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Volumn 76, Issue 5, 1998, Pages 695-708

Spectroscopic and biophysical approaches for studying the structure and function of the P-glycoprotein multidrug transporter

Author keywords

Circular dichroism spectroscopy; Differential scanning calorimetry; Electron microscopy; Fluorescence spectroscopy; Infra red spectroscopy; Multidrug resistance; P glycoprotein

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMIDE; BEAUVERICIN; COLCHICINE; CYCLOSPORIN A; DAUNORUBICIN; DEXAMETHASONE; DOXORUBICIN; FLUPENTIXOL; GLYCOPROTEIN P; GRAMICIDIN D; LEUPEPTIN; NEW DRUG; NONACTIN; PACLITAXEL; PEPSTATIN; PROGESTERONE; QUINIDINE; RESERPINE; RHODAMINE 123; TOPOTECAN; TRIFLUOPERAZINE; TRITON X 100; VALINOMYCIN; VALSPODAR; VERAPAMIL; VINBLASTINE; VINCRISTINE;

EID: 0032461892     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o98-075     Document Type: Conference Paper
Times cited : (37)

References (71)
  • 1
    • 0028307625 scopus 로고
    • Covalent inhibitors of P-glycoprotein ATPase activity
    • al-Shawi, M.K., Urbatsch, I.L., and Senior, A.E. 1994. Covalent inhibitors of P-glycoprotein ATPase activity. J. Biol. Chem. 269: 8986-8992.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8986-8992
    • Al-Shawi, M.K.1    Urbatsch, I.L.2    Senior, A.E.3
  • 2
    • 0028059144 scopus 로고
    • Overexpression and purification of the carboxyl-terminal nucleotide-binding domain from mouse P-glycoprotein. Strategic location of a tryptophan residue
    • Baubichon-Cortay, H., Baggetto, L.G., Dayan, G., and Di Pietro, A. 1994. Overexpression and purification of the carboxyl-terminal nucleotide-binding domain from mouse P-glycoprotein. Strategic location of a tryptophan residue. 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
  • 3
    • 6844258858 scopus 로고    scopus 로고
    • Modeling of nucleotide binding domains of ABC transporter proteins based on a F1-ATPase/recA topology: Structural model of the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Biancet, M.A., Ko, Y.H., Amzel, L.M., and Pedersen, P.L. 1997. Modeling of nucleotide binding domains of ABC transporter proteins based on a F1-ATPase/recA topology: structural model of the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR). J. Bioenerg. Biomembr. 29: 503-524.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 503-524
    • Biancet, M.A.1    Ko, Y.H.2    Amzel, L.M.3    Pedersen, P.L.4
  • 4
    • 0030577119 scopus 로고    scopus 로고
    • P-glycoprotein multidrug resistance and cancer
    • Bosch, I., and Croop, J. 1996. P-glycoprotein multidrug resistance and cancer. Biochim. Biophys. Acta, 1288: F37-F54.
    • (1996) Biochim. Biophys. Acta , vol.1288
    • Bosch, I.1    Croop, J.2
  • 5
    • 0030921564 scopus 로고    scopus 로고
    • The functional purification of P-glycoprotein is dependent on maintenance of a lipid-protein interface
    • Callaghan, R., Berridge, G., Ferry, D.R., and Higgins, C.F. 1997. The functional purification of P-glycoprotein is dependent on maintenance of a lipid-protein interface. Biochim. Biophys. Acta, 1328: 109-124.
    • (1997) Biochim. Biophys. Acta , vol.1328 , pp. 109-124
    • Callaghan, R.1    Berridge, G.2    Ferry, D.R.3    Higgins, C.F.4
  • 6
    • 0021266066 scopus 로고
    • Lipid-protein interactions of the human erythrocyte concanavalin A receptor in phospholipid bilayers
    • Chicken, C.A., and Sharom, F.J. 1984. Lipid-protein interactions of the human erythrocyte concanavalin A receptor in phospholipid bilayers. Biochim. Biophys. Acta, 774: 110-118.
    • (1984) Biochim. Biophys. Acta , vol.774 , pp. 110-118
    • Chicken, C.A.1    Sharom, F.J.2
  • 7
    • 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, J.M., Cortay, J.C., 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
  • 8
    • 0030663804 scopus 로고    scopus 로고
    • Binding of steroid modulators to recombinant cytosolic domain from mouse P-glycoprotein in close proximity to the ATP site
    • Dayan,G., Jalt, J.M., Baubichon-Cortay, H., Baggetto, L.G., Renoir, J.M., Baulieu, E.E., Gros, P., and Di Pietro, A. 1997. Binding of steroid modulators to recombinant cytosolic domain from mouse P-glycoprotein in close proximity to the ATP site. Biochemistry, 36: 15208-15215.
    • (1997) Biochemistry , vol.36 , pp. 15208-15215
    • Dayan, G.1    Jalt, J.M.2    Baubichon-Cortay, H.3    Baggetto, L.G.4    Renoir, J.M.5    Baulieu, E.E.6    Gros, P.7    Di Pietro, A.8
  • 9
    • 0019217744 scopus 로고
    • Calculation on fluorescence resonance energy transfer on surfaces
    • Dewey,T.G., and Hammes, G.G. 1980. Calculation on fluorescence resonance energy transfer on surfaces. Biophys. J. 32: 1023-1035.
    • (1980) Biophys. J. , vol.32 , pp. 1023-1035
    • Dewey, T.G.1    Hammes, G.G.2
  • 11
    • 0030872676 scopus 로고    scopus 로고
    • Interaction of combinations of drugs, chemosensitizers, and peptides with the P-glycoprotein multidrug transporter
    • DiDiodto, G., and Sharom, F.J. 1997. Interaction of combinations of drugs, chemosensitizers, and peptides with the P-glycoprotein multidrug transporter. Biochem. Pharmacol. 53: 1789-1797.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1789-1797
    • DiDiodto, G.1    Sharom, F.J.2
  • 12
    • 0027458116 scopus 로고
    • ATP-dependent transport systems in bacteria and humans: Relevance to cystic fibrosis and multidrug resistance
    • Doige, C.A., and Ames, G.F. 1993. ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance. Annu. Rev. Microbiol. 47: 291-319.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 291-319
    • Doige, C.A.1    Ames, G.F.2
  • 13
    • 0026768856 scopus 로고
    • Transport properties of P-glycoprotein in plasma membrane vesicles from multidrug-resistant Chinese hamster ovary cells
    • Doige, C.A., and Sharom, F.J. 1992. Transport properties of P-glycoprotein in plasma membrane vesicles from multidrug-resistant Chinese hamster ovary cells. Biochim. Biophys. Acta, 1109: 161-171.
    • (1992) Biochim. Biophys. Acta , vol.1109 , pp. 161-171
    • Doige, C.A.1    Sharom, F.J.2
  • 14
    • 0026672405 scopus 로고
    • ATPase activity of partially purified P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Doige, C.A., Yu, X., and Sharom, F.J. 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
    • Doige, C.A.1    Yu, X.2    Sharom, F.J.3
  • 15
    • 0027509809 scopus 로고
    • The effects of lipids and detergents on ATPase-active P-glycoprotein
    • Doige, C.A., Yu, X., and Sharom, F.J. 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
    • Doige, C.A.1    Yu, X.2    Sharom, F.J.3
  • 16
    • 0029804316 scopus 로고    scopus 로고
    • Efficient purification and reconstitution of P-glycoprotein for functional and structural studies
    • Dong, M., Penin, F., and Baggetto, L.G. 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
    • Dong, M.1    Penin, F.2    Baggetto, L.G.3
  • 17
    • 0032574948 scopus 로고    scopus 로고
    • Secondary structure of P-glycoprotein investigated by circular dichroism and amino acid sequence analysis
    • Dong, M., Ladvière, L., Penin, F., Deléage, G., and Baggetto, L.G. 1998. Secondary structure of P-glycoprotein investigated by circular dichroism and amino acid sequence analysis. Biochim. Biophys. Acta, 1371: 317-334.
    • (1998) Biochim. Biophys. Acta , vol.1371 , pp. 317-334
    • Dong, M.1    Ladvière, L.2    Penin, F.3    Deléage, G.4    Baggetto, L.G.5
  • 18
    • 0028020549 scopus 로고
    • Transport of polypeptide ionophores into proteoliposomes reconstituted with rat liver P-glycoprotein
    • Eytan, G.D., Borgnia, M.J., 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
  • 19
    • 0030065776 scopus 로고    scopus 로고
    • Functional reconstitution of P-glycoprotein reveals an apparent near stoichiometric drug transport to ATP hydrolysis
    • Eytan, G.D., Regev, R., and Assaraf, Y.G. 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
    • Eytan, G.D.1    Regev, R.2    Assaraf, Y.G.3
  • 20
    • 0025062843 scopus 로고
    • Studies on the purified Na+,Mg(2+)-ATPase from Acholeplasma laidlawii B membranes: A differential scanning calorimetric study of the protein-phospholipid interactions
    • George, R., Lewis, R.N., and McElhaney, R.N. 1990. Studies on the purified Na+,Mg(2+)-ATPase from Acholeplasma laidlawii B membranes: a differential scanning calorimetric study of the protein-phospholipid interactions. Biochem. Cell Biol. 68: 161-168.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 161-168
    • George, R.1    Lewis, R.N.2    McElhaney, R.N.3
  • 21
    • 0025655675 scopus 로고
    • Multidrug resistance and chemosensitization: Therapeutic implications for cancer chemotherapy
    • Georges, E., Sharom, F.J., and Eing, V. 1990. Multidrug resistance and chemosensitization: therapeutic implications for cancer chemotherapy. Adv. Pharmacol. 21: 185-220.
    • (1990) Adv. Pharmacol. , vol.21 , pp. 185-220
    • Georges, E.1    Sharom, F.J.2    Eing, V.3
  • 22
    • 0029954843 scopus 로고    scopus 로고
    • P-glycoprotein: A mediator of multidrug resistance in tumour cells
    • Germann, U.A. 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
  • 23
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C.F. 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
  • 24
  • 26
    • 0032519693 scopus 로고    scopus 로고
    • A model for the nucleotide-binding domains of ABC transporters based on the large domain of aspartate aminotransferase
    • Hoedemaeker, F.J., Davidson, A.R., and Rose, D.R. 1998. A model for the nucleotide-binding domains of ABC transporters based on the large domain of aspartate aminotransferase. Proteins, 30: 275-286.
    • (1998) Proteins , vol.30 , pp. 275-286
    • Hoedemaeker, F.J.1    Davidson, A.R.2    Rose, D.R.3
  • 29
    • 0025784605 scopus 로고
    • Trinitrophenyl-ATP binding to the ArsA protein: The catalytic subunit of an anion pump
    • Karkaria, C.E., and Rosen, B.P. 1991. Trinitrophenyl-ATP binding to the ArsA protein: the catalytic subunit of an anion pump. Arch. Biochem. Biophys. 288: 107-111.
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 107-111
    • Karkaria, C.E.1    Rosen, B.P.2
  • 30
    • 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
  • 31
    • 0027524866 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator. Overexpression, purification, and characterization of wild type and delta F508 mutant forms of the first nucleotide binding fold in fusion with the maltose-binding protein
    • Ko, Y.H., Thomas, P.J., Delannoy, M.R., and Pedersen, P.L. 1993. The cystic fibrosis transmembrane conductance regulator. Overexpression, purification, and characterization of wild type and delta F508 mutant forms of the first nucleotide binding fold in fusion with the maltose-binding protein. J. Biol. Chem. 268: 24330-24338.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24330-24338
    • Ko, Y.H.1    Thomas, P.J.2    Delannoy, M.R.3    Pedersen, P.L.4
  • 32
    • 0018802935 scopus 로고
    • Intramembrane positions of membrane-bound chromophores determined by excitation energy transfer
    • Koppel, D.E., Fleming, P.J., and Strittmatter, P. 1979. Intramembrane positions of membrane-bound chromophores determined by excitation energy transfer. Biochemistry, 18: 5450-5457.
    • (1979) Biochemistry , vol.18 , pp. 5450-5457
    • Koppel, D.E.1    Fleming, P.J.2    Strittmatter, P.3
  • 33
    • 0032549583 scopus 로고    scopus 로고
    • Steric limitations in the interaction of the ATP binding domains of the ArsA ATPase
    • Li, J., and Rosen, B.P. 1998. Steric limitations in the interaction of the ATP binding domains of the ArsA ATPase. J. Biol. Chem. 273: 6796-6800.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6796-6800
    • Li, J.1    Rosen, B.P.2
  • 34
    • 0029817926 scopus 로고    scopus 로고
    • Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump
    • Li, J., Liu, S., and Rosen, B.P. 1996. Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump. J. Biol. Chem. 271: 25247-25252.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25247-25252
    • Li, J.1    Liu, S.2    Rosen, B.P.3
  • 35
    • 0029840320 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains
    • Liu, R., and Sharom, F.J. 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
  • 36
    • 0030973613 scopus 로고    scopus 로고
    • Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter
    • Liu, R., and Sharom, F.J. 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
  • 37
    • 0032485855 scopus 로고    scopus 로고
    • Proximity of the nucleotide binding domains of the P-glycoprotein multidrug transporter to the membrane surface: A resonance energy transfer study
    • Liu, R., and Sharom, F.J. 1998. Proximity of the nucleotide binding domains of the P-glycoprotein multidrug transporter to the membrane surface: a resonance energy transfer study. Biochemistry, 37: 6503-6512.
    • (1998) Biochemistry , vol.37 , pp. 6503-6512
    • Liu, R.1    Sharom, F.J.2
  • 38
    • 0028229881 scopus 로고
    • Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides
    • Loo, T.W., and Clarke, D.M. 1994. Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides. J. Biol. Chem. 269: 7750-7755.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7750-7755
    • Loo, T.W.1    Clarke, D.M.2
  • 39
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo, T.W., and Clarke, D.M. 1995a. Membrane topology of a cysteine-less 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
  • 40
    • 0029121417 scopus 로고
    • Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity
    • Loo, T.W., and Clarke, D.M. 1995b. Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity. J. Biol. Chem. 270: 22957-22961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22957-22961
    • Loo, T.W.1    Clarke, D.M.2
  • 41
    • 0029909604 scopus 로고    scopus 로고
    • Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates
    • Loo, T.W., and Clarke, D.M. 1996. Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates. J. Biol. Chem. 271: 27482-27487.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27482-27487
    • Loo, T.W.1    Clarke, D.M.2
  • 42
    • 0030779102 scopus 로고    scopus 로고
    • Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12
    • Loo, T.W., and Clarke, D.M. 1997a. Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12. J. Biol. Chem. 272: 20986-20989.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20986-20989
    • Loo, T.W.1    Clarke, D.M.2
  • 43
    • 0031434236 scopus 로고    scopus 로고
    • Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate
    • Loo, T.W., and Clarke, D.M. 1997b. Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate. J. Biol. Chem. 272: 31945-31948.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31945-31948
    • Loo, T.W.1    Clarke, D.M.2
  • 44
    • 0030848099 scopus 로고    scopus 로고
    • Purification of functional human P-glycoprotein expressed in Saccharomyces cerevisiae
    • Mao, Q., and Scarborough, G.A. 1997. Purification of functional human P-glycoprotein expressed in Saccharomyces cerevisiae. Biochim. Biophys. Acta, 1327: 107-118.
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 107-118
    • Mao, Q.1    Scarborough, G.A.2
  • 45
    • 0026053770 scopus 로고
    • Structural model of the nucleotide-binding conserved component of periplasmic permeases
    • Mimura, C.S., Holbrook, S.R., and Ames, G.F. 1991. Structural model of the nucleotide-binding conserved component of periplasmic permeases. Proc. Natl. Acad. Sci. U.S.A. 88: 84-88.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 84-88
    • Mimura, C.S.1    Holbrook, S.R.2    Ames, G.F.3
  • 46
    • 0029071996 scopus 로고
    • Preferential association of membrane phospholipids with the human erythrocyte hexose transporter
    • Naderi, S., Doyle, K., and Melchior, D.L. 1995. Preferential association of membrane phospholipids with the human erythrocyte hexose transporter. Biochim. Biophys. Acta, 1236: 10-14.
    • (1995) Biochim. Biophys. Acta , vol.1236 , pp. 10-14
    • Naderi, S.1    Doyle, K.2    Melchior, D.L.3
  • 47
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • Ramachandra, M., Ambudkar, S.V., Chen, D., Hrycyna, C.A., Dey, S., Gottesman, M.M., and Pastan, I. 1998. Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state. Biochemistry, 37: 5010-5019.
    • (1998) Biochemistry , vol.37 , pp. 5010-5019
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6    Pastan, I.7
  • 48
    • 0028923471 scopus 로고
    • Expression and functional properties of the second predicted nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator fused to glutathione-S-transferase
    • Randak, C., Roscher, A.A., Hadorn, H.B., Assfalg-Machleidt, I., Auerswald, E.A., and Machleidt, W. 1995. Expression and functional properties of the second predicted nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator fused to glutathione-S-transferase. FEBS Lett. 363: 189-194.
    • (1995) FEBS Lett. , vol.363 , pp. 189-194
    • Randak, C.1    Roscher, A.A.2    Hadorn, H.B.3    Assfalg-Machleidt, I.4    Auerswald, E.A.5    Machleidt, W.6
  • 49
    • 0030757153 scopus 로고    scopus 로고
    • Interaction of P-glycoprotein with defined phospholipid bilayers: A differential scanning calorimetric study
    • Romsicki, Y., and Sharom, F.J. 1997. Interaction of P-glycoprotein with defined phospholipid bilayers: a differential scanning calorimetric study. Biochemistry, 36: 9807-9815.
    • (1997) Biochemistry , vol.36 , pp. 9807-9815
    • Romsicki, Y.1    Sharom, F.J.2
  • 50
    • 0032529077 scopus 로고    scopus 로고
    • The ATPase and ATP binding functions of P-glycoprotein: Modulation by interaction with defined phospholipids
    • Romsicki, Y., and Sharom, F.J. 1998. The ATPase and ATP binding functions of P-glycoprotein: modulation by interaction with defined phospholipids. Eur. J. Biochem. 256: 170-178.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 170-178
    • Romsicki, Y.1    Sharom, F.J.2
  • 51
    • 0030971840 scopus 로고    scopus 로고
    • Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis
    • Rosenberg, M.F., Callaghan, R., Ford, R.C., and Higgins, C.F. 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
  • 52
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mdr2 gene
    • Ruetz, S., and Gros, P. 1994. Phosphatidylcholine 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
  • 53
    • 0025051429 scopus 로고
    • Molecular basis of preferential resistance to colchicine in multidrug-resistant human cells conferred by Gly-185 to Val-185 substitution in P-glycoprotein
    • Safa, A.R., Stern, R.K., Choi, K., Agresti, M., Tamai, I., Mehta, N.D., and Roninson, I.B. 1990. Molecular basis of preferential resistance to colchicine in multidrug-resistant human cells conferred by Gly-185 to Val-185 substitution in P-glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 87: 7225-7229.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 54
    • 0031156388 scopus 로고    scopus 로고
    • ATP hydrolysis cycles and mechanism in P-glycoprotein and CFTR
    • Senior, A.E., and Gadsby, D.C. 1997. ATP hydrolysis cycles and mechanism in P-glycoprotein and CFTR. Semin. Cancer Biol. 8: 143-150.
    • (1997) Semin. Cancer Biol. , vol.8 , pp. 143-150
    • Senior, A.E.1    Gadsby, D.C.2
  • 55
  • 56
    • 0028940488 scopus 로고
    • ATP hydrolysis by multidrug-resistance protein from Chinese hamster ovary cells
    • Senior, A.E., al-Shawi, M.K., and Urbatsch, I.L. 1995b. ATP hydrolysis by multidrug-resistance protein from Chinese hamster ovary cells. J. Bioenerg. Biomembr. 27: 31-36.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 31-36
    • Senior, A.E.1    Al-Shawi, M.K.2    Urbatsch, I.L.3
  • 57
    • 0027937143 scopus 로고
    • ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells
    • Shapiro, A.B., 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
  • 58
    • 0029061103 scopus 로고
    • Reconstitution of drug transport by purified P-glycoprotein
    • Shapiro, A.B., 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
  • 59
    • 0030782511 scopus 로고    scopus 로고
    • Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities
    • Shapiro, A.B., and Ling, V. 1997. Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities. Eur. J. Biochem. 250: 130-137.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 130-137
    • Shapiro, A.B.1    Ling, V.2
  • 60
    • 0029041911 scopus 로고
    • Cloning, overexpression, purification, and characterization of the carboxyl-terminal nucleotide binding domain of P-glycoprotein
    • Sharma, S., and Rose, D.R. 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.R.2
  • 61
    • 0031455482 scopus 로고    scopus 로고
    • The P-glycoprotein efflux pump: How does it transport drugs?
    • Sharom, F.J. 1997a. The P-glycoprotein efflux pump: how does it transport drugs? J. Membr. Biol. 160: 161-175.
    • (1997) J. Membr. Biol. , vol.160 , pp. 161-175
    • Sharom, F.J.1
  • 62
    • 0030869122 scopus 로고    scopus 로고
    • The P-glycoprotein multidrug transporter: Interactions with membrane lipids, and their modulation of activity
    • Sharom, F.J. 1997b. The P-glycoprotein multidrug transporter: interactions with membrane lipids, and their modulation of activity. Biochem. Soc. Trans. 25: 1088-1096.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 1088-1096
    • Sharom, F.J.1
  • 63
    • 0027482461 scopus 로고
    • Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein
    • Sharom, F.J., Yu, X., and Doige, C.A. 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
    • Sharom, F.J.1    Yu, X.2    Doige, C.A.3
  • 64
    • 0028920219 scopus 로고
    • Interaction of the P-glycoprotein multidrug transporter with peptides and ionophores
    • Sharom, F.J., DiDiodato, G., Yu, X., and Ashbourne, K.J. 1995a. Interaction of the P-glycoprotein multidrug transporter with peptides and ionophores. J. Biol. Chem. 270: 10334-10341.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10334-10341
    • Sharom, F.J.1    DiDiodato, G.2    Yu, X.3    Ashbourne, K.J.4
  • 65
    • 0029027674 scopus 로고
    • Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Sharom, F.J., Yu, X., Chu, J.W.K., and Doige, C.A. 1995b. Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochem. J. 308: 381-390.
    • (1995) Biochem. J. , vol.308 , pp. 381-390
    • Sharom, F.J.1    Yu, X.2    Chu, J.W.K.3    Doige, C.A.4
  • 66
    • 0029987548 scopus 로고    scopus 로고
    • Synthetic hydrophobic peptides are substrates for P-glycoprotein and stimulate drug transport
    • Sharom, F.J., Yu, X., DiDiodato, G., and Chu, J.W.K. 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.K.4
  • 67
    • 0032144087 scopus 로고    scopus 로고
    • Linear and cyclic peptides as substrates and modulators of P-glycoprotein: Peptide binding and effects on drug transport and accumulation
    • Sharom, F.J., Lu, P., Liu, R., and Yu, X. 1998. Linear and cyclic peptides as substrates and modulators of P-glycoprotein: peptide binding and effects on drug transport and accumulation. Biochem. J. 333: 621-630.
    • (1998) Biochem. J. , vol.333 , pp. 621-630
    • Sharom, F.J.1    Lu, P.2    Liu, R.3    Yu, X.4
  • 68
    • 0033567425 scopus 로고    scopus 로고
    • Interaction of the P-glycoprotein multidrug transporter (MDR1) with high affinity peptide chemosensitizers in isolated membranes, reconstituted systems and intact cells
    • In press
    • Sharom, F.J., Yu, X., Lu, P., Liu, R., Chu, J.W.K, Szabó, K., Müller, M., Hose, C.D., Monks, A., Váradi, A., Sepródi, di, J., and Sarkadi, B. 1999. Interaction of the P-glycoprotein multidrug transporter (MDR1) with high affinity peptide chemosensitizers in isolated membranes, reconstituted systems and intact cells. Biochem. Pharmacol. In press.
    • (1999) Biochem. Pharmacol.
    • Sharom, F.J.1    Yu, X.2    Lu, P.3    Liu, R.4    Chu, J.W.K.5    Szabó, K.6    Müller, M.7    Hose, C.D.8    Monks, A.9    Váradi, A.10    Di Sepródi, J.11    Sarkadi, B.12
  • 69
    • 0029784872 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis
    • Sonveaux, N., Shapiro, A.B., Goormaghtigh, E., Ling, V., and Ruysschaert, J.M. 1996. Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis. J. Biol. Chem. 271: 24617-24624.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24617-24624
    • Sonveaux, N.1    Shapiro, A.B.2    Goormaghtigh, E.3    Ling, V.4    Ruysschaert, J.M.5
  • 70
    • 0028362501 scopus 로고
    • Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch, I.L., al-Shawi, M.K., and Senior, A.E. 1994. Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein. Biochemistry, 33: 7069-7076.
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Urbatsch, I.L.1    Al-Shawi, M.K.2    Senior, A.E.3
  • 71
    • 0032584289 scopus 로고    scopus 로고
    • Mutations in either nucleotide-binding site of P-glycoprotein (mdr3) prevent vanadate trapping of nucleotide at both sites
    • Urbatsch, I.L., Beaudet, L., Carrier, I., and Gros, P. 1998. Mutations in either nucleotide-binding site of P-glycoprotein (mdr3) prevent vanadate trapping of nucleotide at both sites. Biochemistry, 37: 4592-4602.
    • (1998) Biochemistry , vol.37 , pp. 4592-4602
    • Urbatsch, I.L.1    Beaudet, L.2    Carrier, I.3    Gros, P.4


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