메뉴 건너뛰기




Volumn 9, Issue 1, 2008, Pages 105-127

ABC multidrug transporters: Structure, function and role in chemoresistance

Author keywords

ABC superfamily; ABCG2 (BCRP); ATP hydrolysis; Drug efflux; Drug therapy; MRP1 ABCC1; Multidrug resistance; P glycoproteinMDR1 ABCB1; Polymorphisms; Transport mechanism

Indexed keywords

ABC TRANSPORTER; ABC TRANSPORTER C1; ANALGESIC AGENT; ANTHRACYCLINE DERIVATIVE; ANTIHISTAMINIC AGENT; BIRICODAR; BREAST CANCER RESISTANCE PROTEIN; CARDIAC GLYCOSIDE; CARRIER PROTEIN; CISPLATIN; DIGOXIN; DISULFIRAM; ELACRIDAR; FUMITREMORGIN C; GEFITINIB; GLYCOPROTEIN P; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; IMATINIB; IMMUNOMODULATING AGENT; LEUKOTRIENE RECEPTOR BLOCKING AGENT; MITOXANTRONE; MULTIDRUG RESISTANCE PROTEIN 1; PACLITAXEL; PROTEINASE INHIBITOR; TACROLIMUS; TARIQUIDAR; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALSPODAR; VINCA ALKALOID; ZOSUQUIDAR; DRUG;

EID: 40949121607     PISSN: 14622416     EISSN: 17448042     Source Type: Journal    
DOI: 10.2217/14622416.9.1.105     Document Type: Review
Times cited : (846)

References (187)
  • 1
    • 0035014565 scopus 로고    scopus 로고
    • The ABC of ABCs: A phylogenetic and functional classification of ABC systems in living organisms
    • Dassa E, Bouige P: The ABC of ABCs: a phylogenetic and functional classification of ABC systems in living organisms. Res. Microbiol. 152, 211-229 (2001).
    • (2001) Res. Microbiol , vol.152 , pp. 211-229
    • Dassa, E.1    Bouige, P.2
  • 2
    • 0034917716 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • Dean M, Rzhetsky A, Allikmets R: The human ATP-binding cassette (ABC) transporter superfamily. Genome Res. 11, 1156-1166 (2001).
    • (2001) Genome Res , vol.11 , pp. 1156-1166
    • Dean, M.1    Rzhetsky, A.2    Allikmets, R.3
  • 3
    • 4444266487 scopus 로고    scopus 로고
    • The ABC transporter gene family of Caenorhabditis elegans has implications for the evolutionary dynamics of multidrug resistance in eukaryotes
    • Sheps JA, Ralph S, Zhao Z, Baillie DL, Ling V: The ABC transporter gene family of Caenorhabditis elegans has implications for the evolutionary dynamics of multidrug resistance in eukaryotes. Genome Biol. 5, R15 (2004).
    • (2004) Genome Biol , vol.5
    • Sheps, J.A.1    Ralph, S.2    Zhao, Z.3    Baillie, D.L.4    Ling, V.5
  • 4
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst P, Oude Elferink RP: Mammalian ABC transporters in health and disease. Annu. Rev. Biochem. 71, 537-592 (2002).
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 537-592
    • Borst, P.1    Oude Elferink, R.P.2
  • 5
    • 0037457802 scopus 로고    scopus 로고
    • Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: An overview
    • Schinkel AH, Jonker JW: Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: an overview. Adv. Drug Deliv. Rev. 55, 3-29 (2003).
    • (2003) Adv. Drug Deliv. Rev , vol.55 , pp. 3-29
    • Schinkel, A.H.1    Jonker, J.W.2
  • 6
    • 31844444140 scopus 로고    scopus 로고
    • The molecular basis of multidrug resistance in cancer: The early years of P-glycoprotein research
    • Gottesman MM, Ling V: The molecular basis of multidrug resistance in cancer: the early years of P-glycoprotein research. FEBS Lett. 580, 998-1009 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 998-1009
    • Gottesman, M.M.1    Ling, V.2
  • 7
    • 33745699234 scopus 로고    scopus 로고
    • Membrane transporters and channels in chemoresistaice and - sensitivity of tumor cells
    • Huang Y, Sadee W: Membrane transporters and channels in chemoresistaice and - sensitivity of tumor cells. Cancer Lett. 239, 168-182 (2006).
    • (2006) Cancer Lett , vol.239 , pp. 168-182
    • Huang, Y.1    Sadee, W.2
  • 8
    • 0034947674 scopus 로고    scopus 로고
    • From MDR to MXR: New understanding of multidrug resistance systems, their properties and clinical significance
    • Litman T, Druley TE, Stein WD, Bates SE: From MDR to MXR: new understanding of multidrug resistance systems, their properties and clinical significance. Cell. Mol. Life Sci. 58, 931-959 (2001).
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 931-959
    • Litman, T.1    Druley, T.E.2    Stein, W.D.3    Bates, S.E.4
  • 9
    • 0034789387 scopus 로고    scopus 로고
    • Functional characterization of the human multidrug transporter, ABCG2, expressed in insect cells
    • Özvegy C, Litman T, Szakács G et al.: Functional characterization of the human multidrug transporter, ABCG2, expressed in insect cells. Biochem. Biophys Res. Commun. 285, 111-117 (2001).
    • (2001) Biochem. Biophys Res. Commun , vol.285 , pp. 111-117
    • Özvegy, C.1    Litman, T.2    Szakács, G.3
  • 10
    • 0030977145 scopus 로고    scopus 로고
    • Phosphatidylcholine and phosphatidylethanolamine behave as substrates of the human MDR1 P-glycoprotein
    • Bosch I, Dunussi-Joannopoulos K, Wu RL, Furlong ST, Croop J: Phosphatidylcholine and phosphatidylethanolamine behave as substrates of the human MDR1 P-glycoprotein. Biochemistry 36, 5685-5694 (1997).
    • (1997) Biochemistry , vol.36 , pp. 5685-5694
    • Bosch, I.1    Dunussi-Joannopoulos, K.2    Wu, R.L.3    Furlong, S.T.4    Croop, J.5
  • 11
    • 0035849506 scopus 로고    scopus 로고
    • Phospholipid flippase activity of the reconstituted P-glycoprotein multidrug transporter
    • Romsicki Y, Sharom FJ: Phospholipid flippase activity of the reconstituted P-glycoprotein multidrug transporter. Biochemisay, 40, 6937-6947 (2001).
    • (2001) Biochemisay , vol.40 , pp. 6937-6947
    • Romsicki, Y.1    Sharom, F.J.2
  • 12
    • 22544457473 scopus 로고    scopus 로고
    • The reconstituted P-glycoprotein multidrug transporter is a flippase for glucosylceramide and other simple glycosphingolipids
    • Eckford PD, Sharom FJ: The reconstituted P-glycoprotein multidrug transporter is a flippase for glucosylceramide and other simple glycosphingolipids. Biochem. J. 389, 517-526 (2005).
    • (2005) Biochem. J , vol.389 , pp. 517-526
    • Eckford, P.D.1    Sharom, F.J.2
  • 13
    • 0032709624 scopus 로고    scopus 로고
    • Secretion of platelet-activating factor is mediated by MDR1 P-glycoprotein in cultured human mesangial cells
    • Ernest S, Bello-Reuss E: Secretion of platelet-activating factor is mediated by MDR1 P-glycoprotein in cultured human mesangial cells. J. Am. Soc. Nephrol. 10, 2306-2313 (1999).
    • (1999) J. Am. Soc. Nephrol , vol.10 , pp. 2306-2313
    • Ernest, S.1    Bello-Reuss, E.2
  • 14
    • 33947401100 scopus 로고    scopus 로고
    • P-glycoprotein (ABCB1) interacts directly with lipid-based anti-cancer drugs and platelet-activating factors
    • Eckford PD, Sharom FJ: P-glycoprotein (ABCB1) interacts directly with lipid-based anti-cancer drugs and platelet-activating factors. Biochem. Cell Biol. 84, 1022-1033 (2006).
    • (2006) Biochem. Cell Biol , vol.84 , pp. 1022-1033
    • Eckford, P.D.1    Sharom, F.J.2
  • 15
    • 0033946019 scopus 로고    scopus 로고
    • Role of multidrug resistance P-glycoprotein in the secretion of aldosterone by human adrenal NCI-H295 cells
    • Bello-Reuss E, Ernest S, Holland OB, Hellmich MR: Role of multidrug resistance P-glycoprotein in the secretion of aldosterone by human adrenal NCI-H295 cells. Am. J. Physiol. Cell Physiol. 278, C1256-C1265 (2000).
    • (2000) Am. J. Physiol. Cell Physiol , vol.278
    • Bello-Reuss, E.1    Ernest, S.2    Holland, O.B.3    Hellmich, M.R.4
  • 16
    • 0029905171 scopus 로고    scopus 로고
    • MDR1 substrates/modulators protect against β-estradiol-17β-D-glucuronide cholestasis in rat liver
    • Liu Y, Huang L, Hoffman T, Gosland M, Vore M: MDR1 substrates/modulators protect against β-estradiol-17β-D-glucuronide cholestasis in rat liver. Cancer Res. 56, 4992-4997 (1996).
    • (1996) Cancer Res , vol.56 , pp. 4992-4997
    • Liu, Y.1    Huang, L.2    Hoffman, T.3    Gosland, M.4    Vore, M.5
  • 17
    • 0035112889 scopus 로고    scopus 로고
    • β-amyloid efflux mediated by p-glycoprotein
    • Lam FC, Liu R, Lu P et al.: β-amyloid efflux mediated by p-glycoprotein. J. Neurochem. 76, 1121-1128 (2001).
    • (2001) J. Neurochem , vol.76 , pp. 1121-1128
    • Lam, F.C.1    Liu, R.2    Lu, P.3
  • 18
    • 34548100791 scopus 로고    scopus 로고
    • Involvement of P-glycoprotein in the release of cytokines from peripheral blood mononuclear cells treated with methotrexate arid dexamethasone
    • Pawlik A, Baskiewicz-Masiuk M, Machalinski B, Safranow K, Gawronska-Szklarz B: Involvement of P-glycoprotein in the release of cytokines from peripheral blood mononuclear cells treated with methotrexate arid dexamethasone. J. Pharm. Pharmacol. 57, 1421-1425 (2005).
    • (2005) J. Pharm. Pharmacol , vol.57 , pp. 1421-1425
    • Pawlik, A.1    Baskiewicz-Masiuk, M.2    Machalinski, B.3    Safranow, K.4    Gawronska-Szklarz, B.5
  • 19
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mdr2 gene
    • Ruetz S, Gros P: Phosphatidylcholine translocase: a physiological role for the mdr2 gene. Cell 77, 1071-1081 (1994).
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 20
    • 0034604707 scopus 로고    scopus 로고
    • MDR3 P-glycoprotein, a phosphatidylcholine translocase, transports several cytotoxic drugs and directly interacts with drugs as judged by interference with nucleotide trapping
    • Smith AJ, van Helvoort A, van Meer G et al.: MDR3 P-glycoprotein, a phosphatidylcholine translocase, transports several cytotoxic drugs and directly interacts with drugs as judged by interference with nucleotide trapping. J. Biol. Chem. 275, 23530-23539 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 23530-23539
    • Smith, A.J.1    van Helvoort, A.2    van Meer, G.3
  • 21
    • 33846703691 scopus 로고    scopus 로고
    • Portrait of multifaceted transporter, the multidrug resistance-associated protein 1 (MRP1/ABCC1)
    • Bakos E, Homolya L: Portrait of multifaceted transporter, the multidrug resistance-associated protein 1 (MRP1/ABCC1). Pflugers Arch. Eur. J. Physiol. 453, 621-641 (2007).
    • (2007) Pflugers Arch. Eur. J. Physiol , vol.453 , pp. 621-641
    • Bakos, E.1    Homolya, L.2
  • 22
    • 0027960078 scopus 로고
    • Pharmacological characterization of multidrug resistant MRP-transfected human tumor cells
    • Cole SP, Sparks KE, Fraser K et al.: Pharmacological characterization of multidrug resistant MRP-transfected human tumor cells. Cancer Res. 54, 5902-5910 (1994).
    • (1994) Cancer Res , vol.54 , pp. 5902-5910
    • Cole, S.P.1    Sparks, K.E.2    Fraser, K.3
  • 23
    • 28244485775 scopus 로고    scopus 로고
    • Pharmacogenomics of the human ABC transporter ABCG2: From functional evaluation to drug molecular design
    • Ishikawa T, Tamura A, Saito H, Wakabayashi K, Nakagawa H: Pharmacogenomics of the human ABC transporter ABCG2: from functional evaluation to drug molecular design. Naturwissenschaften 92, 451-463 (2005).
    • (2005) Naturwissenschaften , vol.92 , pp. 451-463
    • Ishikawa, T.1    Tamura, A.2    Saito, H.3    Wakabayashi, K.4    Nakagawa, H.5
  • 24
    • 13444288036 scopus 로고    scopus 로고
    • Breast cancer resistance protein (BCRP/ABCG2)
    • Staud F, Pavek P: Breast cancer resistance protein (BCRP/ABCG2). Int. J. Biochem. Cell Biol. 37, 720-725 (2005).
    • (2005) Int. J. Biochem. Cell Biol , vol.37 , pp. 720-725
    • Staud, F.1    Pavek, P.2
  • 25
    • 0242331085 scopus 로고    scopus 로고
    • Multidrug resistance reversal agents
    • Robert J, Jarry C: Multidrug resistance reversal agents. J Med. Chem. 46, 4805-4817 (2003).
    • (2003) J Med. Chem , vol.46 , pp. 4805-4817
    • Robert, J.1    Jarry, C.2
  • 26
    • 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, Jault JM, Baubichon-Cortay H et al.: Binding of steroid modulators to recombinant cytosolic domain from mouse P-glycoprotein in close proximity to the ATP site. Biochemistry 36, 15208-15215 (1997).
    • (1997) Biochemistry , vol.36 , pp. 15208-15215
    • Dayan, G.1    Jault, J.M.2    Baubichon-Cortay, H.3
  • 27
  • 28
    • 1342308328 scopus 로고    scopus 로고
    • The molecular basis of the action of disulfiram as a modulator of the multidrug resistance-linked ATP binding cassette transporters MDR1 (ABCB1) and MRP1 (ABCC1)
    • Sauna ZE, Peng XH, Nandigama K. Tekle S, Ambudkar SV: The molecular basis of the action of disulfiram as a modulator of the multidrug resistance-linked ATP binding cassette transporters MDR1 (ABCB1) and MRP1 (ABCC1). Mol. Pharmacol. 65, 675-684 (2004).
    • (2004) Mol. Pharmacol , vol.65 , pp. 675-684
    • Sauna, Z.E.1    Peng, X.H.2    Nandigama, K.3    Tekle, S.4    Ambudkar, S.V.5
  • 29
    • 17544368685 scopus 로고    scopus 로고
    • Multidrug resistance proteins: Role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense
    • Leslie EM, Deeley RG, Cole SPC: Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense. Toxical. Appl. Pharmacol. 204, 216-237 (2005).
    • (2005) Toxical. Appl. Pharmacol , vol.204 , pp. 216-237
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.C.3
  • 30
    • 0028229150 scopus 로고
    • Disruption of the mouse mdr1a P-glycoprotein gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs
    • Schinkel AH, Smit JJ, van Tellingen O et al.: Disruption of the mouse mdr1a P-glycoprotein gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs. Cell 77, 491-502 (1994).
    • (1994) Cell , vol.77 , pp. 491-502
    • Schinkel, A.H.1    Smit, J.J.2    van Tellingen, O.3
  • 31
    • 0029945113 scopus 로고    scopus 로고
    • What have we learnt thus far from mice with disrupted P-glycoprotein genes?
    • Borst P, Schinkel AH: What have we learnt thus far from mice with disrupted P-glycoprotein genes? Eur. J. Cancer 32A. 985-990 (1996).
    • (1996) Eur. J. Cancer , vol.32 A , pp. 985-990
    • Borst, P.1    Schinkel, A.H.2
  • 32
    • 0032494133 scopus 로고    scopus 로고
    • Multidrug resistance protein 1 protects the oropharyngeal mucosal layer and the testicular tubules against drug-induced damage
    • Wijnholds J, Scheffer GL, van der Valk M et al.: Multidrug resistance protein 1 protects the oropharyngeal mucosal layer and the testicular tubules against drug-induced damage. J. Exp. Med. 188, 797-808 (1998).
    • (1998) J. Exp. Med , vol.188 , pp. 797-808
    • Wijnholds, J.1    Scheffer, G.L.2    van der Valk, M.3
  • 33
    • 0037125973 scopus 로고    scopus 로고
    • Bcrp1 gene expression is required for normal numbers of side population stem cells in mice, and confers relative protection to mitoxantrone in hematopoietic cells in vivo
    • Zhou S, Morris JJ, Barnes YX, Lan L, Schuetz JD, Sorrentino BP: Bcrp1 gene expression is required for normal numbers of side population stem cells in mice, and confers relative protection to mitoxantrone in hematopoietic cells in vivo. Proc. Natl Acad. Sci. USA 99, 12339-12344 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12339-12344
    • Zhou, S.1    Morris, J.J.2    Barnes, Y.X.3    Lan, L.4    Schuetz, J.D.5    Sorrentino, B.P.6
  • 34
    • 19944425121 scopus 로고    scopus 로고
    • The impact of P-glycoprotein on the disposition of drugs targeted for indications of the central nervous system: Evaluation using the MDR1A/1B knockout mouse model
    • Doran A. Obach RS, Smith BJ et al.: The impact of P-glycoprotein on the disposition of drugs targeted for indications of the central nervous system: evaluation using the MDR1A/1B knockout mouse model. Drug Metab. Dispos. 33, 165-174 (2005).
    • (2005) Drug Metab. Dispos , vol.33 , pp. 165-174
    • Doran, A.1    Obach, R.S.2    Smith, B.J.3
  • 35
    • 3242785620 scopus 로고    scopus 로고
    • Importance of P-glycoprotein at blood-tissue barriers
    • Fromm MF: Importance of P-glycoprotein at blood-tissue barriers. Trends Pharmacol. Sci. 25, 423-429 (2004).
    • (2004) Trends Pharmacol. Sci , vol.25 , pp. 423-429
    • Fromm, M.F.1
  • 36
    • 0344440967 scopus 로고    scopus 로고
    • P-glycoprotein and Mrp1 collectively protect the bone marrow from vincristine-induced toxicity in vivo
    • van Tellingen O, Buckle T, Jonker JW, van der Valk MA, Begnen JH: P-glycoprotein and Mrp1 collectively protect the bone marrow from vincristine-induced toxicity in vivo. Br. J. Cancer 89, 1776-1782 (2003).
    • (2003) Br. J. Cancer , vol.89 , pp. 1776-1782
    • van Tellingen, O.1    Buckle, T.2    Jonker, J.W.3    van der Valk, M.A.4    Begnen, J.H.5
  • 37
    • 14644409841 scopus 로고    scopus 로고
    • The breast cancer resistance protein BCRP (ABCG2) concentrates drugs and carcinogenic xenotoxins into milk
    • Jonker JW, Merino G, Musters S et al.: The breast cancer resistance protein BCRP (ABCG2) concentrates drugs and carcinogenic xenotoxins into milk. Nat. Med. 11, 127-129 (2005).
    • (2005) Nat. Med , vol.11 , pp. 127-129
    • Jonker, J.W.1    Merino, G.2    Musters, S.3
  • 38
    • 33846903263 scopus 로고    scopus 로고
    • Multidrug transporter ABCG2/breast cancer resistance protein secretes riboflavin (vitamin B-2) into milk
    • van Herwaarden AE, Wagenaar E, Merino G et al.: Multidrug transporter ABCG2/breast cancer resistance protein secretes riboflavin (vitamin B-2) into milk. Mol. Cell. Biol. 27, 1247-1253 (2007).
    • (2007) Mol. Cell. Biol , vol.27 , pp. 1247-1253
    • van Herwaarden, A.E.1    Wagenaar, E.2    Merino, G.3
  • 39
    • 0037180446 scopus 로고    scopus 로고
    • The breast cancer resistance protein protects against a major chlorophyll-derived dietary phototoxin and protoporphyria
    • Jonker JW, Buitelaar M, Wagenaar E et al.: The breast cancer resistance protein protects against a major chlorophyll-derived dietary phototoxin and protoporphyria. Proc. Natl Acad. Sci. USA 99, 15649-15654 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 15649-15654
    • Jonker, J.W.1    Buitelaar, M.2    Wagenaar, E.3
  • 40
    • 2642526992 scopus 로고    scopus 로고
    • The stem cell marker Bcrp/ABCG2 enhances hypoxic cell survival through interactions with heme
    • Krishnamurthy P, Ross DD, Nakanishi T et al.: The stem cell marker Bcrp/ABCG2 enhances hypoxic cell survival through interactions with heme. J. Biol. Chem. 279, 24218-24225 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 24218-24225
    • Krishnamurthy, P.1    Ross, D.D.2    Nakanishi, T.3
  • 41
    • 31844452412 scopus 로고    scopus 로고
    • Insight in eukaryotic ABC transporter function by mutation analysis
    • Frelet A, Klein M: Insight in eukaryotic ABC transporter function by mutation analysis. FEBS Lett. 580, 1064-1084 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 1064-1084
    • Frelet, A.1    Klein, M.2
  • 42
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher KP, Lee AT, Rees DC: The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296, 1091-1098 (2002).
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 43
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner KP, Karcher A, Shin DS et al.: Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101, 789-800 (2000).
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3
  • 44
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith PC, Karpowich N, Millen L et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3
  • 45
    • 31844434196 scopus 로고    scopus 로고
    • Molecular insights into the mechanism of ATP-hydrolysis by the NBD of the ABC-transporter HlyB
    • Hanekop N, Zaitseva J, Jenewein S, Holland IB, Schmitt L: Molecular insights into the mechanism of ATP-hydrolysis by the NBD of the ABC-transporter HlyB. FEBS Lett. 580, 1036-1041 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 1036-1041
    • Hanekop, N.1    Zaitseva, J.2    Jenewein, S.3    Holland, I.B.4    Schmitt, L.5
  • 46
    • 0030973613 scopus 로고    scopus 로고
    • Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter
    • Liu R. Sharom FJ: Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter. Biochemistry 36, 2836-2843 (1997).
    • (1997) Biochemistry , vol.36 , pp. 2836-2843
    • Liu, R.1    Sharom, F.J.2
  • 47
    • 0033520934 scopus 로고    scopus 로고
    • Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins
    • Lerner-Marmarosh N. Omi K, Urbatsch IL, Gros P, Benior AE: Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type, Walker A, and Walker B mutant proteins. J. Biol. Chem. 274, 34711-34718 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 34711-34718
    • Lerner-Marmarosh, N.1    Omi, K.2    Urbatsch, I.L.3    Gros, P.4    Benior, A.E.5
  • 48
    • 0029027674 scopus 로고
    • Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Sharom FJ, Yu X, Chu JWK, Doige CA: Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochem. J. 308, 381-390 (1995).
    • (1995) Biochem. J , vol.308 , pp. 381-390
    • Sharom, F.J.1    Yu, X.2    Chu, J.W.K.3    Doige, C.A.4
  • 49
    • 0028362501 scopus 로고
    • Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch IL, al-Shawi MK, Senior AE: Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein. Biochemistry 33, 7069-7076 (1994).
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Urbatsch, I.L.1    al-Shawi, M.K.2    Senior, A.E.3
  • 50
    • 0033370596 scopus 로고    scopus 로고
    • ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells
    • Mao QC, Leslie EM, Deeley RG, Cole SPC: ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells. Biochim. Biopbys. Acta 1461, 69-82 (1999).
    • (1999) Biochim. Biopbys. Acta , vol.1461 , pp. 69-82
    • Mao, Q.C.1    Leslie, E.M.2    Deeley, R.G.3    Cole, S.P.C.4
  • 51
    • 0026672405 scopus 로고
    • ATPase activity of partially purified P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Doige CA, Yu X, Sharom FJ: ATPase activity of partially purified P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochim. Biophys. Acta 1109, 149-160 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1109 , pp. 149-160
    • Doige, C.A.1    Yu, X.2    Sharom, F.J.3
  • 52
    • 0031039693 scopus 로고    scopus 로고
    • Garrigos M, Mir LM. Orlowski S: 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).
    • Garrigos M, Mir LM. Orlowski S: 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).
  • 53
    • 0030743356 scopus 로고    scopus 로고
    • Competitive, non-competitive and cooperative interactions between substrates of P-glycoprotein as measured by its ATPase activity
    • Litman T, Zeuthen T, Skovsgaard T, Stein WD: Competitive, non-competitive and cooperative interactions between substrates of P-glycoprotein as measured by its ATPase activity. Biochim. Biophys. Acta 1361, 169-176 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1361 , pp. 169-176
    • Litman, T.1    Zeuthen, T.2    Skovsgaard, T.3    Stein, W.D.4
  • 54
    • 0027509809 scopus 로고
    • The effects of lipids and detergents on ATPase-active P-glycoprotein
    • Doige CA, Yu X, Sharom FJ: The effects of lipids and detergents on ATPase-active P-glycoprotein. Biochim. Biophys. Acta 1146, 65-72 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1146 , pp. 65-72
    • Doige, C.A.1    Yu, X.2    Sharom, F.J.3
  • 55
    • 0028831929 scopus 로고
    • Effects of lipids on ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch IL, Senior AE: Effects of lipids on ATPase activity of purified Chinese hamster P-glycoprotein Arch. Biochem. Biophys. 316, 135-140 (1995).
    • (1995) Arch. Biochem. Biophys , vol.316 , pp. 135-140
    • Urbatsch, I.L.1    Senior, A.E.2
  • 56
    • 0030791978 scopus 로고    scopus 로고
    • Structure-activity relationships of P-glycoprotein interacting drugs: Kinetic characterization of their effects on ATPase activity
    • Litman T, Zeuthen T, Skovsgaard T, Stein WD: Structure-activity relationships of P-glycoprotein interacting drugs: kinetic characterization of their effects on ATPase activity. Biochim. Biophys. Acta 1361, 159-168 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1361 , pp. 159-168
    • Litman, T.1    Zeuthen, T.2    Skovsgaard, T.3    Stein, W.D.4
  • 57
    • 33744902318 scopus 로고    scopus 로고
    • Interaction of transported drugs with the lipid bilayer and P-glycoprotein through a solvation exchange mechanism
    • Omote H, al-Shawi MK: Interaction of transported drugs with the lipid bilayer and P-glycoprotein through a solvation exchange mechanism. Biophys. J. 90, 4046-4059 (2006).
    • (2006) Biophys. J , vol.90 , pp. 4046-4059
    • Omote, H.1    al-Shawi, M.K.2
  • 59
    • 0034724680 scopus 로고    scopus 로고
    • Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1
    • Gao M, Cui HR, Loe DW et al.: Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1. J. Biol. Chem. 275, 13098-13108 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 13098-13108
    • Gao, M.1    Cui, H.R.2    Loe, D.W.3
  • 60
    • 0037417765 scopus 로고    scopus 로고
    • Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle
    • Qu Q, Russell PL, Sharom FJ: Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle. Biochemistry 42, 1170-1177 (2003).
    • (2003) Biochemistry , vol.42 , pp. 1170-1177
    • Qu, Q.1    Russell, P.L.2    Sharom, F.J.3
  • 61
    • 27144547163 scopus 로고    scopus 로고
    • Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy
    • Delannoy S, Urbatsch IL, Tombline G, Senior AE, Vogel PD: Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy. Biochemistry 44, 14010-14019 (2005).
    • (2005) Biochemistry , vol.44 , pp. 14010-14019
    • Delannoy, S.1    Urbatsch, I.L.2    Tombline, G.3    Senior, A.E.4    Vogel, P.D.5
  • 62
    • 0033610801 scopus 로고    scopus 로고
    • Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain
    • Bakos E, Evers R, Szakács G et al.: Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain. J. Biol. Chem. 273, 32167-32175 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 32167-32175
    • Bakos, E.1    Evers, R.2    Szakács, G.3
  • 63
    • 18244399574 scopus 로고    scopus 로고
    • Role of the NH2-terminal membrane spanning domain of multidrug resistance protein 1/ABCC1 in protein processing and trafficking
    • Westlake CJ. Cole SPC, Deeley RG: Role of the NH2-terminal membrane spanning domain of multidrug resistance protein 1/ABCC1 in protein processing and trafficking. Mol. Biol. Cell 16, 2483-2492 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2483-2492
    • Westlake, C.J.1    Cole, S.P.C.2    Deeley, R.G.3
  • 64
    • 34247851070 scopus 로고    scopus 로고
    • Regulation of function by dimerization through the amino-terminal membrane-spanning domain of human ABCC1/MRP1
    • Yang YY, Liu Y, Dong ZZ et al.: Regulation of function by dimerization through the amino-terminal membrane-spanning domain of human ABCC1/MRP1. J. Biol. Chem. 282, 8821-8830 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 8821-8830
    • Yang, Y.Y.1    Liu, Y.2    Dong, Z.Z.3
  • 65
    • 13244292479 scopus 로고    scopus 로고
    • Rosenberg MF, Callaghan R, Modok S, Higgins CF, Ford RC: Three-dimensional structure of P-glycoprotein - the transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state. J Biol. Chem. 280, 2857-286?(2005).
    • Rosenberg MF, Callaghan R, Modok S, Higgins CF, Ford RC: Three-dimensional structure of P-glycoprotein - the transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state. J Biol. Chem. 280, 2857-286?(2005).
  • 66
    • 0035814802 scopus 로고    scopus 로고
    • FRET analysis indicates that the two ATPase active sites of the P-glycoprotein multidrug transporter are closely associated
    • Qu Q, Sharom FJ: FRET analysis indicates that the two ATPase active sites of the P-glycoprotein multidrug transporter are closely associated. Biochemistry 40, 1413-1422 (2001).
    • (2001) Biochemistry , vol.40 , pp. 1413-1422
    • Qu, Q.1    Sharom, F.J.2
  • 67
    • 0035920130 scopus 로고    scopus 로고
    • Cysteines 431 and 1074 are responsible for inhibitory disulfide cross-linking between the two nucleotide-binding sites in human P-glycoprotein
    • Urbatsch IL, Gimi K, Wilke-Mounts S et al.: Cysteines 431 and 1074 are responsible for inhibitory disulfide cross-linking between the two nucleotide-binding sites in human P-glycoprotein. J. Biol. Chem. 276, 26980-26987 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 26980-26987
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3
  • 68
    • 0036829647 scopus 로고    scopus 로고
    • The 'LSGGQ' motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing Walker A sequence
    • Loo TW, Bartlett MC, Clarke DM: The 'LSGGQ' motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing Walker A sequence. J. Biol. Chem. 277, 41303-41306 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 41303-41306
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 69
    • 0035844237 scopus 로고    scopus 로고
    • The structure of the multidrug resistance protein 1 (MRP1/ABCC1) - crystallization and single-particle analysis
    • Rosenberg MF, Mao QC, Holzenburg A, Ford RC, Deeley RG, Cole SPC: The structure of the multidrug resistance protein 1 (MRP1/ABCC1) - crystallization and single-particle analysis. J. Biol. Chem. 276, 16076-16082 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 16076-16082
    • Rosenberg, M.F.1    Mao, Q.C.2    Holzenburg, A.3    Ford, R.C.4    Deeley, R.G.5    Cole, S.P.C.6
  • 70
    • 33750446035 scopus 로고    scopus 로고
    • Purification and 3D structural analysis of oligomeric human multidrug transporter ABCG2
    • McDevitt CA, Collins RF, Conway M et al.: Purification and 3D structural analysis of oligomeric human multidrug transporter ABCG2. Structure 14, 1623-1632 (2006).
    • (2006) Structure , vol.14 , pp. 1623-1632
    • McDevitt, C.A.1    Collins, R.F.2    Conway, M.3
  • 71
    • 32044453808 scopus 로고    scopus 로고
    • Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux
    • Loo TW, Clarke DM: Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux. J. Membr. Biol. 206, 173-185 (2005).
    • (2005) J. Membr. Biol , vol.206 , pp. 173-185
    • Loo, T.W.1    Clarke, D.M.2
  • 72
    • 0030782511 scopus 로고    scopus 로고
    • Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities
    • Shapiro AB, Ling V: Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities. Eur. J. Biochem. 250, 130-137 (1997).
    • (1997) Eur. J. Biochem , vol.250 , pp. 130-137
    • Shapiro, A.B.1    Ling, V.2
  • 74
    • 0141994817 scopus 로고    scopus 로고
    • Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein
    • Loo TW, Bartlett MC, Clarke DM: Simultaneous binding of two different drugs in the binding pocket of the human multidrug resistance P-glycoprotein. J. Biol. Chem. 278, 39706-39710 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 39706-39710
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 75
    • 27144451192 scopus 로고    scopus 로고
    • Interaction of LDS-751 and rhodamine 123 with P-glycoprotein: Evidence for simultaneous binding of both drugs
    • Lugo MR, Sharom FJ: Interaction of LDS-751 and rhodamine 123 with P-glycoprotein: evidence for simultaneous binding of both drugs. Biochemistry 44, 14020-14029 (2005).
    • (2005) Biochemistry , vol.44 , pp. 14020-14029
    • Lugo, M.R.1    Sharom, F.J.2
  • 76
    • 14644425991 scopus 로고    scopus 로고
    • Do drug substrates enter the common drug-binding pocket of P-glycoprotein through 'gates'?
    • Loo TW, Clarke DM: Do drug substrates enter the common drug-binding pocket of P-glycoprotein through 'gates'? Biochem. Biophys. Res. Commun. 329, 419-422 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.329 , pp. 419-422
    • Loo, T.W.1    Clarke, D.M.2
  • 77
    • 0037687304 scopus 로고    scopus 로고
    • Substrate-induced conformational, changes in the transmembrane segments of human P-glycoprotein - direct evidence for the substrate-induced fit mechanism for drug binding
    • Loo TW, Bartlett MC, Clarke DM: Substrate-induced conformational, changes in the transmembrane segments of human P-glycoprotein - direct evidence for the substrate-induced fit mechanism for drug binding. J. Biol. Chem. 278, 13603-13606 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 13603-13606
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 78
    • 4143103793 scopus 로고    scopus 로고
    • Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein
    • Schumacher MA, Miller MC, Brennan RG: Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein. EMBO J. 23, 2923-2930 (2004).
    • (2004) EMBO J , vol.23 , pp. 2923-2930
    • Schumacher, M.A.1    Miller, M.C.2    Brennan, R.G.3
  • 79
    • 4644265234 scopus 로고    scopus 로고
    • The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium
    • Loo TW, Bartlett MC, Clarke DM: The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium. Biochemistry 43, 12081-12089 (2004).
    • (2004) Biochemistry , vol.43 , pp. 12081-12089
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 80
    • 12144262818 scopus 로고    scopus 로고
    • Interaction of LDS-751 with P-glycoprotein and mapping of the location of the R drug binding site
    • Lugo MR, Sharom FJ: Interaction of LDS-751 with P-glycoprotein and mapping of the location of the R drug binding site. Biochemistry 44, 643-655 (2005).
    • (2005) Biochemistry , vol.44 , pp. 643-655
    • Lugo, M.R.1    Sharom, F.J.2
  • 81
    • 0035782973 scopus 로고    scopus 로고
    • Exploring the structure and function of the P-glycoprotein multidrug transporter using fluorescence spectroscopic tools
    • Sharom FJ, Liu R, Qu Q, Romsicki Y: Exploring the structure and function of the P-glycoprotein multidrug transporter using fluorescence spectroscopic tools. Seminars Cell Dev. Biol. 12, 257-266 (2001).
    • (2001) Seminars Cell Dev. Biol , vol.12 , pp. 257-266
    • Sharom, F.J.1    Liu, R.2    Qu, Q.3    Romsicki, Y.4
  • 82
    • 0032518454 scopus 로고    scopus 로고
    • A general pattern for substrate recognition by P-glycoprotein
    • Seelig A: A general pattern for substrate recognition by P-glycoprotein. Eur. J. Biochem. 251, 252-261 (1998).
    • (1998) Eur. J. Biochem , vol.251 , pp. 252-261
    • Seelig, A.1
  • 83
    • 17444419056 scopus 로고    scopus 로고
    • A pharmacophore hypothesis for P-glyroprotein substrate recognition using GRIND-based 3D-QSAR
    • Cianchetta G, Singleton RW, Zhang M et al.: A pharmacophore hypothesis for P-glyroprotein substrate recognition using GRIND-based 3D-QSAR. J. Med. Chem. 48, 2927-2935 (2005).
    • (2005) J. Med. Chem , vol.48 , pp. 2927-2935
    • Cianchetta, G.1    Singleton, R.W.2    Zhang, M.3
  • 84
    • 0037137614 scopus 로고    scopus 로고
    • Pharmacophore model of drugs involved in P-glycoprotein multidrug resistance: Explanation of structural variety (hypothesis)
    • Pajeva IK, Wiese M: Pharmacophore model of drugs involved in P-glycoprotein multidrug resistance: Explanation of structural variety (hypothesis). J. Med. Chem. 45, 5671-5686 (2002).
    • (2002) J. Med. Chem , vol.45 , pp. 5671-5686
    • Pajeva, I.K.1    Wiese, M.2
  • 85
    • 0028097634 scopus 로고
    • Transmembrane aromatic amino acid distribution in P-glycoprotein. A functional role in broad substrate specificity
    • Pawagi AB, Wang J, Silverman M, Reithmeier RA, Deber CM: Transmembrane aromatic amino acid distribution in P-glycoprotein. A functional role in broad substrate specificity. J. Mol. Biol. 235, 554-564 (1994).
    • (1994) J. Mol. Biol , vol.235 , pp. 554-564
    • Pawagi, A.B.1    Wang, J.2    Silverman, M.3    Reithmeier, R.A.4    Deber, C.M.5
  • 86
    • 0034610402 scopus 로고    scopus 로고
    • Intrinsic fluorescence of the P-glycoprotein multidrug transporter: Sensitivity of tryptophan residues to binding of drugs and nucleotides
    • Liu R, Siemiarczuk A, Sharom FJ: Intrinsic fluorescence of the P-glycoprotein multidrug transporter: sensitivity of tryptophan residues to binding of drugs and nucleotides. Biochemistry 39, 14927-14938 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14927-14938
    • Liu, R.1    Siemiarczuk, A.2    Sharom, F.J.3
  • 87
    • 33750478648 scopus 로고    scopus 로고
    • Multiple drugbinding sites on the R482G isoform of the ABCG2 transporter
    • Clark, Kerr ID, Callaghan R: Multiple drugbinding sites on the R482G isoform of the ABCG2 transporter. Br. J. Pharmacol. 149, 506-515 (2006).
    • (2006) Br. J. Pharmacol , vol.149 , pp. 506-515
    • Clark1    Kerr, I.D.2    Callaghan, R.3
  • 88
    • 31844455959 scopus 로고    scopus 로고
    • Substrate recognition and transport by multidrug resistance protein 1 (ABCC1)
    • Deeley RG, Cole SPC: Substrate recognition and transport by multidrug resistance protein 1 (ABCC1). FEBS Lett. 580, 1103-1111 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 1103-1111
    • Deeley, R.G.1    Cole, S.P.C.2
  • 89
    • 0347683446 scopus 로고    scopus 로고
    • Molecular modeling correctly predicts the functional importance of Phe594 in transmembrane Helix 11 of the multidrug resistance protein, MRP1 (ABCC1)
    • Campbell JD, Koike K, Moreau C, Sansom MSP, Deeley RG, Cole SPC: Molecular modeling correctly predicts the functional importance of Phe594 in transmembrane Helix 11 of the multidrug resistance protein, MRP1 (ABCC1). J. Biol. Chem. 279, 463-468 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 463-468
    • Campbell, J.D.1    Koike, K.2    Moreau, C.3    Sansom, M.S.P.4    Deeley, R.G.5    Cole, S.P.C.6
  • 90
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC: An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315, 373-377 (2007).
    • (2007) Science , vol.315 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 91
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein K, Frei DC, Locher KP: Structure of an ABC transporter in complex with its binding protein. Nature 446, 213-216 (2007).
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 92
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson RJ, Locher KP: Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006).
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 93
    • 1942532335 scopus 로고    scopus 로고
    • ABC transporter architecture and mechanism: Implications from the crystal structures of BtuCD and BtuF
    • Locher KP, Berths E: ABC transporter architecture and mechanism: implications from the crystal structures of BtuCD and BtuF. FEBS Lett. 564, 264-268 (2004).
    • (2004) FEBS Lett , vol.564 , pp. 264-268
    • Locher, K.P.1    Berths, E.2
  • 94
    • 31844452870 scopus 로고    scopus 로고
    • The structures of MsbA: Insight into ABC transporter-mediated multidrug efflux
    • Reyes CL, Ward A, Yu J, Chang G: The structures of MsbA: Insight into ABC transporter-mediated multidrug efflux. FEBS Lett. 580, 1042-1048 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 1042-1048
    • Reyes, C.L.1    Ward, A.2    Yu, J.3    Chang, G.4
  • 95
    • 34147208836 scopus 로고    scopus 로고
    • Chang G, Roth CB, Reyes CL, Pornillos O, Chen YJ, Chen AP: Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters (Retraction of 293, 1793, 2001). Science 314, 1875 (2006).
    • Chang G, Roth CB, Reyes CL, Pornillos O, Chen YJ, Chen AP: Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters (Retraction of vol 293, pg 1793, 2001). Science 314, 1875 (2006).
  • 96
    • 0042531543 scopus 로고    scopus 로고
    • A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure
    • Seigneuret M, Garnier-Suillerot A: A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure. J. Biol. Chem. 278, 30115-30124 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 30115-30124
    • Seigneuret, M.1    Garnier-Suillerot, A.2
  • 97
    • 0642272487 scopus 로고    scopus 로고
    • An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling
    • Stenham DR, Campbell JD, Sansom MS, Higgins CF, Kerr ID, Linton KJ: An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling. FASEB J. 17, 2287-2289 (2003).
    • (2003) FASEB J , vol.17 , pp. 2287-2289
    • Stenham, D.R.1    Campbell, J.D.2    Sansom, M.S.3    Higgins, C.F.4    Kerr, I.D.5    Linton, K.J.6
  • 98
    • 31844448665 scopus 로고    scopus 로고
    • The translocation mechanism of P-glycoprotein
    • Callaghan R, Ford RC, Kerr ID: The translocation mechanism of P-glycoprotein. FEBS Lett. 580, 1056-1063 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 1056-1063
    • Callaghan, R.1    Ford, R.C.2    Kerr, I.D.3
  • 100
    • 3843140625 scopus 로고    scopus 로고
    • Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly
    • Tombline G, Bartholomew LA, Urbatsch IL, Senior AE: Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly. J. Biol. Chem. 279, 31212-31220 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 31212-31220
    • Tombline, G.1    Bartholomew, L.A.2    Urbatsch, I.L.3    Senior, A.E.4
  • 101
    • 0038711772 scopus 로고    scopus 로고
    • The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p
    • Janas E, Hofacker M, Chen M, Gompf S, Van der Does C, Tampé R: The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J. Biol. Chem. 278, 26862-26869 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 26862-26869
    • Janas, E.1    Hofacker, M.2    Chen, M.3    Gompf, S.4    Van der Does, C.5    Tampé, R.6
  • 102
    • 33644840984 scopus 로고    scopus 로고
    • The power of the pump: Mechanisms of action of P-glycoprotein (ABCB1)
    • Ambudkar SV, Kim IW, Sauna ZE: The power of the pump: mechanisms of action of P-glycoprotein (ABCB1). Eur. J. Pharm. Sci. 27, 392-400 (2006).
    • (2006) Eur. J. Pharm. Sci , vol.27 , pp. 392-400
    • Ambudkar, S.V.1    Kim, I.W.2    Sauna, Z.E.3
  • 103
    • 0029840320 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains
    • Liu R, Sharom FJ: Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains. Biochemistry 35, 11865-11873 (1996).
    • (1996) Biochemistry , vol.35 , pp. 11865-11873
    • Liu, R.1    Sharom, F.J.2
  • 104
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins CF, Linton KJ: The ATP switch model for ABC transporters. Nature Struct. Biol. 11, 918-926 (2004).
    • (2004) Nature Struct. Biol , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 106
    • 33644672481 scopus 로고    scopus 로고
    • Quantification and characterization of P-glycoprotein-substrate interactions
    • Gatlik-Landwojtowicz E, Aanismaa P, Seelig A: Quantification and characterization of P-glycoprotein-substrate interactions. Biochemistry 45, 3020-3032 (2006).
    • (2006) Biochemistry , vol.45 , pp. 3020-3032
    • Gatlik-Landwojtowicz, E.1    Aanismaa, P.2    Seelig, A.3
  • 107
    • 0033602840 scopus 로고    scopus 로고
    • The membrane lipid environment modulates drug interactions with the P-glycoprotein multidrug transporter
    • Romsicki Y, Sharom FJ: The membrane lipid environment modulates drug interactions with the P-glycoprotein multidrug transporter. Biochemistry 38, 6887-6896 (1999).
    • (1999) Biochemistry , vol.38 , pp. 6887-6896
    • Romsicki, Y.1    Sharom, F.J.2
  • 108
    • 0034818922 scopus 로고    scopus 로고
    • Drug transport by reconstituted P-glycoprotein in proteoliposomes. Effect of substrates and modulators, and dependence on bilayer phase state
    • Lu P, Liu R, Sharom FJ: Drug transport by reconstituted P-glycoprotein in proteoliposomes. Effect of substrates and modulators, and dependence on bilayer phase state. Eur. J. Biochem. 268, 1687-1697 (2001).
    • (2001) Eur. J. Biochem , vol.268 , pp. 1687-1697
    • Lu, P.1    Liu, R.2    Sharom, F.J.3
  • 109
    • 17544365536 scopus 로고    scopus 로고
    • The role of passive transbilayer drug movement in multidrug resistance and its modulation
    • Eytan GD, Regev R, Oren G, Assaraf YG: The role of passive transbilayer drug movement in multidrug resistance and its modulation. J. Biol. Chem. 271, 12897-12902 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 12897-12902
    • Eytan, G.D.1    Regev, R.2    Oren, G.3    Assaraf, Y.G.4
  • 110
    • 33646538823 scopus 로고    scopus 로고
    • New insights into the drug binding, transport and lipid flippase activities of the P-glycoprotein multidrug transporter
    • Sharom FJ, Lugo MR, Eckford PD: New insights into the drug binding, transport and lipid flippase activities of the P-glycoprotein multidrug transporter. J. Bioenerg. Biomembr. 37, 481-487 (2005).
    • (2005) J. Bioenerg. Biomembr , vol.37 , pp. 481-487
    • Sharom, F.J.1    Lugo, M.R.2    Eckford, P.D.3
  • 111
    • 14644444547 scopus 로고    scopus 로고
    • ABC transporters in the balance: Is there a role in multidrug resistance?
    • Polgar O, Bates SE: ABC transporters in the balance: is there a role in multidrug resistance? Biochem. Soc. Trans. 33, 241-245 (2005).
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 241-245
    • Polgar, O.1    Bates, S.E.2
  • 112
    • 34249679271 scopus 로고    scopus 로고
    • ABC transporters and drug resistance in leukemia: Was P-gp nothing but the first head of the Hydra?
    • Steinbach D, Legrand O: ABC transporters and drug resistance in leukemia: was P-gp nothing but the first head of the Hydra? Leukemia 21, 1172-1176 (2007).
    • (2007) Leukemia , vol.21 , pp. 1172-1176
    • Steinbach, D.1    Legrand, O.2
  • 113
    • 0036772386 scopus 로고    scopus 로고
    • Frequent expression of the multi-drug resistance-associated protein BCRP/MXR/ABCP/ ABCG2 in human tumours detected by the BXP-21 monoclonal antibody in paraffin-embedded material
    • Diestra JE, Scheffer GL, Català I et al.: Frequent expression of the multi-drug resistance-associated protein BCRP/MXR/ABCP/ ABCG2 in human tumours detected by the BXP-21 monoclonal antibody in paraffin-embedded material. J. Pathol. 198, 213-219 (2002).
    • (2002) J. Pathol , vol.198 , pp. 213-219
    • Diestra, J.E.1    Scheffer, G.L.2    Català, I.3
  • 116
    • 21744447836 scopus 로고    scopus 로고
    • Anticancer multidrug resistance mediated by MRP1: Recent advances in the discovery of reversal agents
    • Boumendjel A, Baubichon-Cortay H, Trompier D, Perrotton T, Di Pietro A: Anticancer multidrug resistance mediated by MRP1: Recent advances in the discovery of reversal agents. Med. Res. Rev. 25, 453-472 (2005).
    • (2005) Med. Res. Rev , vol.25 , pp. 453-472
    • Boumendjel, A.1    Baubichon-Cortay, H.2    Trompier, D.3    Perrotton, T.4    Di Pietro, A.5
  • 117
    • 25844443754 scopus 로고    scopus 로고
    • Breast cancer resistance protein: Molecular target for anticancer drug resistance and pharmacokinetics/pharmacodynamics
    • Sugimoto Y, Tsukahara S, Ishikawa E, Mitsuhashi J: Breast cancer resistance protein: molecular target for anticancer drug resistance and pharmacokinetics/pharmacodynamics. Jap. J. Cancer Res. 96, 457-465 (2005).
    • (2005) Jap. J. Cancer Res , vol.96 , pp. 457-465
    • Sugimoto, Y.1    Tsukahara, S.2    Ishikawa, E.3    Mitsuhashi, J.4
  • 119
    • 1842532997 scopus 로고    scopus 로고
    • VX-710 (biricodar) increases drug retention and enhances chemosensitivity in resistant cells overexpressing P-glycoprotein, multidrug resistance protein, and breast cancer resistance protein
    • Minderman H, O'Loughlin KL, Pendyala L, Baer MR: VX-710 (biricodar) increases drug retention and enhances chemosensitivity in resistant cells overexpressing P-glycoprotein, multidrug resistance protein, and breast cancer resistance protein. Clin. Cancer Res. 10, 1826-1834 (2004).
    • (2004) Clin. Cancer Res , vol.10 , pp. 1826-1834
    • Minderman, H.1    O'Loughlin, K.L.2    Pendyala, L.3    Baer, M.R.4
  • 120
    • 33847139661 scopus 로고    scopus 로고
    • Implications of ATP-binding cassette transporters for brain pharmacotherapies
    • Hermann DM, Bassetti CL. Implications of ATP-binding cassette transporters for brain pharmacotherapies. Trends Pharmacol. Sci. 28, 128-134 (2007).
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 128-134
    • Hermann, D.M.1    Bassetti, C.L.2
  • 121
    • 23044500398 scopus 로고    scopus 로고
    • Drug resistance in brain diseases and the role of drug efflux transporters
    • Loescher W, Potschka H: Drug resistance in brain diseases and the role of drug efflux transporters. Nat. Rev. Neurosci. 6, 591-602 (2005).
    • (2005) Nat. Rev. Neurosci , vol.6 , pp. 591-602
    • Loescher, W.1    Potschka, H.2
  • 122
    • 0033526176 scopus 로고    scopus 로고
    • P-glycoprotein, a gatekeeper in the blood-brain barrier
    • Schinkel AH: P-glycoprotein, a gatekeeper in the blood-brain barrier. Adv. Drug Deliv. Rev. 36, 179-194 (1999).
    • (1999) Adv. Drug Deliv. Rev , vol.36 , pp. 179-194
    • Schinkel, A.H.1
  • 123
    • 16844384057 scopus 로고    scopus 로고
    • The effect of Bcrp1 (Abcg2) on the in vivo pharmacokinetics and brain penetration of imatinib mesylate (Gleevecc®): Implications for the use of breast cancer resistance protein and P-glycoprotein inhibitors to enable the brain penetration of imatinib in patients
    • Breedveld P, Pluim D, Cipriani G et al.: The effect of Bcrp1 (Abcg2) on the in vivo pharmacokinetics and brain penetration of imatinib mesylate (Gleevecc®): implications for the use of breast cancer resistance protein and P-glycoprotein inhibitors to enable the brain penetration of imatinib in patients. Cancer Res. 65, 2577-2582 (2005).
    • (2005) Cancer Res , vol.65 , pp. 2577-2582
    • Breedveld, P.1    Pluim, D.2    Cipriani, G.3
  • 124
    • 0033975098 scopus 로고    scopus 로고
    • Multidrug resistance protein 1 protects the choroid plexus epithelium and contributes to the blood-cerebrospinal fluid barrier
    • Wijnholds J, De Lange ECM, Scheffer GL et al.: Multidrug resistance protein 1 protects the choroid plexus epithelium and contributes to the blood-cerebrospinal fluid barrier. J. Clin. Invest. 105, 279-285 (2000).
    • (2000) J. Clin. Invest , vol.105 , pp. 279-285
    • Wijnholds, J.1    De Lange, E.C.M.2    Scheffer, G.L.3
  • 125
    • 30344487254 scopus 로고    scopus 로고
    • Use of P-glycoprotein and BCRP inhibitors to improve oral bioavailability and CNS penetration of anticancer drugs
    • Breedveld P, Beijnen JH, Schellens JHM: Use of P-glycoprotein and BCRP inhibitors to improve oral bioavailability and CNS penetration of anticancer drugs. Trends Pharmacol. Sci. 27, 17-24 (2006).
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 17-24
    • Breedveld, P.1    Beijnen, J.H.2    Schellens, J.H.M.3
  • 126
    • 33745831231 scopus 로고    scopus 로고
    • Structure, function, expression, genomic organization, and single nucleotide polymorphisms of human ABCB1 ( MDR1), ABCC (MRP), and ABCG2 (BCRP) efflux transporters
    • Choudhuri S, Klaassen CD: Structure, function, expression, genomic organization, and single nucleotide polymorphisms of human ABCB1 ( MDR1), ABCC (MRP), and ABCG2 (BCRP) efflux transporters. Int. J. Toxicol. 25, 231-259 (2006).
    • (2006) Int. J. Toxicol , vol.25 , pp. 231-259
    • Choudhuri, S.1    Klaassen, C.D.2
  • 127
    • 0024362996 scopus 로고
    • P-glycoprotein gene (MDR1) cDNA from human adrenal: Normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance
    • Kioka N, Tsubota J, Kakehi Y et al.: P-glycoprotein gene (MDR1) cDNA from human adrenal: normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance. Biochem. Biophys. Res. Commun. 162, 224-231 (1989).
    • (1989) Biochem. Biophys. Res. Commun , vol.162 , pp. 224-231
    • Kioka, N.1    Tsubota, J.2    Kakehi, Y.3
  • 128
    • 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 et al.: Multidrug-resistant human sarcoma cells with a mutant P-glycoprotein, altered phenotype, and resistance to cyclosporins. J. Biol. Chem. 272, 5974-5982 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 5974-5982
    • Chen, G.1    Duran, G.E.2    Steger, K.A.3
  • 129
    • 34249058785 scopus 로고    scopus 로고
    • ABCB1 genotype and PGP expression, function and therapeutic drug response: A critical review and recommendations for future research
    • Leschziner GD, Andrew T, Pirmohamed M, Johnson MR: ABCB1 genotype and PGP expression, function and therapeutic drug response: a critical review and recommendations for future research. Pharmacogenomics J. 7, 154-179 (2007).
    • (2007) Pharmacogenomics J , vol.7 , pp. 154-179
    • Leschziner, G.D.1    Andrew, T.2    Pirmohamed, M.3    Johnson, M.R.4
  • 130
    • 1642523162 scopus 로고    scopus 로고
    • Polymorphisms in human MDR1 (P-glycoprotein): Recent advances and clinical relevance
    • Marzolini C, Paus E, Buclin T, Kim RB: Polymorphisms in human MDR1 (P-glycoprotein): Recent advances and clinical relevance. Clin. Pharmacol. Ther. 75, 13-33 (2004).
    • (2004) Clin. Pharmacol. Ther , vol.75 , pp. 13-33
    • Marzolini, C.1    Paus, E.2    Buclin, T.3    Kim, R.B.4
  • 131
    • 18744407592 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms of ABCB1 (MDR1) gene and distinct haplotype profile in a West Black African population
    • Allabi AC, Horsmans Y, Issaoui B, Gala JL: Single nucleotide polymorphisms of ABCB1 (MDR1) gene and distinct haplotype profile in a West Black African population. Eur. J. Clin. Pharmacol. 61, 97-102 (2005).
    • (2005) Eur. J. Clin. Pharmacol , vol.61 , pp. 97-102
    • Allabi, A.C.1    Horsmans, Y.2    Issaoui, B.3    Gala, J.L.4
  • 132
    • 33846558896 scopus 로고    scopus 로고
    • Ethnicity-relaxed polymorphisms ana haplotypes in the human ABCB1 gene
    • Kimchi-Sarfaty C, Marple AH, Shinar S et al.. Ethnicity-relaxed polymorphisms ana haplotypes in the human ABCB1 gene. Pharmacogenomics 8, 29-39 (2007).
    • (2007) Pharmacogenomics , vol.8 , pp. 29-39
    • Kimchi-Sarfaty, C.1    Marple, A.H.2    Shinar, S.3
  • 134
    • 33744501248 scopus 로고    scopus 로고
    • Exon sequencing and high resolution haplotype analysis of ABC transporter genes implicated in drug resistance
    • Leschziner G, Zabaneh D, Pirmohamed M et al.: Exon sequencing and high resolution haplotype analysis of ABC transporter genes implicated in drug resistance. Pharmacogenet. Genomics 16, 439-450 (2006).
    • (2006) Pharmacogenet. Genomics , vol.16 , pp. 439-450
    • Leschziner, G.1    Zabaneh, D.2    Pirmohamed, M.3
  • 135
    • 3042772026 scopus 로고    scopus 로고
    • Identification of functionally variant MDR1 alleles among European Americans and African-Americans
    • Kim RB, Leake BF, Choo EF et al.: Identification of functionally variant MDR1 alleles among European Americans and African-Americans. Clin. Pharmacol. Ther. 70, 189-199 (2001).
    • (2001) Clin. Pharmacol. Ther , vol.70 , pp. 189-199
    • Kim, R.B.1    Leake, B.F.2    Choo, E.F.3
  • 136
    • 33846504706 scopus 로고    scopus 로고
    • A 'silent' polymorphism in the MDR1 gene changes substrate specificity
    • Kimchi-Sarfaty C, Oh JM, Kim IW et al.: A 'silent' polymorphism in the MDR1 gene changes substrate specificity. Science 315, 525-528 (2007).
    • (2007) Science , vol.315 , pp. 525-528
    • Kimchi-Sarfaty, C.1    Oh, J.M.2    Kim, I.W.3
  • 137
    • 0036082545 scopus 로고    scopus 로고
    • Functional characterization of coding polymorphisms in the human MDR1 gene using a vaccinia virus expression system
    • Kimchi-Sarfaty C, Gribar JJ, Gottesman MM: Functional characterization of coding polymorphisms in the human MDR1 gene using a vaccinia virus expression system. Mol. Pharmacol. 62, 1-6 (2002).
    • (2002) Mol. Pharmacol , vol.62 , pp. 1-6
    • Kimchi-Sarfaty, C.1    Gribar, J.J.2    Gottesman, M.M.3
  • 138
    • 0038323843 scopus 로고    scopus 로고
    • Human MDR1 polymorophism: G2677T/A and C3435T have no effect on MDR1 transport activities
    • Morita N, Yasumori T, Nakayama K: Human MDR1 polymorophism: G2677T/A and C3435T have no effect on MDR1 transport activities. Biochem. Pharmacol. 65, 1843-1852 (2003).
    • (2003) Biochem. Pharmacol , vol.65 , pp. 1843-1852
    • Morita, N.1    Yasumori, T.2    Nakayama, K.3
  • 139
    • 34347363131 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship analysis and molecular dynamics simulation to functionally validate nonsynonymous polymorphisms of human ABC transporter ABCB1 (P-glycoprotein/MDR1)
    • Sakurai A, Onishi Y, Hirano H et al.: Quantitative structure-activity relationship analysis and molecular dynamics simulation to functionally validate nonsynonymous polymorphisms of human ABC transporter ABCB1 (P-glycoprotein/MDR1). Biochemistry 46, 7678-7693 (2007).
    • (2007) Biochemistry , vol.46 , pp. 7678-7693
    • Sakurai, A.1    Onishi, Y.2    Hirano, H.3
  • 140
    • 27144514512 scopus 로고    scopus 로고
    • MDR1 G1199A polymorphism alters permeability of HIV protease inhibitors across P-glycoprotein-expressing epithelial cells
    • Woodahl EL, Yang ZP, Bui T, Shen DD, Ho RJY: MDR1 G1199A polymorphism alters permeability of HIV protease inhibitors across P-glycoprotein-expressing epithelial cells. AIDS 19, 1617-1625 (2005).
    • (2005) AIDS , vol.19 , pp. 1617-1625
    • Woodahl, E.L.1    Yang, Z.P.2    Bui, T.3    Shen, D.D.4    Ho, R.J.Y.5
  • 141
    • 0034724324 scopus 로고    scopus 로고
    • Functional polymorphisms of the human multidrug-resistance gene: Multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo
    • Hoffmeyer S, Burk O, Von Richter O et al.: Functional polymorphisms of the human multidrug-resistance gene: multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo. Proc. Natl Acad. Sci. USA 97, 3473-3478 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3473-3478
    • Hoffmeyer, S.1    Burk, O.2    Von Richter, O.3
  • 142
    • 0037022006 scopus 로고    scopus 로고
    • Response to antiretroviral treatment in HIV-1-infected individuals with allelic variants of the multidrug resistance transporter 1: A pharmacogenetics study
    • Fellay J, Marzolini C, Meaden ER et al.: Response to antiretroviral treatment in HIV-1-infected individuals with allelic variants of the multidrug resistance transporter 1: a pharmacogenetics study. Lancet 359, 30-36 (2002).
    • (2002) Lancet , vol.359 , pp. 30-36
    • Fellay, J.1    Marzolini, C.2    Meaden, E.R.3
  • 143
    • 0037462209 scopus 로고    scopus 로고
    • Influence of polymorphisms within the CX3CR1 and MDR-1 genes on initial antiretroviral therapy response
    • Brumme ZL, Dong WW, Chan KJ et al.: Influence of polymorphisms within the CX3CR1 and MDR-1 genes on initial antiretroviral therapy response. AIDS 17, 201-208 (2003).
    • (2003) AIDS , vol.17 , pp. 201-208
    • Brumme, Z.L.1    Dong, W.W.2    Chan, K.J.3
  • 144
    • 15944414161 scopus 로고    scopus 로고
    • An MDR1-3435 variant is associated with higher plasma nelfinavir levels and more rapid virologic response in HIV-1 infected children
    • Saitoh A, Singh KK, Powell CA et al.: An MDR1-3435 variant is associated with higher plasma nelfinavir levels and more rapid virologic response in HIV-1 infected children. AIDS 19, 371-380 (2005).
    • (2005) AIDS , vol.19 , pp. 371-380
    • Saitoh, A.1    Singh, K.K.2    Powell, C.A.3
  • 145
    • 0037431040 scopus 로고    scopus 로고
    • Association of multidrug resistance in epilepsy with a polymorphism in the drug-transporter gene ABCB1
    • Siddiqui A, Kerb R, Weale ME et al.: Association of multidrug resistance in epilepsy with a polymorphism in the drug-transporter gene ABCB1. N. Engl. J. Med. 348, 1442-1448 (2003).
    • (2003) N. Engl. J. Med , vol.348 , pp. 1442-1448
    • Siddiqui, A.1    Kerb, R.2    Weale, M.E.3
  • 146
    • 18244365827 scopus 로고    scopus 로고
    • Lack of association between the C3435T polymorphism in the human multidrug resistance (MDR1) gene and response to antiepileptic drug treatment
    • Sills GJ, Mohanraj R, Butler E et al.: Lack of association between the C3435T polymorphism in the human multidrug resistance (MDR1) gene and response to antiepileptic drug treatment. Epilepsia 46, 643-647 (2005).
    • (2005) Epilepsia , vol.46 , pp. 643-647
    • Sills, G.J.1    Mohanraj, R.2    Butler, E.3
  • 147
    • 4644230833 scopus 로고    scopus 로고
    • Failure to confirm association of a polymorphism in ABCB1 with multidrug-resistant epilepsy
    • Tan NCK, Heron SE, Scheffer IE et al.: Failure to confirm association of a polymorphism in ABCB1 with multidrug-resistant epilepsy. Neurology 63, 1090-1092 (2004).
    • (2004) Neurology , vol.63 , pp. 1090-1092
    • Tan, N.C.K.1    Heron, S.E.2    Scheffer, I.E.3
  • 148
    • 33645289956 scopus 로고    scopus 로고
    • Lack of association between the C3435T polymorphism in the human multidrug resistance (MDR1) gene and response to antiepileptic drug treatment
    • Basic S, Hajnsek S, Poljakovic Z, Basic M: Lack of association between the C3435T polymorphism in the human multidrug resistance (MDR1) gene and response to antiepileptic drug treatment. Epilepsia 47, 449 (2006).
    • (2006) Epilepsia , vol.47 , pp. 449
    • Basic, S.1    Hajnsek, S.2    Poljakovic, Z.3    Basic, M.4
  • 149
    • 1842637753 scopus 로고    scopus 로고
    • Polymorphisms in the multidrug resistance-1 (MDR1) gene influence the response to atorvastatin treatment in a gender-specific manner
    • Kajinami K, Brousseau ME, Ordovas JM, Schaefer EJ: Polymorphisms in the multidrug resistance-1 (MDR1) gene influence the response to atorvastatin treatment in a gender-specific manner. Am. J. Cardiol. 93, 1046-1050 (2004).
    • (2004) Am. J. Cardiol , vol.93 , pp. 1046-1050
    • Kajinami, K.1    Brousseau, M.E.2    Ordovas, J.M.3    Schaefer, E.J.4
  • 150
    • 30944434673 scopus 로고    scopus 로고
    • The association of common SNPs and haplotypes in the CETP and MDR1 genes with lipids response to fluvastatin in familial hypercholesterolemia
    • Bercovich D, Friedlander Y, Korem S et al.: The association of common SNPs and haplotypes in the CETP and MDR1 genes with lipids response to fluvastatin in familial hypercholesterolemia. Atherosclerosis 185, 97-107 (2006).
    • (2006) Atherosclerosis , vol.185 , pp. 97-107
    • Bercovich, D.1    Friedlander, Y.2    Korem, S.3
  • 151
    • 33644666953 scopus 로고    scopus 로고
    • An association study of 43 SNPs in 16 candidate genes with atorvastatin response
    • Thompson JF, Man M, Johnson KJ et al.: An association study of 43 SNPs in 16 candidate genes with atorvastatin response. Pharmacogenomics J. 5, 352-358 (2005).
    • (2005) Pharmacogenomics J , vol.5 , pp. 352-358
    • Thompson, J.F.1    Man, M.2    Johnson, K.J.3
  • 153
    • 9144224852 scopus 로고    scopus 로고
    • MDR1 Ala893 polymorphism is associated with inflammatory bowel disease
    • Brant SR, Panhuysen CIM, Nicolae D et al.: MDR1 Ala893 polymorphism is associated with inflammatory bowel disease. Am. J. Hum. Genet. 73, 1282-1292 (2003).
    • (2003) Am. J. Hum. Genet , vol.73 , pp. 1282-1292
    • Brant, S.R.1    Panhuysen, C.I.M.2    Nicolae, D.3
  • 154
    • 0037223561 scopus 로고    scopus 로고
    • Association between the C3435T MDR1 gene polymorphism and susceptibility for ulcerative colitis
    • Schwab M, Schaeffeler E, Marx C et al.: Association between the C3435T MDR1 gene polymorphism and susceptibility for ulcerative colitis. Gastroenterology 124, 26-33 (2003).
    • (2003) Gastroenterology , vol.124 , pp. 26-33
    • Schwab, M.1    Schaeffeler, E.2    Marx, C.3
  • 155
    • 8844229534 scopus 로고    scopus 로고
    • Polymorphisms in multidrug resistance 1 (MDR1) gene are associated with refractory Crohn disease and ulcerative colitis
    • Potocnik U, Ferkolj I, Glavac D, Dean M: Polymorphisms in multidrug resistance 1 (MDR1) gene are associated with refractory Crohn disease and ulcerative colitis. Genes Immun. 5, 530-539 (2004).
    • (2004) Genes Immun , vol.5 , pp. 530-539
    • Potocnik, U.1    Ferkolj, I.2    Glavac, D.3    Dean, M.4
  • 156
    • 33845878539 scopus 로고    scopus 로고
    • Association of MDR1 genotypes with susceptibility to colorectal cancer in older non-smokers
    • Osswald E, Johne A, Laschinski G et al.: Association of MDR1 genotypes with susceptibility to colorectal cancer in older non-smokers. Eur. J. Clin. Pharmacol. 63, 9-16 (2007).
    • (2007) Eur. J. Clin. Pharmacol , vol.63 , pp. 9-16
    • Osswald, E.1    Johne, A.2    Laschinski, G.3
  • 157
    • 27644581876 scopus 로고    scopus 로고
    • Polymorphism in the P-glycoprotein drug transporter MDR1 gene in colon cancer patients
    • Kurzawski M, Drozdzik M, Suchy J et al.: Polymorphism in the P-glycoprotein drug transporter MDR1 gene in colon cancer patients. Eur. J. Clin. Pharmacol. 61, 389-394 (2005).
    • (2005) Eur. J. Clin. Pharmacol , vol.61 , pp. 389-394
    • Kurzawski, M.1    Drozdzik, M.2    Suchy, J.3
  • 158
    • 0034811618 scopus 로고    scopus 로고
    • The role of P-glycoprotein (MDR1) polymorphisms and mutations in colorectal cancer
    • Potocnik U, Glavac MR, Golouh R, Glavac D: The role of P-glycoprotein (MDR1) polymorphisms and mutations in colorectal cancer. Pflugers Arch. 442, R182-R183 (2001).
    • (2001) Pflugers Arch , vol.442
    • Potocnik, U.1    Glavac, M.R.2    Golouh, R.3    Glavac, D.4
  • 159
    • 18444404305 scopus 로고    scopus 로고
    • Association of the P-glycoprotein transporter MDR1 C3435T polymorphism with the susceptibility to renal epithelial tumors
    • Siegsmund M, Brinkmann U, Schäffeler E et al.: Association of the P-glycoprotein transporter MDR1 C3435T polymorphism with the susceptibility to renal epithelial tumors. J Am. Soc. Nephrol. 13, 1847-1854 (2002).
    • (2002) J Am. Soc. Nephrol , vol.13 , pp. 1847-1854
    • Siegsmund, M.1    Brinkmann, U.2    Schäffeler, E.3
  • 160
    • 20344397913 scopus 로고    scopus 로고
    • The anti-Parkinson drug budipine is exported actively out of the brain by P-glycoprotein in mice
    • Uhr M, Ebinger M, Rosenhagen MC, Grauer MT: The anti-Parkinson drug budipine is exported actively out of the brain by P-glycoprotein in mice. Neurosci. Lett. 383, 73-76 (2005).
    • (2005) Neurosci. Lett , vol.383 , pp. 73-76
    • Uhr, M.1    Ebinger, M.2    Rosenhagen, M.C.3    Grauer, M.T.4
  • 161
    • 34247625517 scopus 로고    scopus 로고
    • Common ABCB1 polymorphisms are not associated with multidrug resistance in epilepsy using a gene-wide tagging approach
    • Leschziner GD, Andrew T, Leach JP et al.: Common ABCB1 polymorphisms are not associated with multidrug resistance in epilepsy using a gene-wide tagging approach. Pharmacogenet. Genomics 17, 217-220 (2007).
    • (2007) Pharmacogenet. Genomics , vol.17 , pp. 217-220
    • Leschziner, G.D.1    Andrew, T.2    Leach, J.P.3
  • 162
    • 33847366654 scopus 로고    scopus 로고
    • The controversial association of ABCB1 polymorphisms in refractory epilepsy: An analysis of multiple SNPs in an Irish population
    • Shahwan A, Murphy K, Doherty C et al.: The controversial association of ABCB1 polymorphisms in refractory epilepsy: an analysis of multiple SNPs in an Irish population. Epilepsy Res. 73, 192-198 (2007).
    • (2007) Epilepsy Res , vol.73 , pp. 192-198
    • Shahwan, A.1    Murphy, K.2    Doherty, C.3
  • 163
    • 22944446748 scopus 로고    scopus 로고
    • Polymorphisms of MRP1 (ABCC1) and related ATP-dependent drug transporters
    • Conseil G, Deeley RG, Cole SP: Polymorphisms of MRP1 (ABCC1) and related ATP-dependent drug transporters. Pharmacogenet. Genomics 15, 523-533 (2005).
    • (2005) Pharmacogenet. Genomics , vol.15 , pp. 523-533
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.3
  • 164
    • 26444438734 scopus 로고    scopus 로고
    • A functional polymorphism within the MRP1 gene locus identified through its genomic signature of positive selection
    • Wang Z, Wang B, Tang K, Lee EJ, Chong SS, Lee CG: A functional polymorphism within the MRP1 gene locus identified through its genomic signature of positive selection. Hum. Mol. Genet. 14, 2075-2087 (2005).
    • (2005) Hum. Mol. Genet , vol.14 , pp. 2075-2087
    • Wang, Z.1    Wang, B.2    Tang, K.3    Lee, E.J.4    Chong, S.S.5    Lee, C.G.6
  • 165
    • 0041410061 scopus 로고    scopus 로고
    • Frequency of MRP1 genetic polymorphisms and their functional significance in Caucasians: Detection of a novel mutation G816A in the human MRP1 gene
    • Oselin K, Mrozikiewicz PM, Gaikovitch E, Pähkla R, Roots I: Frequency of MRP1 genetic polymorphisms and their functional significance in Caucasians: detection of a novel mutation G816A in the human MRP1 gene. Eur. J. Clin. Pharmacol. 59, 347-350 (2003).
    • (2003) Eur. J. Clin. Pharmacol , vol.59 , pp. 347-350
    • Oselin, K.1    Mrozikiewicz, P.M.2    Gaikovitch, E.3    Pähkla, R.4    Roots, I.5
  • 166
    • 23444447815 scopus 로고    scopus 로고
    • Functional characterization of non-synonymous single nucleotide polymorphisms in the gene encoding human multidrug resistance protein 1 (MRP1/ABCC1)
    • Letourneau IJ, Deeley RG, Cole SP: Functional characterization of non-synonymous single nucleotide polymorphisms in the gene encoding human multidrug resistance protein 1 (MRP1/ABCC1). Pharmacogenet. Genomics 15, 647-657 (2005).
    • (2005) Pharmacogenet. Genomics , vol.15 , pp. 647-657
    • Letourneau, I.J.1    Deeley, R.G.2    Cole, S.P.3
  • 167
    • 0036016317 scopus 로고    scopus 로고
    • A naturally occurring mutation in MRP1 results in a selective decrease in organic anion transport and in increased doxorubicin resistance
    • Conrad S, Kauffmann HM, Ito K et al.: A naturally occurring mutation in MRP1 results in a selective decrease in organic anion transport and in increased doxorubicin resistance. Pharmacogenetics 12, 321-330 (2002).
    • (2002) Pharmacogenetics , vol.12 , pp. 321-330
    • Conrad, S.1    Kauffmann, H.M.2    Ito, K.3
  • 168
    • 0037882044 scopus 로고    scopus 로고
    • Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1)
    • Leslie EM, Létourneau IJ, Deeley RG, Cole SPC: Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1). Biochemistry 42, 5214-5224 (2003).
    • (2003) Biochemistry , vol.42 , pp. 5214-5224
    • Leslie, E.M.1    Létourneau, I.J.2    Deeley, R.G.3    Cole, S.P.C.4
  • 169
    • 0032920492 scopus 로고    scopus 로고
    • Interpatient variability in bioavailability of the intravenous formulation of topotecan given orally to children with recurrent solid tumors
    • Zamboni WC, Bowman LC, Tan M et al.: Interpatient variability in bioavailability of the intravenous formulation of topotecan given orally to children with recurrent solid tumors. Cancer Chemother. Pharmacol. 43, 454-460 (1999).
    • (1999) Cancer Chemother. Pharmacol , vol.43 , pp. 454-460
    • Zamboni, W.C.1    Bowman, L.C.2    Tan, M.3
  • 170
    • 33745286306 scopus 로고    scopus 로고
    • Functional validation of the genetic polymorphisms of human ATP-binding cassette (ABC) transporter ABCG2: Identification of alleles that are defective in porphyrin transport
    • Tamura A, Watanabe M, Saito H et al.: Functional validation of the genetic polymorphisms of human ATP-binding cassette (ABC) transporter ABCG2: Identification of alleles that are defective in porphyrin transport. Mol. Pharmacol. 70, 287-296 (2006).
    • (2006) Mol. Pharmacol , vol.70 , pp. 287-296
    • Tamura, A.1    Watanabe, M.2    Saito, H.3
  • 171
    • 6344284092 scopus 로고    scopus 로고
    • Functional analysis of SNPs variants of BCRP/ABCG2
    • Kondo C, Suzuki H, Itoda M et al.: Functional analysis of SNPs variants of BCRP/ABCG2. Pharm. Res. 21, 1895-1903 (2004).
    • (2004) Pharm. Res , vol.21 , pp. 1895-1903
    • Kondo, C.1    Suzuki, H.2    Itoda, M.3
  • 172
    • 21244443380 scopus 로고    scopus 로고
    • Morisaki K, Robey R. Oezvegy-Laczka C et al.: Single nucleotide polymorphisms modify the transporter activity of ABCG2. Cancer Chemother. Pbarmacol. 56; 161-172 (2005).
    • Morisaki K, Robey R. Oezvegy-Laczka C et al.: Single nucleotide polymorphisms modify the transporter activity of ABCG2. Cancer Chemother. Pbarmacol. 56; 161-172 (2005).
  • 173
    • 1242319383 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms resuit in impaired membrane localization and reduced atpase activity in multidrug transporter ABCG2
    • Mizuarai S, Aozasa N, Kotani H: Single nucleotide polymorphisms resuit in impaired membrane localization and reduced atpase activity in multidrug transporter ABCG2. Int. J. Cancer 109, 238-246 (2004).
    • (2004) Int. J. Cancer , vol.109 , pp. 238-246
    • Mizuarai, S.1    Aozasa, N.2    Kotani, H.3
  • 174
    • 33845655480 scopus 로고    scopus 로고
    • Re-evaluation and functional classification of non-synonymous single nucleotide polymorphisms of the human ATP-binding cassette transporter ABCG2
    • Tamura A, Wakabayashi K, Onishi Y et al.: Re-evaluation and functional classification of non-synonymous single nucleotide polymorphisms of the human ATP-binding cassette transporter ABCG2. Cancer Sci. 98, 231-239 (2007).
    • (2007) Cancer Sci , vol.98 , pp. 231-239
    • Tamura, A.1    Wakabayashi, K.2    Onishi, Y.3
  • 175
    • 33644811431 scopus 로고    scopus 로고
    • The role of the human ABCG2 multidrug transporter and its variants in cancer therapy and toxicology
    • Cervenak J, Andrikovics H, Oezvegy-Laczka C et al.: The role of the human ABCG2 multidrug transporter and its variants in cancer therapy and toxicology. Cancer Lett. 234, 62-72 (2006).
    • (2006) Cancer Lett , vol.234 , pp. 62-72
    • Cervenak, J.1    Andrikovics, H.2    Oezvegy-Laczka, C.3
  • 176
    • 19944399722 scopus 로고    scopus 로고
    • Functional assessment of ABCG2 (BCRP) gene polymorphisms to protein expression in human placenta
    • Kobayashi D, Ieiri I, Hirota T et al.: Functional assessment of ABCG2 (BCRP) gene polymorphisms to protein expression in human placenta. Drug Metab. Dispos. 33, 94-101 (2005).
    • (2005) Drug Metab. Dispos , vol.33 , pp. 94-101
    • Kobayashi, D.1    Ieiri, I.2    Hirota, T.3
  • 177
    • 4444381535 scopus 로고    scopus 로고
    • ABCG2 pharmacogenetics: Ethnic differences in allele frequency and assessment of influence on irinotecan disposition
    • de Jong FA, Marsh S, Mathijssen RH et al.: ABCG2 pharmacogenetics: ethnic differences in allele frequency and assessment of influence on irinotecan disposition. Clin. Cancer Res. 10, 5889-5894 (2004).
    • (2004) Clin. Cancer Res , vol.10 , pp. 5889-5894
    • de Jong, F.A.1    Marsh, S.2    Mathijssen, R.H.3
  • 178
    • 25144462079 scopus 로고    scopus 로고
    • Effect of ABCG2 genotype on the oral bioavailability of topotecan
    • Sparreboom A, Loos WJ, Burger H et al.: Effect of ABCG2 genotype on the oral bioavailability of topotecan. Cancer Biol. Ther. 4, 650-658 (2005).
    • (2005) Cancer Biol. Ther , vol.4 , pp. 650-658
    • Sparreboom, A.1    Loos, W.J.2    Burger, H.3
  • 179
    • 3042651340 scopus 로고    scopus 로고
    • Diflomotecan pharmacokinetics in celation to ABCG2 421C>A genotype
    • Sparreboom A, Gelderblom H, Marsh S et al.: Diflomotecan pharmacokinetics in celation to ABCG2 421C>A genotype. Clin. Pharmacol. Ther. 76, 38-44 (2004).
    • (2004) Clin. Pharmacol. Ther , vol.76 , pp. 38-44
    • Sparreboom, A.1    Gelderblom, H.2    Marsh, S.3
  • 180
    • 33745020069 scopus 로고    scopus 로고
    • Disposition of 9-nitrocamptothecin and its 9-aminocamptothecin metabolite in relation to ABC transporter genotypes
    • Zamboni WC, Ramanathan RK, McLeod HL et al.: Disposition of 9-nitrocamptothecin and its 9-aminocamptothecin metabolite in relation to ABC transporter genotypes. Invest. New Drugs 24, 393-401 (2006).
    • (2006) Invest. New Drugs , vol.24 , pp. 393-401
    • Zamboni, W.C.1    Ramanathan, R.K.2    McLeod, H.L.3
  • 181
    • 34548240764 scopus 로고    scopus 로고
    • Association of variant ABCG2 and the pharmacokinetics of epidermal growth factor receptor tyrosine kinase inhibitors in cancer patients
    • Li J, Cusatis G, Brahmer J et al.: Association of variant ABCG2 and the pharmacokinetics of epidermal growth factor receptor tyrosine kinase inhibitors in cancer patients. Cancer Biol Ther. 6, 432-438 (2007).
    • (2007) Cancer Biol Ther , vol.6 , pp. 432-438
    • Li, J.1    Cusatis, G.2    Brahmer, J.3
  • 182
    • 26444605446 scopus 로고    scopus 로고
    • Association of the BCRPC421A polymorphism with nonpapillary renal cell carcinoma
    • Korenaga Y, Naito K, Okayama N et al.: Association of the BCRPC421A polymorphism with nonpapillary renal cell carcinoma. Int. J. Cancer 117, 431-434 (2005).
    • (2005) Int. J. Cancer , vol.117 , pp. 431-434
    • Korenaga, Y.1    Naito, K.2    Okayama, N.3
  • 183
    • 0035884595 scopus 로고    scopus 로고
    • Acquired mutations in the MXR/BCRP/ABCP gene alter substrate specificity in MXR/BCRP/ ABCP-overexpressing cells
    • Honjo Y, Hrycyna CA, Yan QW et al.: Acquired mutations in the MXR/BCRP/ABCP gene alter substrate specificity in MXR/BCRP/ ABCP-overexpressing cells. Cancer Res. 61, 6635-6639 (2001).
    • (2001) Cancer Res , vol.61 , pp. 6635-6639
    • Honjo, Y.1    Hrycyna, C.A.2    Yan, Q.W.3
  • 184
    • 0042068263 scopus 로고    scopus 로고
    • A functional study on polymorphism of the ATP-binding cassette transporter ABCG2: Critical role of arginine-482 in methotrexate transport
    • Mitomo H, Kato R, Ito A et al.: A functional study on polymorphism of the ATP-binding cassette transporter ABCG2: critical role of arginine-482 in methotrexate transport. Biochem. J. 373, 767-774 (2003).
    • (2003) Biochem. J , vol.373 , pp. 767-774
    • Mitomo, H.1    Kato, R.2    Ito, A.3
  • 185
    • 0025951859 scopus 로고
    • Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation
    • Zhang JT, Ling V: Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation. J. Biol. Chem. 266, 18224-18232 (1991).
    • (1991) J. Biol. Chem , vol.266 , pp. 18224-18232
    • Zhang, J.T.1    Ling, V.2
  • 186
    • 0030863293 scopus 로고    scopus 로고
    • Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus
    • Hipfner DR, Almquist KC, Leslie EM et al.: Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus. J. Biol. Chem. 272, 23623-23630 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 23623-23630
    • Hipfner, D.R.1    Almquist, K.C.2    Leslie, E.M.3
  • 187
    • 16844386327 scopus 로고    scopus 로고
    • N-linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane
    • Diop NK, Hrycyna CA: N-linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane. Biochemistry 44, 5420-5429 (2005).
    • (2005) Biochemistry , vol.44 , pp. 5420-5429
    • Diop, N.K.1    Hrycyna, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.