaghan, R.4    Gros, P.5    McNaughton, P.A.6    Higgins, C.F.7
  • 104
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman MM and Pastan I (1993) Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu Rev Biochem 62: 385-427.
    • (1993) Annu Rev Biochem , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 107
    • 0025216388 scopus 로고
    • Photoaffinity probes for the alpha 1-adrenergic receptor and the calcium channel bind to a common domain in P-glycoprotein
    • Greenberger LM, Yang CH, Gindin E and Horwitz SB (1990) Photoaffinity probes for the alpha 1-adrenergic receptor and the calcium channel bind to a common domain in P-glycoprotein. J Biol Chem 265: 4394-4401.
    • (1990) J Biol Chem , vol.265 , pp. 4394-4401
    • Greenberger, L.M.1    Ch, Y.2    Gindin, E.3    Horwitz, S.B.4
  • 108
    • 0025872032 scopus 로고
    • Domain mapping of the photoaffinity drug-binding sites in P-glycoprotein encoded mouse mdr1b
    • Greenberger LM, Lisanti CJ, Silva JT and Horwitz SB (1991) Domain mapping of the photoaffinity drug-binding sites in P-glycoprotein encoded mouse mdr1b. J Biol Chem 266: 20744-20751.
    • (1991) J Biol Chem , vol.266 , pp. 20744-20751
    • Greenberger, L.M.1    Lisanti, C.J.2    Silva, J.T.3    Horwitz, S.B.4
  • 109
    • 0027216104 scopus 로고
    • Major photoaffinity drug labeling sites for iodoaryl azidoprazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domain-6 and domain-12
    • Greenberger LM (1993) Major photoaffinity drug labeling sites for iodoaryl azidoprazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domain-6 and domain-12. J Biol Chem 268: 11417-11425.
    • (1993) J Biol Chem , vol.268 , pp. 11417-11425
    • Greenberger, L.M.1
  • 110
    • 0023006005 scopus 로고
    • Isolation and characterization of a complementary DNA that confers multidrug resistance
    • Gros P, Ben Neriah Y, Croop J and Housman DE (1986a) Isolation and characterization of a complementary DNA that confers multidrug resistance. Nature 323: 728-731.
    • (1986) Nature , vol.323 , pp. 728-731
    • Gros, P.1    Ben Neriah, Y.2    Croop, J.3    De Housman4
  • 111
    • 0022993652 scopus 로고
    • Mammalian multidrug resistance gene: Complete cDNA sequence indicates strong homology to bacterial transport proteins
    • Gros P, Croop J and Housman DE (1986b) Mammalian multidrug resistance gene: Complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell 47: 371-380.
    • (1986) Cell , vol.47 , pp. 371-380
    • Croop J, G.P.1    De Housman2
  • 112
    • 0022515908 scopus 로고
    • Isolation and characterization of DNA sequences amplified in multidrug-resistant hamster cells
    • Gros P, Croop J, Roninson IB, Varshavsky A and Housman DE (1986c) Isolation and characterization of DNA sequences amplified in multidrug-resistant hamster cells. Proc Natl Acad Sci USA 83: 337-341.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 337-341
    • Gros, P.1    Croop, J.2    Roninson, I.B.3    Varshavsky, A.4    De Housman5
  • 113
    • 0024044158 scopus 로고
    • Cloning and characterization of a second member of the mouse mdr gene family
    • Gros P, Raymond M, Bell J and Housman DE (1988) Cloning and characterization of a second member of the mouse mdr gene family. Mol Cell Biol 8: 2770-2778.
    • (1988) Mol Cell Biol , vol.8 , pp. 2770-2778
    • Gros, P.1    Raymond, M.2    Bell, J.3    De Housman4
  • 114
    • 0025766958 scopus 로고
    • A single amino acid substitution strongly modulates the activity and substrate specificity of the mouse mdr1 and mdr3 drug efflux pumps
    • Gros P, Dhir R, Croop J and Talbot F (1991) A single amino acid substitution strongly modulates the activity and substrate specificity of the mouse mdr1 and mdr3 drug efflux pumps. Proc Natl Acad Sci USA 88: 7289-7293.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7289-7293
    • Gros, P.1    Dhir, R.2    Croop, J.3    Talbot, F.4
  • 115
    • 0027957568 scopus 로고
    • Effect of Calphostin C (PKC inhibitor) on daunorubicin resistance in P388/ADR and HL60/AR cells: Reversal of drug resistance possibly via P-glycoprotein
    • Gupta S, Patel K, Singh H and Gollapudi S (1994) Effect of Calphostin C (PKC inhibitor) on daunorubicin resistance in P388/ADR and HL60/AR cells: reversal of drug resistance possibly via P-glycoprotein. Cancer Lett 76: 139-145.
    • (1994) Cancer Lett , vol.76 , pp. 139-145
    • Gupta, S.1    Patel, K.2    Singh, H.3    Gollapudi, S.4
  • 116
    • 0030027552 scopus 로고    scopus 로고
    • Partial reversal of multidrug resistance in human breast cancer cells by an N-myristoylated protein kinase C-alpha pseudosubstrate peptide
    • Gupta KP, Ward NE, Gravitt KR, Bergman PJ and O'Brian CA (1996) Partial reversal of multidrug resistance in human breast cancer cells by an N-myristoylated protein kinase C-alpha pseudosubstrate peptide. J Biol Chem 271: 2102-2111.
    • (1996) J Biol Chem , vol.271 , pp. 2102-2111
    • Kp, G.1    Ward, N.E.2    Gravitt, K.R.3    Bergman, P.J.4    O'Brian, C.A.5
  • 117
    • 0023161075 scopus 로고
    • Phosphorylation of the Mr 170 000 to 180 000 glycoprotein specific to multidrug-resistant tumor cells: Effects of verapamil, trifluoperazine, and phorbol esters
    • Hamada H, Hagiwara K-I, Nakajima T and Tsuruo T (1987) Phosphorylation of the Mr 170 000 to 180 000 glycoprotein specific to multidrug-resistant tumor cells: effects of verapamil, trifluoperazine, and phorbol esters. Cancer Res 47: 2860-2865.
    • (1987) Cancer Res , vol.47 , pp. 2860-2865
    • Hamada, H.1    Hagiwara, K.-I.2    Nakajima, T.3    Tsuruo, T.4
  • 118
    • 0023813001 scopus 로고
    • Characterization of the ATPase activity of the Mr 170 000 to 180 000 membrane glycoprotein (P-glycoprotein) associated with multidrug resistance in K562/ADM cells
    • Hamada H and Tsuruo T (1988a) Characterization of the ATPase activity of the Mr 170 000 to 180 000 membrane glycoprotein (P-glycoprotein) associated with multidrug resistance in K562/ADM cells. Cancer Res 48: 4926-4932.
    • (1988) Cancer Res , vol.48 , pp. 4926-4932
    • Hamada, H.1    Tsuruo, T.2
  • 119
    • 0023840065 scopus 로고
    • Purification of the 170- To 180-kilodalton membrane glycoprotein associated with multidrug resistance - 170- to 180-kilodalton membrane glycoprotein is an ATPase
    • Hamada H and Tsuruo T (1988b) Purification of the 170- to 180-kilodalton membrane glycoprotein associated with multidrug resistance - 170- to 180-kilodalton membrane glycoprotein is an ATPase. J Biol Chem 263: 1454-1458.
    • (1988) J Biol Chem , vol.263 , pp. 1454-1458
    • Hamada, H.1    Tsuruo, T.2
  • 120
    • 0029879199 scopus 로고    scopus 로고
    • Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning
    • Hanna M, Brault M, Kwan T, Kast C and Gros P (1996) Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning. Biochemistry 35: 3625-3635.
    • (1996) Biochemistry , vol.35 , pp. 3625-3635
    • Hanna, M.1    Brault, M.2    Kwan, T.3    Kast, C.4    Gros, P.5
  • 121
    • 0028876622 scopus 로고
    • Protein kinase C-mediated phosphorylation of the human multidrug resistance P-glycoprotein regulates cell volume-activated chloride channels
    • Hardy SP, Goodfellow HR, Valverde MA, Gill DR, Sepulveda V and Higgins CF (1995) Protein kinase C-mediated phosphorylation of the human multidrug resistance P-glycoprotein regulates cell volume-activated chloride channels. Embo J 14: 68-75.
    • (1995) Embo J , vol.14 , pp. 68-75
    • Goodfellow Hr, H.S.P.1    Valverde, Ma.2    Gill, D.R.3    Sepulveda, V.4    Higgins, C.F.5
  • 122
    • 0029018919 scopus 로고
    • Expression of multidrug resistance-associated protein (MRP), MDR1 and DNA topoisomerase II in human multidrug-resistant bladder cancer cell lines
    • Hasegawa S, Abe T, Naito S, Kotoh S, Kumazawa J, Hipfner DR, Deeley RG, Cole SP and Kuwano M (1995) Expression of multidrug resistance-associated protein (MRP), MDR1 and DNA topoisomerase II in human multidrug-resistant bladder cancer cell lines. Br J Cancer 71: 907-913.
    • (1995) Br J Cancer , vol.71 , pp. 907-913
    • Hasegawa, S.1    Abe, T.2    Naito, S.3    Kotoh, S.4    Kumazawa, J.5    Hipfner, D.R.6    Deeley, R.G.7    Cole, S.P.8    Kuwano, M.9
  • 123
    • 0026621245 scopus 로고
    • ABC transporters - From microorganisms to man
    • Higgins CF (1992) ABC transporters - from microorganisms to man. Annu Rev Cell Biol 8: 67-113.
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 125
    • 0002568489 scopus 로고
    • The ABC transporter channel superfamily - An overview
    • Higgins CF (1993) The ABC transporter channel superfamily - an overview. Semin Cell Biol 4: 1-5.
    • (1993) Semin Cell Biol , vol.4 , pp. 1-5
    • Higgins, C.F.1
  • 126
    • 0028914113 scopus 로고
    • P-glycoprotein and cell volume-activated chloride channels
    • Higgins CF (1995) P-glycoprotein and cell volume-activated chloride channels. J Bioenerg Biomembr 27: 63-70.
    • (1995) J Bioenerg Biomembr , vol.27 , pp. 63-70
    • Higgins, C.F.1
  • 127
  • 128
    • 0028033550 scopus 로고
    • Cystic fibrosis-type mutational analysis in the ATP-binding cassette transporter signature of human P-glycoprotein MDR1
    • Hoof T, Demmer A, Hadam MR, Riordan JR and Tummler B (1994) Cystic fibrosis-type mutational analysis in the ATP-binding cassette transporter signature of human P-glycoprotein MDR1. J Biol Chem 269: 20575-20583.
    • (1994) J Biol Chem , vol.269 , pp. 20575-20583
    • Hoof, T.1    Demmer, A.2    Hadam, M.R.3    Riordan, J.R.4    Tummler, B.5
  • 129
    • 0007630205 scopus 로고
    • ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells
    • Horio M, Gottesman MM and Pastan I (1988) ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells. Proc Natl Acad Sci USA 85: 3580-3584.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3580-3584
    • Gottesman Mm, H.M.1    Pastan, I.2
  • 130
  • 131
    • 0024344261 scopus 로고
    • Differential overexpression of three mdr gene family members in multidrug-resistant J774.2 mouse cells
    • Hsu SI, Lothstein L and Horwitz SB (1989) Differential overexpression of three mdr gene family members in multidrug-resistant J774.2 mouse cells. J Biol Chem 264: 12053-12062.
    • (1989) J Biol Chem , vol.264 , pp. 12053-12062
    • Lothstein L, H.S.I.1    Horwitz, S.B.2
  • 132
    • 0030568089 scopus 로고    scopus 로고
    • Relationship between the inhibition of azidopine binding to P-glycoprotein by MDR modulators and their efficiency in restoring doxorubicin intracellular accumulation
    • Hu YP, Chapey C and Robert J (1996) Relationship between the inhibition of azidopine binding to P-glycoprotein by MDR modulators and their efficiency in restoring doxorubicin intracellular accumulation. Cancer Lett 109: 203-209.
    • (1996) Cancer Lett , vol.109 , pp. 203-209
    • Chapey C, H.Y.P.1    Robert, J.2
  • 133
    • 0031045308 scopus 로고    scopus 로고
    • Co-expression of several molecular mechanisms of multidrug resistance and their significance for paclitaxel cytotoxicity in human AML HL-60 cells
    • Huang Y, Ibrado AM, Reed JC, Bullock G, Ray S, Tang C and Bhalla K (1997) Co-expression of several molecular mechanisms of multidrug resistance and their significance for paclitaxel cytotoxicity in human AML HL-60 cells. Leukemia 11: 253-257.
    • (1997) Leukemia , vol.11 , pp. 253-257
    • Huang, Y.1    Ibrado, A.M.2    Reed, J.C.3    Bullock, G.4    Ray, S.5    Tang, C.6    Bhalla, K.7
  • 136
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano RL and Ling V (1976) A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim Biophys Acta 455: 152-162.
    • (1976) Biochim Biophys Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 137
    • 0031566187 scopus 로고    scopus 로고
    • Domain organization of murine mdrlb P-glycoprotein: The cytoplasmic linker region is a potential dimerization domain
    • Juvvadi SR, Glavy JS, Horwitz SB and Orr GA (1997) Domain organization of murine mdrlb P-glycoprotein: the cytoplasmic linker region is a potential dimerization domain. Biochem Biophys Res Commun 230: 442-447.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 442-447
    • Juvvadi, S.R.1    Glavy, J.S.2    Horwitz, S.B.3    Orr, G.A.4
  • 138
    • 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, Vandykephillips V, Agresti M, Safa AR and Gros P (1993) Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain-11 as a putative drug binding site. Biochemistry 32: 4185-4194.
    • (1993) Biochemistry , vol.32 , pp. 4185-4194
    • Kajiji, S.1    Talbot, F.2    Grizzuti, K.3    Vandykephillips, V.4    Agresti, M.5    Safa, A.R.6    Gros, P.7
  • 139
    • 0028318223 scopus 로고
    • Structurally distinct MDR modulators show specific patterns of reversal against P-glycoproteins bearing unique mutations at serine 939/941
    • Kajiji S, Dreslin JA, Grizzuti K and Gros P (1994) Structurally distinct MDR modulators show specific patterns of reversal against P-glycoproteins bearing unique mutations at serine 939/941. Biochemistry 33: 5041-5048.
    • (1994) Biochemistry , vol.33 , pp. 5041-5048
    • Kajiji, S.1    Dreslin, J.A.2    Grizzuti, K.3    Gros, P.4
  • 140
    • 0024371025 scopus 로고
    • The function of Gp170, the multidrug resistance gene product, in rat liver canalicular membrane vesicles
    • Kamimoto Y, Gatmaitan Z, Hsu J and Arias IM (1989) The function of Gp170, the multidrug resistance gene product, in rat liver canalicular membrane vesicles. J Biol Chem 264: 11693-11698.
    • (1989) J Biol Chem , vol.264 , pp. 11693-11698
    • Kamimoto, Y.1    Gatmaitan, Z.2    Hsu, J.3    Arias, I.M.4
  • 141
    • 0029821966 scopus 로고    scopus 로고
    • Multidrug resistance in cancer cells
    • Kane SE (1996) Multidrug resistance in cancer cells. Advances Drug Research 28: 181-252.
    • (1996) Advances Drug Research , vol.28 , pp. 181-252
    • Kane, S.E.1
  • 142
    • 0021852930 scopus 로고
    • Detection of P-glycoprotein in multidrug-resistant cell lines by monoclonal antibodies
    • Kartner N, Evernden-Porelle D, Bradley G and Ling V (1985) Detection of P-glycoprotein in multidrug-resistant cell lines by monoclonal antibodies. Nature 316: 820-823.
    • (1985) Nature , vol.316 , pp. 820-823
    • Kartner, N.1    Evernden-Porelle, D.2    Bradley, G.3    Ling, V.4
  • 143
    • 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 (1995) Membrane topology of P-glycoprotein as determined by epitope insertion: transmembrane organization of the N-terminal domain of mdr3. Biochemistry 34: 4402-4411.
    • (1995) Biochemistry , vol.34 , pp. 4402-4411
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 144
    • 0029918133 scopus 로고    scopus 로고
    • Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence
    • Kast C, Canfield V, Levenson R and Gros P (1996) Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence. J Biol Chem 271: 9240-9248.
    • (1996) J Biol Chem , vol.271 , pp. 9240-9248
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 145
    • 0014290206 scopus 로고
    • Uptake and retention of daunomycin by mouse leukemic cells as factors in drug response
    • Kessel D, Botterill V and Wodinsky I (1968) Uptake and retention of daunomycin by mouse leukemic cells as factors in drug response. Cancer Res 28: 938-941.
    • (1968) Cancer Res , vol.28 , pp. 938-941
    • Kessel, D.1    Botterill, V.2    Wodinsky, I.3
  • 147
    • 0031566177 scopus 로고    scopus 로고
    • Functional modulation of ATPase of P-glycoprotein by C219, a monoclonal antibody against P-glycoprotein
    • Kokubu N, Cohen D and Watanabe T (1997) Functional modulation of ATPase of P-glycoprotein by C219, a monoclonal antibody against P-glycoprotein. Biochem Biophys Res Commun 230: 398-401.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 398-401
    • Cohen D, K.N.1    Watanabe, T.2
  • 148
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • Kyriakis JM, Avruch, J (1996) Sounding the alarm: protein kinase cascades activated by stress and inflammation. J Biol Chem 271: 24313-24316.
    • (1996) J Biol Chem , vol.271 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 149
    • 0027994354 scopus 로고
    • Cholesterol movement from plasma membrane to rough endoplasmic reticulum. Inhibition by progesterone
    • Lange Y (1994) Cholesterol movement from plasma membrane to rough endoplasmic reticulum. Inhibition by progesterone. J Biol Chem 269: 3411-3414.
    • (1994) J Biol Chem , vol.269 , pp. 3411-3414
    • Lange, Y.1
  • 150
    • 0029117020 scopus 로고
    • P-glycoprotein is hyperphosphorylated in multidrug resistant HOB1 lymphoma cells treated with overdose of vincristine
    • Lee WP (1995) P-glycoprotein is hyperphosphorylated in multidrug resistant HOB1 lymphoma cells treated with overdose of vincristine. Biochim Biophys Acta 1245: 57-61.
    • (1995) Biochim Biophys Acta , vol.1245 , pp. 57-61
    • Lee, W.P.1
  • 151
    • 0026723940 scopus 로고
    • ATP and GTP as alternative energy sources for vinblastine transport by P-170 in KB-V1 plasma membrane vesicles
    • Lelong IH, Padmanabhan R, Lovelace E, Pastan I and Gottesman MM (1992) ATP and GTP as alternative energy sources for vinblastine transport by P-170 in KB-V1 plasma membrane vesicles. FEBS Lett 304: 256-260.
    • (1992) FEBS Lett , vol.304 , pp. 256-260
    • Lelong, I.H.1    Padmanabhan, R.2    Lovelace, E.3    Pastan, I.4    Gottesman, M.M.5
  • 153
    • 0030334864 scopus 로고    scopus 로고
    • Membrane proteins which exhibit multiple topological orientations
    • Levy D (1996) Membrane proteins which exhibit multiple topological orientations. Essays Biochem 31: 49-60.
    • (1996) Essays Biochem , vol.31 , pp. 49-60
    • Levy, D.1
  • 154
    • 0029585247 scopus 로고
    • P-glycoprotein: Its role in drug resistance
    • Ling V (1995) P-glycoprotein: its role in drug resistance. Am J Med 99: 31S-34S.
    • (1995) Am J Med , vol.99
    • Ling, V.1
  • 155
    • 0029840320 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains
    • Liu R and Sharom FJ (1996) Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains. Biochemistry 35: 11865-11873.
    • (1996) Biochemistry , vol.35 , pp. 11865-11873
    • Liu, R.1    Sharom, F.J.2
  • 156
    • 0030973613 scopus 로고    scopus 로고
    • Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter
    • Liu R and Sharom FJ (1997) Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter. Biochemistry 36: 2836-2843.
    • (1997) Biochemistry , vol.36 , pp. 2836-2843
    • Liu, R.1    Sharom, F.J.2
  • 157
    • 0027260959 scopus 로고
    • Functional consequences of phenylalanine mutations in the predicted transmembrane domain of p-glycoprotein
    • Loo TW and Clarke DM (1993a) Functional consequences of phenylalanine mutations in the predicted transmembrane domain of p-glycoprotein. J Biol Chem 268: 19965-19972.
    • (1993) J Biol Chem , vol.268 , pp. 19965-19972
    • Loo, T.W.1    Clarke, D.M.2
  • 158
    • 0027512768 scopus 로고
    • Functional consequences of proline mutations in the predicted transmembrane domain of P-Glycoprotein
    • Loo TW and Clarke DM (1993b) Functional consequences of proline mutations in the predicted transmembrane domain of P-Glycoprotein. J Biol Chem 268: 3143-3149.
    • (1993) J Biol Chem , vol.268 , pp. 3143-3149
    • Loo, T.W.1    Clarke, D.M.2
  • 159
    • 0028245416 scopus 로고
    • Functional consequences of glycine mutations in the predicted cytoplasmic loops of P-glycoprotein
    • Loo TW and Clarke DM (1994a) Functional consequences of glycine mutations in the predicted cytoplasmic loops of P-glycoprotein. J Biol Chem 269: 7243-7248.
    • (1994) J Biol Chem , vol.269 , pp. 7243-7248
    • Loo, T.W.1    Clarke, D.M.2
  • 160
    • 0027997698 scopus 로고
    • Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein
    • Loo TW and Clarke DM (1994b) Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein. Biochemistry 33: 14049-14057.
    • (1994) Biochemistry , vol.33 , pp. 14049-14057
    • Loo, T.W.1    Clarke, D.M.2
  • 161
    • 0028229881 scopus 로고
    • Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides
    • Loo TW and Clarke DM (1994c) Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides. J Biol Chem 269: 7750-7755.
    • (1994) J Biol Chem , vol.269 , pp. 7750-7755
    • Loo, T.W.1    Clarke, D.M.2
  • 162
    • 0029121417 scopus 로고
    • Covalent modification of human P-glycoprotein mutants containing a single cysteine at either nucleotide-binding fold abolishes drug-stimulated ATPase activity
    • Loo TW and Clarke DM (1995a) Covalent modification of human P-glycoprotein mutants containing a single cysteine at either nucleotide-binding fold abolishes drug-stimulated ATPase activity. J Biol Chem 270: 22957-22961.
    • (1995) J Biol Chem , vol.270 , pp. 22957-22961
    • Loo, T.W.1    Clarke, D.M.2
  • 163
    • 0028928984 scopus 로고
    • Membrane topology of a cysteineless mutant of human P-glycoprotein
    • Loo TW and Clarke DM (1995b) Membrane topology of a cysteineless mutant of human P-glycoprotein. J Biol Chem 270: 843-848.
    • (1995) J Biol Chem , vol.270 , pp. 843-848
    • Loo, T.W.1    Clarke, D.M.2
  • 164
    • 0029099301 scopus 로고
    • P-glycoprotein: Associations between domains and between domains and molecular chaperones
    • Loo TW and Clarke DM (1995c) P-glycoprotein: associations between domains and between domains and molecular chaperones. J Biol Chem 270: 21839-21844.
    • (1995) J Biol Chem , vol.270 , pp. 21839-21844
    • Loo, T.W.1    Clarke, D.M.2
  • 165
    • 0029100095 scopus 로고
    • Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities
    • Loo TW and Clarke DM (1995d) Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities. J Biol Chem 270: 21449-21452.
    • (1995) J Biol Chem , vol.270 , pp. 21449-21452
    • Loo, T.W.1    Clarke, D.M.2
  • 166
    • 0029909604 scopus 로고    scopus 로고
    • Inhibition of oxidative crosslinking 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 TW and Clarke DM (1996a) Inhibition of oxidative crosslinking 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: 27482-27487.
    • (1996) J Biol Chem , vol.271 , pp. 27482-27487
    • Loo, T.W.1    Clarke, D.M.2
  • 167
    • 0029910016 scopus 로고    scopus 로고
    • The minimum functional unit of human P-glycoprotein appears to be a monomer
    • Loo TW and Clarke DM (1996b) The minimum functional unit of human P-glycoprotein appears to be a monomer. J Biol Chem 271: 27488-27492.
    • (1996) J Biol Chem , vol.271 , pp. 27488-27492
    • Loo, T.W.1    Clarke, D.M.2
  • 168
    • 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 TW and Clarke DM (1996c) 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: 15414-15419.
    • (1996) J Biol Chem , vol.271 , pp. 15414-15419
    • Loo, T.W.1    Clarke, D.M.2
  • 169
    • 0028042172 scopus 로고
    • Selection for MDR1/P-glycoprotein enhances swelling-activated K+ and Cl- Currents in NIH/3T3 cells
    • Luckie DB, Krouse ME, Harper KL, Law TC and Wine JJ (1994) Selection for MDR1/P-glycoprotein enhances swelling-activated K+ and Cl- currents in NIH/3T3 cells. Am J Physiol 267: C650-C658.
    • (1994) Am J Physiol , vol.267
    • Luckie, D.B.1    Krouse, M.E.2    Harper, K.L.3    Law, T.C.4    Wine, J.J.5
  • 170
    • 0027538652 scopus 로고
    • Molecular targets in oncology: Implications of the multidrug resistance gene
    • Lum BL, Gosland MP, Kaubisch S and Sikic BI (1993) Molecular targets in oncology: Implications of the multidrug resistance gene. Pharmacotherapy 13: 88-109.
    • (1993) Pharmacotherapy , vol.13 , pp. 88-109
    • Lum, B.L.1    Gosland, M.P.2    Kaubisch, S.3    Sikic, B.I.4
  • 171
    • 0025945570 scopus 로고
    • Analysis of P-glycoprotein phosphorylation in HL60 cells isolated for resistance to vincristine
    • Ma LD, Marquardt D, Takemoto L and Center MS (1991) Analysis of P-glycoprotein phosphorylation in HL60 cells isolated for resistance to vincristine. J Biol Chem 266: 5593-5599.
    • (1991) J Biol Chem , vol.266 , pp. 5593-5599
    • Ma, L.D.1    Marquardt, D.2    Takemoto, L.3    Center, M.S.4
  • 172
    • 0028589070 scopus 로고
    • Dexniguldipine-HCl is a potent allosteric inhibitor of [3H]vinblastine binding to P-glycoprotein of CCRF ADR 5000 cells
    • Malkhandi J, Ferry DR, Boer R, Gekeler V, Ise W and Kerr DJ (1994) Dexniguldipine-HCl is a potent allosteric inhibitor of [3H]vinblastine binding to P-glycoprotein of CCRF ADR 5000 cells. Eur J Pharmacol 288: 105-114.
    • (1994) Eur J Pharmacol , vol.288 , pp. 105-114
    • Malkhandi, J.1    Ferry, D.R.2    Boer, R.3    Gekeler, V.4    Ise, W.5    Kerr, D.J.6
  • 173
    • 0023508529 scopus 로고
    • Phosphorylation of the multidrug resistance associated glycoprotein
    • Mellado W and Horwitz SB (1987) Phosphorylation of the multidrug resistance associated glycoprotein. Biochemistry 26: 6900-6904.
    • (1987) Biochemistry , vol.26 , pp. 6900-6904
    • Mellado, W.1    Horwitz, S.B.2
  • 174
    • 0030022955 scopus 로고    scopus 로고
    • Role of multidrug resistance P-glycoproteins in cholesterol biosynthesis
    • Metherall JE, Li H and Waugh K (1996a) Role of multidrug resistance P-glycoproteins in cholesterol biosynthesis. J Biol Chem 271: 2634-2640.
    • (1996) J Biol Chem , vol.271 , pp. 2634-2640
    • Li H, M.J.E.1    Waugh, K.2
  • 175
    • 0030027903 scopus 로고    scopus 로고
    • Progesterone inhibits cholesterol biosynthesis in cultured cells. Accumulation of cholesterol precursors
    • Metherall JE, Waugh K and Li H (1996b) Progesterone inhibits cholesterol biosynthesis in cultured cells. Accumulation of cholesterol precursors. J Biol Chem 271: 2627-2633.
    • (1996) J Biol Chem , vol.271 , pp. 2627-2633
    • Waugh K, M.J.E.1    Li, H.2
  • 176
    • 0026053770 scopus 로고
    • Structural model of the nucleotide-binding conserved component of periplasmic permeases
    • Mimura CS, Holbrook SR and Ames GF-L (1991) Structural model of the nucleotide-binding conserved component of periplasmic permeases. Proc Natl Acad Sci US. 88: 84-88.
    • (1991) Proc Natl Acad Sci US. , vol.88 , pp. 84-88
    • Mimura, C.S.1    Holbrook, S.R.2    Ames, G.F.-L.3
  • 177
  • 178
    • 0028128286 scopus 로고
    • Localization of the forskolin labeling sites to both halves of P-glycoprotein: Similarity of the sites labeled by forskolin and prazosin
    • Morris DI, Greenberger LM, Bruggemann EP, Cardarelli C, Gottesman MM, Pastan I and Seamon KB (1994) Localization of the forskolin labeling sites to both halves of P-glycoprotein: similarity of the sites labeled by forskolin and prazosin. Mol. Pharmacol 46: 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    Seamon, K.B.7
  • 180
    • 0026748955 scopus 로고
    • Functionally active homodimer of P-glycoprotein in multidrug-resistant tumor cells
    • Naito M and Tsuruo T (1992) Functionally active homodimer of P-glycoprotein in multidrug-resistant tumor cells. Biochem Biophys Res Commun 185: 284-290.
    • (1992) Biochem Biophys Res Commun , vol.185 , pp. 284-290
    • Naito, M.1    Tsuruo, T.2
  • 181
    • 0027406201 scopus 로고
    • Enhancement of cellular accumulation of cyclosporin by anti-P-glycoprotein monoclonal antibody MRK-16 and synergistic modulation of multidrug resistance
    • Naito M, Tsuge H, Kuroko C, Koyama T, Tomida A, Tatsuta T, Heike Y and Tsuruo T (1993) Enhancement of cellular accumulation of cyclosporin by anti-P-glycoprotein monoclonal antibody MRK-16 and synergistic modulation of multidrug resistance. J Nat Cancer Inst 85: 311-316.
    • (1993) J Nat Cancer Inst , vol.85 , pp. 311-316
    • Naito, M.1    Tsuge, H.2    Kuroko, C.3    Koyama, T.4    Tomida, A.5    Tatsuta, T.6    Heike, Y.7    Tsuruo, T.8
  • 182
    • 0028825869 scopus 로고
    • A new paclitaxel photoaffinity analog with a 3-(4-benzoylphenyl)propanoyl probe for characterization of drug-binding sites on tubulin and P-glycoprotein
    • Ojima I, Duclos O, Dorman G, Simonot B, Prestwich GD, Rao S, Lerro KA and Horwitz SB (1995) A new paclitaxel photoaffinity analog with a 3-(4-benzoylphenyl)propanoyl probe for characterization of drug-binding sites on tubulin and P-glycoprotein. J Med Chem 38: 3891-3894.
    • (1995) J Med Chem , vol.38 , pp. 3891-3894
    • Ojima, I.1    Duclos, O.2    Dorman, G.3    Simonot, B.4    Prestwich, G.D.5    Rao, S.6    Lerro, K.A.7    Horwitz, S.B.8
  • 183
    • 0030035535 scopus 로고    scopus 로고
    • Effects of steroids and verapamil on P-glycoprotein ATPase activity: Progesterone, desoxycorticosterone, corticosterone and verapamil are mutually non-exclusive modulators
    • Orlowski S, Mir LM, Belehradek J, Jr. and Garrigos M (1996) Effects of steroids and verapamil on P-glycoprotein ATPase activity: progesterone, desoxycorticosterone, corticosterone and verapamil are mutually non-exclusive modulators. Biochem J 317: 515-522.
    • (1996) Biochem J , vol.317 , pp. 515-522
    • Orlowski, S.1    Mir, L.M.2    Belehradek, J.3    Jr4    Garrigos, M.5
  • 185
    • 0029851730 scopus 로고    scopus 로고
    • 2-terminal protein kinase pathway in the cellular response to Adriamycin and other chemotherapeutic drugs
    • 2-terminal protein kinase pathway in the cellular response to Adriamycin and other chemotherapeutic drugs. J Biol Chem 271: 30950-30955.
    • (1996) J Biol Chem , vol.271 , pp. 30950-30955
    • Osborn, M.T.1    Chambers, T.C.2
  • 186
    • 0028850221 scopus 로고
    • The role of mdr2 P-glycoprotein in biliary lipid secretion. Cross-talk between cancer research and biliary physiology
    • Oude Elferink RPJ and Groen AK (1995) The role of mdr2 P-glycoprotein in biliary lipid secretion. Cross-talk between cancer research and biliary physiology. J Hepatol 23: 617-625.
    • (1995) J Hepatol , vol.23 , pp. 617-625
    • Oude Elferink, R.P.J.1    Groen, A.K.2
  • 188
    • 0029036714 scopus 로고
    • Isolation of antigenic mimics of MDR1-P-glycoprotein by phagedisplayed peptide libraries
    • Poloni F, Romagnoli G, Cianfriglia M and Felici F (1995) Isolation of antigenic mimics of MDR1-P-glycoprotein by phagedisplayed peptide libraries. Int J Cancer 61: 727-731.
    • (1995) Int J Cancer , vol.61 , pp. 727-731
    • Poloni, F.1    Romagnoli, G.2    Cianfriglia, M.3    Felici, F.4
  • 189
    • 0028203332 scopus 로고
    • Detection of oligomeric and monomeric forms of P-glycoprotein in multidrug resistant cells [published erratum appears in Biochemistry (1994) 33: 9032]
    • Poruchynsky MS and Ling V (1994) Detection of oligomeric and monomeric forms of P-glycoprotein in multidrug resistant cells [published erratum appears in Biochemistry (1994) 33: 9032]. Biochemistry 33: 4163-4174.
    • (1994) Biochemistry , vol.33 , pp. 4163-4174
    • Poruchynsky, M.S.1    Ling, V.2
  • 190
    • 0025131387 scopus 로고
    • Progesterone photoaffinity labels P-glycoprotein in multidrug-resistant human leukemic lymphoblasts
    • Qian XD and Beck WT (1990) Progesterone photoaffinity labels P-glycoprotein in multidrug-resistant human leukemic lymphoblasts. J Biol Chem 265: 18753-18756.
    • (1990) J Biol Chem , vol.265 , pp. 18753-18756
    • Qian, X.D.1    Beck, W.T.2
  • 191
    • 0029797074 scopus 로고    scopus 로고
    • Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system
    • Ramachandra M, Ambudkar SV, Gottesman MM, Pastan I and Hrycyna CA (1996) Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system. Mol Biol Cell 7: 1485-1498.
    • (1996) Mol Biol Cell , vol.7 , pp. 1485-1498
    • Ramachandra, M.1    Ambudkar, S.V.2    Gottesman, M.M.3    Pastan, I.4    Hrycyna, C.A.5
  • 192
    • 0028217326 scopus 로고
    • Direct demonstration of high affinity interactions of immunosuppressant drugs with the drug binding site of the human P-glycoprotein
    • Rao US and Scarborough GA (1994) Direct demonstration of high affinity interactions of immunosuppressant drugs with the drug binding site of the human P-glycoprotein. Mol Pharmacol 45: 773-776.
    • (1994) Mol Pharmacol , vol.45 , pp. 773-776
    • Rao, U.S.1    Scarborough, G.A.2
  • 193
    • 0028899422 scopus 로고
    • Mutation of glycine 185 to valine alters the ATPase function of the human P-glycoprotein expressed in Sf9 cells
    • Rao US (1995) Mutation of glycine 185 to valine alters the ATPase function of the human P-glycoprotein expressed in Sf9 cells. J Biol Chem 270: 6686-6690.
    • (1995) J Biol Chem , vol.270 , pp. 6686-6690
    • Rao, U.S.1
  • 194
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Raviv Y, Pollard HB, Bruggemann EP, Pastan I and Gottesman MM (1990) Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells. J Biol Chem 265: 3975-3980.
    • (1990) J Biol Chem , vol.265 , pp. 3975-3980
    • Raviv, Y.1    Pollard, H.B.2    Bruggemann, E.P.3    Pastan, I.4    Gottesman, M.M.5
  • 195
    • 0029190287 scopus 로고
    • The role of the MDR protein in altered drug translocation across tumor cell membranes
    • Roepe PD (1995) The role of the MDR protein in altered drug translocation across tumor cell membranes. Biochim Biophys Acta 1241: 385-405.
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 385-405
    • Roepe, P.D.1
  • 196
  • 197
    • 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 MF, Callaghan R, Ford RC and Higgins CF (1997) Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J Biol Chem 272: 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
  • 198
    • 0028234560 scopus 로고
    • Functional expression of P-glycoprotein in secretory vesicles
    • Ruetz S and Gros P (1994a) Functional expression of P-glycoprotein in secretory vesicles. J Biol Chem 269: 12277-12284.
    • (1994) J Biol Chem , vol.269 , pp. 12277-12284
    • Ruetz, S.1    Gros, P.2
  • 199
    • 0028307550 scopus 로고
    • Phospatidylcholine translocase: A physiological role for the mdr2 gene
    • Ruetz S and Gros P (1994b) Phospatidylcholine translocase: a physiological role for the mdr2 gene. Cell 77: 1071-1081.
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 200
    • 0028820769 scopus 로고
    • Enhancement of Mdr2-mediated phosphatidylcholine translocation by the bile salt taurocholate
    • Ruetz S and Gros P (1995) Enhancement of Mdr2-mediated phosphatidylcholine translocation by the bile salt taurocholate. J Biol Chem 270: 25388-25395.
    • (1995) J Biol Chem , vol.270 , pp. 25388-25395
    • Ruetz, S.1    Gros, P.2
  • 201
    • 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 CW, Safa AR, Harrison SD and Fine RL (1995) 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: 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
  • 203
    • 0027418815 scopus 로고
    • Human P-glycoprotein transports cyclosporin A and FK506
    • Saeki T, Ueda K, Tanigawara Y Hori R and Komano T (1993a) Human P-glycoprotein transports cyclosporin A and FK506. J Biol Chem 268: 6077-6080.
    • (1993) J Biol Chem , vol.268 , pp. 6077-6080
    • Saeki, T.1    Ueda, K.2    Hori R, T.Y.3    Komano, T.4
  • 204
    • 0027309055 scopus 로고
    • PGlycoprotein-mediated transcellular transport of MDR-reversing agents
    • Saeki T, Ueda K, Tanigawara Y Hori R and Komano T (1993b) PGlycoprotein-mediated transcellular transport of MDR-reversing agents. FEBS Lett 324: 99-102.
    • (1993) FEBS Lett , vol.324 , pp. 99-102
    • Saeki, T.1    Ueda, K.2    Hori R, T.Y.3    Komano, T.4
  • 205
    • 0022975468 scopus 로고
    • Vinblastine photoaffinity labeling of a high-molecular-weight surface membrane glycoprotein specific for multidrug-resistant cells
    • Safa AR, Glover CJ, Meyets MB, Biedler JL and Felsted RL (1986) Vinblastine photoaffinity labeling of a high-molecular-weight surface membrane glycoprotein specific for multidrug-resistant cells. J Biol Chem 261: 6137-6140.
    • (1986) J Biol Chem , vol.261 , pp. 6137-6140
    • Safa, A.R.1    Glover, C.J.2    Meyets, M.B.3    Biedler, J.L.4    Felsted, R.L.5
  • 206
    • 0023226943 scopus 로고
    • Identification of the multidrug-resistance-related membrane glycoprotein as an acceptor for calcium channel blockers
    • Safa AR, Glover CJ, Sewell JL, Meyers MB, Biedler JL and Felsted RL (1987) Identification of the multidrug-resistance-related membrane glycoprotein as an acceptor for calcium channel blockers. J Biol Chem 262: 7884-7888.
    • (1987) J Biol Chem , vol.262 , pp. 7884-7888
    • Safa, A.R.1    Glover, C.J.2    Sewell, J.L.3    Meyers, M.B.4    Biedler, J.L.5    Felsted, R.L.6
  • 207
    • 0000622931 scopus 로고
    • Photoaffinity labeling of the multidrug-resistancerelated P-glycoprotein with photoactive analogs of verapamil
    • Safa AR (1988) Photoaffinity labeling of the multidrug-resistancerelated P-glycoprotein with photoactive analogs of verapamil. Proc Natl Acad Sci USA 85: 7187-7191.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7187-7191
    • Safa, A.R.1
  • 208
    • 0024378411 scopus 로고
    • Photoaffinity labeling of P-glycoprotein in multidrug-resistant cells with photoactive analogs of colchicine
    • Safa AR, Mehta ND and Agresti M (1989) Photoaffinity labeling of P-glycoprotein in multidrug-resistant cells with photoactive analogs of colchicine. Biochem Biophys Res Commun 161: 1402-1408.
    • (1989) Biochem Biophys Res Commun , vol.161 , pp. 1402-1408
    • Mehta Nd, S.A.R.1    Agresti, M.2
  • 209
    • 0025051429 scopus 로고
    • Molecular basis of preferential resistance to colchicine in multidrug-resistant human cells conferred by Gly to Val-185 substitution in P-glycoprotein
    • Safa AR, Stern RK, Choi K, Agresti M, Tamai I, Mehta ND and Roninson IB (1990) Molecular basis of preferential resistance to colchicine in multidrug-resistant human cells conferred by Gly to Val-185 substitution in P-glycoprotein. Proc Natl Acad Sci USA 87: 7225-7229.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7225-7229
    • Safa, A.R.1    Stern, R.K.2    Choi, K.3    Agresti, M.4    Tamai, I.5    Mehta, N.D.6    Roninson, I.B.7
  • 210
    • 0027396980 scopus 로고
    • Photoaffinity labeling of P-glycoprotein in multidrug-resistant cells
    • Safa AR (1993) Photoaffinity labeling of P-glycoprotein in multidrug-resistant cells. Cancer Invest 11: 46-56.
    • (1993) Cancer Invest , vol.11 , pp. 46-56
    • Safa, A.R.1
  • 211
    • 0028142326 scopus 로고
    • Tamoxifen aziridine, a novel affinity probe for P-glycoprotein in multidrug resistant cells
    • Safa AR, Roberts S, Agresti M and Fine RL (1994) Tamoxifen aziridine, a novel affinity probe for P-glycoprotein in multidrug resistant cells. Biochem Biophys Res Commun 202: 606-612.
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 606-612
    • Safa, A.R.1    Roberts, S.2    Agresti, M.3    Fine, R.L.4
  • 212
    • 0026722467 scopus 로고
    • Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase
    • Sarkadi B, Price EM, Boucher RC, Germann UA and Scarborough GA (1992) Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase. J Biol Chem 267: 4854-4858.
    • (1992) J Biol Chem , vol.267 , pp. 4854-4858
    • Sarkadi, B.1    Price, E.M.2    Boucher, R.C.3    Germann, U.A.4    Scarborough, G.A.5
  • 213
    • 0025565954 scopus 로고
    • Staurosporine, a potent inhibitor of C-kinase, enhances drug accumulation in multidrug-resistant cells
    • Sato W, Yusa K, Naito M and Tsuruo T (1990) Staurosporine, a potent inhibitor of C-kinase, enhances drug accumulation in multidrug-resistant cells. Biochem Biophys Res Commun 173: 1252-1257.
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 1252-1257
    • Sato, W.1    Yusa, K.2    Naito, M.3    Tsuruo, T.4
  • 214
    • 0025893114 scopus 로고
    • Characterization of the human MDR3 P-glycoprotein and its recognition by P-glycoprotein-specific monoclonal antibodies
    • Schinkel AH, Roelofs MEM and Borst P (1991) Characterization of the human MDR3 P-glycoprotein and its recognition by P-glycoprotein-specific monoclonal antibodies. Cancer Res 51: 2628-2635.
    • (1991) Cancer Res , vol.51 , pp. 2628-2635
    • Schinkel, A.H.1    Roelofs, M.E.M.2    Borst, P.3
  • 215
    • 0027408359 scopus 로고
    • N-glycosylation and deletion mutants of the human MDR1 P-Glycoprotein
    • Schinkel AH, Kemp S, Dolle M, Rudenko G and Wagenaar E (1993) N-glycosylation and deletion mutants of the human MDR1 P-Glycoprotein. J Biol Chem 268: 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
  • 216
    • 0027970462 scopus 로고
    • Functional studies of P-glycoprotein in inside-out plasma membrane vesicles derived from murine erythroleukemia cells overexpressing MDR3
    • Schlemmer SR and Sirotnak FM (1994) Functional studies of P-glycoprotein in inside-out plasma membrane vesicles derived from murine erythroleukemia cells overexpressing MDR3. J Biol Chem 269: 31059-31066.
    • (1994) J Biol Chem , vol.269 , pp. 31059-31066
    • Schlemmer, S.R.1    Sirotnak, F.M.2
  • 217
    • 0024378054 scopus 로고
    • Characterization of the multidrug resistance protein expressed in cell clones stably transfected with the mouse mdrl cDNA
    • Schurr E, Raymond M, Bell JC and Gros P (1989) Characterization of the multidrug resistance protein expressed in cell clones stably transfected with the mouse mdrl cDNA. Cancer Res 49: 2729-2734.
    • (1989) Cancer Res , vol.49 , pp. 2729-2734
    • Schurr, E.1    Raymond, M.2    Bell, J.C.3    Gros, P.4
  • 218
    • 0029559159 scopus 로고
    • The catalytic cycle of P-glycoprotein
    • Senior AE, Al-Shawi MK and Urbatsch IL (1995) The catalytic cycle of P-glycoprotein. FEBS Lett 377: 285-289.
    • (1995) FEBS Lett , vol.377 , pp. 285-289
    • Al-Shawi Mk, S.A.E.1    Urbatsch, I.L.2
  • 219
    • 0027937143 scopus 로고
    • ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells
    • Shapiro AB and Ling V (1994) ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells. J Biol Chem 269: 3745-3754.
    • (1994) J Biol Chem , vol.269 , pp. 3745-3754
    • Shapiro, A.B.1    Ling, V.2
  • 220
    • 0029061103 scopus 로고
    • Reconstitution of drug transport by purified P-glycoprotein
    • Shapiro AB and Ling V (1995) Reconstitution of drug transport by purified P-glycoprotein. J Biol Chem 270: 16167-16175.
    • (1995) J Biol Chem , vol.270 , pp. 16167-16175
    • Shapiro, A.B.1    Ling, V.2
  • 221
    • 0029041911 scopus 로고
    • Cloning, overexpression, purification, and characterization of the carboxyl-terminal nucleotide binding domain of P-glycoprotein
    • Sharma S and Rose D (1995) Cloning, overexpression, purification, and characterization of the carboxyl-terminal nucleotide binding domain of P-glycoprotein. J Biol Chem 270: 14085-14093.
    • (1995) J Biol Chem , vol.270 , pp. 14085-14093
    • Sharma, S.1    Rose, D.2
  • 222
    • 0027482461 scopus 로고
    • Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein
    • Sharom FJ, Yu X and Doige CA (1993) Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein. J Biol Chem 268: 24197-24202.
    • (1993) J Biol Chem , vol.268 , pp. 24197-24202
    • Yu X, S.F.J.1    Doige, C.A.2
  • 223
    • 0029987548 scopus 로고    scopus 로고
    • Synthetic hydrophobic peptides are substrates for P-glycoprotein and stimulate drug transport
    • Sharom FJ, Yu X, DiDiodato G and Chu JW (1996) Synthetic hydrophobic peptides are substrates for P-glycoprotein and stimulate drug transport. Biochem J 320: 421-428.
    • (1996) Biochem J , vol.320 , pp. 421-428
    • Sharom, F.J.1    Yu, X.2    Didiodato, G.3    Chu, J.W.4
  • 224
    • 0023030685 scopus 로고
    • Multiple drug resistant human KB carcinoma cells independently selected for high-level resistance to colchicine, Adriamycin or vinblastine show changes in expression of specific proteins
    • Shen D-W, Cardarelli C, Hwang J, Cornwell M, Richert N, Ishii S, Pastan I and Gottesman MM (1986) Multiple drug resistant human KB carcinoma cells independently selected for high-level resistance to colchicine, Adriamycin or vinblastine show changes in expression of specific proteins. J Biol Chem 261: 7762-7770.
    • (1986) J Biol Chem , vol.261 , pp. 7762-7770
    • Shen, D.-W.1    Cardarelli, C.2    Hwang, J.3    Cornwell, M.4    Richert, N.5    Ishii, S.6    Pastan, I.7    Gottesman, M.M.8
  • 225
    • 0026756347 scopus 로고
    • P-glycoprotein-ATP hydrolysis by the N-terminal nucleotidebinding domain
    • Shimabuku AM, Nishimoto T, Ueda K and Komano T (1992) P-glycoprotein-ATP hydrolysis by the N-terminal nucleotidebinding domain. J Biol Chem 267: 4308-4311.
    • (1992) J Biol Chem , vol.267 , pp. 4308-4311
    • Shimabuku, A.M.1    Nishimoto, T.2    Ueda, K.3    Komano, T.4
  • 226
    • 0028918796 scopus 로고
    • P-glycoprotein-mediated multidrug resistance in tumor cells: Biochemistry, clinical relevance and modulation
    • Shustik C, Dalton W and Gros P (1995) P-glycoprotein-mediated multidrug resistance in tumor cells: biochemistry, clinical relevance and modulation. Mol Aspects Med 16: 1-78.
    • (1995) Mol Aspects Med , vol.16 , pp. 1-78
    • Dalton W, S.C.1    Gros, P.2
  • 227
    • 0025954269 scopus 로고
    • Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations
    • Shyamala V, Baichwald V, Beall E and Ames GF-L (1991) Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations. J Biol Chem 266: 18714-18719.
    • (1991) J Biol Chem , vol.266 , pp. 18714-18719
    • Shyamala, V.1    Baichwald, V.2    Beall, E.3    Ames, G.F.-L.4
  • 228
    • 0025946645 scopus 로고
    • Cloning and characterization of a member of the rat multidrug resistance (mdr) gene family
    • Silverman JA, Raunio H, Gant TW and Thorgeirsson SS (1991) Cloning and characterization of a member of the rat multidrug resistance (mdr) gene family. Gene 106: 229-236.
    • (1991) Gene , vol.106 , pp. 229-236
    • Silverman, J.A.1    Raunio, H.2    Gant, T.W.3    Thorgeirsson, S.S.4
  • 229
    • 0027519416 scopus 로고
    • Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences
    • Skach WR and Lingappa VR (1993) Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences. J Biol Chem 268: 23552-23561.
    • (1993) J Biol Chem , vol.268 , pp. 23552-23561
    • Skach, W.R.1    Lingappa, V.R.2
  • 230
    • 0027512232 scopus 로고
    • Evidence for an alternate model of human P-Glycoprotein structure and biogenesis
    • Skach WR, Calayag MC and Lingappa VR (1993) Evidence for an alternate model of human P-Glycoprotein structure and biogenesis. J Biol Chem 268: 6903-6908.
    • (1993) J Biol Chem , vol.268 , pp. 6903-6908
    • Calayag Mc, S.W.R.1    Lingappa, V.R.2
  • 231
    • 0028343114 scopus 로고
    • Transmembrane orientation and topogenesis of the third and fourth membrane-spanning regions of human P-glycoprotein (MDR1)
    • Skach WR and Lingappa VR (1994) Transmembrane orientation and topogenesis of the third and fourth membrane-spanning regions of human P-glycoprotein (MDR1).Cancer Res 54: 3202-3209.
    • (1994) Cancer Res , vol.54 , pp. 3202-3209
    • Skach, W.R.1    Lingappa, V.R.2
  • 233
    • 0028081258 scopus 로고
    • Expression of the multidrug resistance associated protein and P-glycoprotein in doxorubicin-selected human myeloid leukemia cells
    • Slapak CA, Mizunuma N and Kufe DW (1994) Expression of the multidrug resistance associated protein and P-glycoprotein in doxorubicin-selected human myeloid leukemia cells. Blood 84: 3113-3121.
    • (1994) Blood , vol.84 , pp. 3113-3121
    • Mizunuma N, S.C.A.1    Kufe, D.W.2
  • 235
    • 0028112934 scopus 로고
    • Tissue distribution of the human MDR3 P-glycoprotein [see comments] [published erratum appears in Lab Invest (1995) 72:following table of contents]
    • Smit JJ, Schinkel AH, Mol CA, Majoor D, Mooi WJ, Jongsma AP, Lincke CR and Borst P (1994) Tissue distribution of the human MDR3 P-glycoprotein [see comments] [published erratum appears in Lab Invest (1995) 72:following table of contents]. Lab Invest 71: 638-649.
    • (1994) Lab Invest , vol.71 , pp. 638-649
    • Smit, J.J.1    Schinkel, A.H.2    Mol, C.A.3    Majoor, D.4    Mooi, W.J.5    Jongsma, A.P.6    Lincke, C.R.7    Borst, P.8
  • 236
    • 0028818853 scopus 로고
    • Circumvention of P-glycoproteinmediated multiple drug resistance by phosphorylation modulators is independent of protein kinases
    • Smith CD and Zilfou JT (1995) Circumvention of P-glycoproteinmediated multiple drug resistance by phosphorylation modulators is independent of protein kinases. J Biol Chem: 28145-28152.
    • (1995) J Biol Chem , pp. 28145-28152
    • Smith, C.D.1    Zilfou, J.T.2
  • 237
    • 0025231578 scopus 로고
    • Characterization of a membrane-associated protein kinase of multidrug- Resistant HL60 cells which phosphorylates P-glycoprotein
    • Staats J, Marquardt D and Center MS (1990) Characterization of a membrane-associated protein kinase of multidrug- resistant HL60 cells which phosphorylates P-glycoprotein. J Biol Chem 265: 4084-4090.
    • (1990) J Biol Chem , vol.265 , pp. 4084-4090
    • Marquardt D, S.J.1    Center, M.S.2
  • 238
    • 0003133632 scopus 로고
    • Development of multidrug resistance in rodent cell lines
    • Roninson IB (ed) Plenum Publishing Corporation: New York
    • Sugimoto Y and Tsuruo T (1991) Development of multidrug resistance in rodent cell lines. In: Roninson IB (ed) Molecular and Cellular Biology of Multidrug Resistance in Tumor Cells (pp. 57-70). Plenum Publishing Corporation: New York.
    • (1991) Molecular and Cellular Biology of Multidrug Resistance in Tumor Cells , pp. 57-70
    • Sugimoto, Y.1    Tsuruo, T.2
  • 239
    • 0025991731 scopus 로고
    • Azidopine noncompetitively interacts with vinblastine and cyclosporin A binding to P-glycoprotein in multidrug resistant cells
    • Tamai I and Safa AR (1991) Azidopine noncompetitively interacts with vinblastine and cyclosporin A binding to P-glycoprotein in multidrug resistant cells. J Biol Chem 266: 16796-16800.
    • (1991) J Biol Chem , vol.266 , pp. 16796-16800
    • Tamai, I.1    Safa, A.R.2
  • 240
    • 0028961304 scopus 로고
    • Human (MDR1) and mouse (mdrl, mdr3) P-glycoproteins can be distinguished by their respective drug resistance profiles and sensitivity to modulators
    • Tang-Wai DE, Kajiji S, DiCapua F, de Graaf D, Roninson IB and Gros P (1995) Human (MDR1) and mouse (mdrl, mdr3) P-glycoproteins can be distinguished by their respective drug resistance profiles and sensitivity to modulators. Biochemistry 34: 32-39.
    • (1995) Biochemistry , vol.34 , pp. 32-39
    • De Tang-Wai1    Kajiji, S.2    Dicapua, F.3    De Graaf, D.4    Roninson, I.B.5    Gros, P.6
  • 241
    • 0019430432 scopus 로고
    • Overcoming of vincristine resistance in P388 leukemia in vivo and in vitro through enhanced cytotoxicity of vincristine and vinblastine by verapamil
    • Tsuruo T, Iida H, Tsukagoshi S and Sakurai Y (1981) Overcoming of vincristine resistance in P388 leukemia in vivo and in vitro through enhanced cytotoxicity of vincristine and vinblastine by verapamil. Cancer Res 41: 1967-1972.
    • (1981) Cancer Res , vol.41 , pp. 1967-1972
    • Tsuruo, T.1    Iida, H.2    Tsukagoshi, S.3    Sakurai, Y.4
  • 242
    • 0020426820 scopus 로고
    • Increased accumulation of vincristine and Adriamycin in drug-resistant P388 tumor cells following incubation with calcium antagonists and calmodulin inhibitors
    • Tsuruo T, Iida H, Tsukagoshi S and Sakurai Y (1982) Increased accumulation of vincristine and Adriamycin in drug-resistant P388 tumor cells following incubation with calcium antagonists and calmodulin inhibitors. Cancer Res 42: 4730-4733.
    • (1982) Cancer Res , vol.42 , pp. 4730-4733
    • Tsuruo, T.1    Iida, H.2    Tsukagoshi, S.3    Sakurai, Y.4
  • 243
    • 0008632564 scopus 로고
    • Expression of a full-length cDNA for the human 'MDR1' (Pglycoprotein) gene confers multidrug resistance to colchicine, doxorubicin, and vinblastine
    • Ueda K, Cardarelli C, Gottesman MM and Pastan I (1987) Expression of a full-length cDNA for the human 'MDR1' (Pglycoprotein) gene confers multidrug resistance to colchicine, doxorubicin, and vinblastine. Proc Natl Acad Sci USA 84: 3004-3008.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3004-3008
    • Ueda, K.1    Cardarelli, C.2    Gottesman, M.M.3    Pastan, I.4
  • 244
    • 0026487058 scopus 로고
    • Human P-glycoprotein transports cortisol, aldosterone, and dexamethasone, but not progesterone
    • Ueda K, Okamura N, Hirai M, Tanigawara Y Saeki T, Kioka N, Komano T and Hori R (1992) Human P-glycoprotein transports cortisol, aldosterone, and dexamethasone, but not progesterone. J Biol Chem 267: 24248-24252.
    • (1992) J Biol Chem , vol.267 , pp. 24248-24252
    • Ueda, K.1    Okamura, N.2    Hirai, M.3    Saeki T, T.Y.4    Kioka, N.5    Komano, T.6    Hori, R.7
  • 245
    • 0028362501 scopus 로고
    • Character-ization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch IL, Al-Shawi MK and Senior AE (1994) Character-ization of the ATPase activity of purified Chinese hamster P-glycoprotein. Biochemistry 33: 7069-7076.
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Al-Shawi Mk, U.I.L.1    Senior, A.E.2
  • 246
    • 0028831929 scopus 로고
    • Effects of lipids on ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch IL and Senior AE (1995) Effects of lipids on ATPase activity of purified Chinese hamster P-glycoprotein. Arch Biochem Biophys 316: 135-140.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 135-140
    • Urbatsch, I.L.1    Senior, A.E.2
  • 247
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide binding sites are catalytically active
    • Urbatsch IL, Sankaran B, Bhagat S and Senior AE (1995) Both P-glycoprotein nucleotide binding sites are catalytically active. J Biol Chem 270: 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
  • 248
    • 0026536805 scopus 로고
    • Volume-regulated chloride channels associated with the human multidrug resistance P-glycoprotein
    • Valverde MA, Diáz M, Sepúlveda FV, Gill DR, Hyde SC and Higgins CF (1992) Volume-regulated chloride channels associated with the human multidrug resistance P-glycoprotein. Nature 355: 830-833.
    • (1992) Nature , vol.355 , pp. 830-833
    • Valverde, M.A.1    Diáz, M.2    Sepúlveda, F.V.3    Gill, D.R.4    Hyde, S.C.5    Higgins, C.F.6
  • 249
  • 250
  • 252
    • 0007544439 scopus 로고    scopus 로고
    • MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine
    • Van Helvoort A, Smith AJ, Sprong H, Fritzsche I, Schinkel AH, Borst P and van Meer G (1996) MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. Cell 87: 507-517.
    • (1996) Cell , vol.87 , pp. 507-517
    • Van Helvoort, A.1    Smith, A.J.2    Sprong, H.3    Fritzsche, I.4    Schinkel, A.H.5    Borst, P.6    Van Meer, G.7
  • 253
    • 0030988015 scopus 로고    scopus 로고
    • Biophysical aspects of P-glycoprotein-mediated multidrug resistance
    • Wadkins RM and Roepe PD (1997) Biophysical aspects of P-glycoprotein-mediated multidrug resistance. Int Rev Cytol 171: 121-165.
    • (1997) Int Rev Cytol , vol.171 , pp. 121-165
    • Wadkins, R.M.1    Roepe, P.D.2
  • 254
    • 0001607723 scopus 로고
    • Distantly related sequences in the a- And b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ and Gay NJ (1982) Distantly related sequences in the a- and b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1: 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
  • 255
    • 0025176784 scopus 로고
    • P-glycoproteins in pathology: The multidrug resistance gene family in humans
    • Weinstein RS, Kuszak JR, Kluskens LF and Coon JS (1990) P-glycoproteins in pathology: the multidrug resistance gene family in humans. Human Path 21: 34-48.
    • (1990) Human Path , vol.21 , pp. 34-48
    • Weinstein, R.S.1    Kuszak, J.R.2    Kluskens, L.F.3    Coon, J.S.4
  • 256
    • 0030450337 scopus 로고    scopus 로고
    • Cell-volume regulation: P-glycoprotein-a cautionary tale
    • Wine JJ and Luckie DB (1996) Cell-volume regulation: P-glycoprotein-a cautionary tale. Curr Biol 6: 1410-1412.
    • (1996) Curr Biol , vol.6 , pp. 1410-1412
    • Wine, J.J.1    Luckie, D.B.2
  • 257
    • 0024340307 scopus 로고
    • A volumesensitive chloride conductance in human colonie cell line T84
    • Worrel RT, Butt AG, Cliff WH and Frizzel RA (1989) A volumesensitive chloride conductance in human colonie cell line T84. Am J Physiol 256: C1111-C1119.
    • (1989) Am J Physiol , vol.256
    • Worrel, R.T.1    Butt, A.G.2    Cliff, W.H.3    Frizzel, R.A.4
  • 258
    • 0022366994 scopus 로고
    • Phospholipid and ether linked phospholipid content alter with cellular resistance to vinblastine
    • Wright LC, Dyne M, Holmes KT and Mountford CE (1985) Phospholipid and ether linked phospholipid content alter with cellular resistance to vinblastine. Biochem Biophys Res Commun 133: 539-545.
    • (1985) Biochem Biophys Res Commun , vol.133 , pp. 539-545
    • Wright, L.C.1    Dyne, M.2    Holmes, K.T.3    Mountford, C.E.4
  • 259
    • 0024501045 scopus 로고
    • Progesterone interacts with P-glycoprotein in multidrug resistant cells and in the endometrium of gravid uterus
    • Yang C-PH, DePinho SG, Greenberger LM, Arceci RJ and Horwitz SB (1989) Progesterone interacts with P-glycoprotein in multidrug resistant cells and in the endometrium of gravid uterus. J Biol Chem 264: 782-788.
    • (1989) J Biol Chem , vol.264 , pp. 782-788
    • Yang, C.-P.H.1    Depinho, S.G.2    Greenberger, L.M.3    Arceci, R.J.4    Horwitz, S.B.5
  • 260
    • 0029009668 scopus 로고
    • Involvement of phospholipase C in heat-shock-induced phosphorylation of P-glycoprotein in multidrug resistant human breast cancer cells
    • Yang JM, Chin KV and Hait WN (1995) Involvement of phospholipase C in heat-shock-induced phosphorylation of P-glycoprotein in multidrug resistant human breast cancer cells. Biochem Biophys Res Commun 210: 21-30.
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 21-30
    • Chin Kv, Y.J.M.1    Hait, W.N.2
  • 261
    • 0029683163 scopus 로고    scopus 로고
    • Interaction of P-glycoprotein with protein kinase C in human multidrug resistant carcinoma cells
    • Yang JM, Chin KV and Hait WN (1996) Interaction of P-glycoprotein with protein kinase C in human multidrug resistant carcinoma cells. Cancer Res 56: 3490-3494.
    • (1996) Cancer Res , vol.56 , pp. 3490-3494
    • Chin Kv, Y.J.M.1    Hait, W.N.2
  • 262
    • 0024441318 scopus 로고
    • Cytoplasmic orientation and two-domain structure of the multidrug transporter, P-glycoprotein, demonstrated with sequence-specific antibodies
    • Yoshimura A, Kuwazuru Y, Sumizawa T, Ichikawa M, Ikeda S, Ueda T and Akiyama S-I (1989) Cytoplasmic orientation and two-domain structure of the multidrug transporter, P-glycoprotein, demonstrated with sequence-specific antibodies. J BiolChem264: 16282-16291.
    • (1989) J BiolChem , vol.264 , pp. 16282-16291
    • Yoshimura, A.1    Kuwazuru, Y.2    Sumizawa, T.3    Ichikawa, M.4    Ikeda, S.5    Ueda, T.6    Akiyama, S.-I.7
  • 264
    • 0024421664 scopus 로고
    • Reversal mechanism of multidrug resistance by verapamil: Direct binding of verapamil to P-glycoprotein on specific sites and transport of verapamil outward across the plasma membrane of K562/ADM cells
    • Yusa K and Tsuruo T (1989) Reversal mechanism of multidrug resistance by verapamil: direct binding of verapamil to P-glycoprotein on specific sites and transport of verapamil outward across the plasma membrane of K562/ADM cells. Cancer Res 49: 5002-5006.
    • (1989) Cancer Res , vol.49 , pp. 5002-5006
    • Yusa, K.1    Tsuruo, T.2
  • 265
    • 0025951859 scopus 로고
    • Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation
    • Zhang J-T and Ling V (1991) Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation. J Biol Chem 266: 18224-18232.
    • (1991) J Biol Chem , vol.266 , pp. 18224-18232
    • Zhang, J.-T.1    Ling, V.2
  • 266
    • 0027284115 scopus 로고
    • Membrane topology of the N-terminal half of the hamster P-glycoprotein molecule
    • Zhang JT, Duthie M and Ling V (1993) Membrane topology of the N-terminal half of the hamster P-glycoprotein molecule. J Biol Chem 268: 15101-15110.
    • (1993) J Biol Chem , vol.268 , pp. 15101-15110
    • Duthie M, Z.J.T.1    Ling, V.2
  • 267
    • 0029116124 scopus 로고
    • Involvement of cytoplasmic factors regulating the membrane orientation of P-glycoprotein sequences
    • Zhang JT and Ling V (1995) Involvement of cytoplasmic factors regulating the membrane orientation of P-glycoprotein sequences. Biochemistry 34: 9159-9165.
    • (1995) Biochemistry , vol.34 , pp. 9159-9165
    • Zhang, J.T.1    Ling, V.2
  • 268
    • 0028938775 scopus 로고
    • Topological determinants of internal transmembrane segments in P-glycoprotein sequences
    • Zhang JT, Lee CH, Duthie M and Ling V (1995a) Topological determinants of internal transmembrane segments in P-glycoprotein sequences. J Biol Chem 270: 1742-1746.
    • (1995) J Biol Chem , vol.270 , pp. 1742-1746
    • Zhang, J.T.1    Ch, L.2    Duthie, M.3    Ling, V.4
  • 269
    • 0028901538 scopus 로고
    • Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by MDR1
    • Zhang X, Collins KI and Greenberger LM (1995b) Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by MDR1. J Biol Chem 270: 5441-5448.
    • (1995) J Biol Chem , vol.270 , pp. 5441-5448
    • Collins Ki, Z.X.1    Greenberger, L.M.2
  • 270
    • 0029744137 scopus 로고    scopus 로고
    • Topological folding and proteolysis profile of P-glycoprotein in membranes of multidrug-resistant cells: Implications for the drug- Transport mechanism
    • Zhang M, Wang G, Shapiro A and Zhang JT (1996) Topological folding and proteolysis profile of P-glycoprotein in membranes of multidrug-resistant cells: implications for the drug- transport mechanism. Biochemistry 35: 9728-9736.
    • (1996) Biochemistry , vol.35 , pp. 9728-9736
    • Zhang, M.1    Wang, G.2    Shapiro, A.3    Zhang, J.T.4
  • 271
    • 33847507772 scopus 로고    scopus 로고
    • Ursula A. Germann, Vertex Pharmaceuticals Incorporated, 130 Waverly Street, Cambridge, Massachusetts 02139-4242, U.S.A. Germann@macnet.vpharm.com
    • Ursula A. Germann, Vertex Pharmaceuticals Incorporated, 130 Waverly Street, Cambridge, Massachusetts 02139-4242, U.S.A. Germann@macnet.vpharm.com


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.