메뉴 건너뛰기




Volumn 18, Issue 3, 2011, Pages 439-481

Structural and functional properties of human multidrug resistance protein 1 (MRP1/ABCC1)

Author keywords

Homology model; Inhibitor; MRP1; Mutation; Structure activity relationship; Substrate

Indexed keywords

ANTHRACYCLINE; ANTINEOPLASTIC AGENT; ANTISENSE OLIGONUCLEOTIDE; CONJUGATED ESTROGEN; DOXORUBICIN; EPIPODOPHYLLOTOXIN; GLYCOPROTEIN P; LEUKOTRIENE; MITOXANTRONE; MULTIDRUG RESISTANCE PROTEIN 1; SMALL INTERFERING RNA; VINCRISTINE; XENOBIOTIC AGENT;

EID: 79251514280     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986711794839197     Document Type: Article
Times cited : (122)

References (459)
  • 2
    • 70349335633 scopus 로고    scopus 로고
    • ABC transporters: A riddle wrapped in a mystery inside an enigma
    • Jones, P.M.; O'Mara, M.L.; George, A.M. ABC transporters: A riddle wrapped in a mystery inside an enigma. Trends Biochem. Sci. 2009, 34, 520-531.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 520-531
    • Jones, P.M.1    O'Mara, M.L.2    George, A.M.3
  • 3
    • 1842610700 scopus 로고    scopus 로고
    • The ABC transporter structure and mechanism: Perspectives on recent research
    • Jones, P.M.; George, A.M. The ABC transporter structure and mechanism: Perspectives on recent research. Cell. Mol. Life Sci. 2004, 61, 682-699.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 682-699
    • Jones, P.M.1    George, A.M.2
  • 4
    • 34147214716 scopus 로고    scopus 로고
    • Multiple molecular mechanisms for multidrug resistance transporters
    • Higgins, C.F. Multiple molecular mechanisms for multidrug resistance transporters. Nature 2007, 446, 749-757.
    • (2007) Nature , vol.446 , pp. 749-757
    • Higgins, C.F.1
  • 6
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst, P.; Elferink, R.O. Mammalian ABC transporters in health and disease. Annu. Rev. Biochem. 2002, 71, 537-592.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 537-592
    • Borst, P.1    Elferink, R.O.2
  • 8
    • 64649090980 scopus 로고    scopus 로고
    • Molecular basis of multidrug transport by ABC transporters
    • Seeger, M.A.; van Veen, H.W. Molecular basis of multidrug transport by ABC transporters. Biochim. Biophys. Acta. 2009, 1794, 725-737.
    • (2009) Biochim. Biophys. Acta. , vol.1794 , pp. 725-737
    • Seeger, M.A.1    Van Veen, H.W.2
  • 9
    • 43149118341 scopus 로고    scopus 로고
    • The role of ABC transporters in drug absorption, distribution, metabolism, excretion and toxicity (ADME-Tox)
    • Szakacs, G.; Varadi, A.; Ozvegy-Laczka, C.; Sarkadi, B. The role of ABC transporters in drug absorption, distribution, metabolism, excretion and toxicity (ADME-Tox). Drug Discov. Today 2008, 13, 379-393.
    • (2008) Drug Discov. Today , vol.13 , pp. 379-393
    • Szakacs, G.1    Varadi, A.2    Ozvegy-Laczka, C.3    Sarkadi, B.4
  • 10
    • 59149089885 scopus 로고    scopus 로고
    • The role of ATP binding cassette transporters in tissue defense and organ regeneration
    • Huls, M.; Russel, F.G.; Masereeuw, R. The role of ATP binding cassette transporters in tissue defense and organ regeneration. J. Pharmacol. Exp. Ther. 2009, 328, 3-9.
    • (2009) J. Pharmacol. Exp. Ther. , vol.328 , pp. 3-9
    • Huls, M.1    Russel, F.G.2    Masereeuw, R.3
  • 11
    • 0034674901 scopus 로고    scopus 로고
    • A family of drug transporters: The multidrug resistance-associated proteins
    • Borst, P.; Evers, R.; Kool, M.; Wijnholds, J. A family of drug transporters: The multidrug resistance-associated proteins. J. Natl. Cancer Inst. 2000, 92, 1295-1302.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1295-1302
    • Borst, P.1    Evers, R.2    Kool, M.3    Wijnholds, J.4
  • 12
    • 67650685020 scopus 로고    scopus 로고
    • ABC efflux pump-based resistance to chemotherapy drugs
    • Eckford, P.D.; Sharom, F.J. ABC efflux pump-based resistance to chemotherapy drugs. Chem. Rev. 2009, 109, 2989-3011.
    • (2009) Chem. Rev. , vol.109 , pp. 2989-3011
    • Eckford, P.D.1    Sharom, F.J.2
  • 14
    • 34250219965 scopus 로고    scopus 로고
    • Chemotherapy-induced resistance by ATP-binding cassette transporter genes
    • Gillet, J.P.; Efferth, T.; Remacle, J. Chemotherapy-induced resistance by ATP-binding cassette transporter genes. Biochim. Biophys. Acta 2007, 1775, 237-262.
    • (2007) Biochim. Biophys. Acta , vol.1775 , pp. 237-262
    • Gillet, J.P.1    Efferth, T.2    Remacle, J.3
  • 16
    • 4143115811 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Locher, K.P. Structure and mechanism of ABC transporters. Curr. Opin. Struct. Biol. 2004, 14, 426-431.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 426-431
    • Locher, K.P.1
  • 18
    • 0035823134 scopus 로고    scopus 로고
    • Structural biology. The xyz of ABC transporters
    • Higgins, C.F.; Linton, K.J. Structural biology. The xyz of ABC transporters. Science 2001, 293, 1782-1784.
    • (2001) Science , vol.293 , pp. 1782-1784
    • Higgins, C.F.1    Linton, K.J.2
  • 19
    • 40949121607 scopus 로고    scopus 로고
    • ABC multidrug transporters: Structure, function and role in chemoresistance
    • Sharom, F.J. ABC multidrug transporters: Structure, function and role in chemoresistance. Pharmacogenomics 2008, 9, 105-127.
    • (2008) Pharmacogenomics , vol.9 , pp. 105-127
    • Sharom, F.J.1
  • 21
    • 0033361943 scopus 로고    scopus 로고
    • Genomic structure of the canalicular multispecific organic anion-transporter gene (MRP2/cMOAT) and mutations in the ATP-binding-cassette region in Dubin-Johnson syndrome
    • Toh, S.; Wada, M.; Uchiumi, T.; Inokuchi, A.; Makino, Y.; Horie, Y.; Adachi, Y.; Sakisaka, S.; Kuwano, M. Genomic structure of the canalicular multispecific organic anion-transporter gene (MRP2/cMOAT) and mutations in the ATP-binding-cassette region in Dubin-Johnson syndrome. Am. J. Hum. Genet. 1999, 64, 739-746.
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 739-746
    • Toh, S.1    Wada, M.2    Uchiumi, T.3    Inokuchi, A.4    Makino, Y.5    Horie, Y.6    Adachi, Y.7    Sakisaka, S.8    Kuwano, M.9
  • 22
    • 33645104459 scopus 로고    scopus 로고
    • Altered hepatobiliary disposition of 5 (and 6)- carboxy-2',7'- dichlorofluorescein in Abcg2 (Bcrp1) and Abcc2 (Mrp2) knockout mice
    • Nezasa, K.; Tian, X.; Zamek-Gliszczynski, M.J.; Patel, N.J.; Raub, T.J.; Brouwer, K.L. Altered hepatobiliary disposition of 5 (and 6)- carboxy-2',7'-dichlorofluorescein in Abcg2 (Bcrp1) and Abcc2 (Mrp2) knockout mice. Drug Metab. Dispos. 2006, 34, 718-723.
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 718-723
    • Nezasa, K.1    Tian, X.2    Zamek-Gliszczynski, M.J.3    Patel, N.J.4    Raub, T.J.5    Brouwer, K.L.6
  • 24
    • 0035823559 scopus 로고    scopus 로고
    • Transport of cyclic nucleotides and estradiol 17-β-D-glucuronide by multidrug resistance protein 4. Resistance to 6-mercaptopurine and 6-thioguanine
    • Chen, Z.S.; Lee, K.; Kruh, G.D. Transport of cyclic nucleotides and estradiol 17-β-D-glucuronide by multidrug resistance protein 4. Resistance to 6-mercaptopurine and 6-thioguanine. J. Biol. Chem. 2001, 276, 33747-33754.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33747-33754
    • Chen, Z.S.1    Lee, K.2    Kruh, G.D.3
  • 26
    • 0033551671 scopus 로고    scopus 로고
    • PABC11 (also known as MOAT-C and MRP5), a member of the ABC family of proteins, has anion transporter activity but does not confer multidrug resistance when overexpressed in human embryonic kidney 293 cells
    • McAleer, M.A.; Breen, M.A.; White, N.L.; Matthews, N. pABC11 (also known as MOAT-C and MRP5), a member of the ABC family of proteins, has anion transporter activity but does not confer multidrug resistance when overexpressed in human embryonic kidney 293 cells. J. Biol. Chem. 1999, 274, 23541-23548.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23541-23548
    • McAleer, M.A.1    Breen, M.A.2    White, N.L.3    Matthews, N.4
  • 27
    • 0034282991 scopus 로고    scopus 로고
    • Transport of amphipathic anions by human multidrug resistance protein 3
    • Zeng, H.; Liu, G.; Rea, P.A.; Kruh, G.D. Transport of amphipathic anions by human multidrug resistance protein 3. Cancer Res. 2000, 60, 4779-4784.
    • (2000) Cancer Res. , vol.60 , pp. 4779-4784
    • Zeng, H.1    Liu, G.2    Rea, P.A.3    Kruh, G.D.4
  • 28
    • 0030063480 scopus 로고    scopus 로고
    • Transport of glutathione, glucuronate, and sulfate conjugates by the MRP gene-encoded conjugate export pump
    • Jedlitschky, G.; Leier, I.; Buchholz, U.; Barnouin, K.; Kurz, G.; Keppler, D. Transport of glutathione, glucuronate, and sulfate conjugates by the MRP gene-encoded conjugate export pump. Cancer Res. 1996, 56, 988-994. (Pubitemid 26065391)
    • (1996) Cancer Research , vol.56 , Issue.5 , pp. 988-994
    • Jedlitschky, G.1    Leier, I.2    Buchholz, U.3    Barnouin, K.4    Kurz, G.5    Keppler, D.6
  • 29
    • 0029918142 scopus 로고    scopus 로고
    • ATPdependent 17 beta-estradiol 17-(beta-D-glucuronide) transport by multidrug resistance protein (MRP). Inhibition by cholestatic steroids
    • Loe, D.W.; Almquist, K.C.; Cole, S.P.; Deeley, R.G. ATPdependent 17 beta-estradiol 17-(beta-D-glucuronide) transport by multidrug resistance protein (MRP). Inhibition by cholestatic steroids. J. Biol. Chem. 1996, 271, 9683-9689.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9683-9689
    • Loe, D.W.1    Almquist, K.C.2    Cole, S.P.3    Deeley, R.G.4
  • 31
    • 0036829109 scopus 로고    scopus 로고
    • Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6)
    • Belinsky, M.G.; Chen, Z.S.; Shchaveleva, I.; Zeng, H.; Kruh, G.D. Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6). Cancer Res. 2002, 62, 6172-6177.
    • (2002) Cancer Res. , vol.62 , pp. 6172-6177
    • Belinsky, M.G.1    Chen, Z.S.2    Shchaveleva, I.3    Zeng, H.4    Kruh, G.D.5
  • 34
    • 57649232758 scopus 로고    scopus 로고
    • Pseudoxanthoma elasticum: Clinical phenotypes, molecular genetics and putative pathomechanisms
    • Li, Q.; Jiang, Q.; Pfendner, E.; Varadi, A.; Uitto, J. Pseudoxanthoma elasticum: Clinical phenotypes, molecular genetics and putative pathomechanisms. Exp. Dermatol. 2009, 18, 1-11.
    • (2009) Exp. Dermatol. , vol.18 , pp. 1-11
    • Li, Q.1    Jiang, Q.2    Pfendner, E.3    Varadi, A.4    Uitto, J.5
  • 35
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • Gadsby, D.C.; Vergani, P.; Csanady, L. The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature 2006, 440, 477-483.
    • (2006) Nature , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanady, L.3
  • 36
    • 50649123290 scopus 로고    scopus 로고
    • CFTR function and prospects for therapy
    • Riordan, J.R. CFTR function and prospects for therapy. Annu. Rev. Biochem. 2008, 77, 701-726.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 701-726
    • Riordan, J.R.1
  • 38
    • 77249144771 scopus 로고    scopus 로고
    • Cystic fibrosis: Exploiting its genetic basis in the hunt for new therapies
    • Kreindler, J.L. Cystic fibrosis: Exploiting its genetic basis in the hunt for new therapies. Pharmacol. Ther. 2010, 125, 219-229.
    • (2010) Pharmacol. Ther. , Issue.125 , pp. 219-229
    • Kreindler, J.L.1
  • 40
    • 41149127307 scopus 로고    scopus 로고
    • The sulfonylurea receptor, an atypical ATP-binding cassette protein, and its regulation of the KATP channel
    • Burke, M.A.; Mutharasan, R.K.; Ardehali, H. The sulfonylurea receptor, an atypical ATP-binding cassette protein, and its regulation of the KATP channel. Circ. Res. 2008, 102, 164-176.
    • (2008) Circ. Res. , vol.102 , pp. 164-176
    • Burke, M.A.1    Mutharasan, R.K.2    Ardehali, H.3
  • 41
    • 77955569283 scopus 로고    scopus 로고
    • Human KATP channelopathies: Diseases of metabolic homeostasis
    • Olson, T.M.; Terzic, A. Human KATP channelopathies: Diseases of metabolic homeostasis. Pflugers Arch. 2010, 460, 295-306.
    • (2010) Pflugers Arch. , Issue.460 , pp. 295-306
    • Olson, T.M.1    Terzic, A.2
  • 43
  • 44
    • 33645221787 scopus 로고    scopus 로고
    • Mutations in the genes encoding the pancreatic β-cell KATP channel subunits Kir6.2 (KCNJ11) and SUR1 (ABCC8) in diabetes mellitus and hyperinsulinism
    • Gloyn, A.L.; Siddiqui, J.; Ellard, S. Mutations in the genes encoding the pancreatic β-cell KATP channel subunits Kir6.2 (KCNJ11) and SUR1 (ABCC8) in diabetes mellitus and hyperinsulinism. Hum. Mutat. 2006, 27, 220-231.
    • (2006) Hum. Mutat. , vol.27 , pp. 220-231
    • Gloyn, A.L.1    Siddiqui, J.2    Ellard, S.3
  • 45
    • 78650546048 scopus 로고    scopus 로고
    • Permanent neonatal diabetes due to activating mutations in ABCC8 and KCNJ11
    • Edghill, E.L.; Flanagan, S.E.; Ellard, S. Permanent neonatal diabetes due to activating mutations in ABCC8 and KCNJ11. Rev. Endocr. Metab. Disord. 2010, 11, 193-198.
    • (2010) Rev. Endocr. Metab. Disord. , Issue.11 , pp. 193-198
    • Edghill, E.L.1    Flanagan, S.E.2    Ellard, S.3
  • 46
    • 0037311274 scopus 로고    scopus 로고
    • Characterization of the transport properties of human multidrug resistance protein 7 (MRP7, ABCC10)
    • Chen, Z.S.; Hopper-Borge, E.; Belinsky, M.G.; Shchaveleva, I.; Kotova, E.; Kruh, G.D. Characterization of the transport properties of human multidrug resistance protein 7 (MRP7, ABCC10). Mol. Pharmacol. 2003, 63, 351-358.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 351-358
    • Chen, Z.S.1    Hopper-Borge, E.2    Belinsky, M.G.3    Shchaveleva, I.4    Kotova, E.5    Kruh, G.D.6
  • 47
    • 3142752689 scopus 로고    scopus 로고
    • Analysis of the drug resistance profile of multidrug resistance protein 7 (ABCC10): Resistance to docetaxel
    • Hopper-Borge, E.; Chen, Z.S.; Shchaveleva, I.; Belinsky, M.G.; Kruh, G.D. Analysis of the drug resistance profile of multidrug resistance protein 7 (ABCC10): Resistance to docetaxel. Cancer Res. 2004, 64, 4927-4930.
    • (2004) Cancer Res. , vol.64 , pp. 4927-4930
    • Hopper-Borge, E.1    Chen, Z.S.2    Shchaveleva, I.3    Belinsky, M.G.4    Kruh, G.D.5
  • 48
    • 0042531890 scopus 로고    scopus 로고
    • MRP8, ATP-binding cassette C11 (ABCC11), is a cyclic nucleotide efflux pump and a resistance factor for fluoropyrimidines 2',3'-dideoxycytidine and 9'-(2'- phosphonylmethoxyethyl)adenine
    • Guo, Y.; Kotova, E.; Chen, Z.S.; Lee, K.; Hopper-Borge, E.; Belinsky, M.G.; Kruh, G.D. MRP8, ATP-binding cassette C11 (ABCC11), is a cyclic nucleotide efflux pump and a resistance factor for fluoropyrimidines 2',3'-dideoxycytidine and 9'-(2'- phosphonylmethoxyethyl)adenine. J. Biol. Chem. 2003, 278, 29509-29514.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29509-29514
    • Guo, Y.1    Kotova, E.2    Chen, Z.S.3    Lee, K.4    Hopper-Borge, E.5    Belinsky, M.G.6    Kruh, G.D.7
  • 51
    • 31144475523 scopus 로고    scopus 로고
    • Human multidrug resistance protein 8 (MRP8/ABCC11), an apical efflux pump for steroid sulfates, is an axonal protein of the CNS and peripheral nervous system
    • Bortfeld, M.; Rius, M.; Konig, J.; Herold-Mende, C.; Nies, A.T.; Keppler, D. Human multidrug resistance protein 8 (MRP8/ABCC11), an apical efflux pump for steroid sulfates, is an axonal protein of the CNS and peripheral nervous system. Neuroscience 2006, 137, 1247-1257.
    • (2006) Neuroscience , vol.137 , pp. 1247-1257
    • Bortfeld, M.1    Rius, M.2    Konig, J.3    Herold-Mende, C.4    Nies, A.T.5    Keppler, D.6
  • 55
    • 2942555284 scopus 로고    scopus 로고
    • Degeneration of an ATP-binding cassette transporter gene, ABCC13, in different mammalian lineages
    • Annilo, T.; Dean, M. Degeneration of an ATP-binding cassette transporter gene, ABCC13, in different mammalian lineages. Genomics 2004, 84, 34-46.
    • (2004) Genomics , vol.84 , pp. 34-46
    • Annilo, T.1    Dean, M.2
  • 56
    • 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. 2007, 453, 621-641.
    • (2007) Pflugers Arch. , vol.453 , pp. 621-641
    • Bakos, E.1    Homolya, L.2
  • 57
    • 33646741238 scopus 로고    scopus 로고
    • The ATP-binding cassette transporters and their implication in drug disposition: A special look at the heart
    • Couture, L.; Nash, J.A.; Turgeon, J. The ATP-binding cassette transporters and their implication in drug disposition: A special look at the heart. Pharmacol. Rev. 2006, 58, 244-258.
    • (2006) Pharmacol. Rev. , vol.58 , pp. 244-258
    • Couture, L.1    Nash, J.A.2    Turgeon, J.3
  • 58
    • 33745835398 scopus 로고    scopus 로고
    • Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins
    • Deeley, R.G.; Westlake, C.; Cole, S.P. Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. Physiol. Rev. 2006, 86, 849-899.
    • (2006) Physiol. Rev. , vol.86 , pp. 849-899
    • Deeley, R.G.1    Westlake, C.2    Cole, S.P.3
  • 59
    • 48749108121 scopus 로고    scopus 로고
    • MRP class of human ATP binding cassette (ABC) transporters: Historical background and new research directions
    • Toyoda, Y.; Hagiya, Y.; Adachi, T.; Hoshijima, K.; Kuo, M.T.; Ishikawa, T. MRP class of human ATP binding cassette (ABC) transporters: Historical background and new research directions. Xenobiotica 2008, 38, 833-862.
    • (2008) Xenobiotica , vol.38 , pp. 833-862
    • Toyoda, Y.1    Hagiya, Y.2    Adachi, T.3    Hoshijima, K.4    Kuo, M.T.5    Ishikawa, T.6
  • 61
    • 0027161846 scopus 로고
    • Localization of a novel multidrug resistance-associated gene in the HT1080/DR4 and H69AR human tumor cell lines
    • Slovak, M.L.; Ho, J.P.; Bhardwaj, G.; Kurz, E.U.; Deeley, R.G.; Cole, S.P. Localization of a novel multidrug resistance-associated gene in the HT1080/DR4 and H69AR human tumor cell lines. Cancer Res. 1993, 53, 3221-3225.
    • (1993) Cancer Res. , vol.53 , pp. 3221-3225
    • Slovak, M.L.1    Ho, J.P.2    Bhardwaj, G.3    Kurz, E.U.4    Deeley, R.G.5    Cole, S.P.6
  • 62
    • 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, D.R.; Almquist, K.C.; Leslie, E.M.; Gerlach, J.H.; Grant, C.E.; Deeley, R.G.; Cole, S.P. Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus. J. Biol. Chem. 1997, 272, 23623-23630.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23623-23630
    • Hipfner, D.R.1    Almquist, K.C.2    Leslie, E.M.3    Gerlach, J.H.4    Grant, C.E.5    Deeley, R.G.6    Cole, S.P.7
  • 63
    • 0142254146 scopus 로고    scopus 로고
    • Cloning and functional characterization of the multidrug resistance-associated protein (MRP1/ABCC1) from the cynomolgus monkey
    • Godinot, N.; Iversen, P.W.; Tabas, L.; Xia, X.; Williams, D.C.; Dantzig, A.H.; Perry, W.L. 3rd, Cloning and functional characterization of the multidrug resistance-associated protein (MRP1/ABCC1) from the cynomolgus monkey. Mol. Cancer Ther. 2003, 2, 307-316.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 307-316
    • Godinot, N.1    Iversen, P.W.2    Tabas, L.3    Xia, X.4    Williams, D.C.5    Dantzig, A.H.6    Perry III, W.L.7
  • 64
    • 0037704286 scopus 로고    scopus 로고
    • Identification and characterization of the canine multidrug resistance-associated protein
    • Ma, L.; Pratt, S.E.; Cao, J.; Dantzig, A.H.; Moore, R.E.; Slapak, C.A. Identification and characterization of the canine multidrug resistance- associated protein. Mol. Cancer Ther. 2002, 1, 1335-1342.
    • (2002) Mol. Cancer Ther. , vol.1 , pp. 1335-1342
    • Ma, L.1    Pratt, S.E.2    Cao, J.3    Dantzig, A.H.4    Moore, R.E.5    Slapak, C.A.6
  • 65
    • 0041524278 scopus 로고    scopus 로고
    • Molecular cloning and pharmacological characterization of rat multidrug resistance protein 1 (MRP1)
    • Nunoya, K.; Grant, C.E.; Zhang, D.; Cole, S.P.; Deeley, R.G. Molecular cloning and pharmacological characterization of rat multidrug resistance protein 1 (MRP1). Drug Metab. Dispos. 2003, 31, 1016-1026.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 1016-1026
    • Nunoya, K.1    Grant, C.E.2    Zhang, D.3    Cole, S.P.4    Deeley, R.G.5
  • 66
    • 0030775395 scopus 로고    scopus 로고
    • Pharmacological characterization of the murine and human orthologs of multidrug-resistance protein in transfected human embryonic kidney cells
    • Stride, B.D.; Grant, C.E.; Loe, D.W.; Hipfner, D.R.; Cole, S.P.; Deeley, R.G. Pharmacological characterization of the murine and human orthologs of multidrug-resistance protein in transfected human embryonic kidney cells. Mol. Pharmacol. 1997, 52, 344-353.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 344-353
    • Stride, B.D.1    Grant, C.E.2    Loe, D.W.3    Hipfner, D.R.4    Cole, S.P.5    Deeley, R.G.6
  • 67
    • 53349117254 scopus 로고    scopus 로고
    • Substrates and inhibitors of human multidrug resistance associated proteins and the implications in drug development
    • Zhou, S.F.; Wang, L.L.; Di, Y.M.; Xue, C.C.; Duan, W.; Li, C.G.; Li, Y. Substrates and inhibitors of human multidrug resistance associated proteins and the implications in drug development. Curr. Med. Chem. 2008, 15, 1981-2039.
    • (2008) Curr. Med. Chem. , vol.15 , pp. 1981-2039
    • Zhou, S.F.1    Wang, L.L.2    Di, Y.M.3    Xue, C.C.4    Duan, W.5    Li, C.G.6    Li, Y.7
  • 68
    • 31844455959 scopus 로고    scopus 로고
    • Substrate recognition and transport by multidrug resistance protein 1 (ABCC1)
    • Deeley, R.G.; Cole, S.P. Substrate recognition and transport by multidrug resistance protein 1 (ABCC1). FEBS Lett. 2006, 580, 1103-1111.
    • (2006) FEBS Lett. , vol.580 , pp. 1103-1111
    • Deeley, R.G.1    Cole, S.P.2
  • 69
    • 33947397241 scopus 로고    scopus 로고
    • A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1
    • Chang, X.B. A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1. Cancer Metastasis Rev. 2007, 26, 15-37.
    • (2007) Cancer Metastasis Rev. , vol.26 , pp. 15-37
    • Chang, X.B.1
  • 70
    • 22944446748 scopus 로고    scopus 로고
    • Polymorphisms of MRP1 (ABCC1) and related ATP-dependent drug transporters
    • Conseil, G.; Deeley, R.G.; Cole, S.P. Polymorphisms of MRP1 (ABCC1) and related ATP-dependent drug transporters. Pharmacogenet. Genomics 2005, 15, 523-533.
    • (2005) Pharmacogenet. Genomics , vol.15 , pp. 523-533
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.3
  • 71
    • 73649120349 scopus 로고    scopus 로고
    • Multidrug resistance-associated proteins and implications in drug development
    • Liu, Y.H.; Di, Y.M.; Zhou, Z.W.; Mo, S.L.; Zhou, S.F. Multidrug resistance-associated proteins and implications in drug development. Clin. Exp. Pharmacol. Physiol. 2010, 37, 115-120.
    • (2010) Clin. Exp. Pharmacol. Physiol. , vol.37 , pp. 115-120
    • Liu, Y.H.1    Di, Y.M.2    Zhou, Z.W.3    Mo, S.L.4    Zhou, S.F.5
  • 72
    • 70349110758 scopus 로고    scopus 로고
    • Role of multidrug resistance associated proteins in drug development
    • Zhou, S.F. Role of multidrug resistance associated proteins in drug development. Drug Discov. Ther. 2008, 2, 305-332.
    • (2008) Drug Discov. Ther. , vol.2 , pp. 305-332
    • Zhou, S.F.1
  • 73
    • 0008632564 scopus 로고
    • Expression of a full-length cDNA for the human "MDR1" gene confers resistance to colchicine, doxorubicin, and vinblastine
    • Ueda, K.; Cardarelli, C.; Gottesman, M.M.; Pastan, I. Expression of a full-length cDNA for the human "MDR1" gene confers resistance to colchicine, doxorubicin, and vinblastine. Proc. Natl. Acad. Sci. U. S. A. 1987, 84, 3004-3008.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 3004-3008
    • Ueda, K.1    Cardarelli, C.2    Gottesman, M.M.3    Pastan, I.4
  • 74
    • 47349110179 scopus 로고    scopus 로고
    • Structure function and regulation of P-glycoprotein and its clinical relevance in drug disposition
    • Zhou, S.F. Structure, function and regulation of P-glycoprotein and its clinical relevance in drug disposition Xenobiotica 2008, 38, 802-832.
    • (2008) Xenobiotica , vol.38 , pp. 802-832
    • Zhou, S.F.1
  • 75
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: Role of ATP-dependent transporters
    • Gottesman, M.M.; Fojo, T.; Bates, S.E. Multidrug resistance in cancer: Role of ATP-dependent transporters. Nat. Rev. Cancer 2002, 2, 48-58.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 76
    • 0023278796 scopus 로고
    • Multidrug resistance in a human small cell lung cancer cell line selected in adriamycin
    • Mirski, S.E.; Gerlach, J.H.; Cole, S.P. Multidrug resistance in a human small cell lung cancer cell line selected in adriamycin. Cancer Res. 1987, 47, 2594-2598.
    • (1987) Cancer Res. , vol.47 , pp. 2594-2598
    • Mirski, S.E.1    Gerlach, J.H.2    Cole, S.P.3
  • 77
    • 0023278073 scopus 로고
    • Adriamycin resistance in HL60 cells in the absence of detectable P-glycoprotein
    • McGrath, T.; Center, M.S. Adriamycin resistance in HL60 cells in the absence of detectable P-glycoprotein. Biochem. Biophys. Res. Commun. 1987, 145, 1171-1176.
    • (1987) Biochem. Biophys. Res. Commun. , vol.145 , pp. 1171-1176
    • McGrath, T.1    Center, M.S.2
  • 78
    • 0025331434 scopus 로고
    • Patterns of cross-resistance in a multidrug-resistant small-cell lung carcinoma cell line
    • Cole, S.P. Patterns of cross-resistance in a multidrug-resistant small-cell lung carcinoma cell line. Cancer Chemother. Pharmacol. 1990, 26, 250-256.
    • (1990) Cancer Chemother. Pharmacol. , vol.26 , pp. 250-256
    • Cole, S.P.1
  • 79
    • 0025099593 scopus 로고
    • Alterations in glutathione and glutathione-related enzymes in a multidrugresistant small cell lung cancer cell line
    • Cole, S.P.; Downes, H.F.; Mirski, S.E.; Clements, D.J. Alterations in glutathione and glutathione-related enzymes in a multidrugresistant small cell lung cancer cell line. Mol. Pharmacol. 1990, 37, 192-197.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 192-197
    • Cole, S.P.1    Downes, H.F.2    Mirski, S.E.3    Clements, D.J.4
  • 80
    • 0027960078 scopus 로고
    • Pharmacological characterization of multidrug resistant MRP-transfected human tumor cells
    • Cole, S.P.; Sparks, K.E.; Fraser, K.; Loe, D.W.; Grant, C.E.; Wilson, G.M.; Deeley, R.G. Pharmacological characterization of multidrug resistant MRP-transfected human tumor cells. Cancer Res. 1994, 54, 5902-5910.
    • (1994) Cancer Res. , vol.54 , pp. 5902-5910
    • Cole, S.P.1    Sparks, K.E.2    Fraser, K.3    Loe, D.W.4    Grant, C.E.5    Wilson, G.M.6    Deeley, R.G.7
  • 81
    • 0024501402 scopus 로고
    • Effect of calcium antagonists on the chemosensitivity of two multidrug-resistant human tumour cell lines which do not overexpress P-glycoprotein
    • Cole, S.P.; Downes, H.F.; Slovak, M.L. Effect of calcium antagonists on the chemosensitivity of two multidrug-resistant human tumour cell lines which do not overexpress P-glycoprotein. Br. J. Cancer 1989, 59, 42-46.
    • (1989) Br. J. Cancer , vol.59 , pp. 42-46
    • Cole, S.P.1    Downes, H.F.2    Slovak, M.L.3
  • 82
    • 0025939987 scopus 로고
    • Non-P-glycoprotein-mediated multidrug resistance in a small cell lung cancer cell line: Evidence for decreased susceptibility to druginduced DNA damage and reduced levels of topoisomerase II
    • Cole, S.P.; Chanda, E.R.; Dicke, F.P.; Gerlach, J.H.; Mirski, S.E. Non-P-glycoprotein-mediated multidrug resistance in a small cell lung cancer cell line: Evidence for decreased susceptibility to druginduced DNA damage and reduced levels of topoisomerase II. Cancer Res. 1991, 51, 3345-3352.
    • (1991) Cancer Res. , vol.51 , pp. 3345-3352
    • Cole, S.P.1    Chanda, E.R.2    Dicke, F.P.3    Gerlach, J.H.4    Mirski, S.E.5
  • 83
    • 0028985382 scopus 로고
    • Characterization of the Mr 190,000 multidrug resistance protein (MRP) in drug-selected and transfected human tumor cell
    • Almquist, K.C.; Loe, D.W.; Hipfner, D.R.; Mackie, J.E.; Cole, S.P.; Deeley, R.G. Characterization of the Mr 190,000 multidrug resistance protein (MRP) in drug-selected and transfected human tumor cell. Cancer Res. 1995, 55, 102-110.
    • (1995) Cancer Res. , vol.55 , pp. 102-110
    • Almquist, K.C.1    Loe, D.W.2    Hipfner, D.R.3    Mackie, J.E.4    Cole, S.P.5    Deeley, R.G.6
  • 84
    • 0028000734 scopus 로고
    • Immunochemical detection of the multidrug resistance-associated protein MRP in human multidrugresistant tumor cells by monoclonal antibodies
    • Flens, M.J.; Izquierdo, M.A.; Scheffer, G.L.; Fritz, J.M.; Meijer, C.J.; Scheper, R.J.; Zaman, G.J. Immunochemical detection of the multidrug resistance-associated protein MRP in human multidrugresistant tumor cells by monoclonal antibodies. Cancer Res. 1994, 54, 4557-4563.
    • (1994) Cancer Res. , vol.54 , pp. 4557-4563
    • Flens, M.J.1    Izquierdo, M.A.2    Scheffer, G.L.3    Fritz, J.M.4    Meijer, C.J.5    Scheper, R.J.6    Zaman, G.J.7
  • 86
    • 0028054888 scopus 로고
    • Overexpression of multidrug resistanceassociated protein (MRP) increases resistance to natural product drugs
    • Grant, C.E.; Valdimarsson, G.; Hipfner, D.R.; Almquist, K.C.; Cole, S.P.; Deeley, R.G. Overexpression of multidrug resistanceassociated protein (MRP) increases resistance to natural product drugs. Cancer Res. 1994, 54, 357-361.
    • (1994) Cancer Res. , vol.54 , pp. 357-361
    • Grant, C.E.1    Valdimarsson, G.2    Hipfner, D.R.3    Almquist, K.C.4    Cole, S.P.5    Deeley, R.G.6
  • 88
    • 0028578004 scopus 로고
    • Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport
    • Muller, M.; Meijer, C.; Zaman, G.J.; Borst, P.; Scheper, R.J.; Mulder, N.H.; de Vries, E.G.; Jansen, P.L. Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport. Proc. Natl. Acad. Sci. U. S. A. 1994, 91, 13033-13037.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 13033-13037
    • Muller, M.1    Meijer, C.2    Zaman, G.J.3    Borst, P.4    Scheper, R.J.5    Mulder, N.H.6    De Vries, E.G.7    Jansen, P.L.8
  • 89
    • 0029912351 scopus 로고    scopus 로고
    • ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pump
    • Leier, I.; Jedlitschky, G.; Buchholz, U.; Center, M.; Cole, S.P.; Deeley, R.G.; Keppler, D. ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pump. Biochem. J. 1996, 314 (Pt 2), 433-437. (Pubitemid 26075650)
    • (1996) Biochemical Journal , vol.314 , Issue.2 , pp. 433-437
    • Leier, I.1    Jedlitschky, G.2    Buchholz, U.3    Center, M.4    Cole, S.P.C.5    Deeley, R.G.6    Keppler, D.7
  • 91
    • 0028334006 scopus 로고
    • Expression of the multidrug resistance-associated protein (MRP) in acute and chronic leukemias
    • Burger, H.; Nooter, K.; Zaman, G.J.; Sonneveld, P.; van Wingerden, K.E.; Oostrum, R.G.; Stoter, G. Expression of the multidrug resistance-associated protein (MRP) in acute and chronic leukemias. Leukemia 1994, 8, 990-997. (Pubitemid 24181302)
    • (1994) Leukemia , vol.8 , Issue.6 , pp. 990-997
    • Burger, H.1    Nooter, K.2    Zaman, G.J.R.3    Sonneveld, P.4    Van Wingerden, K.E.5    Oostrum, R.G.6    Stoter, G.7
  • 92
    • 77951289110 scopus 로고    scopus 로고
    • ABC transporters in human lymphocytes: Expression, activity and role, modulating factors and consequences for antiretroviral therapies
    • Giraud, C.; Manceau, S.; Treluyer, J.M. ABC transporters in human lymphocytes: Expression, activity and role, modulating factors and consequences for antiretroviral therapies. Expert Opin. Drug Metab. Toxicol. 2010, 6, 571-589.
    • (2010) Expert Opin. Drug Metab. Toxicol. , Issue.6 , pp. 571-589
    • Giraud, C.1    Manceau, S.2    Treluyer, J.M.3
  • 93
    • 34447527910 scopus 로고    scopus 로고
    • Expression localisation and activity of ATP binding cassette (ABC) family of drug transporters in human amnion membranes
    • Aye, I.L.; Paxton, J.W.; Evseenko, D.A.; Keelan, J.A. Expression, localisation and activity of ATP binding cassette (ABC) family of drug transporters in human amnion membranes. Placenta 2007, 28, 868-877.
    • (2007) Placenta , vol.28 , pp. 868-877
    • Aye, I.L.1    Paxton, J.W.2    Evseenko, D.A.3    Keelan, J.A.4
  • 94
    • 77951277135 scopus 로고    scopus 로고
    • Drug transporters in the lung-do they play a role in the biopharmaceutics of inhaled drugs?
    • Bosquillon, C. Drug transporters in the lung-do they play a role in the biopharmaceutics of inhaled drugs? J. Pharm. Sci. 2010, 99, 2240-2255.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 2240-2255
    • Bosquillon, C.1
  • 95
    • 33646754516 scopus 로고    scopus 로고
    • Multidrug resistanceassociated proteins: Expression and function in the central nervous system
    • Dallas, S.; Miller, D.S.; Bendayan, R. Multidrug resistanceassociated proteins: Expression and function in the central nervous system. Pharmacol. Rev. 2006, 58, 140-161.
    • (2006) Pharmacol. Rev. , vol.58 , pp. 140-161
    • Dallas, S.1    Miller, D.S.2    Bendayan, R.3
  • 96
    • 77953141219 scopus 로고    scopus 로고
    • ABC transporters and drug efflux at the bloodbrain barrier
    • Shen, S.; Zhang, W. ABC transporters and drug efflux at the bloodbrain barrier. Rev. Neurosci. 2010, 21, 29-53.
    • (2010) Rev. Neurosci. , vol.21 , pp. 29-53
    • Shen, S.1    Zhang, W.2
  • 97
    • 77953687856 scopus 로고    scopus 로고
    • Regulation of P-glycoprotein and other ABC drug transporters at the blood-brain barrier
    • Miller, D.S. Regulation of P-glycoprotein and other ABC drug transporters at the blood-brain barrier. Trends Pharmacol. Sci. 2010, 31, 246-254.
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 246-254
    • Miller, D.S.1
  • 98
  • 99
    • 0037134795 scopus 로고    scopus 로고
    • Functional analysis of MRP1 cloned from bovine
    • Taguchi, Y.; Saeki, K.; Komano, T. Functional analysis of MRP1 cloned from bovine. FEBS Lett. 2002, 521, 211-213.
    • (2002) FEBS Lett. , vol.521 , pp. 211-213
    • Taguchi, Y.1    Saeki, K.2    Komano, T.3
  • 100
    • 0029939542 scopus 로고    scopus 로고
    • Structure and expression of the messenger RNA encoding the murine multidrug resistance protein, an ATP-binding cassette transporter
    • Stride, B.D.; Valdimarsson, G.; Gerlach, J.H.; Wilson, G.M.; Cole, S.P.; Deeley, R.G. Structure and expression of the messenger RNA encoding the murine multidrug resistance protein, an ATP-binding cassette transporter. Mol. Pharmacol. 1996, 49, 962-971.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 962-971
    • Stride, B.D.1    Valdimarsson, G.2    Gerlach, J.H.3    Wilson, G.M.4    Cole, S.P.5    Deeley, R.G.6
  • 103
    • 22344432207 scopus 로고    scopus 로고
    • Tissue distribution and hepatic and renal ontogeny of the multidrug resistance-associated protein (Mrp) family in mice
    • Maher, J.M.; Slitt, A.L.; Cherrington, N.J.; Cheng, X.; Klaassen, C.D. Tissue distribution and hepatic and renal ontogeny of the multidrug resistance-associated protein (Mrp) family in mice. Drug Metab. Dispos. 2005, 33, 947-955.
    • (2005) Drug Metab. Dispos. , vol.33 , pp. 947-955
    • Maher, J.M.1    Slitt, A.L.2    Cherrington, N.J.3    Cheng, X.4    Klaassen, C.D.5
  • 104
    • 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, G.L.; van der Valk, M.; van der Valk, P.; Beijnen, J.H.; Scheper, R.J.; Borst, P. Multidrug resistance protein 1 protects the oropharyngeal mucosal layer and the testicular tubules against drug-induced damage. J .Exp. Med. 1998, 188, 797-808.
    • (1998) J .Exp. Med. , vol.188 , pp. 797-808
    • Wijnholds, J.1    Scheffer, G.L.2    Van Der Valk, M.3    Van Der Valk, P.4    Beijnen, J.H.5    Scheper, R.J.6    Borst, P.7
  • 105
    • 0035794228 scopus 로고    scopus 로고
    • Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1
    • Qian, Y.M.; Song, W.C.; Cui, H.; Cole, S.P.; Deeley, R.G. Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1. J. Biol. Chem. 2001, 276, 6404-6411.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6404-6411
    • Qian, Y.M.1    Song, W.C.2    Cui, H.3    Cole, S.P.4    Deeley, R.G.5
  • 107
    • 34250824087 scopus 로고    scopus 로고
    • Multidrug resistance protein 1 (MRP1) in rabbit conjunctival epithelial cells: Its effect on drug efflux and its regulation by adenoviral infection
    • Yang, J.J.; Ann, D.K.; Kannan, R.; Lee, V.H. Multidrug resistance protein 1 (MRP1) in rabbit conjunctival epithelial cells: Its effect on drug efflux and its regulation by adenoviral infection. Pharm. Res. 2007, 24, 1490-500.
    • (2007) Pharm. Res. , vol.24 , pp. 1490-1500
    • Yang, J.J.1    Ann, D.K.2    Kannan, R.3    Lee, V.H.4
  • 108
    • 0029133131 scopus 로고
    • Expression of the MRP gene-encoded conjugate export pump in liver and its selective absence from the canalicular membrane in transport-deficient mutant hepatocytes
    • Mayer, R.; Kartenbeck, J.; Buchler, M.; Jedlitschky, G.; Leier, I.; Keppler, D. Expression of the MRP gene-encoded conjugate export pump in liver and its selective absence from the canalicular membrane in transport-deficient mutant hepatocytes. J. Cell. Biol. 1995, 131, 137-150.
    • (1995) J. Cell. Biol. , vol.131 , pp. 137-150
    • Mayer, R.1    Kartenbeck, J.2    Buchler, M.3    Jedlitschky, G.4    Leier, I.5    Keppler, D.6
  • 110
    • 0036122824 scopus 로고    scopus 로고
    • Increased expression of multidrug resistance-associated protein 1 (MRP1) in hepatocyte basolateral membrane and renal tubular epithelia after bile duct ligation in rats
    • Pei, Q.L.; Kobayashi, Y.; Tanaka, Y.; Taguchi, Y.; Higuchi, K.; Kaito, M.; Ma, N.; Semba, R.; Kamisako, T.; Adachi, Y. Increased expression of multidrug resistance-associated protein 1 (MRP1) in hepatocyte basolateral membrane and renal tubular epithelia after bile duct ligation in rats. Hepatol. Res. 2002, 22, 58-64.
    • (2002) Hepatol. Res. , vol.22 , pp. 58-64
    • Pei, Q.L.1    Kobayashi, Y.2    Tanaka, Y.3    Taguchi, Y.4    Higuchi, K.5    Kaito, M.6    Ma, N.7    Semba, R.8    Kamisako, T.9    Adachi, Y.10
  • 113
    • 6344240461 scopus 로고    scopus 로고
    • Plasma membrane localization of multidrug resistance-associated protein homologs in brain capillary endothelial cells
    • Zhang, Y.; Schuetz, J.D.; Elmquist, W.F.; Miller, D.W. Plasma membrane localization of multidrug resistance-associated protein homologs in brain capillary endothelial cells. J. Pharmacol. Exp. Ther. 2004, 311, 449-455.
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 449-455
    • Zhang, Y.1    Schuetz, J.D.2    Elmquist, W.F.3    Miller, D.W.4
  • 114
    • 0028171453 scopus 로고
    • Detection of the Mr 190,000 multidrug resistance protein, MRP, with monoclonal antibodies
    • Hipfner, D.R.; Gauldie, S.D.; Deeley, R.G.; Cole, S.P. Detection of the Mr 190,000 multidrug resistance protein, MRP, with monoclonal antibodies. Cancer Res. 1994, 54, 5788-5792.
    • (1994) Cancer Res. , vol.54 , pp. 5788-5792
    • Hipfner, D.R.1    Gauldie, S.D.2    Deeley, R.G.3    Cole, S.P.4
  • 115
    • 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, C.J.; Cole, S.P.; Deeley, R.G. Role of the NH2-terminal membrane spanning domain of multidrug resistance protein 1/ABCC1 in protein processing and trafficking. Mol. Biol. Cell 2005, 16, 2483-2492.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2483-2492
    • Westlake, C.J.1    Cole, S.P.2    Deeley, R.G.3
  • 117
    • 0041968944 scopus 로고    scopus 로고
    • Subcellular localization and activity of multidrug resistance proteins
    • Rajagopal, A.; Simon, S.M. Subcellular localization and activity of multidrug resistance proteins. Mol. Biol. Cell 2003, 14, 3389-3399.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3389-3399
    • Rajagopal, A.1    Simon, S.M.2
  • 121
    • 0034502842 scopus 로고    scopus 로고
    • Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1)
    • Bakos, E.; Evers, R.; Calenda, G.; Tusnady, G.E.; Szakacs, G.; Varadi, A.; Sarkadi, B. Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1). J. Cell Sci. 2000, 113 Pt 24, 4451-4461. (Pubitemid 32117906)
    • (2000) Journal of Cell Science , vol.113 , Issue.24 , pp. 4451-4461
    • Bakos, E.1    Evers, R.2    Calenda, G.3    Tusnady, G.E.4    Szakacs, G.5    Varadi, A.6    Sarkadi, B.7
  • 122
    • 0344629891 scopus 로고    scopus 로고
    • Identification of the structural and functional boundaries of the multidrug resistance protein 1 cytoplasmic loop 3
    • Westlake, C.J.; Qian, Y.M.; Gao, M.; Vasa, M.; Cole, S.P.; Deeley, R.G. Identification of the structural and functional boundaries of the multidrug resistance protein 1 cytoplasmic loop 3. Biochemistry 2003, 42, 14099-14113.
    • (2003) Biochemistry , vol.42 , pp. 14099-14113
    • Westlake, C.J.1    Qian, Y.M.2    Gao, M.3    Vasa, M.4    Cole, S.P.5    Deeley, R.G.6
  • 123
    • 0028080927 scopus 로고
    • Overexpression of the multidrug resistance-associated protein (MRP) gene in vincristine but not doxorubicin-selected multidrug-resistant murine erythroleukemia cells
    • Slapak, C.A.; Fracasso, P.M.; Martell, R.L.; Toppmeyer, D.L.; Lecerf, J.M.; Levy, S.B. Overexpression of the multidrug resistance-associated protein (MRP) gene in vincristine but not doxorubicin-selected multidrug-resistant murine erythroleukemia cells. Cancer Res. 1994, 54, 5607-5613.
    • (1994) Cancer Res. , vol.54 , pp. 5607-5613
    • Slapak, C.A.1    Fracasso, P.M.2    Martell, R.L.3    Toppmeyer, D.L.4    Lecerf, J.M.5    Levy, S.B.6
  • 124
    • 0032493638 scopus 로고    scopus 로고
    • Coordinated action of glutathione S-transferases (GSTs) and multidrug resistance protein 1 (MRP1) in antineoplastic drug detoxification. Mechanism of GST A1-1- and MRP1-associated resistance to chlorambucil in MCF7 breast carcinoma cells
    • Morrow, C.S.; Smitherman, P.K.; Diah, S.K.; Schneider, E.; Townsend, A.J. Coordinated action of glutathione S-transferases (GSTs) and multidrug resistance protein 1 (MRP1) in antineoplastic drug detoxification. Mechanism of GST A1-1- and MRP1-associated resistance to chlorambucil in MCF7 breast carcinoma cells. J. Biol. Chem. 1998, 273, 20114-20120.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20114-20120
    • Morrow, C.S.1    Smitherman, P.K.2    Diah, S.K.3    Schneider, E.4    Townsend, A.J.5
  • 125
    • 33644777840 scopus 로고    scopus 로고
    • Multidrug resistance protein 1 (MRP1, ABCC1) mediates resistance to mitoxantrone via glutathione-dependent drug efflux
    • Morrow, C.S.; Peklak-Scott, C.; Bishwokarma, B.; Kute, T.E.; Smitherman, P.K.; Townsend, A.J. Multidrug resistance protein 1 (MRP1, ABCC1) mediates resistance to mitoxantrone via glutathione-dependent drug efflux. Mol. Pharmacol. 2006, 69, 1499-1505.
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1499-1505
    • Morrow, C.S.1    Peklak-Scott, C.2    Bishwokarma, B.3    Kute, T.E.4    Smitherman, P.K.5    Townsend, A.J.6
  • 128
    • 0032446450 scopus 로고    scopus 로고
    • Enhancement of glucuronosyl etoposide transport by glutathione in multidrug resistance-associated protein-overexpressing cells
    • Sakamoto, H.; Hara, H.; Hirano, K.; Adachi, T. Enhancement of glucuronosyl etoposide transport by glutathione in multidrug resistance-associated protein-overexpressing cells. Cancer Lett. 1999, 135, 113-119.
    • (1999) Cancer Lett. , vol.135 , pp. 113-119
    • Sakamoto, H.1    Hara, H.2    Hirano, K.3    Adachi, T.4
  • 131
    • 0037470032 scopus 로고    scopus 로고
    • Loss of multidrug resistance protein 1 expression and folate efflux activity results in a highly concentrative folate transport in human leukemia cells
    • Assaraf, Y.G.; Rothem, L.; Hooijberg, J.H.; Stark, M.; Ifergan, I.; Kathmann, I.; Dijkmans, B.A.; Peters, G.J.; Jansen, G. Loss of multidrug resistance protein 1 expression and folate efflux activity results in a highly concentrative folate transport in human leukemia cells. J. Biol. Chem. 2003, 278, 6680-6686.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6680-6686
    • Assaraf, Y.G.1    Rothem, L.2    Hooijberg, J.H.3    Stark, M.4    Ifergan, I.5    Kathmann, I.6    Dijkmans, B.A.7    Peters, G.J.8    Jansen, G.9
  • 132
    • 0035476729 scopus 로고    scopus 로고
    • Transport of methotrexate (MTX) and folates by multidrug resistance protein (MRP) 3 and MRP1: Effect of polyglutamylation on MTX transport
    • Zeng, H.; Chen, Z.S.; Belinsky, M.G.; Rea, P.A.; Kruh, G.D. Transport of methotrexate (MTX) and folates by multidrug resistance protein (MRP) 3 and MRP1: Effect of polyglutamylation on MTX transport. Cancer Res. 2001, 61, 7225-7232.
    • (2001) Cancer Res. , vol.61 , pp. 7225-7232
    • Zeng, H.1    Chen, Z.S.2    Belinsky, M.G.3    Rea, P.A.4    Kruh, G.D.5
  • 134
    • 0035896509 scopus 로고    scopus 로고
    • Role of multidrug resistance protein 1 (MRP1) and glutathione S-transferase A1-1 in alkylating agent resistance. Kinetics of glutathione conjugate formation and efflux govern differential cellular sensitivity to chlorambucil versus melphalan toxicity
    • Paumi, C.M.; Ledford, B.G.; Smitherman, P.K.; Townsend, A.J.; Morrow, C.S. Role of multidrug resistance protein 1 (MRP1) and glutathione S-transferase A1-1 in alkylating agent resistance. Kinetics of glutathione conjugate formation and efflux govern differential cellular sensitivity to chlorambucil versus melphalan toxicity. J. Biol. Chem. 2001, 276, 7952-7956.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7952-7956
    • Paumi, C.M.1    Ledford, B.G.2    Smitherman, P.K.3    Townsend, A.J.4    Morrow, C.S.5
  • 136
    • 0022632982 scopus 로고
    • Cross-resistance to intercalating agents in an epipodophyllotoxin- resistant Chinese hamster ovary cell line: Evidence for a common intracellular target
    • Glisson, B.; Gupta, R.; Hodges, P.; Ross, W. Cross-resistance to intercalating agents in an epipodophyllotoxin-resistant Chinese hamster ovary cell line: Evidence for a common intracellular target. Cancer Res. 1986, 46, 1939-1942.
    • (1986) Cancer Res. , vol.46 , pp. 1939-1942
    • Glisson, B.1    Gupta, R.2    Hodges, P.3    Ross, W.4
  • 137
    • 0028844581 scopus 로고
    • Expression of multidrug resistanceassociated protein in NIH/3T3 cells confers multidrug resistance associated with increased drug efflux and altered intracellular drug distribution
    • Breuninger, L.M.; Paul, S.; Gaughan, K.; Miki, T.; Chan, A.; Aaronson, S.A.; Kruh, G.D. Expression of multidrug resistanceassociated protein in NIH/3T3 cells confers multidrug resistance associated with increased drug efflux and altered intracellular drug distribution. Cancer Res. 1995, 55, 5342-5347.
    • (1995) Cancer Res. , vol.55 , pp. 5342-5347
    • Breuninger, L.M.1    Paul, S.2    Gaughan, K.3    Miki, T.4    Chan, A.5    Aaronson, S.A.6    Kruh, G.D.7
  • 138
    • 0028009810 scopus 로고
    • Multidrug resistance-associated protein gene overexpression and reduced drug sensitivity of topoisomerase II in a human breast carcinoma MCF7 cell line selected for etoposide resistance
    • Schneider, E.; Horton, J.K.; Yang, C.H.; Nakagawa, M.; Cowan, K.H. Multidrug resistance-associated protein gene overexpression and reduced drug sensitivity of topoisomerase II in a human breast carcinoma MCF7 cell line selected for etoposide resistance. Cancer Res. 1994, 54, 152-158.
    • (1994) Cancer Res. , vol.54 , pp. 152-158
    • Schneider, E.1    Horton, J.K.2    Yang, C.H.3    Nakagawa, M.4    Cowan, K.H.5
  • 139
    • 0035878996 scopus 로고    scopus 로고
    • Resistance to mitoxantrone in multidrug-resistant MCF7 breast cancer cells: Evaluation of mitoxantrone transport and the role of multidrug resistance protein family proteins
    • Diah, S.K.; Smitherman, P.K.; Aldridge, J.; Volk, E.L.; Schneider, E.; Townsend, A.J.; Morrow, C.S. Resistance to mitoxantrone in multidrug-resistant MCF7 breast cancer cells: Evaluation of mitoxantrone transport and the role of multidrug resistance protein family proteins. Cancer Res. 2001, 61, 5461-5467.
    • (2001) Cancer Res. , vol.61 , pp. 5461-5467
    • Diah, S.K.1    Smitherman, P.K.2    Aldridge, J.3    Volk, E.L.4    Schneider, E.5    Townsend, A.J.6    Morrow, C.S.7
  • 140
    • 0037843545 scopus 로고    scopus 로고
    • Effect of the multidrug resistance protein on the transport of the antiandrogen flutamide
    • Grzywacz, M.J.; Yang, J.M.; Hait, W.N. Effect of the multidrug resistance protein on the transport of the antiandrogen flutamide. Cancer Res. 2003, 63, 2492-2498.
    • (2003) Cancer Res. , vol.63 , pp. 2492-2498
    • Grzywacz, M.J.1    Yang, J.M.2    Hait, W.N.3
  • 141
    • 0035142865 scopus 로고    scopus 로고
    • Human CYP1B1 and anticancer agent metabolism: Mechanism for tumor-specific drug inactivation?
    • Rochat, B.; Morsman, J.M.; Murray, G.I.; Figg, W.D.; McLeod, H.L. Human CYP1B1 and anticancer agent metabolism: Mechanism for tumor-specific drug inactivation? J. Pharmacol. Exp. Ther. 2001, 296, 537-541.
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 537-541
    • Rochat, B.1    Morsman, J.M.2    Murray, G.I.3    Figg, W.D.4    McLeod, H.L.5
  • 144
    • 0036839699 scopus 로고    scopus 로고
    • Direct evidence that saquinavir is transported by multidrug resistance-associated protein (MRP1) and canalicular multispecific organic anion transporter (MRP2)
    • Williams, G.C.; Liu, A.; Knipp, G.; Sinko, P.J. Direct evidence that saquinavir is transported by multidrug resistance-associated protein (MRP1) and canalicular multispecific organic anion transporter (MRP2). Antimicrob. Agents Chemother. 2002, 46, 3456-3462.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3456-3462
    • Williams, G.C.1    Liu, A.2    Knipp, G.3    Sinko, P.J.4
  • 145
    • 0031788927 scopus 로고    scopus 로고
    • Human immunodeficiency virus protease inhibitors serve as substrates for multidrug transporter proteins MDR1 and MRP1 but retain antiviral efficacy in cell lines expressing these transporters
    • Srinivas, R.V.; Middlemas, D.; Flynn, P.; Fridland, A. Human immunodeficiency virus protease inhibitors serve as substrates for multidrug transporter proteins MDR1 and MRP1 but retain antiviral efficacy in cell lines expressing these transporters. Antimicrob. Agents Chemother. 1998, 42, 3157-3162.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 3157-3162
    • Srinivas, R.V.1    Middlemas, D.2    Flynn, P.3    Fridland, A.4
  • 146
    • 0035958776 scopus 로고    scopus 로고
    • P-Glycoprotein and transporter MRP1 reduce HIV protease inhibitor uptake in CD4 cells: Potential for accelerated viral drug resistance?
    • Jones, K.; Bray, P.G.; Khoo, S.H.; Davey, R.A.; Meaden, E.R.; Ward, S.A.; Back, D.J. P-Glycoprotein and transporter MRP1 reduce HIV protease inhibitor uptake in CD4 cells: Potential for accelerated viral drug resistance? Aids 2001, 15, 1353-1358.
    • (2001) Aids , vol.15 , pp. 1353-1358
    • Jones, K.1    Bray, P.G.2    Khoo, S.H.3    Davey, R.A.4    Meaden, E.R.5    Ward, S.A.6    Back, D.J.7
  • 148
    • 0032518290 scopus 로고    scopus 로고
    • The drug transporter P-glycoprotein limits oral absorption and brain entry of HIV-1 protease inhibitors
    • Kim, R.B.; Fromm, M.F.; Wandel, C.; Leake, B.; Wood, A.J.; Roden, D.M.; Wilkinson, G.R. The drug transporter P-glycoprotein limits oral absorption and brain entry of HIV-1 protease inhibitors. J. Clin. Invest. 1998, 101, 289-294.
    • (1998) J. Clin. Invest. , vol.101 , pp. 289-294
    • Kim, R.B.1    Fromm, M.F.2    Wandel, C.3    Leake, B.4    Wood, A.J.5    Roden, D.M.6    Wilkinson, G.R.7
  • 149
    • 14344264538 scopus 로고    scopus 로고
    • P-glycoprotein and mutlidrug resistanceassociated proteins limit the brain uptake of saquinavir in mice
    • Park, S.; Sinko, P.J. P-glycoprotein and mutlidrug resistanceassociated proteins limit the brain uptake of saquinavir in mice. J. Pharmacol. Exp. Ther. 2005, 312, 1249-1256.
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 1249-1256
    • Park, S.1    Sinko, P.J.2
  • 151
  • 153
    • 0032530924 scopus 로고    scopus 로고
    • Direct binding of chloroquine to the multidrug resistance protein (MRP): Possible role for MRP in chloroquine drug transport and resistance in tumor cells
    • Vezmar, M.; Georges, E. Direct binding of chloroquine to the multidrug resistance protein (MRP): Possible role for MRP in chloroquine drug transport and resistance in tumor cells. Biochem. Pharmacol. 1998, 56, 733-742.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 733-742
    • Vezmar, M.1    Georges, E.2
  • 155
    • 34249035885 scopus 로고    scopus 로고
    • Transport of cryptotanshinone, a major active triterpenoid in Salvia miltiorrhiza bunge widely used in the treatment of stroke and Alzheimer's disease, across the blood-brain barrier
    • Yu, X.Y.; Lin, S.G.; Chen, X.; Zhou, Z.W.; Liang, J.; Duan, W.; Chowbay, B.; Wen, J.Y.; Chan, E.; Cao, J.; Li, C.G.; Zhou, S.F. Transport of cryptotanshinone, a major active triterpenoid in Salvia miltiorrhiza bunge widely used in the treatment of stroke and Alzheimer's disease, across the blood-brain barrier. Curr. Drug Metab. 2007, 8, 365-378.
    • (2007) Curr. Drug Metab. , vol.8 , pp. 365-378
    • Yu, X.Y.1    Lin, S.G.2    Chen, X.3    Zhou, Z.W.4    Liang, J.5    Duan, W.6    Chowbay, B.7    Wen, J.Y.8    Chan, E.9    Cao, J.10    Li, C.G.11    Zhou, S.F.12
  • 156
    • 34249093067 scopus 로고    scopus 로고
    • Role of P-Glycoprotein in the intestinal absorption of tanshinone IIA, a major active ingredient in the root of Salvia miltiorrhiza Bunge
    • DOI 10.2174/138920007780655450
    • Yu, X.Y.; Lin, S.G.; Zhou, Z.W.; Chen, X.; Liang, J.; Liu, P.Q.; Duan, W.; Chowbay, B.; Wen, J.Y.; Li, C.G.; Zhou, S.F. Role of Pglycoprotein in the intestinal absorption of tanshinone IIA, a major active ingredient in the root of Salvia miltiorrhiza Bunge. Curr. Drug Metab. 2007, 8, 325-340. (Pubitemid 46780062)
    • (2007) Current Drug Metabolism , vol.8 , Issue.4 , pp. 325-340
    • Yu, X.-Y.1    Lin, S.-G.2    Zhou, Z.-W.3    Chen, X.4    Liang, J.5    Liu, P.-Q.6    Duan, W.7    Chowbay, B.8    Wen, J.-Y.9    Li, C.-G.10    Zhou, S.-F.11
  • 157
    • 34147092656 scopus 로고    scopus 로고
    • Role of ATP-binding cassette drug transporters in the intestinal absorption of tanshinone IIB, one of the major active diterpenoids from the root of Salvia miltiorrhiza
    • DOI 10.1080/00498250701230559, PII 777020209
    • Yu, X.Y.; Zhou, Z.W.; Lin, S.G.; Chen, X.; Yu, X.Q.; Liang, J.; Duan, W.; Wen, J.Y.; Li, X.T.; Zhou, S.F. Role of ATP-binding cassette drug transporters in the intestinal absorption of tanshinone IIB, one of the major active diterpenoids from the root of Salvia miltiorrhiza. Xenobiotica 2007, 37, 375-415. (Pubitemid 46572883)
    • (2007) Xenobiotica , vol.37 , Issue.4 , pp. 375-415
    • Yu, X.-Y.1    Zhou, Z.-W.2    Lin, S.-G.3    Chen, X.4    Yu, X.-Q.5    Liang, J.6    Duan, W.7    Wen, J.-Y.8    Li, X.-T.9    Zhou, S.-F.10
  • 159
    • 34447118246 scopus 로고    scopus 로고
    • Role of Pglycoprotein in restricting the brain penetration of tanshinone IIA, a major active constituent from the root of Salvia miltiorrhiza Bunge, across the blood-brain barrier
    • Chen, X.; Zhou, Z.W.; Xue, C.C.; Li, X.X.; Zhou, S.F. Role of Pglycoprotein in restricting the brain penetration of tanshinone IIA, a major active constituent from the root of Salvia miltiorrhiza Bunge, across the blood-brain barrier. Xenobiotica 2007, 37, 635-678.
    • (2007) Xenobiotica , vol.37 , pp. 635-678
    • Chen, X.1    Zhou, Z.W.2    Xue, C.C.3    Li, X.X.4    Zhou, S.F.5
  • 160
    • 53349107914 scopus 로고    scopus 로고
    • Involvement of P-glycoprotein and multidrug resistance associated protein 1 in the transport of tanshinone IIB, a primary active diterpenoid quinone from the roots of Salvia miltiorrhiza, across the blood-brain barrier
    • Zhou, Z.W.; Chen, X.; Liang, J.; Yu, X.Y.; Wen, J.W.; Zhou, S.F. Involvement of P-glycoprotein and multidrug resistance associated protein 1 in the transport of tanshinone IIB, a primary active diterpenoid quinone from the roots of Salvia miltiorrhiza, across the blood-brain barrier. Drug Metab. Lett. 2007, 1, 205-217.
    • (2007) Drug Metab. Lett. , vol.1 , pp. 205-217
    • Zhou, Z.W.1    Chen, X.2    Liang, J.3    Yu, X.Y.4    Wen, J.W.5    Zhou, S.F.6
  • 161
    • 27844511101 scopus 로고    scopus 로고
    • Danshen: An overview of its chemistry, pharmacology, pharmacokinetics, and clinical use
    • Zhou, L.; Zuo, Z.; Chow, M.S. Danshen: An overview of its chemistry, pharmacology, pharmacokinetics, and clinical use. J. Clin. Pharmacol. 2005, 45, 1345-1359.
    • (2005) J. Clin. Pharmacol. , vol.45 , pp. 1345-1359
    • Zhou, L.1    Zuo, Z.2    Chow, M.S.3
  • 163
    • 0034257083 scopus 로고    scopus 로고
    • Effects of MDR1 and MDR3 Pglycoproteins, MRP1, and BCRP/MXR/ABCP on the transport of 99mTc-tetrofosmin
    • Chen, W.S.; Luker, K.E.; Dahlheimer, J.L.; Pica, C.M.; Luker, G.D.; Piwnica-Worms, D. Effects of MDR1 and MDR3 Pglycoproteins, MRP1, and BCRP/MXR/ABCP on the transport of 99mTc-tetrofosmin. Biochem. Pharmacol. 2000, 60, 413-426.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 413-426
    • Chen, W.S.1    Luker, K.E.2    Dahlheimer, J.L.3    Pica, C.M.4    Luker, G.D.5    Piwnica-Worms, D.6
  • 164
    • 0036290428 scopus 로고    scopus 로고
    • In vitro and in vivo hepatic transport of the magnetic resonance imaging contrast agent B22956/1: Role of MRP proteins
    • Lorusso, V.; Pascolo, L.; Fernetti, C.; Visigalli, M.; Anelli, P.; Tiribelli, C. In vitro and in vivo hepatic transport of the magnetic resonance imaging contrast agent B22956/1: Role of MRP proteins. Biochem. Biophys. Res. Commun. 2002, 293, 100-105.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 100-105
    • Lorusso, V.1    Pascolo, L.2    Fernetti, C.3    Visigalli, M.4    Anelli, P.5    Tiribelli, C.6
  • 165
    • 3543045528 scopus 로고    scopus 로고
    • Arsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required
    • Leslie, E.M.; Haimeur, A.; Waalkes, M.P. Arsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required. J. Biol. Chem. 2004, 279, 32700-32708.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32700-32708
    • Leslie, E.M.1    Haimeur, A.2    Waalkes, M.P.3
  • 166
    • 0035844142 scopus 로고    scopus 로고
    • Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport
    • Ito, K.; Olsen, S.L.; Qiu, W.; Deeley, R.G.; Cole, S.P. Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport. J. Biol. Chem. 2001, 276, 15616-15624.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15616-15624
    • Ito, K.1    Olsen, S.L.2    Qiu, W.3    Deeley, R.G.4    Cole, S.P.5
  • 167
    • 0036255533 scopus 로고    scopus 로고
    • The MRP1- mediated effluxes of arsenic and antimony do not require arsenicglutathione and antimony-glutathione complex formation
    • Salerno, M.; Petroutsa, M.; Garnier-Suillerot, A. The MRP1- mediated effluxes of arsenic and antimony do not require arsenicglutathione and antimony-glutathione complex formation. J. Bioenerg. Biomembr. 2002, 34, 135-145.
    • (2002) J. Bioenerg. Biomembr. , vol.34 , pp. 135-145
    • Salerno, M.1    Petroutsa, M.2    Garnier-Suillerot, A.3
  • 168
    • 0036295810 scopus 로고    scopus 로고
    • Role of the multidrug resistance protein 1 in protection from heavy metal oxyanions: Investigations in vitro and in MRP1-deficient mice
    • Lorico, A.; Bertola, A.; Baum, C.; Fodstad, O.; Rappa, G. Role of the multidrug resistance protein 1 in protection from heavy metal oxyanions: Investigations in vitro and in MRP1-deficient mice. Biochem. Biophys. Res. Commun. 2002, 291, 617-622.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 617-622
    • Lorico, A.1    Bertola, A.2    Baum, C.3    Fodstad, O.4    Rappa, G.5
  • 169
    • 0034925678 scopus 로고    scopus 로고
    • Overexpression of glutathione S-transferase II and multidrug resistance transport proteins is associated with acquired tolerance to inorganic arsenic
    • Liu, J.; Chen, H.; Miller, D.S.; Saavedra, J.E.; Keefer, L.K.; Johnson, D.R.; Klaassen, C.D.; Waalkes, M.P. Overexpression of glutathione S-transferase II and multidrug resistance transport proteins is associated with acquired tolerance to inorganic arsenic. Mol. Pharmacol. 2001, 60, 302-309.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 302-309
    • Liu, J.1    Chen, H.2    Miller, D.S.3    Saavedra, J.E.4    Keefer, L.K.5    Johnson, D.R.6    Klaassen, C.D.7    Waalkes, M.P.8
  • 170
    • 0030450845 scopus 로고    scopus 로고
    • Double knockout of the MRP gene leads to increased drug sensitivity in vitro
    • Lorico, A.; Rappa, G.; Flavell, R.A.; Sartorelli, A.C. Double knockout of the MRP gene leads to increased drug sensitivity in vitro. Cancer Res. 1996, 56, 5351-5355.
    • (1996) Cancer Res. , vol.56 , pp. 5351-5355
    • Lorico, A.1    Rappa, G.2    Flavell, R.A.3    Sartorelli, A.C.4
  • 171
    • 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, E.M.; Letourneau, I.J.; Deeley, R.G.; Cole, S.P. Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1). Biochemistry 2003, 42, 5214-5224.
    • (2003) Biochemistry , vol.42 , pp. 5214-5224
    • Leslie, E.M.1    Letourneau, I.J.2    Deeley, R.G.3    Cole, S.P.4
  • 172
    • 0030962253 scopus 로고    scopus 로고
    • ATP-dependent transport of aflatoxin B1 and its glutathione conjugates by the product of the multidrug resistance protein (MRP) gene
    • Loe, D.W.; Stewart, R.K.; Massey, T.E.; Deeley, R.G.; Cole, S.P. ATP-dependent transport of aflatoxin B1 and its glutathione conjugates by the product of the multidrug resistance protein (MRP) gene. Mol. Pharmacol. 1997, 51, 1034-1041.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 1034-1041
    • Loe, D.W.1    Stewart, R.K.2    Massey, T.E.3    Deeley, R.G.4    Cole, S.P.5
  • 173
    • 0037186337 scopus 로고    scopus 로고
    • Role of the multidrug resistance protein 1 gene in the carcinogenicity of aflatoxin B1: Investigations using mrp1-null mice
    • DOI 10.1016/S0300-483X(01)00584-4, PII S0300483X01005844
    • Lorico, A.; Nesland, J.; Emilsen, E.; Fodstad, O.; Rappa, G. Role of the multidrug resistance protein 1 gene in the carcinogenicity of aflatoxin B1: Investigations using Mrp1-null mice. Toxicology 2002, 171, 201-205. (Pubitemid 34142493)
    • (2002) Toxicology , vol.171 , Issue.2-3 , pp. 201-205
    • Lorico, A.1    Nesland, J.2    Emilsen, E.3    Fodstad, O.4    Rappa, G.5
  • 175
    • 0033152624 scopus 로고    scopus 로고
    • Detoxification of 1-chloro-2,4-dinitrobenzene in MCF7 breast cancer cells expressing glutathione S-transferase P1-1 and/or multidrug resistance protein 1
    • Diah, S.K.; Smitherman, P.K.; Townsend, A.J.; Morrow, C.S. Detoxification of 1-chloro-2,4-dinitrobenzene in MCF7 breast cancer cells expressing glutathione S-transferase P1-1 and/or multidrug resistance protein 1. Toxicol. Appl. Pharmacol. 1999, 157, 85-93.
    • (1999) Toxicol. Appl. Pharmacol. , vol.157 , pp. 85-93
    • Diah, S.K.1    Smitherman, P.K.2    Townsend, A.J.3    Morrow, C.S.4
  • 176
    • 0031867669 scopus 로고    scopus 로고
    • Multidrug resistance protein and glutathione Stransferase P1-1 act in synergy to confer protection from 4- nitroquinoline 1-oxide toxicity
    • Morrow, C.S.; Diah, S.; Smitherman, P.K.; Schneider, E.; Townsend, A.J. Multidrug resistance protein and glutathione Stransferase P1-1 act in synergy to confer protection from 4- nitroquinoline 1-oxide toxicity. Carcinogenesis 1998, 19, 109-115.
    • (1998) Carcinogenesis , vol.19 , pp. 109-115
    • Morrow, C.S.1    Diah, S.2    Smitherman, P.K.3    Schneider, E.4    Townsend, A.J.5
  • 177
    • 0035958862 scopus 로고    scopus 로고
    • Transport of the β-O-glucuronide conjugate of the tobacco-specific carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)- 1-butanol (NNAL) by the multidrug resistance protein 1 (MRP1). Requirement for glutathione or a non-sulfur-containing analog
    • Leslie, E.M.; Ito, K.; Upadhyaya, P.; Hecht, S.S.; Deeley, R.G.; Cole, S.P. Transport of the β-O-glucuronide conjugate of the tobacco-specific carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)- 1-butanol (NNAL) by the multidrug resistance protein 1 (MRP1). Requirement for glutathione or a non-sulfur-containing analog. J. Biol. Chem. 2001, 276, 27846-27854.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27846-27854
    • Leslie, E.M.1    Ito, K.2    Upadhyaya, P.3    Hecht, S.S.4    Deeley, R.G.5    Cole, S.P.6
  • 178
    • 0028001416 scopus 로고
    • ATP-dependent transport of glutathione S-conjugates by the multidrug resistance-associated protein
    • Jedlitschky, G.; Leier, I.; Buchholz, U.; Center, M.; Keppler, D. ATP-dependent transport of glutathione S-conjugates by the multidrug resistance-associated protein. Cancer Res. 1994, 54, 4833-4836.
    • (1994) Cancer Res. , vol.54 , pp. 4833-4836
    • Jedlitschky, G.1    Leier, I.2    Buchholz, U.3    Center, M.4    Keppler, D.5
  • 179
    • 0037443509 scopus 로고    scopus 로고
    • Kinetic analysis of fluorescein and dihydrofluorescein effluxes in tumour cells expressing the multidrug resistance protein, MRP1
    • Saengkhae, C.; Loetchutinat, C.; Garnier-Suillerot, A. Kinetic analysis of fluorescein and dihydrofluorescein effluxes in tumour cells expressing the multidrug resistance protein, MRP1. Biochem. Pharmacol. 2003, 65, 969-977.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 969-977
    • Saengkhae, C.1    Loetchutinat, C.2    Garnier-Suillerot, A.3
  • 180
    • 0042823385 scopus 로고    scopus 로고
    • Kinetic analysis of rhodamines efflux mediated by the multidrug resistance protein (MRP1)
    • Saengkhae, C.; Loetchutinat, C.; Garnier-Suillerot, A. Kinetic analysis of rhodamines efflux mediated by the multidrug resistance protein (MRP1). Biophys. J. 2003, 85, 2006-2014.
    • (2003) Biophys. J. , vol.85 , pp. 2006-2014
    • Saengkhae, C.1    Loetchutinat, C.2    Garnier-Suillerot, A.3
  • 181
    • 0035870580 scopus 로고    scopus 로고
    • Detection of MRP functional activity: Calcein AM but not BCECF AM as a multidrug resistancerelated protein (MRP1) substrate
    • Olson, D.P.; Taylor, B.J.; Ivy, S.P. Detection of MRP functional activity: Calcein AM but not BCECF AM as a multidrug resistancerelated protein (MRP1) substrate. Cytometry 2001, 46, 105-113.
    • (2001) Cytometry , vol.46 , pp. 105-113
    • Olson, D.P.1    Taylor, B.J.2    Ivy, S.P.3
  • 182
    • 0035879951 scopus 로고    scopus 로고
    • Influences of glutathione on anionic substrate efflux in tumour cells expressing the multidrug resistance-associated protein, MRP1
    • Bagrij, T.; Klokouzas, A.; Hladky, S.B.; Barrand, M.A. Influences of glutathione on anionic substrate efflux in tumour cells expressing the multidrug resistance-associated protein, MRP1. Biochem. Pharmacol. 2001, 62, 199-206.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 199-206
    • Bagrij, T.1    Klokouzas, A.2    Hladky, S.B.3    Barrand, M.A.4
  • 183
    • 0036449401 scopus 로고    scopus 로고
    • Monitoring intracellular pH changes in response to osmotic stress and membrane transport activity using 5-chloromethylfluorescein
    • Salvi, A.; Quillan, J.M.; Sadee, W. Monitoring intracellular pH changes in response to osmotic stress and membrane transport activity using 5-chloromethylfluorescein. AAPS Pharm. Sci. 2002, 4, E21.
    • (2002) AAPS Pharm. Sci. , vol.4
    • Salvi, A.1    Quillan, J.M.2    Sadee, W.3
  • 184
    • 0034650332 scopus 로고    scopus 로고
    • The multidrug resistance protein 1: A functionally important activation marker for murine Th1 cells
    • Prechtl, S.; Roellinghoff, M.; Scheper, R.; Cole, S.P.; Deeley, R.G.; Lohoff, M. The multidrug resistance protein 1: A functionally important activation marker for murine Th1 cells. J. Immunol. 2000, 164, 754-761.
    • (2000) J. Immunol. , vol.164 , pp. 754-761
    • Prechtl, S.1    Roellinghoff, M.2    Scheper, R.3    Cole, S.P.4    Deeley, R.G.5    Lohoff, M.6
  • 185
    • 0032855145 scopus 로고    scopus 로고
    • Export pumps for anionic conjugates encoded by MRP genes
    • Keppler, D.; Cui, Y.; Konig, J.; Leier, I.; Nies, A. Export pumps for anionic conjugates encoded by MRP genes. Adv. Enzyme Regul. 1999, 39, 237-246.
    • (1999) Adv. Enzyme Regul. , vol.39 , pp. 237-246
    • Keppler, D.1    Cui, Y.2    Konig, J.3    Leier, I.4    Nies, A.5
  • 186
    • 2142648906 scopus 로고    scopus 로고
    • Evaluation and comparison of MRP1 activity with three fluorescent dyes and three modulators in leukemic cell lines
    • Dogan, A.L.; Legrand, O.; Faussat, A.M.; Perrot, J.Y.; Marie, J.P. Evaluation and comparison of MRP1 activity with three fluorescent dyes and three modulators in leukemic cell lines. Leuk. Res. 2004, 28, 619-622.
    • (2004) Leuk. Res. , vol.28 , pp. 619-622
    • Dogan, A.L.1    Legrand, O.2    Faussat, A.M.3    Perrot, J.Y.4    Marie, J.P.5
  • 187
    • 7444248391 scopus 로고    scopus 로고
    • The human multidrug-resistance-associated protein MRP1 mediates ATP-dependent transport of unconjugated bilirubin
    • Rigato, I.; Pascolo, L.; Fernetti, C.; Ostrow, J.D.; Tiribelli, C. The human multidrug-resistance-associated protein MRP1 mediates ATP-dependent transport of unconjugated bilirubin. Biochem. J. 2004, 383, 335-341.
    • (2004) Biochem. J. , vol.383 , pp. 335-341
    • Rigato, I.1    Pascolo, L.2    Fernetti, C.3    Ostrow, J.D.4    Tiribelli, C.5
  • 188
  • 189
    • 0029789027 scopus 로고    scopus 로고
    • Induction of MRP/GS-X pump and cellular resistance to anticancer prostaglandins
    • Akimaru, K.; Kuo, M.T.; Furuta, K.; Suzuki, M.; Noyori, R.; Ishikawa, T. Induction of MRP/GS-X pump and cellular resistance to anticancer prostaglandins. Cytotechnology 1996, 19, 221-227.
    • (1996) Cytotechnology , vol.19 , pp. 221-227
    • Akimaru, K.1    Kuo, M.T.2    Furuta, K.3    Suzuki, M.4    Noyori, R.5    Ishikawa, T.6
  • 190
    • 0029918142 scopus 로고    scopus 로고
    • ATPdependent 17 β-estradiol 17-(β-D-glucuronide) transport by multidrug resistance protein (MRP). Inhibition by cholestatic steroids
    • Loe, D.W.; Almquist, K.C.; Cole, S.P.; Deeley, R.G. ATPdependent 17 β-estradiol 17-(β-D-glucuronide) transport by multidrug resistance protein (MRP). Inhibition by cholestatic steroids. J. Biol. Chem. 1996, 271, 9683-9689.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9683-9689
    • Loe, D.W.1    Almquist, K.C.2    Cole, S.P.3    Deeley, R.G.4
  • 191
    • 0030009305 scopus 로고    scopus 로고
    • 4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transport
    • 4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transport. J. Biol. Chem. 1996, 271, 9675-9682.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9675-9682
    • Loe, D.W.1    Almquist, K.C.2    Deeley, R.G.3    Cole, S.P.4
  • 192
    • 0032534064 scopus 로고    scopus 로고
    • Characterization of vincristine transport by the Mr 190,000 multidrug resistance protein (MRP): Evidence for cotransport with reduced glutathione
    • Loe, D.W.; Deeley, R.G.; Cole, S.P. Characterization of vincristine transport by the Mr 190,000 multidrug resistance protein (MRP): Evidence for cotransport with reduced glutathione. Cancer Res. 1998, 58, 5130-5136.
    • (1998) Cancer Res. , vol.58 , pp. 5130-5136
    • Loe, D.W.1    Deeley, R.G.2    Cole, S.P.3
  • 194
    • 0030665969 scopus 로고    scopus 로고
    • Disruption of the murine MRP (multidrug resistance protein) gene leads to increased sensitivity to etoposide (VP-16) and increased levels of glutathione
    • Lorico, A.; Rappa, G.; Finch, R.A.; Yang, D.; Flavell, R.A.; Sartorelli, A.C. Disruption of the murine MRP (multidrug resistance protein) gene leads to increased sensitivity to etoposide (VP-16) and increased levels of glutathione. Cancer Res. 1997, 57, 5238-5242.
    • (1997) Cancer Res. , vol.57 , pp. 5238-5242
    • Lorico, A.1    Rappa, G.2    Finch, R.A.3    Yang, D.4    Flavell, R.A.5    Sartorelli, A.C.6
  • 195
    • 33845899686 scopus 로고    scopus 로고
    • Role of multidrug resistance-associated protein 1 expression in the in vitro susceptibility of rat nerve cell to unconjugated bilirubin
    • Falcao, A.S.; Bellarosa, C.; Fernandes, A.; Brito, M.A.; Silva, R.F.; Tiribelli, C.; Brites, D. Role of multidrug resistance-associated protein 1 expression in the in vitro susceptibility of rat nerve cell to unconjugated bilirubin. Neuroscience 2007, 144, 878-888.
    • (2007) Neuroscience , vol.144 , pp. 878-888
    • Falcao, A.S.1    Bellarosa, C.2    Fernandes, A.3    Brito, M.A.4    Silva, R.F.5    Tiribelli, C.6    Brites, D.7
  • 196
    • 0035917888 scopus 로고    scopus 로고
    • Mechanisms for the transport of unconjugated bilirubin in human trophoblastic BeWo cells
    • Pascolo, L.; Fernetti, C.; Garcia-Mediavilla, M.V.; Ostrow, J.D.; Tiribelli, C. Mechanisms for the transport of unconjugated bilirubin in human trophoblastic BeWo cells. FEBS Lett. 2001, 495, 94-99.
    • (2001) FEBS Lett. , vol.495 , pp. 94-99
    • Pascolo, L.1    Fernetti, C.2    Garcia-Mediavilla, M.V.3    Ostrow, J.D.4    Tiribelli, C.5
  • 197
    • 0034283373 scopus 로고    scopus 로고
    • Multidrug resistance protein MRP1 protects against the toxicity of the major lipid peroxidation product 4-hydroxynonenal
    • Renes, J.; de Vries, E.E.; Hooiveld, G.J.; Krikken, I.; Jansen, P.L.; Muller, M. Multidrug resistance protein MRP1 protects against the toxicity of the major lipid peroxidation product 4-hydroxynonenal. Biochem. J. 2000, 350(Pt 2), 555-561.
    • (2000) Biochem. J. , vol.350 , Issue.PART 2 , pp. 555-561
    • Renes, J.1    De Vries, E.E.2    Hooiveld, G.J.3    Krikken, I.4    Jansen, P.L.5    Muller, M.6
  • 198
    • 0029954845 scopus 로고    scopus 로고
    • Biology of the multidrug resistance-associated protein, MRP
    • Loe, D.W.; Deeley, R.G.; Cole, S.P. Biology of the multidrug resistance-associated protein, MRP. Eur. J. Cancer 1996, 32A, 945-957.
    • (1996) Eur. J. Cancer , vol.32 A , pp. 945-957
    • Loe, D.W.1    Deeley, R.G.2    Cole, S.P.3
  • 199
    • 0029821995 scopus 로고    scopus 로고
    • Multidrug resistance mediated by the multidrug resistance protein (MRP) gene
    • Lautier, D.; Canitrot, Y.; Deeley, R.G.; Cole, S.P. Multidrug resistance mediated by the multidrug resistance protein (MRP) gene. Biochem. Pharmacol. 1996, 52, 967-977.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 967-977
    • Lautier, D.1    Canitrot, Y.2    Deeley, R.G.3    Cole, S.P.4
  • 200
    • 0026089343 scopus 로고
    • Transgenic mice that express the human multidrugresistance gene in bone marrow enable a rapid identification of agents that reverse drug resistance
    • Mickisch, G.H.; Merlino, G.T.; Galski, H.; Gottesman, M.M.; Pastan, I. Transgenic mice that express the human multidrugresistance gene in bone marrow enable a rapid identification of agents that reverse drug resistance. Proc. Natl. Acad. Sci. U. S. A. 1991, 88, 547-551.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 547-551
    • Mickisch, G.H.1    Merlino, G.T.2    Galski, H.3    Gottesman, M.M.4    Pastan, I.5
  • 202
    • 0033377523 scopus 로고    scopus 로고
    • Physiology and pathology of the blood-brain barrier: Implications for microbial pathogenesis, drug delivery and neurodegenerative disorders
    • Banks, W.A. Physiology and pathology of the blood-brain barrier: Implications for microbial pathogenesis, drug delivery and neurodegenerative disorders. J. Neurovirol. 1999, 5, 538-555.
    • (1999) J. Neurovirol. , vol.5 , pp. 538-555
    • Banks, W.A.1
  • 203
    • 12344262373 scopus 로고    scopus 로고
    • Blood-brain barrier active efflux transporters: ATP-binding cassette gene family
    • Loscher, W.; Potschka, H. Blood-brain barrier active efflux transporters: ATP-binding cassette gene family. NeuroRx 2005, 2, 86-98.
    • (2005) NeuroRx , vol.2 , pp. 86-98
    • Loscher, W.1    Potschka, H.2
  • 204
    • 33750589959 scopus 로고    scopus 로고
    • Membrane transporter proteins: A challenge for CNS drug development
    • Girardin, F. Membrane transporter proteins: A challenge for CNS drug development. Dialogues Clin. Neurosci. 2006, 8, 311-321.
    • (2006) Dialogues Clin. Neurosci. , vol.8 , pp. 311-321
    • Girardin, F.1
  • 207
    • 0035866385 scopus 로고    scopus 로고
    • The pharmacological phenotype of combined multidrug-resistance mdr1a/1b- and mrp1-deficient mice
    • Johnson, D.R.; Finch, R.A.; Lin, Z.P.; Zeiss, C.J.; Sartorelli, A.C. The pharmacological phenotype of combined multidrug-resistance mdr1a/1b- and mrp1-deficient mice. Cancer Res. 2001, 61, 1469-1476.
    • (2001) Cancer Res. , vol.61 , pp. 1469-1476
    • Johnson, D.R.1    Finch, R.A.2    Lin, Z.P.3    Zeiss, C.J.4    Sartorelli, A.C.5
  • 211
    • 0036381121 scopus 로고    scopus 로고
    • Mice lacking the multidrug resistance protein 1 have a transiently impaired immune response during tuberculosis
    • Verbon, A.; Leemans, J.C.; Weijer, S.; Florquin, S.; Van Der Poll, T. Mice lacking the multidrug resistance protein 1 have a transiently impaired immune response during tuberculosis. Clin. Exp. Immunol. 2002, 130, 32-36.
    • (2002) Clin. Exp. Immunol. , vol.130 , pp. 32-36
    • Verbon, A.1    Leemans, J.C.2    Weijer, S.3    Florquin, S.4    Van Der Poll, T.5
  • 212
    • 63549110729 scopus 로고    scopus 로고
    • Development and characterization of a recombinant Madin-Darby canine kidney cell line that expresses rat multidrug resistance-associated protein 1 (rMRP1)
    • Yang, Z.; Horn, M.; Wang, J.; Shen, D.D.; Ho, R.J. Development and characterization of a recombinant Madin-Darby canine kidney cell line that expresses rat multidrug resistance-associated protein 1 (rMRP1). AAPS Pharm. Sci. 2004, 6, E8.
    • (2004) AAPS Pharm. Sci. , vol.6
    • Yang, Z.1    Horn, M.2    Wang, J.3    Shen, D.D.4    Ho, R.J.5
  • 213
    • 0035860688 scopus 로고    scopus 로고
    • Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: Evidence for functional interaction between transmembrane helices 14 and 17
    • Zhang, D.W.; Cole, S.P.; Deeley, R.G. Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: Evidence for functional interaction between transmembrane helices 14 and 17. J. Biol. Chem. 2001, 276, 34966-34974.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34966-34974
    • Zhang, D.W.1    Cole, S.P.2    Deeley, R.G.3
  • 214
    • 77958012886 scopus 로고    scopus 로고
    • Modulators of multidrug resistance associated proteins in the management of anticancer and antimicrobial drug resistance and the treatment of inflammatory diseases
    • Yang, A.K.; Zhou, Z.W.; Wei, M.Q.; Liu, J.P.; Zhou, S.F. Modulators of multidrug resistance associated proteins in the management of anticancer and antimicrobial drug resistance and the treatment of inflammatory diseases. Curr. Top. Med. Chem. 2010, 10, 1732-1756.
    • (2010) Curr. Top. Med. Chem. , vol.10 , pp. 1732-1756
    • Yang, A.K.1    Zhou, Z.W.2    Wei, M.Q.3    Liu, J.P.4    Zhou, S.F.5
  • 215
    • 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. 2005, 25, 453-472.
    • (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
  • 216
    • 73949118463 scopus 로고    scopus 로고
    • Reversing agents for ATP-binding cassette drug transporters
    • Lee, C.H. Reversing agents for ATP-binding cassette drug transporters. Methods Mol. Biol. 2010, 596, 325-340.
    • (2010) Methods Mol. Biol. , vol.596 , pp. 325-340
    • Lee, C.H.1
  • 217
    • 0030953774 scopus 로고    scopus 로고
    • Probenecid reverses multidrug resistance in multidrug resistanceassociated protein-overexpressing HL60/AR and H69/AR cells but not in P-glycoprotein-overexpressing HL60/Tax and P388/ADR cells
    • Gollapudi, S.; Kim, C.H.; Tran, B.N.; Sangha, S.; Gupta, S. Probenecid reverses multidrug resistance in multidrug resistanceassociated protein-overexpressing HL60/AR and H69/AR cells but not in P-glycoprotein- overexpressing HL60/Tax and P388/ADR cells. Cancer Chemother. Pharmacol. 1997, 40, 150-158.
    • (1997) Cancer Chemother. Pharmacol. , vol.40 , pp. 150-158
    • Gollapudi, S.1    Kim, C.H.2    Tran, B.N.3    Sangha, S.4    Gupta, S.5
  • 218
    • 0031053478 scopus 로고    scopus 로고
    • Indomethacin-mediated reversal of multidrug resistance and drug efflux in human and murine cell lines overexpressing MRP, but not P-glycoprotein
    • Draper, M.P.; Martell, R.L.; Levy, S.B. Indomethacin-mediated reversal of multidrug resistance and drug efflux in human and murine cell lines overexpressing MRP, but not P-glycoprotein. Br. J. Cancer 1997, 75, 810-815.
    • (1997) Br. J. Cancer , vol.75 , pp. 810-815
    • Draper, M.P.1    Martell, R.L.2    Levy, S.B.3
  • 219
    • 0034072174 scopus 로고    scopus 로고
    • Interactions of the human multidrug resistance proteins MRP1 and MRP2 with organic anions
    • Bakos, E.; Evers, R.; Sinko, E.; Varadi, A.; Borst, P.; Sarkadi, B. Interactions of the human multidrug resistance proteins MRP1 and MRP2 with organic anions. Mol. Pharmacol. 2000, 57, 760-768.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 760-768
    • Bakos, E.1    Evers, R.2    Sinko, E.3    Varadi, A.4    Borst, P.5    Sarkadi, B.6
  • 221
    • 33947365498 scopus 로고    scopus 로고
    • Emerging therapies in the long-term management of hyperuricaemia and gout
    • Stamp, L.K.; O'Donnell, J.L.; Chapman, P.T. Emerging therapies in the long-term management of hyperuricaemia and gout. Intern. Med. J. 2007, 37, 258-266.
    • (2007) Intern. Med. J. , vol.37 , pp. 258-266
    • Stamp, L.K.1    O'Donnell, J.L.2    Chapman, P.T.3
  • 222
    • 0033936291 scopus 로고    scopus 로고
    • Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export
    • Evers, R.; de Haas, M.; Sparidans, R.; Beijnen, J.; Wielinga, P.R.; Lankelma, J.; Borst, P. Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export. Br. J. Cancer 2000, 83, 375-383.
    • (2000) Br. J. Cancer , vol.83 , pp. 375-383
    • Evers, R.1    De Haas, M.2    Sparidans, R.3    Beijnen, J.4    Wielinga, P.R.5    Lankelma, J.6    Borst, P.7
  • 224
    • 0028986245 scopus 로고
    • The leukotriene LTD4 receptor antagonist MK571 specifically modulates MRP associated multidrug resistance
    • Gekeler, V.; Ise, W.; Sanders, K.H.; Ulrich, W.R.; Beck, J. The leukotriene LTD4 receptor antagonist MK571 specifically modulates MRP associated multidrug resistance. Biochem. Biophys. Res. Commun. 1995, 208, 345-352.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 345-352
    • Gekeler, V.1    Ise, W.2    Sanders, K.H.3    Ulrich, W.R.4    Beck, J.5
  • 225
    • 18044376796 scopus 로고    scopus 로고
    • Multidrug resistance proteins (MRPs) and implication in drug development
    • Tian, Q.; Zhang, J.; Chan, E.; Duan, W.; Zhou, S.F. Multidrug resistance proteins (MRPs) and implication in drug development. Drug Dev. Res. 2005, 51, 1-18.
    • (2005) Drug Dev. Res. , vol.51 , pp. 1-18
    • Tian, Q.1    Zhang, J.2    Chan, E.3    Duan, W.4    Zhou, S.F.5
  • 230
    • 33846932096 scopus 로고    scopus 로고
    • Contribution of UDP-glucuronosyltransferases 1A9 and 2B7 to the glucuronidation of indomethacin in the human liver
    • DOI 10.1007/s00228-007-0261-0
    • Mano, Y.; Usui, T.; Kamimura, H. Contribution of UDPglucuronosyltransferases 1A9 and 2B7 to the glucuronidation of indomethacin in the human liver. Eur. J. Clin. Pharmacol. 2007, 63, 289-296. (Pubitemid 46233157)
    • (2007) European Journal of Clinical Pharmacology , vol.63 , Issue.3 , pp. 289-296
    • Mano, Y.1    Usui, T.2    Kamimura, H.3
  • 231
    • 22344442057 scopus 로고    scopus 로고
    • Glucuronidation of nonsteroidal anti-inflammatory drugs: Identifying the enzymes responsible in human liver microsomes
    • Kuehl, G.E.; Lampe, J.W.; Potter, J.D.; Bigler, J. Glucuronidation of nonsteroidal anti-inflammatory drugs: Identifying the enzymes responsible in human liver microsomes. Drug Metab. Dispos. 2005, 33, 1027-1035.
    • (2005) Drug Metab. Dispos. , vol.33 , pp. 1027-1035
    • Kuehl, G.E.1    Lampe, J.W.2    Potter, J.D.3    Bigler, J.4
  • 232
    • 0027473114 scopus 로고
    • Chemosensitisation and drug accumulation effects of cyclosporin A, PSC-833 and verapamil in human MDR large cell lung cancer cells expressing a 190k membrane protein distinct from Pglycoprotein
    • Barrand, M.A.; Rhodes, T.; Center, M.S.; Twentyman, P.R. Chemosensitisation and drug accumulation effects of cyclosporin A, PSC-833 and verapamil in human MDR large cell lung cancer cells expressing a 190k membrane protein distinct from Pglycoprotein. Eur. J. Cancer 1993, 29A, 408-415.
    • (1993) Eur. J. Cancer , vol.29 A , pp. 408-415
    • Barrand, M.A.1    Rhodes, T.2    Center, M.S.3    Twentyman, P.R.4
  • 233
    • 0030878058 scopus 로고    scopus 로고
    • Modulation by (iso)flavonoids of the ATPase activity of the multidrug resistance protein
    • Hooijberg, J.H.; Broxterman, H.J.; Heijn, M.; Fles, D.L.; Lankelma, J.; Pinedo, H.M. Modulation by (iso)flavonoids of the ATPase activity of the multidrug resistance protein. FEBS Lett. 1997, 413, 344-348.
    • (1997) FEBS Lett. , vol.413 , pp. 344-348
    • Hooijberg, J.H.1    Broxterman, H.J.2    Heijn, M.3    Fles, D.L.4    Lankelma, J.5    Pinedo, H.M.6
  • 235
    • 0028136603 scopus 로고
    • Competitive inhibition by genistein and ATP dependence of daunorubicin transport in intact MRP overexpressing human small cell lung cancer cells
    • Versantvoort, C.H.; Broxterman, H.J.; Lankelma, J.; Feller, N.; Pinedo, H.M. Competitive inhibition by genistein and ATP dependence of daunorubicin transport in intact MRP overexpressing human small cell lung cancer cells. Biochem. Pharmacol. 1994, 48, 1129-1136.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1129-1136
    • Versantvoort, C.H.1    Broxterman, H.J.2    Lankelma, J.3    Feller, N.4    Pinedo, H.M.5
  • 236
    • 0037311322 scopus 로고    scopus 로고
    • Effect of flavonoids on MRP1-mediated transport in Panc-1 cells
    • Nguyen, H.; Zhang, S.; Morris, M.E. Effect of flavonoids on MRP1-mediated transport in Panc-1 cells. J. Pharm. Sci. 2003, 92, 250-257.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 250-257
    • Nguyen, H.1    Zhang, S.2    Morris, M.E.3
  • 237
    • 0034677912 scopus 로고    scopus 로고
    • Inhibition of the P-glycoprotein- and multidrug resistance proteinmediated efflux of anthracyclines and calceinacetoxymethyl ester by PAK-104P
    • Marbeuf-Gueye, C.; Salerno, M.; Quidu, P.; Garnier-Suillerot, A. Inhibition of the P-glycoprotein- and multidrug resistance proteinmediated efflux of anthracyclines and calceinacetoxymethyl ester by PAK-104P. Eur. J. Pharmacol. 2000, 391, 207-216.
    • (2000) Eur. J. Pharmacol. , vol.391 , pp. 207-216
    • Marbeuf-Gueye, C.1    Salerno, M.2    Quidu, P.3    Garnier-Suillerot, A.4
  • 238
    • 0034827621 scopus 로고    scopus 로고
    • Reversing effect of agosterol A, a spongean sterol acetate, on multidrug resistance in human carcinoma cells
    • Aoki, S.; Chen, Z.S.; Higasiyama, K.; Setiawan, A.; Akiyama, S.; Kobayashi, M. Reversing effect of agosterol A, a spongean sterol acetate, on multidrug resistance in human carcinoma cells. Jpn. J. Cancer Res. 2001, 92, 886-895.
    • (2001) Jpn. J. Cancer Res. , vol.92 , pp. 886-895
    • Aoki, S.1    Chen, Z.S.2    Higasiyama, K.3    Setiawan, A.4    Akiyama, S.5    Kobayashi, M.6
  • 240
    • 0031782105 scopus 로고    scopus 로고
    • S9788 modulation of P-glycoprotein- and multidrug-related protein-mediated multidrug resistance by Servier 9788 in doxorubicin-resistant MCF7 cells
    • Bichat, F.; Solis-Recendez, G.; Poullain, M.G.; Poupon, M.F.; Khayat, D.; Bastian, G. S9788 modulation of P-glycoprotein- and multidrug-related protein-mediated multidrug resistance by Servier 9788 in doxorubicin-resistant MCF7 cells. Biochem. Pharmacol. 1998, 56, 497-502.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 497-502
    • Bichat, F.1    Solis-Recendez, G.2    Poullain, M.G.3    Poupon, M.F.4    Khayat, D.5    Bastian, G.6
  • 241
    • 0031041043 scopus 로고    scopus 로고
    • Chemosensitization and drug accumulation effects of VX- 710, verapamil, cyclosporin A, MS-209 and GF120918 in multidrug resistant HL60/ADR cells expressing the multidrug resistance-associated protein MRP
    • Germann, U.A.; Ford, P.J.; Shlyakhter, D.; Mason, V.S.; Harding, M.W. Chemosensitization and drug accumulation effects of VX- 710, verapamil, cyclosporin A, MS-209 and GF120918 in multidrug resistant HL60/ADR cells expressing the multidrug resistance-associated protein MRP. Anticancer Drugs 1997, 8, 141-155.
    • (1997) Anticancer Drugs , vol.8 , pp. 141-155
    • Germann, U.A.1    Ford, P.J.2    Shlyakhter, D.3    Mason, V.S.4    Harding, M.W.5
  • 242
    • 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, K.L.; Pendyala, L.; Baer, M.R. 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. 2004, 10, 1826-1834.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 1826-1834
    • Minderman, H.1    O'Loughlin, K.L.2    Pendyala, L.3    Baer, M.R.4
  • 243
    • 0037084154 scopus 로고    scopus 로고
    • Budesonide reduces multidrug resistance-associated protein 1 expression in an airway epithelial cell line (Calu-1)
    • Bandi, N.; Kompella, U.B. Budesonide reduces multidrug resistance-associated protein 1 expression in an airway epithelial cell line (Calu-1). Eur. J. Pharmacol. 2002, 437, 9-17.
    • (2002) Eur. J. Pharmacol. , vol.437 , pp. 9-17
    • Bandi, N.1    Kompella, U.B.2
  • 244
    • 0033583767 scopus 로고    scopus 로고
    • Reversal of MRP-mediated multidrug resistance in human lung cancer cells by the antiprogestatin drug RU486
    • Payen, L.; Delugin, L.; Courtois, A.; Trinquart, Y.; Guillouzo, A.; Fardel, O. Reversal of MRP-mediated multidrug resistance in human lung cancer cells by the antiprogestatin drug RU486. Biochem. Biophys. Res. Commun. 1999, 258, 513-518.
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 513-518
    • Payen, L.1    Delugin, L.2    Courtois, A.3    Trinquart, Y.4    Guillouzo, A.5    Fardel, O.6
  • 245
    • 33845643674 scopus 로고    scopus 로고
    • Schisandrin B: A dual inhibitor of P-glycoprotein and multidrug resistance-associated protein 1
    • Sun, M.; Xu, X.; Lu, Q.; Pan, Q.; Hu, X. Schisandrin B: A dual inhibitor of P-glycoprotein and multidrug resistance-associated protein 1. Cancer Lett. 2007, 246, 300-307.
    • (2007) Cancer Lett. , vol.246 , pp. 300-307
    • Sun, M.1    Xu, X.2    Lu, Q.3    Pan, Q.4    Hu, X.5
  • 246
    • 0031635486 scopus 로고    scopus 로고
    • Development of novel reversal agents, imidazothiazole derivatives, targeting MDR1- and MRP-mediated multidrug resistance
    • Naito, S.; Koike, K.; Ono, M.; Machida, T.; Tasaka, S.; Kiue, A.; Koga, H.; Kumazawa, J. Development of novel reversal agents, imidazothiazole derivatives, targeting MDR1- and MRP-mediated multidrug resistance. Oncol. Res. 1998, 10, 123-132.
    • (1998) Oncol. Res. , vol.10 , pp. 123-132
    • Naito, S.1    Koike, K.2    Ono, M.3    Machida, T.4    Tasaka, S.5    Kiue, A.6    Koga, H.7    Kumazawa, J.8
  • 248
    • 33846233855 scopus 로고    scopus 로고
    • Dibenzocyclooctadiene lignans: A class of novel inhibitors of multidrug resistanceassociated protein 1
    • Li, L.; Pan, Q.; Sun, M.; Lu, Q.; Hu, X. Dibenzocyclooctadiene lignans: A class of novel inhibitors of multidrug resistanceassociated protein 1. Life Sci. 2007, 80, 741-748.
    • (2007) Life Sci. , vol.80 , pp. 741-748
    • Li, L.1    Pan, Q.2    Sun, M.3    Lu, Q.4    Hu, X.5
  • 249
    • 31044456677 scopus 로고    scopus 로고
    • Schisandrin B enhances doxorubicin-induced apoptosis of cancer cells but not normal cells
    • Li, L.; Lu, Q.; Shen, Y.; Hu, X. Schisandrin B enhances doxorubicin-induced apoptosis of cancer cells but not normal cells. Biochem. Pharmacol. 2006, 71, 584-595.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 584-595
    • Li, L.1    Lu, Q.2    Shen, Y.3    Hu, X.4
  • 250
    • 0035033774 scopus 로고    scopus 로고
    • Modulation of multidrug resistance protein 1 (MRP1/ABCC1) transport and atpase activities by interaction with dietary flavonoids
    • Leslie, E.M.; Mao, Q.; Oleschuk, C.J.; Deeley, R.G.; Cole, S.P. Modulation of multidrug resistance protein 1 (MRP1/ABCC1) transport and atpase activities by interaction with dietary flavonoids. Mol. Pharmacol. 2001, 59, 1171-1180.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1171-1180
    • Leslie, E.M.1    Mao, Q.2    Oleschuk, C.J.3    Deeley, R.G.4    Cole, S.P.5
  • 252
    • 33847366629 scopus 로고    scopus 로고
    • Inhibition of MRP1/ABCC1, MRP2/ABCC2, and MRP3/ABCC3 by nucleoside, nucleotide, and non-nucleoside reverse transcriptase inhibitors
    • Weiss, J.; Theile, D.; Ketabi-Kiyanvash, N.; Lindenmaier, H.; Haefeli, W.E. Inhibition of MRP1/ABCC1, MRP2/ABCC2, and MRP3/ABCC3 by nucleoside, nucleotide, and non-nucleoside reverse transcriptase inhibitors. Drug Metab. Dispos. 2007, 35, 340-344.
    • (2007) Drug Metab. Dispos. , vol.35 , pp. 340-344
    • Weiss, J.1    Theile, D.2    Ketabi-Kiyanvash, N.3    Lindenmaier, H.4    Haefeli, W.E.5
  • 253
    • 34250695989 scopus 로고    scopus 로고
    • Abcg2/Bcrp1 mediates the polarized transport of antiretroviral nucleosides abacavir and Zidovudine
    • Pan, G.; Giri, N.; Elmquist, W.F. Abcg2/Bcrp1 mediates the polarized transport of antiretroviral nucleosides abacavir and Zidovudine. Drug Metab. Dispos. 2007, 35, 1165-1173.
    • (2007) Drug Metab. Dispos. , vol.35 , pp. 1165-1173
    • Pan, G.1    Giri, N.2    Elmquist, W.F.3
  • 254
    • 0036841396 scopus 로고    scopus 로고
    • Inhibition of the multidrug resistance protein 1 (MRP1) by peptidomimetic glutathione-conjugate analogs
    • Burg, D.; Wielinga, P.; Zelcer, N.; Saeki, T.; Mulder, G.J.; Borst, P. Inhibition of the multidrug resistance protein 1 (MRP1) by peptidomimetic glutathione-conjugate analogs. Mol. Pharmacol. 2002, 62, 1160-1166.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 1160-1166
    • Burg, D.1    Wielinga, P.2    Zelcer, N.3    Saeki, T.4    Mulder, G.J.5    Borst, P.6
  • 255
    • 0032731289 scopus 로고    scopus 로고
    • Glutathione peptidomimetic drug modulator of multidrug resistance-associated protein
    • O'Brien, M.L.; Vulevic, B.; Freer, S.; Boyd, J.; Shen, H.; Tew, K.D. Glutathione peptidomimetic drug modulator of multidrug resistance-associated protein. J. Pharmacol. Exp. Ther. 1999, 291, 1348-1355.
    • (1999) J. Pharmacol. Exp. Ther. , vol.291 , pp. 1348-1355
    • O'Brien, M.L.1    Vulevic, B.2    Freer, S.3    Boyd, J.4    Shen, H.5    Tew, K.D.6
  • 256
    • 0035115578 scopus 로고    scopus 로고
    • The sulphonylurea glibenclamide inhibits multidrug resistance protein (MRP1) activity in human lung cancer cells
    • Payen, L.; Delugin, L.; Courtois, A.; Trinquart, Y.; Guillouzo, A.; Fardel, O. The sulphonylurea glibenclamide inhibits multidrug resistance protein (MRP1) activity in human lung cancer cells. Br. J. Pharmacol. 2001, 132, 778-784.
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 778-784
    • Payen, L.1    Delugin, L.2    Courtois, A.3    Trinquart, Y.4    Guillouzo, A.5    Fardel, O.6
  • 258
    • 53849120916 scopus 로고    scopus 로고
    • Investigating the potential role of multi-drug resistance protein (MRP) transporters in fetal to maternal glyburide efflux in the human placenta
    • Gedeon, C.; Anger, G.; Lubetsky, A.; Miller, M.P.; Koren, G. Investigating the potential role of multi-drug resistance protein (MRP) transporters in fetal to maternal glyburide efflux in the human placenta. J. Obstet. Gynaecol. 2008, 28, 485-489.
    • (2008) J. Obstet. Gynaecol. , vol.28 , pp. 485-489
    • Gedeon, C.1    Anger, G.2    Lubetsky, A.3    Miller, M.P.4    Koren, G.5
  • 259
    • 70450245353 scopus 로고    scopus 로고
    • Substrates inducers, inhibitors and structure-activity relationships of human cytochrome P450 2C9 and implications in drug development
    • Zhou, S.F.; Zhou, Z.W.; Yang, L.P.; Cai, J.P. Substrates, inducers, inhibitors and structure-activity relationships of human cytochrome P450 2C9 and implications in drug development. Curr. Med. Chem. 2009, 16, 3480-3675.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 3480-3675
    • Zhou, S.F.1    Zhou, Z.W.2    Yang, L.P.3    Cai, J.P.4
  • 260
    • 0023873591 scopus 로고
    • Tolbutamide hydroxylation by human liver microsomes. Kinetic characterisation and relationship to other cytochrome P-450 dependent xenobiotic oxidations
    • Miners, J.O.; Smith, K.J.; Robson, R.A.; McManus, M.E.; Veronese, M.E.; Birkett, D.J. Tolbutamide hydroxylation by human liver microsomes. Kinetic characterisation and relationship to other cytochrome P-450 dependent xenobiotic oxidations. Biochem. Pharmacol. 1988, 37, 1137-1144.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 1137-1144
    • Miners, J.O.1    Smith, K.J.2    Robson, R.A.3    McManus, M.E.4    Veronese, M.E.5    Birkett, D.J.6
  • 261
    • 0034616637 scopus 로고    scopus 로고
    • Blockage of drug resistance in vitro by disulfiram, a drug used to treat alcoholism
    • Loo, T.W.; Clarke, D.M. Blockage of drug resistance in vitro by disulfiram, a drug used to treat alcoholism. J. Natl. Cancer Inst. 2000, 92, 898-902.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 898-902
    • Loo, T.W.1    Clarke, D.M.2
  • 262
    • 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, Z.E.; Peng, X.H.; Nandigama, K.; Tekle, S.; Ambudkar, S.V. 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. 2004, 65, 675-684.
    • (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
  • 264
    • 69049090809 scopus 로고    scopus 로고
    • Cediranib (recentin AZD2171) reverses ABCB1- and ABCC1-mediated multidrug resistance by inhibition of their transport function
    • Tao, L.Y.; Liang, Y.J.; Wang, F.; Chen, L.M.; Yan, Y.Y.; Dai, C.L.; Fu, L.W. Cediranib (recentin, AZD2171) reverses ABCB1- and ABCC1-mediated multidrug resistance by inhibition of their transport function. Cancer Chemother. Pharmacol. 2009, 64, 961-969.
    • (2009) Cancer Chemother. Pharmacol. , vol.64 , pp. 961-969
    • Tao, L.Y.1    Liang, Y.J.2    Wang, F.3    Chen, L.M.4    Yan, Y.Y.5    Dai, C.L.6    Fu, L.W.7
  • 266
    • 59649129538 scopus 로고    scopus 로고
    • Sunitinib (Sutent SU11248) a small-molecule receptor tyrosine kinase inhibitor, blocks function of the ATP-binding cassette (ABC) transporters P-glycoprotein (ABCB1) and ABCG2
    • Shukla, S.; Robey, R.W.; Bates, S.E.; Ambudkar, S.V. Sunitinib (Sutent, SU11248), a small-molecule receptor tyrosine kinase inhibitor, blocks function of the ATP-binding cassette (ABC) transporters P-glycoprotein (ABCB1) and ABCG2. Drug Metab. Dispos. 2009, 37, 359-365.
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 359-365
    • Shukla, S.1    Robey, R.W.2    Bates, S.E.3    Ambudkar, S.V.4
  • 270
    • 0037047386 scopus 로고    scopus 로고
    • GSHdependent photolabeling of multidrug resistance protein MRP1 (ABCC1) by [125I]LY475776. Evidence of a major binding site in the COOH-proximal membrane spanning domain
    • Mao, Q.; Qiu, W.; Weigl, K.E.; Lander, P.A.; Tabas, L.B.; Shepard, R.L.; Dantzig, A.H.; Deeley, R.G.; Cole, S.P. GSHdependent photolabeling of multidrug resistance protein MRP1 (ABCC1) by [125I]LY475776. Evidence of a major binding site in the COOH-proximal membrane spanning domain. J. Biol. Chem. 2002, 277, 28690-28699.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28690-28699
    • Mao, Q.1    Qiu, W.2    Weigl, K.E.3    Lander, P.A.4    Tabas, L.B.5    Shepard, R.L.6    Dantzig, A.H.7    Deeley, R.G.8    Cole, S.P.9
  • 271
    • 0037144505 scopus 로고    scopus 로고
    • Photolabeling of human and murine multidrug resistance protein 1 with the high affinity inhibitor [125I] LY475776 and azidophenacyl-[35S]glutathione
    • Qian, Y.M.; Grant, C.E.; Westlake, C.J.; Zhang, D.W.; Lander, P.A.; Shepard, R.L.; Dantzig, A.H.; Cole, S.P.; Deeley, R.G. Photolabeling of human and murine multidrug resistance protein 1 with the high affinity inhibitor [125I]LY475776 and azidophenacyl-[35S]glutathione. J. Biol. Chem. 2002, 277, 35225-35231.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35225-35231
    • Qian, Y.M.1    Grant, C.E.2    Westlake, C.J.3    Zhang, D.W.4    Lander, P.A.5    Shepard, R.L.6    Dantzig, A.H.7    Cole, S.P.8    Deeley, R.G.9
  • 272
    • 0030071190 scopus 로고    scopus 로고
    • Reduction of expression of the multidrug resistance protein (MRP) in human tumor cells by antisense phosphorothioate oligonucleotides
    • Stewart, A.J.; Canitrot, Y.; Baracchini, E.; Dean, N.M.; Deeley, R.G.; Cole, S.P. Reduction of expression of the multidrug resistance protein (MRP) in human tumor cells by antisense phosphorothioate oligonucleotides. Biochem. Pharmacol. 1996, 51, 461-469.
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 461-469
    • Stewart, A.J.1    Canitrot, Y.2    Baracchini, E.3    Dean, N.M.4    Deeley, R.G.5    Cole, S.P.6
  • 274
    • 0034584676 scopus 로고    scopus 로고
    • Multidrug resistance-associated protein-reduction of expression in human leukaemia cells by antisense phosphorothioate olignucleotides
    • Niewiarowski, W.; Gendaszewska, E.; Rebowski, G.; Wojcik, M.; Mikolajczyk, B.; Goss, W.; Soszynski, M.; Bartosz, G. Multidrug resistance-associated protein-reduction of expression in human leukaemia cells by antisense phosphorothioate olignucleotides. Acta Biochim. Pol. 2000, 47, 1183-1188.
    • (2000) Acta Biochim. Pol. , vol.47 , pp. 1183-1188
    • Niewiarowski, W.1    Gendaszewska, E.2    Rebowski, G.3    Wojcik, M.4    Mikolajczyk, B.5    Goss, W.6    Soszynski, M.7    Bartosz, G.8
  • 275
    • 0036498029 scopus 로고    scopus 로고
    • In vitro and in vivo downregulation of MRP1 by antisense oligonucleotides: A potential role in neuroblastoma therapy
    • Kuss, B.J.; Corbo, M.; Lau, W.M.; Fennell, D.A.; Dean, N.M.; Cotter, F.E. In vitro and in vivo downregulation of MRP1 by antisense oligonucleotides: A potential role in neuroblastoma therapy. Int. J. Cancer 2002, 98, 128-133.
    • (2002) Int. J. Cancer , vol.98 , pp. 128-133
    • Kuss, B.J.1    Corbo, M.2    Lau, W.M.3    Fennell, D.A.4    Dean, N.M.5    Cotter, F.E.6
  • 280
    • 70449714688 scopus 로고    scopus 로고
    • Combined pharmacophore modeling, docking, and 3D QSAR studies of ABCB1 and ABCC1 transporter inhibitors
    • Pajeva, I.K.; Globisch, C.; Wiese, M. Combined pharmacophore modeling, docking, and 3D QSAR studies of ABCB1 and ABCC1 transporter inhibitors. Chem. Med. Chem. 2009, 4, 1883-1896.
    • (2009) Chem. Med. Chem. , vol.4 , pp. 1883-1896
    • Pajeva, I.K.1    Globisch, C.2    Wiese, M.3
  • 281
    • 25844493053 scopus 로고    scopus 로고
    • Topological model for the prediction of MRP1 inhibitory activity of pyrrolopyrimidines and templates derived from pyrrolopyrimidine
    • Lather, V.; Madan, A.K. Topological model for the prediction of MRP1 inhibitory activity of pyrrolopyrimidines and templates derived from pyrrolopyrimidine. Bioorg. Med. Chem. Lett. 2005, 15, 4967-4972.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 4967-4972
    • Lather, V.1    Madan, A.K.2
  • 282
    • 69949099322 scopus 로고    scopus 로고
    • Modulation of multidrug resistance protein 1 (MRP1/ABCC1)-mediated multidrug resistance by bivalent apigenin homodimers and their derivatives
    • Wong, I.L.; Chan, K.F.; Tsang, K.H.; Lam, C.Y.; Zhao, Y.; Chan, T.H.; Chow, L.M. Modulation of multidrug resistance protein 1 (MRP1/ABCC1)-mediated multidrug resistance by bivalent apigenin homodimers and their derivatives. J. Med. Chem. 2009, 52, 5311-5322.
    • (2009) J. Med. Chem. , vol.52 , pp. 5311-5322
    • Wong, I.L.1    Chan, K.F.2    Tsang, K.H.3    Lam, C.Y.4    Zhao, Y.5    Chan, T.H.6    Chow, L.M.7
  • 283
    • 68549126957 scopus 로고    scopus 로고
    • Aromatic 2-(thio)ureidocarboxylic acids as a new family of modulators of multidrug resistance-associated protein 1: Synthesis, biological evaluation, and structure-activity relationships
    • Hacker, H.G.; Leyers, S.; Wiendlocha, J.; Gutschow, M.; Wiese, M. Aromatic 2-(thio)ureidocarboxylic acids as a new family of modulators of multidrug resistance-associated protein 1: Synthesis, biological evaluation, and structure-activity relationships. J. Med. Chem. 2009, 52, 4586-4595.
    • (2009) J. Med. Chem. , vol.52 , pp. 4586-4595
    • Hacker, H.G.1    Leyers, S.2    Wiendlocha, J.3    Gutschow, M.4    Wiese, M.5
  • 284
    • 64349101278 scopus 로고    scopus 로고
    • Topological polar surface area defines substrate transport by multidrug resistance associated protein 1 (MRP1/ABCC1)
    • Fernandes, J.; Gattass, C.R. Topological polar surface area defines substrate transport by multidrug resistance associated protein 1 (MRP1/ABCC1). J. Med. Chem. 2009, 52, 1214-1218.
    • (2009) J. Med. Chem. , vol.52 , pp. 1214-1218
    • Fernandes, J.1    Gattass, C.R.2
  • 285
    • 0032518454 scopus 로고    scopus 로고
    • A general pattern for substrate recognition by Pglycoprotein
    • Seelig, A. A general pattern for substrate recognition by Pglycoprotein.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 252-261
    • Seelig, A.1
  • 286
    • 0034055630 scopus 로고    scopus 로고
    • Substrate recognition by Pglycoprotein and the multidrug resistance-associated protein MRP1: A comparison
    • Seelig, A.; Blatter, X.L.; Wohnsland, F. Substrate recognition by Pglycoprotein and the multidrug resistance-associated protein MRP1: A comparison. Int. J. Clin. Pharmacol. Ther. 2000, 38, 111-121.
    • (2000) Int. J. Clin. Pharmacol. Ther. , vol.38 , pp. 111-121
    • Seelig, A.1    Blatter, X.L.2    Wohnsland, F.3
  • 287
    • 0033058419 scopus 로고    scopus 로고
    • The human multidrug resistance protein MRP1 translocates sphingolipid analogs across the plasma membrane
    • Raggers, R.J.; van Helvoort, A.; Evers, R.; van Meer, G. The human multidrug resistance protein MRP1 translocates sphingolipid analogs across the plasma membrane. J. Cell Sci. 1999, 112 (Pt 3), 415-422.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 3 , pp. 415-422
    • Raggers, R.J.1    Van Helvoort, A.2    Evers, R.3    Van Meer, G.4
  • 290
    • 0141843591 scopus 로고    scopus 로고
    • Development of a chemical structure comparison method for integrated analysis of chemical and genomic information in the metabolic pathways
    • Hattori, M.; Okuno, Y.; Goto, S.; Kanehisa, M. Development of a chemical structure comparison method for integrated analysis of chemical and genomic information in the metabolic pathways. J. Am. Chem. Soc. 2003, 125, 11853-11865.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11853-11865
    • Hattori, M.1    Okuno, Y.2    Goto, S.3    Kanehisa, M.4
  • 291
    • 50349094786 scopus 로고    scopus 로고
    • Pharmacophore mapping of a series of pyrrolopyrimidines, indolopyrimidines and their congeners as multidrug-resistance-associated protein (MRP1) modulators
    • Tawari, N.R.; Bag, S.; Degani, M.S. Pharmacophore mapping of a series of pyrrolopyrimidines, indolopyrimidines and their congeners as multidrug-resistance-associated protein (MRP1) modulators. J. Mol. Model. 2008, 14, 911-921.
    • (2008) J. Mol. Model. , vol.14 , pp. 911-921
    • Tawari, N.R.1    Bag, S.2    Degani, M.S.3
  • 292
    • 33751301012 scopus 로고    scopus 로고
    • Pharmacophorebased discovery of ligands for drug transporters
    • Chang, C.; Ekins, S.; Bahadduri, P.; Swaan, P.W. Pharmacophorebased discovery of ligands for drug transporters. Adv. Drug Deliv. Rev. 2006, 58, 1431-1450.
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , pp. 1431-1450
    • Chang, C.1    Ekins, S.2    Bahadduri, P.3    Swaan, P.W.4
  • 295
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward, A.; Reyes, C.L.; Yu, J.; Roth, C.B.; Chang, G. Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 19005-19010.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 296
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R.J.; Locher, K.P. Structure of a bacterial multidrug ABC transporter. Nature 2006, 443, 180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 297
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K.P.; Lee, A.T.; Rees, D.C. The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism. Science 2002, 296, 1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 298
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein, K.; Frei, D.C.; Locher, K.P. Structure of an ABC transporter in complex with its binding protein. Nature 2007, 446, 213-216.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 299
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • Pinkett, H.W.; Lee, A.T.; Lum, P.; Locher, K.P.; Rees, D.C. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 2007, 315, 373-377.
    • (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
  • 300
    • 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, J.D.; Koike, K.; Moreau, C.; Sansom, M.S.; Deeley, R.G.; Cole, S.P. Molecular modeling correctly predicts the functional importance of Phe594 in transmembrane helix 11 of the multidrug resistance protein, MRP1 (ABCC1). J. Biol. Chem. 2004, 279, 463-468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 463-468
    • Campbell, J.D.1    Koike, K.2    Moreau, C.3    Sansom, M.S.4    Deeley, R.G.5    Cole, S.P.6
  • 305
    • 0042009288 scopus 로고    scopus 로고
    • Mutation of proline residues in the NH2-terminal region of the multidrug resistance protein, MRP1 (ABCC1): Effects on protein expression, membrane localization, and transport function
    • Ito, K.; Weigl, K.E.; Deeley, R.G.; Cole, S.P. Mutation of proline residues in the NH2-terminal region of the multidrug resistance protein, MRP1 (ABCC1): Effects on protein expression, membrane localization, and transport function. Biochim. Biophys. Acta 2003, 1615, 103-114.
    • (2003) Biochim. Biophys. Acta , vol.1615 , pp. 103-114
    • Ito, K.1    Weigl, K.E.2    Deeley, R.G.3    Cole, S.P.4
  • 306
    • 34247851070 scopus 로고    scopus 로고
    • Regulation of function by dimerization through the amino-terminal membrane-spanning domain of human ABCC1/MRP1
    • Yang, Y.; Liu, Y.; Dong, Z.; Xu, J.; Peng, H.; Liu, Z.; Zhang, J.T. Regulation of function by dimerization through the amino-terminal membrane-spanning domain of human ABCC1/MRP1. J. Biol. Chem. 2007, 282, 8821-8830.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8821-8830
    • Yang, Y.1    Liu, Y.2    Dong, Z.3    Xu, J.4    Peng, H.5    Liu, Z.6    Zhang, J.T.7
  • 307
    • 0037162429 scopus 로고    scopus 로고
    • Cytoplasmic retraction of the amino terminus of human multidrug resistance protein 1
    • Chen, Q.; Yang, Y.; Liu, Y.; Han, B.; Zhang, J.T. Cytoplasmic retraction of the amino terminus of human multidrug resistance protein 1. Biochemistry 2002, 41, 9052-9062.
    • (2002) Biochemistry , vol.41 , pp. 9052-9062
    • Chen, Q.1    Yang, Y.2    Liu, Y.3    Han, B.4    Zhang, J.T.5
  • 308
    • 33750046916 scopus 로고    scopus 로고
    • The amino terminus of the human multidrug resistance transporter ABCC1 has a U-shaped folding with a gating function
    • Chen, Q.; Yang, Y.; Li, L.; Zhang, J.T. The amino terminus of the human multidrug resistance transporter ABCC1 has a U-shaped folding with a gating function. J. Biol. Chem. 2006, 281, 31152-31163.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31152-31163
    • Chen, Q.1    Yang, Y.2    Li, L.3    Zhang, J.T.4
  • 309
    • 0030685129 scopus 로고    scopus 로고
    • Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofluorescence
    • Kast, C.; Gros, P. Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofluorescence. J. Biol. Chem. 1997, 272, 26479-26487.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26479-26487
    • Kast, C.1    Gros, P.2
  • 310
    • 0032562137 scopus 로고    scopus 로고
    • Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein
    • Kast, C.; Gros, P. Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein. Biochemistry 1998, 37, 2305-2313.
    • (1998) Biochemistry , vol.37 , pp. 2305-2313
    • Kast, C.1    Gros, P.2
  • 311
    • 0029985152 scopus 로고    scopus 로고
    • 4 transport by Coexpression of both half-molecules of human multidrug resistance protein in insect cells
    • 4 transport by Coexpression of both half-molecules of human multidrug resistance protein in insect cells. J. Biol. Chem. 1996, 271, 27782-27787.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27782-27787
    • Gao, M.1    Loe, D.W.2    Grant, C.E.3    Cole, S.P.4    Deeley, R.G.5
  • 312
    • 0030446722 scopus 로고    scopus 로고
    • The high-affinity sulfonylurea receptor: Distribution, glycosylation, purification, and immunoprecipitation of two forms from endocrine and neuroendocrine cell lines
    • Nelson, D.A.; Bryan, J.; Wechsler, S.; Clement, J.P.t.; Aguilar- Bryan, L. The high-affinity sulfonylurea receptor: Distribution, glycosylation, purification, and immunoprecipitation of two forms from endocrine and neuroendocrine cell lines. Biochemistry 1996, 35, 14793-14799.
    • (1996) Biochemistry , vol.35 , pp. 14793-14799
    • Nelson, D.A.1    Bryan, J.2    Wechsler, S.3    Clement, J.P.T.4    Aguilar- Bryan, L.5
  • 315
    • 0035951692 scopus 로고    scopus 로고
    • Analysis of the structure and expression pattern of MRP7 (ABCC10), a new member of the MRP subfamily
    • Hopper, E.; Belinsky, M.G.; Zeng, H.; Tosolini, A.; Testa, J.R.; Kruh, G.D. Analysis of the structure and expression pattern of MRP7 (ABCC10), a new member of the MRP subfamily. Cancer Lett. 2001, 162, 181-191.
    • (2001) Cancer Lett. , vol.162 , pp. 181-191
    • Hopper, E.1    Belinsky, M.G.2    Zeng, H.3    Tosolini, A.4    Testa, J.R.5    Kruh, G.D.6
  • 316
    • 0037031316 scopus 로고    scopus 로고
    • Evidence for the role of glycosylation in accessibility of the extracellular domains of human MRP1 (ABCC1)
    • Muller, M.; Yong, M.; Peng, X.H.; Petre, B.; Arora, S.; Ambudkar, S.V. Evidence for the role of glycosylation in accessibility of the extracellular domains of human MRP1 (ABCC1). Biochemistry 2002, 41, 10123-10132.
    • (2002) Biochemistry , vol.41 , pp. 10123-10132
    • Muller, M.1    Yong, M.2    Peng, X.H.3    Petre, B.4    Arora, S.5    Ambudkar, S.V.6
  • 317
    • 0033370596 scopus 로고    scopus 로고
    • ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells
    • Mao, Q.; Leslie, E.M.; Deeley, R.G.; Cole, S.P. ATPase activity of purified and reconstituted multidrug resistance protein MRP1 from drug-selected H69AR cells. Biochim. Biophys. Acta 1999, 1461, 69-82.
    • (1999) Biochim. Biophys. Acta , vol.1461 , pp. 69-82
    • Mao, Q.1    Leslie, E.M.2    Deeley, R.G.3    Cole, S.P.4
  • 318
    • 0034602270 scopus 로고    scopus 로고
    • Functional reconstitution of substrate transport by purified multidrug resistance protein MRP1 (ABCC1) in phospholipid vesicles
    • Mao, Q.; Deeley, R.G.; Cole, S.P. Functional reconstitution of substrate transport by purified multidrug resistance protein MRP1 (ABCC1) in phospholipid vesicles. J. Biol. Chem. 2000, 275, 34166-34172.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34166-34172
    • Mao, Q.1    Deeley, R.G.2    Cole, S.P.3
  • 319
    • 0347356332 scopus 로고    scopus 로고
    • Biochemical characterization and NMR studies of the nucleotidebinding domain 1 of multidrug-resistance-associated protein 1: Evidence for interaction between ATP and Trp653
    • Ramaen, O.; Masscheleyn, S.; Duffieux, F.; Pamlard, O.; Oberkampf, M.; Lallemand, J.Y.; Stoven, V.; Jacquet, E. Biochemical characterization and NMR studies of the nucleotidebinding domain 1 of multidrug-resistance-associated protein 1: Evidence for interaction between ATP and Trp653. Biochem. J. 2003, 376, 749-756.
    • (2003) Biochem. J. , vol.376 , pp. 749-756
    • Ramaen, O.1    Masscheleyn, S.2    Duffieux, F.3    Pamlard, O.4    Oberkampf, M.5    Lallemand, J.Y.6    Stoven, V.7    Jacquet, E.8
  • 320
    • 27744498371 scopus 로고    scopus 로고
    • Attempts to characterize the NBD heterodimer of MRP1: Transient complex formation involves Gly771 of the ABC signature sequence but does not enhance the intrinsic ATPase activity
    • Ramaen, O.; Sizun, C.; Pamlard, O.; Jacquet, E.; Lallemand, J.Y. Attempts to characterize the NBD heterodimer of MRP1: Transient complex formation involves Gly771 of the ABC signature sequence but does not enhance the intrinsic ATPase activity. Biochem. J. 2005, 391, 481-490.
    • (2005) Biochem. J. , vol.391 , pp. 481-490
    • Ramaen, O.1    Sizun, C.2    Pamlard, O.3    Jacquet, E.4    Lallemand, J.Y.5
  • 321
    • 33744791529 scopus 로고    scopus 로고
    • Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site
    • Ramaen, O.; Leulliot, N.; Sizun, C.; Ulryck, N.; Pamlard, O.; Lallemand, J.Y.; Tilbeurgh, H.; Jacquet, E. Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site. J. Mol. Biol. 2006, 359, 940-949.
    • (2006) J. Mol. Biol. , vol.359 , pp. 940-949
    • Ramaen, O.1    Leulliot, N.2    Sizun, C.3    Ulryck, N.4    Pamlard, O.5    Lallemand, J.Y.6    Tilbeurgh, H.7    Jacquet, E.8
  • 322
    • 0141755312 scopus 로고    scopus 로고
    • Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1)
    • Payen, L.F.; Gao, M.; Westlake, C.J.; Cole, S.P.; Deeley, R.G. Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1). J. Biol. Chem. 2003, 278, 38537-38547.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38537-38547
    • Payen, L.F.1    Gao, M.2    Westlake, C.J.3    Cole, S.P.4    Deeley, R.G.5
  • 323
    • 0029121417 scopus 로고
    • Covalent modification of human Pglycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity
    • Loo, T.W.; Clarke, D.M. Covalent modification of human Pglycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity. J. Biol. Chem. 1995, 270, 22957-22961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22957-22961
    • Loo, T.W.1    Clarke, D.M.2
  • 324
    • 0034625350 scopus 로고    scopus 로고
    • Nonequivalent nucleotide trapping in the two nucleotide binding folds of the human multidrug resistance protein MRP1
    • Nagata, K.; Nishitani, M.; Matsuo, M.; Kioka, N.; Amachi, T.; Ueda, K. Nonequivalent nucleotide trapping in the two nucleotide binding folds of the human multidrug resistance protein MRP1. J. Biol. Chem. 2000, 275, 17626-17630.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17626-17630
    • Nagata, K.1    Nishitani, M.2    Matsuo, M.3    Kioka, N.4    Amachi, T.5    Ueda, K.6
  • 325
    • 0034724680 scopus 로고    scopus 로고
    • Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1
    • Gao, M.; Cui, H.R.; Loe, D.W.; Grant, C.E.; Almquist, K.C.; Cole, S.P.; Deeley, R.G. Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1. J. Biol. Chem. 2000, 275, 13098-13108.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13098-13108
    • Gao, M.1    Cui, H.R.2    Loe, D.W.3    Grant, C.E.4    Almquist, K.C.5    Cole, S.P.6    Deeley, R.G.7
  • 326
    • 0034617097 scopus 로고    scopus 로고
    • Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1
    • Hou, Y.; Cui, L.; Riordan, J.R.; Chang, X. Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1. J. Biol. Chem. 2000, 275, 20280-20287.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20280-20287
    • Hou, Y.1    Cui, L.2    Riordan, J.R.3    Chang, X.4
  • 327
    • 0030689692 scopus 로고    scopus 로고
    • ATPase activity of purified multidrug resistance-associated protein
    • Chang, X.B.; Hou, Y.X.; Riordan, J.R. ATPase activity of purified multidrug resistance-associated protein. J. Biol. Chem. 1997, 272, 30962-30968.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30962-30968
    • Chang, X.B.1    Hou, Y.X.2    Riordan, J.R.3
  • 328
    • 0035902506 scopus 로고    scopus 로고
    • Functional expression of multidrug resistance protein 1 in Pichia pastoris
    • Cai, J.; Daoud, R.; Georges, E.; Gros, P. Functional expression of multidrug resistance protein 1 in Pichia pastoris. Biochemistry 2001, 40, 8307-8316.
    • (2001) Biochemistry , vol.40 , pp. 8307-8316
    • Cai, J.1    Daoud, R.2    Georges, E.3    Gros, P.4
  • 329
    • 0042131621 scopus 로고    scopus 로고
    • Expression of functional multidrugresistance protein 1 in Saccharomyces cerevisiae: Effects of N- and C-terminal affinity tags
    • Lee, S.H.; Altenberg, G.A. Expression of functional multidrugresistance protein 1 in Saccharomyces cerevisiae: Effects of N- and C-terminal affinity tags. Biochem. Biophys. Res. Commun. 2003, 306, 644-649.
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 644-649
    • Lee, S.H.1    Altenberg, G.A.2
  • 330
    • 0035844237 scopus 로고    scopus 로고
    • The structure of the multidrug resistance protein 1 (MRP1/ABCC1). crystallization and single-particle analysis
    • Rosenberg, M.F.; Mao, Q.; Holzenburg, A.; Ford, R.C.; Deeley, R.G.; Cole, S.P. The structure of the multidrug resistance protein 1 (MRP1/ABCC1). crystallization and single-particle analysis. J. Biol. Chem. 2001, 276, 16076-16082.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16076-16082
    • Rosenberg, M.F.1    Mao, Q.2    Holzenburg, A.3    Ford, R.C.4    Deeley, R.G.5    Cole, S.P.6
  • 331
    • 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.; Higgins, C.F. Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J. Biol. Chem. 1997, 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
  • 332
    • 0034711094 scopus 로고    scopus 로고
    • Multidrug resistance protein MRP1 reconstituted into lipid vesicles: Secondary structure and nucleotide-induced tertiary structure changes
    • Manciu, L.; Chang, X.B.; Riordan, J.R.; Ruysschaert, J.M. Multidrug resistance protein MRP1 reconstituted into lipid vesicles: Secondary structure and nucleotide-induced tertiary structure changes. Biochemistry 2000, 39, 13026-13033.
    • (2000) Biochemistry , vol.39 , pp. 13026-13033
    • Manciu, L.1    Chang, X.B.2    Riordan, J.R.3    Ruysschaert, J.M.4
  • 333
    • 0035937483 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes in the human multidrug resistance protein MRP1 are related to the capacity of chemotherapeutic drugs to accumulate or not in resistant cells
    • Manciu, L.; Chang, X.; Riordan, J.R.; Buyse, F.; Ruysschaert, J.M. Nucleotide-induced conformational changes in the human multidrug resistance protein MRP1 are related to the capacity of chemotherapeutic drugs to accumulate or not in resistant cells. FEBS Lett. 2001, 493, 31-35.
    • (2001) FEBS Lett. , vol.493 , pp. 31-35
    • Manciu, L.1    Chang, X.2    Riordan, J.R.3    Buyse, F.4    Ruysschaert, J.M.5
  • 335
    • 0032526848 scopus 로고    scopus 로고
    • Radiation inactivation suggests that human multidrug resistanceassociated protein 1 occurs as a dimer in the human erythrocyte membrane
    • Soszynski, M.; Kaluzna, A.; Rychlik, B.; Sokal, A.; Bartosz, G. Radiation inactivation suggests that human multidrug resistanceassociated protein 1 occurs as a dimer in the human erythrocyte membrane. Arch. Biochem. Biophys. 1998, 354, 311-316.
    • (1998) Arch. Biochem. Biophys. , vol.354 , pp. 311-316
    • Soszynski, M.1    Kaluzna, A.2    Rychlik, B.3    Sokal, A.4    Bartosz, G.5
  • 338
    • 0035933744 scopus 로고    scopus 로고
    • Glutathione-dependent binding of a photoaffinity analog of agosterol A to the C-terminal half of human multidrug resistance protein
    • Ren, X.Q.; Furukawa, T.; Aoki, S.; Nakajima, T.; Sumizawa, T.; Haraguchi, M.; Chen, Z.S.; Kobayashi, M.; Akiyama, S. Glutathione-dependent binding of a photoaffinity analog of agosterol A to the C-terminal half of human multidrug resistance protein. J. Biol. Chem. 2001, 276, 23197-23206.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23197-23206
    • Ren, X.Q.1    Furukawa, T.2    Aoki, S.3    Nakajima, T.4    Sumizawa, T.5    Haraguchi, M.6    Chen, Z.S.7    Kobayashi, M.8    Akiyama, S.9
  • 339
    • 2442660256 scopus 로고    scopus 로고
    • Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1)
    • Haimeur, A.; Conseil, G.; Deeley, R.G.; Cole, S.P. Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1). Mol. Pharmacol. 2004, 65, 1375-1385.
    • (2004) Mol. Pharmacol. , vol.65 , pp. 1375-1385
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.4
  • 340
    • 0036828695 scopus 로고    scopus 로고
    • Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity
    • Haimeur, A.; Deeley, R.G.; Cole, S.P. Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity. J. Biol. Chem. 2002, 277, 41326-41333.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41326-41333
    • Haimeur, A.1    Deeley, R.G.2    Cole, S.P.3
  • 341
    • 67649398901 scopus 로고    scopus 로고
    • Molecular basis for reduced estrone sulfate transport and altered modulator sensitivity of transmembrane helix (TM) 6 and TM17 mutants of multidrug resistance protein 1 (ABCC1)
    • Maeno, K.; Nakajima, A.; Conseil, G.; Rothnie, A.; Deeley, R.G.; Cole, S.P. Molecular basis for reduced estrone sulfate transport and altered modulator sensitivity of transmembrane helix (TM) 6 and TM17 mutants of multidrug resistance protein 1 (ABCC1). Drug Metab. Dispos. 2009, 37, 1411-1420.
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1411-1420
    • Maeno, K.1    Nakajima, A.2    Conseil, G.3    Rothnie, A.4    Deeley, R.G.5    Cole, S.P.6
  • 343
    • 33645103630 scopus 로고    scopus 로고
    • Mutational analysis of polar amino acid residues within predicted transmembrane helices 10 and 16 of multidrug resistance protein 1 (ABCC1): Effect on substrate specificity
    • Zhang, D.W.; Nunoya, K.; Vasa, M.; Gu, H.M.; Cole, S.P.; Deeley, R.G. Mutational analysis of polar amino acid residues within predicted transmembrane helices 10 and 16 of multidrug resistance protein 1 (ABCC1): Effect on substrate specificity. Drug Metab. Dispos. 2006, 34, 539-546.
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 539-546
    • Zhang, D.W.1    Nunoya, K.2    Vasa, M.3    Gu, H.M.4    Cole, S.P.5    Deeley, R.G.6
  • 344
    • 0037147341 scopus 로고    scopus 로고
    • Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1
    • Koike, K.; Oleschuk, C.J.; Haimeur, A.; Olsen, S.L.; Deeley, R.G.; Cole, S.P. Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1. J. Biol. Chem. 2002, 277, 49495-49503.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49495-49503
    • Koike, K.1    Oleschuk, C.J.2    Haimeur, A.3    Olsen, S.L.4    Deeley, R.G.5    Cole, S.P.6
  • 345
    • 1242267914 scopus 로고    scopus 로고
    • Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity, and nucleotide interactions
    • Koike, K.; Conseil, G.; Leslie, E.M.; Deeley, R.G.; Cole, S.P. Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity, and nucleotide interactions. J. Biol. Chem. 2004, 279, 12325-12336.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12325-12336
    • Koike, K.1    Conseil, G.2    Leslie, E.M.3    Deeley, R.G.4    Cole, S.P.5
  • 346
    • 11844276978 scopus 로고    scopus 로고
    • 4 binding sites in multidrug resistance protein 1 (ABCC1) include the first membrane multiple spanning domain
    • 4 binding sites in multidrug resistance protein 1 (ABCC1) include the first membrane multiple spanning domain. Biochemistry 2005, 44, 340-351.
    • (2005) Biochemistry , vol.44 , pp. 340-351
    • Karwatsky, J.1    Leimanis, M.2    Cai, J.3    Gros, P.4    Georges, E.5
  • 347
    • 40949146910 scopus 로고    scopus 로고
    • Role of proline 1150 in functional interactions between the membrane spanning domains and nucleotide binding domains of the MRP1 (ABCC1) transporter
    • Letourneau, I.J.; Nakajima, A.; Deeley, R.G.; Cole, S.P. Role of proline 1150 in functional interactions between the membrane spanning domains and nucleotide binding domains of the MRP1 (ABCC1) transporter. Biochem. Pharmacol. 2008, 75, 1659-1669.
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 1659-1669
    • Letourneau, I.J.1    Nakajima, A.2    Deeley, R.G.3    Cole, S.P.4
  • 348
    • 34547153777 scopus 로고    scopus 로고
    • Mutational analysis of a highly conserved proline residue in MRP1, MRP2, and MRP3 reveals a partially conserved function
    • Letourneau, I.J.; Slot, A.J.; Deeley, R.G.; Cole, S.P. Mutational analysis of a highly conserved proline residue in MRP1, MRP2, and MRP3 reveals a partially conserved function. Drug Metab. Dispos. 2007, 35, 1372-1379.
    • (2007) Drug Metab. Dispos. , vol.35 , pp. 1372-1379
    • Letourneau, I.J.1    Slot, A.J.2    Deeley, R.G.3    Cole, S.P.4
  • 349
    • 33846367006 scopus 로고    scopus 로고
    • Hydrogen-bond formation of the residue in H-loop of the nucleotide binding domain 2 with the ATP in this site and/or other residues of multidrug resistance protein MRP1 plays a crucial role during ATP-dependent solute transport
    • Yang, R.; Chang, X.B. Hydrogen-bond formation of the residue in H-loop of the nucleotide binding domain 2 with the ATP in this site and/or other residues of multidrug resistance protein MRP1 plays a crucial role during ATP-dependent solute transport. Biochim. Biophys. Acta 2007, 1768, 324-335.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 324-335
    • Yang, R.1    Chang, X.B.2
  • 350
    • 33745573710 scopus 로고    scopus 로고
    • Replacement of the positively charged Walker A lysine residue with a hydrophobic leucine residue and conformational alterations caused by this mutation in MRP1 impair ATP binding and hydrolysis
    • Buyse, F.; Hou, Y.X.; Vigano, C.; Zhao, Q.; Ruysschaert, J.M.; Chang, X.B. Replacement of the positively charged Walker A lysine residue with a hydrophobic leucine residue and conformational alterations caused by this mutation in MRP1 impair ATP binding and hydrolysis. Biochem. J. 2006, 397, 121-130.
    • (2006) Biochem. J. , vol.397 , pp. 121-130
    • Buyse, F.1    Hou, Y.X.2    Vigano, C.3    Zhao, Q.4    Ruysschaert, J.M.5    Chang, X.B.6
  • 351
    • 10344236531 scopus 로고    scopus 로고
    • Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1
    • Zhao, Q.; Chang, X.B. Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1. J. Biol. Chem. 2004, 279, 48505-48512.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48505-48512
    • Zhao, Q.1    Chang, X.B.2
  • 352
    • 4744347692 scopus 로고    scopus 로고
    • The role of the conserved glycines of ATP-binding cassette signature motifs of MRP1 in the communication between the substrate-binding site and the catalytic centers
    • Szentpetery, Z.; Kern, A.; Liliom, K.; Sarkadi, B.; Varadi, A.; Bakos, E. The role of the conserved glycines of ATP-binding cassette signature motifs of MRP1 in the communication between the substrate-binding site and the catalytic centers. J. Biol. Chem. 2004, 279, 41670-41678.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41670-41678
    • Szentpetery, Z.1    Kern, A.2    Liliom, K.3    Sarkadi, B.4    Varadi, A.5    Bakos, E.6
  • 353
    • 38349065419 scopus 로고    scopus 로고
    • The hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function
    • Yang, R.; Scavetta, R.; Chang, X.B. The hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function. Biochim. Biophys. Acta 2008, 1778, 454-465.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 454-465
    • Yang, R.1    Scavetta, R.2    Chang, X.B.3
  • 354
    • 31844446751 scopus 로고    scopus 로고
    • Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1)
    • Conseil, G.; Deeley, R.G.; Cole, S.P. Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1). J. Biol. Chem. 2006, 281, 43-50.
    • (2006) J. Biol. Chem. , vol.281 , pp. 43-50
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.3
  • 355
    • 59449105325 scopus 로고    scopus 로고
    • Multiple roles of charged amino acids in cytoplasmic loop 7 for expression and function of the multidrug and organic anion transporter MRP1 (ABCC1)
    • Conseil, G.; Rothnie, A.J.; Deeley, R.G.; Cole, S.P. Multiple roles of charged amino acids in cytoplasmic loop 7 for expression and function of the multidrug and organic anion transporter MRP1 (ABCC1). Mol. Pharmacol. 2009, 75, 397-406.
    • (2009) Mol. Pharmacol. , vol.75 , pp. 397-406
    • Conseil, G.1    Rothnie, A.J.2    Deeley, R.G.3    Cole, S.P.4
  • 356
    • 11144231983 scopus 로고    scopus 로고
    • Identification and characterization of functionally important elements in the multidrug resistance protein 1 COOH-terminal region
    • Westlake, C.J.; Payen, L.; Gao, M.; Cole, S.P.; Deeley, R.G. Identification and characterization of functionally important elements in the multidrug resistance protein 1 COOH-terminal region. J. Biol. Chem. 2004, 279, 53571-53583.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53571-53583
    • Westlake, C.J.1    Payen, L.2    Gao, M.3    Cole, S.P.4    Deeley, R.G.5
  • 357
    • 4644278479 scopus 로고    scopus 로고
    • Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): Glutamate 1204 is important for both the expression and catalytic activity of the transporter
    • Situ, D.; Haimeur, A.; Conseil, G.; Sparks, K.E.; Zhang, D.; Deeley, R.G.; Cole, S.P. Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): Glutamate 1204 is important for both the expression and catalytic activity of the transporter. J. Biol. Chem. 2004, 279, 38871-38880.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38871-38880
    • Situ, D.1    Haimeur, A.2    Conseil, G.3    Sparks, K.E.4    Zhang, D.5    Deeley, R.G.6    Cole, S.P.7
  • 358
    • 0037036427 scopus 로고    scopus 로고
    • Determinants of the substrate specificity of multidrug resistance protein 1: Role of amino acid residues with hydrogen bonding potential in predicted transmembrane helix 17
    • Zhang, D.W.; Cole, S.P.; Deeley, R.G. Determinants of the substrate specificity of multidrug resistance protein 1: Role of amino acid residues with hydrogen bonding potential in predicted transmembrane helix 17. J. Biol. Chem. 2002, 277, 20934-20941.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20934-20941
    • Zhang, D.W.1    Cole, S.P.2    Deeley, R.G.3
  • 359
    • 0042473136 scopus 로고    scopus 로고
    • Characterization of the role of polar amino acid residues within predicted transmembrane helix 17 in determining the substrate specificity of multidrug resistance protein 3
    • Zhang, D.W.; Gu, H.M.; Vasa, M.; Muredda, M.; Cole, S.P.; Deeley, R.G. Characterization of the role of polar amino acid residues within predicted transmembrane helix 17 in determining the substrate specificity of multidrug resistance protein 3. Biochemistry 2003, 42, 9989-10000.
    • (2003) Biochemistry , vol.42 , pp. 9989-10000
    • Zhang, D.W.1    Gu, H.M.2    Vasa, M.3    Muredda, M.4    Cole, S.P.5    Deeley, R.G.6
  • 360
    • 3242738307 scopus 로고    scopus 로고
    • Transmembrane helix 11 of multidrug resistance protein 1 (MRP1/ABCC1): Identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1
    • Zhang, D.W.; Nunoya, K.; Vasa, M.; Gu, H.M.; Theis, A.; Cole, S.P.; Deeley, R.G. Transmembrane helix 11 of multidrug resistance protein 1 (MRP1/ABCC1): Identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1. Biochemistry 2004, 43, 9413-9425.
    • (2004) Biochemistry , vol.43 , pp. 9413-9425
    • Zhang, D.W.1    Nunoya, K.2    Vasa, M.3    Gu, H.M.4    Theis, A.5    Cole, S.P.6    Deeley, R.G.7
  • 361
    • 0035424958 scopus 로고    scopus 로고
    • Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation
    • Cui, L.; Hou, Y.X.; Riordan, J.R.; Chang, X.B. Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation. Arch. Biochem. Biophys. 2001, 392, 153-161.
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 153-161
    • Cui, L.1    Hou, Y.X.2    Riordan, J.R.3    Chang, X.B.4
  • 362
    • 0035212059 scopus 로고    scopus 로고
    • Identification of human multidrug resistance protein 1 (MRP1) mutations and characterization of a G671V substitution
    • Conrad, S.; Kauffmann, H.M.; Ito, K.; Deeley, R.G.; Cole, S.P.; Schrenk, D. Identification of human multidrug resistance protein 1 (MRP1) mutations and characterization of a G671V substitution. J. Hum. Genet. 2001, 46, 656-663.
    • (2001) J. Hum. Genet. , vol.46 , pp. 656-663
    • Conrad, S.1    Kauffmann, H.M.2    Ito, K.3    Deeley, R.G.4    Cole, S.P.5    Schrenk, D.6
  • 363
    • 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, H.M.; Ito, K.; Leslie, E.M.; Deeley, R.G.; Schrenk, D.; Cole, S.P. A naturally occurring mutation in MRP1 results in a selective decrease in organic anion transport and in increased doxorubicin resistance. Pharmacogenetics 2002, 12, 321-330.
    • (2002) Pharmacogenetics , vol.12 , pp. 321-330
    • Conrad, S.1    Kauffmann, H.M.2    Ito, K.3    Leslie, E.M.4    Deeley, R.G.5    Schrenk, D.6    Cole, S.P.7
  • 366
    • 62349110987 scopus 로고    scopus 로고
    • Characterization and analyses of multidrug resistance-associated protein 1 (MRP1/ABCC1) polymorphisms in Chinese population
    • Yin, J.Y.; Huang, Q.; Yang, Y.; Zhang, J.T.; Zhong, M.Z.; Zhou, H.H.; Liu, Z.Q. Characterization and analyses of multidrug resistance-associated protein 1 (MRP1/ABCC1) polymorphisms in Chinese population. Pharmacogenet. Genomics 2009, 19, 206-216.
    • (2009) Pharmacogenet. Genomics , vol.19 , pp. 206-216
    • Yin, J.Y.1    Huang, Q.2    Yang, Y.3    Zhang, J.T.4    Zhong, M.Z.5    Zhou, H.H.6    Liu, Z.Q.7
  • 367
    • 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, I.J.; Deeley, R.G.; Cole, S.P. Functional characterization of non-synonymous single nucleotide polymorphisms in the gene encoding human multidrug resistance protein 1 (MRP1/ABCC1). Pharmacogenet. Genomics 2005, 15, 647-657.
    • (2005) Pharmacogenet. Genomics , vol.15 , pp. 647-657
    • Letourneau, I.J.1    Deeley, R.G.2    Cole, S.P.3
  • 368
    • 11844297796 scopus 로고    scopus 로고
    • Role of two adjacent cytoplasmic tyrosine residues in MRP1 (ABCC1) transport activity and sensitivity to sulfonylureas
    • Conseil, G.; Deeley, R.G.; Cole, S.P. Role of two adjacent cytoplasmic tyrosine residues in MRP1 (ABCC1) transport activity and sensitivity to sulfonylureas. Biochem. Pharmacol. 2005, 69, 451-461.
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 451-461
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.3
  • 369
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • Hirokawa, T.; Boon-Chieng, S.; Mitaku, S. SOSUI: Classification and secondary structure prediction system for membrane proteins. Bioinformatics 1998, 14, 378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 370
    • 0034327611 scopus 로고    scopus 로고
    • Hinges swivels and switches: The role of prolines in signalling via transmembrane β-helices
    • Sansom, M.S.; Weinstein, H. Hinges, swivels and switches: The role of prolines in signalling via transmembrane β-helices. Trends Pharmacol. Sci. 2000, 21, 445-451.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 371
    • 0035958862 scopus 로고    scopus 로고
    • Transport of the β-O-glucuronide conjugate of the tobacco-specific carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)- 1-butanol (NNAL) by the multidrug resistance protein 1 (MRP1). Requirement for glutathione or a non-sulfur-containing analog
    • Leslie, E.M.; Ito, K.; Upadhyaya, P.; Hecht, S.S.; Deeley, R.G.; Cole, S.P. Transport of the β-O-glucuronide conjugate of the tobacco-specific carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)- 1-butanol (NNAL) by the multidrug resistance protein 1 (MRP1). Requirement for glutathione or a non-sulfur-containing analog. J. Biol. Chem. 2001, 276, 27846-27854.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27846-27854
    • Leslie, E.M.1    Ito, K.2    Upadhyaya, P.3    Hecht, S.S.4    Deeley, R.G.5    Cole, S.P.6
  • 372
    • 0033924206 scopus 로고    scopus 로고
    • Functional analysis of a tryptophan-less Pglycoprotein: A tool for tryptophan insertion and fluorescence spectroscopy
    • Kwan, T.; Loughrey, H.; Brault, M.; Gruenheid, S.; Urbatsch, I.L.; Senior, A.E.; Gros, P. Functional analysis of a tryptophan-less Pglycoprotein: A tool for tryptophan insertion and fluorescence spectroscopy. Mol. Pharmacol. 2000, 58, 37-47.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 37-47
    • Kwan, T.1    Loughrey, H.2    Brault, M.3    Gruenheid, S.4    Urbatsch, I.L.5    Senior, A.E.6    Gros, P.7
  • 373
    • 0035824674 scopus 로고    scopus 로고
    • Characterization of drug transport by the human multidrug resistance protein 3 (ABCC3)
    • Zelcer, N.; Saeki, T.; Reid, G.; Beijnen, J.H.; Borst, P. Characterization of drug transport by the human multidrug resistance protein 3 (ABCC3). J. Biol. Chem. 2001, 276, 46400-46407.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46400-46407
    • Zelcer, N.1    Saeki, T.2    Reid, G.3    Beijnen, J.H.4    Borst, P.5
  • 374
    • 57349152178 scopus 로고    scopus 로고
    • Structural determinants of substrate specificity differences between human multidrug resistance protein (MRP) 1 (ABCC1) and MRP3 (ABCC3)
    • Grant, C.E.; Gao, M.; DeGorter, M.K.; Cole, S.P.; Deeley, R.G. Structural determinants of substrate specificity differences between human multidrug resistance protein (MRP) 1 (ABCC1) and MRP3 (ABCC3). Drug Metab. Dispos. 2008, 36, 2571-2581.
    • (2008) Drug Metab. Dispos. , vol.36 , pp. 2571-2581
    • Grant, C.E.1    Gao, M.2    DeGorter, M.K.3    Cole, S.P.4    Deeley, R.G.5
  • 375
    • 0029944981 scopus 로고    scopus 로고
    • Detection of a de novo R1066H mutation in an Italian patient affected by cystic fibrosis
    • Cremonesi, L.; Cainarca, S.; Rossi, A.; Padoan, R.; Ferrari, M. Detection of a de novo R1066H mutation in an Italian patient affected by cystic fibrosis. Hum. Genet. 1996, 98, 119-121.
    • (1996) Hum. Genet. , vol.98 , pp. 119-121
    • Cremonesi, L.1    Cainarca, S.2    Rossi, A.3    Padoan, R.4    Ferrari, M.5
  • 376
    • 0034705145 scopus 로고    scopus 로고
    • Pseudoxanthoma elasticum: Mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter
    • Ringpfeil, F.; Lebwohl, M.G.; Christiano, A.M.; Uitto, J. Pseudoxanthoma elasticum: Mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter. Proc. Natl. Acad. Sci. U. S. A. 2000, 97, 6001-6006.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6001-6006
    • Ringpfeil, F.1    Lebwohl, M.G.2    Christiano, A.M.3    Uitto, J.4
  • 377
    • 33745769743 scopus 로고    scopus 로고
    • Nucleotide sequence analyses of the MRP1 gene in four populations suggest negative selection on its coding region
    • Wang, Z.; Sew, P.H.; Ambrose, H.; Ryan, S.; Chong, S.S.; Lee, E.J.; Lee, C.G. Nucleotide sequence analyses of the MRP1 gene in four populations suggest negative selection on its coding region. BMC Genomics 2006, 7, 111.
    • (2006) BMC Genomics , vol.7 , pp. 111
    • Wang, Z.1    Sew, P.H.2    Ambrose, H.3    Ryan, S.4    Chong, S.S.5    Lee, E.J.6    Lee, C.G.7
  • 379
    • 11144329541 scopus 로고    scopus 로고
    • Linkage disequilibrium and haplotype architecture for two ABC transporter genes (ABCC1 and ABCG2) in Chinese population: Implications for pharmacogenomic association studies
    • Wang, H.; Hao, B.; Zhou, K.; Chen, X.; Wu, S.; Zhou, G.; Zhu, Y.; He, F. Linkage disequilibrium and haplotype architecture for two ABC transporter genes (ABCC1 and ABCG2) in Chinese population: Implications for pharmacogenomic association studies. Ann. Hum. Genet. 2004, 68, 563-573.
    • (2004) Ann. Hum. Genet. , vol.68 , pp. 563-573
    • Wang, H.1    Hao, B.2    Zhou, K.3    Chen, X.4    Wu, S.5    Zhou, G.6    Zhu, Y.7    He, F.8
  • 380
    • 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, E.J.; Chong, S.S.; Lee, C.G. A functional polymorphism within the MRP1 gene locus identified through its genomic signature of positive selection. Hum. Mol. Genet. 2005, 14, 2075-2087.
    • (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
  • 382
    • 0035103009 scopus 로고    scopus 로고
    • Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in healthy Japanese subjects
    • Ito, S.; Ieiri, I.; Tanabe, M.; Suzuki, A.; Higuchi, S.; Otsubo, K. Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in healthy Japanese subjects. Pharmacogenetics 2001, 11, 175-184.
    • (2001) Pharmacogenetics , vol.11 , pp. 175-184
    • Ito, S.1    Ieiri, I.2    Tanabe, M.3    Suzuki, A.4    Higuchi, S.5    Otsubo, K.6
  • 383
    • 0035219750 scopus 로고    scopus 로고
    • Identification of novel polymorphisms in the pM5 and MRP1 (ABCC1) genes at locus 16p13.1 and exclusion of both genes as responsible for pseudoxanthoma elasticum
    • Perdu, J.; Germain, D.P. Identification of novel polymorphisms in the pM5 and MRP1 (ABCC1) genes at locus 16p13.1 and exclusion of both genes as responsible for pseudoxanthoma elasticum. Hum. Mutat. 2001, 17, 74-75.
    • (2001) Hum. Mutat. , vol.17 , pp. 74-75
    • Perdu, J.1    Germain, D.P.2
  • 384
    • 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, P.M.; Gaikovitch, E.; Pahkla, 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. 2003, 59, 347-350.
    • (2003) Eur. J. Clin. Pharmacol. , vol.59 , pp. 347-350
    • Oselin, K.1    Mrozikiewicz, P.M.2    Gaikovitch, E.3    Pahkla, R.4    Roots, I.5
  • 385
    • 78651437999 scopus 로고    scopus 로고
    • Phenotype prediction of non-synonymous single-nucleotide polymorphisms in human ATP-binding cassette transporter genes
    • in press
    • Wang, L.L.; Liu, Y.H.; Meng, L.L.; Li, C.G.; Zhou, S.F. Phenotype prediction of non-synonymous single-nucleotide polymorphisms in human ATP-binding cassette transporter genes. Basic Clin. Pharmacol. Toxicol. 2011, (in press).
    • Basic Clin. Pharmacol. Toxicol. , vol.2011
    • Wang, L.L.1    Liu, Y.H.2    Meng, L.L.3    Li, C.G.4    Zhou, S.F.5
  • 386
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins, C.F.; Linton, K.J. The ATP switch model for ABC transporters. Nat. Struct. Mol. Biol. 2004, 11, 918-926.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 387
    • 1242335471 scopus 로고    scopus 로고
    • The MRPrelated and BCRP/ABCG2 multidrug resistance proteins: Biology, substrate specificity and regulation
    • Haimeur, A.; Conseil, G.; Deeley, R.G.; Cole, S.P. The MRPrelated and BCRP/ABCG2 multidrug resistance proteins: Biology, substrate specificity and regulation. Curr. Drug Metab. 2004, 5, 21-53.
    • (2004) Curr. Drug Metab. , vol.5 , pp. 21-53
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.4
  • 388
    • 0029029449 scopus 로고
    • Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein
    • Versantvoort, C.H.; Broxterman, H.J.; Bagrij, T.; Scheper, R.J.; Twentyman, P.R. Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein. Br. J. Cancer 1995, 72, 82-89.
    • (1995) Br. J. Cancer , vol.72 , pp. 82-89
    • Versantvoort, C.H.1    Broxterman, H.J.2    Bagrij, T.3    Scheper, R.J.4    Twentyman, P.R.5
  • 389
    • 33744946318 scopus 로고    scopus 로고
    • Role of GSH in estrone sulfate binding and translocation by the multidrug resistance protein 1 (MRP1/ABCC1)
    • Rothnie, A.; Callaghan, R.; Deeley, R.G.; Cole, S.P. Role of GSH in estrone sulfate binding and translocation by the multidrug resistance protein 1 (MRP1/ABCC1). J. Biol. Chem. 2006, 281, 13906-13914.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13906-13914
    • Rothnie, A.1    Callaghan, R.2    Deeley, R.G.3    Cole, S.P.4
  • 390
    • 57349196661 scopus 로고    scopus 로고
    • Mechanistic differences between GSH transport by multidrug resistance protein 1 (MRP1/ABCC1) and GSH modulation of MRP1-mediated transport
    • Rothnie, A.; Conseil, G.; Lau, A.Y.; Deeley, R.G.; Cole, S.P. Mechanistic differences between GSH transport by multidrug resistance protein 1 (MRP1/ABCC1) and GSH modulation of MRP1-mediated transport. Mol. Pharmacol. 2008, 74, 1630-1640.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 1630-1640
    • Rothnie, A.1    Conseil, G.2    Lau, A.Y.3    Deeley, R.G.4    Cole, S.P.5
  • 391
    • 0033021424 scopus 로고    scopus 로고
    • ATP-and glutathione-dependent transport of chemotherapeutic drugs by the multidrug resistance protein MRP1
    • Renes, J.; de Vries, E.G.; Nienhuis, E.F.; Jansen, P.L.; Muller, M. ATP- and glutathione-dependent transport of chemotherapeutic drugs by the multidrug resistance protein MRP1. Br. J. Pharmacol. 1999, 126, 681-688.
    • (1999) Br. J. Pharmacol. , vol.126 , pp. 681-688
    • Renes, J.1    De Vries, E.G.2    Nienhuis, E.F.3    Jansen, P.L.4    Muller, M.5
  • 392
    • 1642330416 scopus 로고    scopus 로고
    • Transport of ethinylestradiol glucuronide and ethinylestradiol sulfate by the multidrug resistance proteins MRP1, MRP2, and MRP3
    • Chu, X.Y.; Huskey, S.E.; Braun, M.P.; Sarkadi, B.; Evans, D.C.; Evers, R. Transport of ethinylestradiol glucuronide and ethinylestradiol sulfate by the multidrug resistance proteins MRP1, MRP2, and MRP3. J. Pharmacol. Exp. Ther. 2004, 309, 156-164.
    • (2004) J. Pharmacol. Exp. Ther. , vol.309 , pp. 156-164
    • Chu, X.Y.1    Huskey, S.E.2    Braun, M.P.3    Sarkadi, B.4    Evans, D.C.5    Evers, R.6
  • 393
    • 15544376626 scopus 로고    scopus 로고
    • Dynamics of glutathione conjugation and conjugate efflux in detoxification of the carcinogen, 4-nitroquinoline 1-oxide: Contributions of glutathione, glutathione S-transferase, and MRP1
    • Peklak-Scott, C.; Townsend, A.J.; Morrow, C.S. Dynamics of glutathione conjugation and conjugate efflux in detoxification of the carcinogen, 4-nitroquinoline 1-oxide: Contributions of glutathione, glutathione S-transferase, and MRP1. Biochemistry 2005, 44, 4426-4433.
    • (2005) Biochemistry , vol.44 , pp. 4426-4433
    • Peklak-Scott, C.1    Townsend, A.J.2    Morrow, C.S.3
  • 395
    • 14844313300 scopus 로고    scopus 로고
    • Physiological and pathological aspects of GSH metabolism
    • Njalsson, R.; Norgren, S. Physiological and pathological aspects of GSH metabolism. Acta Paediatr. 2005, 94, 132-137.
    • (2005) Acta Paediatr. , vol.94 , pp. 132-137
    • Njalsson, R.1    Norgren, S.2
  • 396
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathionedependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes, A.P.; Holmgren, A. Glutaredoxins: Glutathionedependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 2004, 6, 63-74.
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 398
    • 64549106959 scopus 로고    scopus 로고
    • Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation
    • Gallogly, M.M.; Starke, D.W.; Mieyal, J.J. Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation. Antioxid. Redox Signal. 2009, 11, 1059-1081.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1059-1081
    • Gallogly, M.M.1    Starke, D.W.2    Mieyal, J.J.3
  • 400
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich, D.; Powis, G. Thioredoxin reductase. Biochem. J. 2000, 346 Pt 1, 1-8.
    • (2000) Biochem. J. , vol.346 , Issue.PART 1 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 401
    • 0030678131 scopus 로고    scopus 로고
    • Evidence that the multidrug resistance protein (MRP) functions as a cotransporter of glutathione and natural product toxins
    • Rappa, G.; Lorico, A.; Flavell, R.A.; Sartorelli, A.C. Evidence that the multidrug resistance protein (MRP) functions as a cotransporter of glutathione and natural product toxins. Cancer Res. 1997, 57, 5232-5237.
    • (1997) Cancer Res. , vol.57 , pp. 5232-5237
    • Rappa, G.1    Lorico, A.2    Flavell, R.A.3    Sartorelli, A.C.4
  • 402
    • 0033104810 scopus 로고    scopus 로고
    • Canalicular multispecific organic anion transporter/multidrug resistance protein 2 mediates lowaffinity transport of reduced glutathione
    • Paulusma, C.C.; van Geer, M.A.; Evers, R.; Heijn, M.; Ottenhoff, R.; Borst, P.; Oude Elferink, R.P. Canalicular multispecific organic anion transporter/multidrug resistance protein 2 mediates lowaffinity transport of reduced glutathione. Biochem. J. 1999, 338, 393-401.
    • (1999) Biochem. J. , vol.338 , pp. 393-401
    • Paulusma, C.C.1    Van Geer, M.A.2    Evers, R.3    Heijn, M.4    Ottenhoff, R.5    Borst, P.6    Oude Elferink, R.P.7
  • 403
    • 30144440842 scopus 로고    scopus 로고
    • Multidrug resistance protein 1-mediated export of glutathione and glutathione disulfide from brain astrocytes
    • Hirrlinger, J.; Dringen, R. Multidrug resistance protein 1-mediated export of glutathione and glutathione disulfide from brain astrocytes. Methods Enzymol. 2005, 400, 395-409.
    • (2005) Methods Enzymol. , vol.400 , pp. 395-409
    • Hirrlinger, J.1    Dringen, R.2
  • 404
    • 0035145779 scopus 로고    scopus 로고
    • The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress
    • Hirrlinger, J.; Konig, J.; Keppler, D.; Lindenau, J.; Schulz, J.B.; Dringen, R. The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress. J. Neurochem. 2001, 76, 627-636.
    • (2001) J. Neurochem. , vol.76 , pp. 627-636
    • Hirrlinger, J.1    Konig, J.2    Keppler, D.3    Lindenau, J.4    Schulz, J.B.5    Dringen, R.6
  • 405
    • 31844450741 scopus 로고    scopus 로고
    • On the putative co-transport of drugs by multidrug resistance proteins
    • Borst, P.; Zelcer, N.; van de Wetering, K.; Poolman, B. On the putative co-transport of drugs by multidrug resistance proteins. FEBS Lett. 2006, 580, 1085-1093.
    • (2006) FEBS Lett. , vol.580 , pp. 1085-1093
    • Borst, P.1    Zelcer, N.2    Van De Wetering, K.3    Poolman, B.4
  • 406
    • 17444419342 scopus 로고    scopus 로고
    • Molecular mechanisms of reduced glutathione transport: Role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins
    • Ballatori, N.; Hammond, C.L.; Cunningham, J.B.; Krance, S.M.; Marchan, R. Molecular mechanisms of reduced glutathione transport: Role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins. Toxicol. Appl. Pharmacol. 2005, 204, 238-255.
    • (2005) Toxicol. Appl. Pharmacol. , vol.204 , pp. 238-255
    • Ballatori, N.1    Hammond, C.L.2    Cunningham, J.B.3    Krance, S.M.4    Marchan, R.5
  • 407
    • 0032568838 scopus 로고    scopus 로고
    • 4 as a substrate for oatp1, the hepatic sinusoidal organic solute transporter
    • 4 as a substrate for oatp1, the hepatic sinusoidal organic solute transporter. J. Biol. Chem. 1998, 273, 16184-16191.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16184-16191
    • Li, L.1    Lee, T.K.2    Meier, P.J.3    Ballatori, N.4
  • 409
    • 33749540617 scopus 로고    scopus 로고
    • SLCO/OATP-like transport of glutathione in FasL-induced apoptosis: Glutathione efflux is coupled to an organic anion exchange and is necessary for the progression of the execution phase of apoptosis
    • Franco, R.; Cidlowski, J.A. SLCO/OATP-like transport of glutathione in FasL-induced apoptosis: Glutathione efflux is coupled to an organic anion exchange and is necessary for the progression of the execution phase of apoptosis. J. Biol. Chem. 2006, 281, 29542-29557.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29542-29557
    • Franco, R.1    Cidlowski, J.A.2
  • 410
    • 0037424431 scopus 로고    scopus 로고
    • Role of reduced glutathione efflux in apoptosis of immortalized human keratinocytes induced by UVA
    • He, Y.Y.; Huang, J.L.; Ramirez, D.C.; Chignell, C.F. Role of reduced glutathione efflux in apoptosis of immortalized human keratinocytes induced by UVA. J. Biol. Chem. 2003, 278, 8058-8064.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8058-8064
    • He, Y.Y.1    Huang, J.L.2    Ramirez, D.C.3    Chignell, C.F.4
  • 412
    • 0842281349 scopus 로고    scopus 로고
    • Activation of plasma membrane reduced glutathione transport in death receptor apoptosis of HepG2 cells
    • Hammond, C.L.; Madejczyk, M.S.; Ballatori, N. Activation of plasma membrane reduced glutathione transport in death receptor apoptosis of HepG2 cells. Toxicol. Appl. Pharmacol. 2004, 195, 12-22.
    • (2004) Toxicol. Appl. Pharmacol. , vol.195 , pp. 12-22
    • Hammond, C.L.1    Madejczyk, M.S.2    Ballatori, N.3
  • 414
    • 0029885118 scopus 로고    scopus 로고
    • Relation of oxidative stress and glutathione synthesis to CD95(Fas/APO-1)- mediated apoptosis of adult T cell leukemia cells
    • Kohno, T.; Yamada, Y.; Hata, T.; Mori, H.; Yamamura, M.; Tomonaga, M.; Urata, Y.; Goto, S.; Kondo, T. Relation of oxidative stress and glutathione synthesis to CD95(Fas/APO-1)- mediated apoptosis of adult T cell leukemia cells. J. Immunol. 1996, 156, 4722-4728.
    • (1996) J. Immunol. , vol.156 , pp. 4722-4728
    • Kohno, T.1    Yamada, Y.2    Hata, T.3    Mori, H.4    Yamamura, M.5    Tomonaga, M.6    Urata, Y.7    Goto, S.8    Kondo, T.9
  • 415
    • 34347230130 scopus 로고    scopus 로고
    • Glutathione export during apoptosis requires functional multidrug resistance-associated proteins
    • Hammond, C.L.; Marchan, R.; Krance, S.M.; Ballatori, N. Glutathione export during apoptosis requires functional multidrug resistance-associated proteins. J. Biol. Chem. 2007, 282, 14337-14347.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14337-14347
    • Hammond, C.L.1    Marchan, R.2    Krance, S.M.3    Ballatori, N.4
  • 416
    • 0013016426 scopus 로고    scopus 로고
    • Bioflavonoid stimulation of glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1)
    • Leslie, E.M.; Deeley, R.G.; Cole, S.P. Bioflavonoid stimulation of glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1). Drug Metab. Dispos. 2003, 31, 11-15.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 11-15
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.3
  • 417
    • 0033052299 scopus 로고    scopus 로고
    • Glutathione-dependent generation of reactive oxygen species by the peroxidase-catalyzed redox cycling of flavonoids
    • Galati, G.; Chan, T.; Wu, B.; O'Brien, P.J. Glutathione-dependent generation of reactive oxygen species by the peroxidase-catalyzed redox cycling of flavonoids. Chem. Res. Toxicol. 1999, 12, 521-525.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 521-525
    • Galati, G.1    Chan, T.2    Wu, B.3    O'Brien, P.J.4
  • 418
    • 0029074372 scopus 로고
    • ATPdependent efflux of calcein by the multidrug resistance protein (MRP): No inhibition by intracellular glutathione depletion
    • Feller, N.; Broxterman, H.J.; Wahrer, D.C.; Pinedo, H.M. ATPdependent efflux of calcein by the multidrug resistance protein (MRP): No inhibition by intracellular glutathione depletion. FEBS Lett. 1995, 368, 385-388.
    • (1995) FEBS Lett. , vol.368 , pp. 385-388
    • Feller, N.1    Broxterman, H.J.2    Wahrer, D.C.3    Pinedo, H.M.4
  • 419
    • 0032946239 scopus 로고    scopus 로고
    • ATP-dependent efflux of CPT-11 and SN-38 by the multidrug resistance protein (MRP) and its inhibition by PAK- 104P
    • Chen, Z.S.; Furukawa, T.; Sumizawa, T.; Ono, K.; Ueda, K.; Seto, K.; Akiyama, S.I. ATP-dependent efflux of CPT-11 and SN-38 by the multidrug resistance protein (MRP) and its inhibition by PAK- 104P. Mol. Pharmacol. 1999, 55, 921-928.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 921-928
    • Chen, Z.S.1    Furukawa, T.2    Sumizawa, T.3    Ono, K.4    Ueda, K.5    Seto, K.6    Akiyama, S.I.7
  • 420
    • 17544398019 scopus 로고    scopus 로고
    • The quinolinebased drug, N- [4- [1-hydroxy-2-(dibutylamino)ethyl] quinolin-8- yl]-4-azidosalicylamide, photoaffinity labels the multidrug resistance protein (MRP) at a biologically relevant site
    • Vezmar, M.; Deady, L.W.; Tilley, L.; Georges, E. The quinolinebased drug, N- [4- [1-hydroxy-2-(dibutylamino)ethyl] quinolin-8- yl]-4-azidosalicylamide, photoaffinity labels the multidrug resistance protein (MRP) at a biologically relevant site. Biochem. Biophys. Res. Commun. 1997, 241, 104-111.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 104-111
    • Vezmar, M.1    Deady, L.W.2    Tilley, L.3    Georges, E.4
  • 421
    • 0028930054 scopus 로고
    • Buthionine sulphoximine-mediated sensitisation of etoposide-resistant human breast cancer MCF7 cells overexpressing the multidrug resistanceassociated protein involves increased drug accumulation
    • Schneider, E.; Yamazaki, H.; Sinha, B.K.; Cowan, K.H. Buthionine sulphoximine-mediated sensitisation of etoposide-resistant human breast cancer MCF7 cells overexpressing the multidrug resistanceassociated protein involves increased drug accumulation. Br. J. Cancer 1995, 71, 738-743.
    • (1995) Br. J. Cancer , vol.71 , pp. 738-743
    • Schneider, E.1    Yamazaki, H.2    Sinha, B.K.3    Cowan, K.H.4
  • 424
    • 0035882764 scopus 로고    scopus 로고
    • Verapamil-stimulated glutathione transport by the multidrug resistance-associated protein (MRP1) in leukaemia cells
    • Cullen, K.V.; Davey, R.A.; Davey, M.W. Verapamil-stimulated glutathione transport by the multidrug resistance-associated protein (MRP1) in leukaemia cells. Biochem. Pharmacol. 2001, 62, 417-424.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 417-424
    • Cullen, K.V.1    Davey, R.A.2    Davey, M.W.3
  • 425
    • 36949010980 scopus 로고    scopus 로고
    • Multidrug resistance associated proteins as determining factors of pharmacokinetics and pharmacodynamics of drugs
    • Yu, X.Q.; Xue, C.C.; Wang, G.; Zhou, S.F. Multidrug resistance associated proteins as determining factors of pharmacokinetics and pharmacodynamics of drugs. Curr. Drug Metab. 2007, 8, 787-802.
    • (2007) Curr. Drug Metab. , vol.8 , pp. 787-802
    • Yu, X.Q.1    Xue, C.C.2    Wang, G.3    Zhou, S.F.4
  • 426
    • 33749267293 scopus 로고    scopus 로고
    • Role of pharmacogenetics of ATP-binding cassette transporters in the pharmacokinetics of drugs
    • Cascorbi, I. Role of pharmacogenetics of ATP-binding cassette transporters in the pharmacokinetics of drugs. Pharmacol. Ther. 2006, 112, 457-473.
    • (2006) Pharmacol. Ther. , vol.112 , pp. 457-473
    • Cascorbi, I.1
  • 428
    • 67649354458 scopus 로고    scopus 로고
    • Pharmacogenetics of human multidrug resistance associated proteins
    • Zhou, S.F. Pharmacogenetics of human multidrug resistance associated proteins. Curr. Pharmacogenom. Pers. Med. 2008, 6, 134-149.
    • (2008) Curr. Pharmacogenom. Pers. Med. , vol.6 , pp. 134-149
    • Zhou, S.F.1
  • 430
    • 33645747683 scopus 로고    scopus 로고
    • Association of highlevel MRP1 expression with poor clinical outcome in a large prospective study of primary neuroblastoma
    • Haber, M.; Smith, J.; Bordow, S.B.; Flemming, C.; Cohn, S.L.; London, W.B.; Marshall, G.M.; Norris, M.D. Association of highlevel MRP1 expression with poor clinical outcome in a large prospective study of primary neuroblastoma. J. Clin. Oncol. 2006, 24, 1546-1553.
    • (2006) J. Clin. Oncol. , vol.24 , pp. 1546-1553
    • Haber, M.1    Smith, J.2    Bordow, S.B.3    Flemming, C.4    Cohn, S.L.5    London, W.B.6    Marshall, G.M.7    Norris, M.D.8
  • 434
    • 70249108809 scopus 로고    scopus 로고
    • ABCC1 polymorphisms contribute to level and decline of lung function in two population-based cohorts
    • Siedlinski, M.; Boezen, H.M.; Boer, J.M.; Smit, H.A.; Postma, D.S. ABCC1 polymorphisms contribute to level and decline of lung function in two population-based cohorts. Pharmacogenet. Genomics 2009, 19, 675-684.
    • (2009) Pharmacogenet. Genomics , vol.19 , pp. 675-684
    • Siedlinski, M.1    Boezen, H.M.2    Boer, J.M.3    Smit, H.A.4    Postma, D.S.5
  • 435
    • 0034667390 scopus 로고    scopus 로고
    • Extensive contribution of the multidrug transporters P-glycoprotein and Mrp1 to basal drug resistance
    • Allen, J.D.; Brinkhuis, R.F.; van Deemter, L.; Wijnholds, J.; Schinkel, A.H. Extensive contribution of the multidrug transporters P-glycoprotein and Mrp1 to basal drug resistance. Cancer Res. 2000, 60, 5761-5766.
    • (2000) Cancer Res. , vol.60 , pp. 5761-5766
    • Allen, J.D.1    Brinkhuis, R.F.2    Van Deemter, L.3    Wijnholds, J.4    Schinkel, A.H.5
  • 437
    • 61449178747 scopus 로고    scopus 로고
    • Pharmacogenomics approach reveals MRP1 (ABCC1)-mediated resistance to geldanamycins
    • Pham, A.N.; Wang, J.; Fang, J.; Gao, X.; Zhang, Y.; Blower, P.E.; Sadee, W.; Huang, Y. Pharmacogenomics approach reveals MRP1 (ABCC1)-mediated resistance to geldanamycins. Pharm. Res. 2009, 26, 936-945.
    • (2009) Pharm. Res. , vol.26 , pp. 936-945
    • Pham, A.N.1    Wang, J.2    Fang, J.3    Gao, X.4    Zhang, Y.5    Blower, P.E.6    Sadee, W.7    Huang, Y.8
  • 438
    • 27944434891 scopus 로고    scopus 로고
    • Involvement of P-glycoprotein and MRP1 in resistance to cyclic tetrapeptide subfamily of histone deacetylase inhibitors in the drug-resistant osteosarcoma and Ewing's sarcoma cells
    • Okada, T.; Tanaka, K.; Nakatani, F.; Sakimura, R.; Matsunobu, T.; Li, X.; Hanada, M.; Nakamura, T.; Oda, Y.; Tsuneyoshi, M.; Iwamoto, Y. Involvement of P-glycoprotein and MRP1 in resistance to cyclic tetrapeptide subfamily of histone deacetylase inhibitors in the drug-resistant osteosarcoma and Ewing's sarcoma cells. Int. J. Cancer 2006, 118, 90-97.
    • (2006) Int. J. Cancer , vol.118 , pp. 90-97
    • Okada, T.1    Tanaka, K.2    Nakatani, F.3    Sakimura, R.4    Matsunobu, T.5    Li, X.6    Hanada, M.7    Nakamura, T.8    Oda, Y.9    Tsuneyoshi, M.10    Iwamoto, Y.11
  • 440
    • 0037032045 scopus 로고    scopus 로고
    • The protease inhibitor ritonavir inhibits the functional activity of the multidrug resistance related-protein 1 (MRP-1)
    • Olson, D.P.; Scadden, D.T.; D'Aquila, R.T.; De Pasquale, M.P. The protease inhibitor ritonavir inhibits the functional activity of the multidrug resistance related-protein 1 (MRP-1). Aids 2002, 16, 1743-1747.
    • (2002) Aids , vol.16 , pp. 1743-1747
    • Olson, D.P.1    Scadden, D.T.2    D'Aquila, R.T.3    De Pasquale, M.P.4
  • 442
    • 3342900005 scopus 로고    scopus 로고
    • Differential involvement of multidrug resistanceassociated protein 1 and P-glycoprotein in tissue distribution and excretion of grepafloxacin in mice
    • Sasabe, H.; Kato, Y.; Suzuki, T.; Itose, M.; Miyamoto, G.; Sugiyama, Y. Differential involvement of multidrug resistanceassociated protein 1 and P-glycoprotein in tissue distribution and excretion of grepafloxacin in mice. J. Pharmacol. Exp. Ther. 2004, 310, 648-655.
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 648-655
    • Sasabe, H.1    Kato, Y.2    Suzuki, T.3    Itose, M.4    Miyamoto, G.5    Sugiyama, Y.6
  • 443
    • 2142654891 scopus 로고    scopus 로고
    • Functional study of intracellular P-gp- and MRP1-mediated pumping of free cytosolic pirarubicin into acidic organelles in intrinsic resistant SiHa cells
    • Laochariyakul, P.; Ponglikitmongkol, M.; Mankhetkorn, S. Functional study of intracellular P-gp- and MRP1-mediated pumping of free cytosolic pirarubicin into acidic organelles in intrinsic resistant SiHa cells. Can. J. Physiol. Pharmacol. 2003, 81, 790-799.
    • (2003) Can. J. Physiol. Pharmacol. , vol.81 , pp. 790-799
    • Laochariyakul, P.1    Ponglikitmongkol, M.2    Mankhetkorn, S.3
  • 444
    • 0033815392 scopus 로고    scopus 로고
    • Limited distribution of new quinolone antibacterial agents into brain caused by multiple efflux transporters at the blood-brain barrier
    • Tamai, I.; Yamashita, J.; Kido, Y.; Ohnari, A.; Sai, Y.; Shima, Y.; Naruhashi, K.; Koizumi, S.; Tsuji, A. Limited distribution of new quinolone antibacterial agents into brain caused by multiple efflux transporters at the blood-brain barrier. J. Pharmacol. Exp. Ther. 2000, 295, 146-152.
    • (2000) J. Pharmacol. Exp. Ther. , vol.295 , pp. 146-152
    • Tamai, I.1    Yamashita, J.2    Kido, Y.3    Ohnari, A.4    Sai, Y.5    Shima, Y.6    Naruhashi, K.7    Koizumi, S.8    Tsuji, A.9
  • 445
    • 15844416284 scopus 로고    scopus 로고
    • Coordinated induction of MRP/GS-X pump and gamma-glutamylcysteine synthetase by heavy metals in human leukemia cells
    • Ishikawa, T.; Bao, J.J.; Yamane, Y.; Akimaru, K.; Frindrich, K.; Wright, C.D.; Kuo, M.T. Coordinated induction of MRP/GS-X pump and gamma- glutamylcysteine synthetase by heavy metals in human leukemia cells. J. Biol. Chem. 1996, 271, 14981-14988.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14981-14988
    • Ishikawa, T.1    Bao, J.J.2    Yamane, Y.3    Akimaru, K.4    Frindrich, K.5    Wright, C.D.6    Kuo, M.T.7
  • 446
    • 0031026289 scopus 로고    scopus 로고
    • Active efflux of the free acid form of the fluorescent dye 2',7'-bis(2-carboxyethyl)-5(6)- carboxyfluorescein in multidrug-resistance- protein-overexpressing murine and human leukemia cells
    • Draper, M.P.; Martell, R.L.; Levy, S.B. Active efflux of the free acid form of the fluorescent dye 2',7'-bis(2-carboxyethyl)-5(6)- carboxyfluorescein in multidrug-resistance-protein-overexpressing murine and human leukemia cells. Eur. J. Biochem. 1997, 243, 219-224.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 219-224
    • Draper, M.P.1    Martell, R.L.2    Levy, S.B.3
  • 447
    • 0343306779 scopus 로고    scopus 로고
    • Kinetic analysis of calcein and calcein-acetoxymethylester efflux mediated by the multidrug resistance protein and P-glycoprotein
    • Essodaigui, M.; Broxterman, H.J.; Garnier-Suillerot, A. Kinetic analysis of calcein and calcein-acetoxymethylester efflux mediated by the multidrug resistance protein and P-glycoprotein. Biochemistry 1998, 37, 2243-2250.
    • (1998) Biochemistry , vol.37 , pp. 2243-2250
    • Essodaigui, M.1    Broxterman, H.J.2    Garnier-Suillerot, A.3
  • 448
    • 0029958849 scopus 로고    scopus 로고
    • Transport properties of the multidrug resistance-associated protein (MRP) in human tumour cells
    • Hollo, Z.; Homolya, L.; Hegedus, T.; Sarkadi, B. Transport properties of the multidrug resistance-associated protein (MRP) in human tumour cells. FEBS Lett. 1996, 383, 99-104.
    • (1996) FEBS Lett. , vol.383 , pp. 99-104
    • Hollo, Z.1    Homolya, L.2    Hegedus, T.3    Sarkadi, B.4
  • 449
    • 0037473427 scopus 로고    scopus 로고
    • The multidrug resistanceassociated protein 1 transports methoxychlor and protects the seminiferous epithelium from injury
    • Tribull, T.E.; Bruner, R.H.; Bain, L.J. The multidrug resistanceassociated protein 1 transports methoxychlor and protects the seminiferous epithelium from injury. Toxicol. Lett. 2003, 142, 61-70.
    • (2003) Toxicol. Lett. , vol.142 , pp. 61-70
    • Tribull, T.E.1    Bruner, R.H.2    Bain, L.J.3
  • 450
    • 77949904065 scopus 로고    scopus 로고
    • Identification of multidrug resistance protein 1 (MRP1/ABCC1) as a molecular gate for cellular export of cobalamin
    • Beedholm-Ebsen, R.; van de Wetering, K.; Hardlei, T.; Nexo, E.; Borst, P.; Moestrup, S.K. Identification of multidrug resistance protein 1 (MRP1/ABCC1) as a molecular gate for cellular export of cobalamin. Blood 2010, 115, 1632-1639.
    • (2010) Blood , Issue.115 , pp. 1632-1639
    • Beedholm-Ebsen, R.1    Van De Wetering, K.2    Hardlei, T.3    Nexo, E.4    Borst, P.5    Moestrup, S.K.6
  • 451
    • 69449104493 scopus 로고    scopus 로고
    • ABCC1 ABCC2 and ABCC3 are implicated in the transepithelial transport of the myco-estrogen zearalenone and its major metabolites
    • Videmann, B.; Mazallon, M.; Prouillac, C.; Delaforge, M.; Lecoeur, S. ABCC1, ABCC2 and ABCC3 are implicated in the transepithelial transport of the myco-estrogen zearalenone and its major metabolites. Toxicol. Lett. 2009, 190, 215-223.
    • (2009) Toxicol. Lett. , vol.190 , pp. 215-223
    • Videmann, B.1    Mazallon, M.2    Prouillac, C.3    Delaforge, M.4    Lecoeur, S.5
  • 453
    • 17144465167 scopus 로고    scopus 로고
    • ATP-dependent transport of glutathione S-conjugates by the multidrug resistance protein MRP1 and its apical isoform MRP2
    • Keppler, D.; Leier, I.; Jedlitschky, G.; Konig, J. ATP-dependent transport of glutathione S-conjugates by the multidrug resistance protein MRP1 and its apical isoform MRP2. Chem. Biol. Interact. 1998, 111-112, 153-161.
    • (1998) Chem. Biol. Interact. , vol.111-112 , pp. 153-161
    • Keppler, D.1    Leier, I.2    Jedlitschky, G.3    Konig, J.4
  • 455
    • 0030668526 scopus 로고    scopus 로고
    • ATP-dependent transport of bilirubin glucuronides by the multidrug resistance protein MRP1 and its hepatocyte canalicular isoform MRP2
    • Jedlitschky, G.; Leier, I.; Buchholz, U.; Hummel-Eisenbeiss, J.; Burchell, B.; Keppler, D. ATP-dependent transport of bilirubin glucuronides by the multidrug resistance protein MRP1 and its hepatocyte canalicular isoform MRP2. Biochem. J. 1997, 327 (Pt 1), 305-310.
    • (1997) Biochem. J. , vol.327 , Issue.PART 1 , pp. 305-310
    • Jedlitschky, G.1    Leier, I.2    Buchholz, U.3    Hummel-Eisenbeiss, J.4    Burchell, B.5    Keppler, D.6
  • 456
    • 0030752006 scopus 로고    scopus 로고
    • Transport of glutathione conjugates and glucuronides by the multidrug resistance proteins MRP1 and MRP2
    • Keppler, D.; Leier, I.; Jedlitschky, G. Transport of glutathione conjugates and glucuronides by the multidrug resistance proteins MRP1 and MRP2. Biol. Chem. 1997, 378, 787-791.
    • (1997) Biol. Chem. , vol.378 , pp. 787-791
    • Keppler, D.1    Leier, I.2    Jedlitschky, G.3
  • 458
    • 33646732642 scopus 로고    scopus 로고
    • Nitrogen monoxide (NO)-mediated iron release from cells is linked to NOinduced glutathione efflux via multidrug resistance-associated protein 1
    • Watts, R.N.; Hawkins, C.; Ponka, P.; Richardson, D.R. Nitrogen monoxide (NO)-mediated iron release from cells is linked to NOinduced glutathione efflux via multidrug resistance-associated protein 1. Proc. Natl. Acad. Sci. U. S. A. 2006, 103, 7670-7675.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 7670-7675
    • Watts, R.N.1    Hawkins, C.2    Ponka, P.3    Richardson, D.R.4
  • 459
    • 67349170614 scopus 로고    scopus 로고
    • Involvement of the ABCtransporter ABCC1 and the sphingosine 1-phosphate receptor subtype S1P3 in the cytoprotection of human fibroblasts by the glucocorticoid dexamethasone
    • Nieuwenhuis, B.; Luth, A.; Chun, J.; Huwiler, A.; Pfeilschifter, J.; Schafer-Korting, M.; Kleuser, B. Involvement of the ABCtransporter ABCC1 and the sphingosine 1-phosphate receptor subtype S1P3 in the cytoprotection of human fibroblasts by the glucocorticoid dexamethasone. J. Mol. Med. 2009, 87, 645-657.
    • (2009) J. Mol. Med. , vol.87 , pp. 645-657
    • Nieuwenhuis, B.1    Luth, A.2    Chun, J.3    Huwiler, A.4    Pfeilschifter, J.5    Schafer-Korting, M.6    Kleuser, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.