메뉴 건너뛰기




Volumn 48, Issue 38, 2009, Pages 9122-9131

Effects of putative catalytic base mutation E211Q on ABCG2-mediated methotrexate transport

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ANTICANCER DRUG; ATP HYDROLYSIS; ATP-ASE ACTIVITY; ATP-BINDING CASSETTE; CATALYTIC BASE; CATALYTIC RESIDUE; FUSION PROTEINS; HETERODIMERS; HOMODIMERS; MEMBRANE VESICLES; NUCLEOTIDE-BINDING DOMAIN; PLASMA MEMBRANES; TRANS-MEMBRANE DOMAINS; TRANSPORT ACTIVITY;

EID: 70349782468     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900675v     Document Type: Article
Times cited : (11)

References (69)
  • 1
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano, R. L., and Ling, V. (1976) A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim. Biophys. Acta 455, 152-162.
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 3
    • 0032404092 scopus 로고    scopus 로고
    • A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance
    • Allikmets, R., Schriml, L. M., Hutchinson, A., Romano-Spica, V., and Dean, M. (1998) A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance. Cancer Res. 58, 5337-5339. (Pubitemid 28551112)
    • (1998) Cancer Research , vol.58 , Issue.23 , pp. 5337-5339
    • Allikmets, R.1    Schriml, L.M.2    Hutchinson, A.3    Romano-Spica, V.4    Dean, M.5
  • 5
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells
    • Chen, C. J., Chin, J. E., Ueda, K., Clark, D. P., Pastan, I., Gottesman, M. M., and Roninson, I. B. (1986) Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell 47, 381-389. (Pubitemid 17210152)
    • (1986) Cell , vol.47 , Issue.3 , pp. 381-389
    • Chen, C.-J.1    Chin, J.E.2    Ueda, K.3
  • 6
    • 0023278796 scopus 로고
    • Multidrug resistance in a human small cell lung cancer cell line selected in adriamycin
    • Mirski, S. E., Gerlach, J. H., and Cole, S. P. (1987) Multidrug resistance in a human small cell lung cancer cell line selected in adriamycin. Cancer Res. 47, 2594-2598. (Pubitemid 17083146)
    • (1987) Cancer Research , vol.47 , Issue.10 , pp. 2594-2598
    • Mirski, S.E.L.1    Gerlach, J.H.2    Cole, S.P.C.3
  • 7
    • 0032895533 scopus 로고    scopus 로고
    • Molecular cloning of cDNAs which are highly overexpressed in mitoxantrone-resistant cells: Demonstration of homology to ABC transport genes
    • Miyake, K., Mickley, L., Litman, T., Zhan, Z., Robey, R., Cristensen, B., Brangi, M., Greenberger, L., Dean, M., Fojo, T., and Bates, S. E. (1999) Molecular cloning of cDNAs which are highly overexpressed in mitoxantrone-resistant cells: demonstration of homology to ABC transport genes. Cancer Res. 59, 8-13. (Pubitemid 29062946)
    • (1999) Cancer Research , vol.59 , Issue.1 , pp. 8-13
    • Miyake, K.1    Mickley, L.2    Litman, T.3    Zhan, Z.4    Robey, R.5    Cristensen, B.6    Brangi, M.7    Greenberger, L.8    Dean, M.9    Fojo, T.10    Bates, S.E.11
  • 8
    • 0029896988 scopus 로고    scopus 로고
    • Mutational analysis of the predicted first transmembrane segment of each homologous half of human P-glycoprotein suggests that they are symmetrically arranged in the membrane
    • Loo, T. W., and Clarke, D. M. (1996) Mutational analysis of the predicted first transmembrane segment of each homologous half of human P-glycoprotein suggests that they are symmetrically arranged in the membrane. J. Biol. Chem. 271, 15414-15419.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15414-15419
    • Loo, T.W.1    Clarke, D.M.2
  • 11
    • 0037073730 scopus 로고    scopus 로고
    • Characterization of drug transport, ATP hydrolysis, and nucleotide trapping by the human ABCG2 multidrug transporter. Modulation of substrate specificity by a point mutation
    • Ozvegy, C., Varadi, A., and Sarkadi, B. (2002) Characterization of drug transport, ATP hydrolysis, and nucleotide trapping by the human ABCG2 multidrug transporter. Modulation of substrate specificity by a point mutation. J. Biol. Chem. 277, 47980-47990.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47980-47990
    • Ozvegy, C.1    Varadi, A.2    Sarkadi, B.3
  • 12
    • 0037050736 scopus 로고    scopus 로고
    • Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization
    • DOI 10.1002/ijc.10100
    • Kage, K., Tsukahara, S., Sugiyama, T., Asada, S., Ishikawa, E., Tsuruo, T., and Sugimoto, Y. (2002) Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization. Int. J. Cancer 97, 626-630. (Pubitemid 34087801)
    • (2002) International Journal of Cancer , vol.97 , Issue.5 , pp. 626-630
    • Kage, K.1    Tsukahara, S.2    Sugiyama, T.3    Asada, S.4    Ishikawa, E.5    Tsuruo, T.6    Sugimoto, Y.7
  • 14
    • 0347755373 scopus 로고    scopus 로고
    • Multidrug resistance in cancer chemotherapy and xenobiotic protection mediated by the half ATP-binding cassette transporter ABCG2
    • Han, B., and Zhang, J. T. (2004) Multidrug resistance in cancer chemotherapy and xenobiotic protection mediated by the half ATP-binding cassette transporter ABCG2. Curr. Med. Chem. Anti-Cancer Agents 4, 31-42.
    • (2004) Curr. Med. Chem. Anti-Cancer Agents , vol.4 , pp. 31-42
    • Han, B.1    Zhang, J.T.2
  • 15
    • 0027391633 scopus 로고
    • Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody
    • Georges, E., Tsuruo, T., and Ling, V. (1993) Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody. J. Biol. Chem. 268, 1792-1798.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1792-1798
    • Georges, E.1    Tsuruo, T.2    Ling, V.3
  • 16
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • DOI 10.1016/S1097-2765(02)00576-2
    • Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., and Hunt, J. F. (2002) ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149. (Pubitemid 34876568)
    • (2002) Molecular Cell , vol.10 , Issue.1 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 17
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • DOI 10.1016/j.molcel.2003.08.004
    • Chen, J., Lu, G., Lin, J., Davidson, A. L., and Quiocho, F. A. (2003) A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12, 651-661. (Pubitemid 37222486)
    • (2003) Molecular Cell , vol.12 , Issue.3 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 18
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • Moody, J. E., Millen, L., Binns, D., Hunt, J. F., and Thomas, P. J. (2002) Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters. J. Biol. Chem. 277, 21111-21114.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 19
    • 0038374988 scopus 로고    scopus 로고
    • Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: Nucleotide-free and nucleotide-bound conformations
    • Verdon, G., Albers, S. V., Dijkstra, B. W., Driessen, A. J., and Thunnissen, A. M. (2003) Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. J. Mol. Biol. 330, 343-358.
    • (2003) J. Mol. Biol. , vol.330 , pp. 343-358
    • Verdon, G.1    Albers, S.V.2    Dijkstra, B.W.3    Driessen, A.J.4    Thunnissen, A.M.5
  • 20
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • DOI 10.1126/science.1071142
    • Locher, K. P., Lee, A. T., and Rees, D. C. (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296, 1091-1098. (Pubitemid 34517120)
    • (2002) Science , vol.296 , Issue.5570 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 21
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • DOI 10.1038/nature05626, PII NATURE05626
    • Hollenstein, K., Frei, D. C., and Locher, K. P. (2007) Structure of an ABC transporter in complex with its binding protein. Nature 446, 213-216. (Pubitemid 46398672)
    • (2007) Nature , vol.446 , Issue.7132 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 22
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • DOI 10.1038/nature06264
    • Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L., and Chen, J. (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515-521. (Pubitemid 350190241)
    • (2007) Nature , vol.450 , Issue.7169 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 23
    • 0035801375 scopus 로고    scopus 로고
    • Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing
    • DOI 10.1093/emboj/20.17.4964
    • Gaudet, R., and Wiley, D. C. (2001) Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing. EMBO J. 20, 4964-4972. (Pubitemid 32848648)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4964-4972
    • Gaudet, R.1    Wiley, D.C.2
  • 24
    • 29144502288 scopus 로고    scopus 로고
    • ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation
    • Lu, G., Westbrooks, J. M., Davidson, A. L., and Chen, J. (2005) ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation. Proc. Natl. Acad. Sci. U.S.A. 102, 17969-17974.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 17969-17974
    • Lu, G.1    Westbrooks, J.M.2    Davidson, A.L.3    Chen, J.4
  • 25
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K. P., Karcher, A., Shin, D. S., Craig, L., Arthur, L. M., Carney, J. P., and Tainer, J. A. (2000) Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101, 789-800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 26
    • 0035943735 scopus 로고    scopus 로고
    • The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter
    • Yuan, Y. R., Blecker, S., Martsinkevich, O., Millen, L., Thomas, P. J., and Hunt, J. F. (2001) The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter. J. Biol. Chem. 276, 32313-32321.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32313-32321
    • Yuan, Y.R.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas, P.J.5    Hunt, J.F.6
  • 27
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • DOI 10.1038/25393
    • Hung, L. W., Wang, I. X., Nikaido, K., Liu, P. Q., Ames, G. F., and Kim, S. H. (1998) Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396, 703-707. (Pubitemid 29003952)
    • (1998) Nature , vol.396 , Issue.6712 , pp. 703-707
    • Hung, L.-W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.-Q.4    Ames, G.F.-L.5    Kim, S.-H.6
  • 28
    • 33749076230 scopus 로고    scopus 로고
    • Distinct Structural and Functional Properties of the ATPase Sites in an Asymmetric ABC Transporter
    • DOI 10.1016/j.molcel.2006.07.034, PII S1097276506005363
    • Procko, E., Ferrin-O'Connell, I., Ng, S. L., and Gaudet, R. (2006) Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter. Mol. Cell 24, 51-62. (Pubitemid 44466678)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 51-62
    • Procko, E.1    Ferrin-O'Connell, I.2    Ng, S.-L.3    Gaudet, R.4
  • 29
    • 0035964385 scopus 로고    scopus 로고
    • Sequence requirements of the ATP-binding site within the C-terminal nucleotide-binding domain of mouse P-glycoprotein: Structure-activity relationships for flavonoid binding
    • DOI 10.1021/bi010657c
    • de Wet, H., McIntosh, D. B., Conseil, G., Baubichon-Cortay, H., Krell, T., Jault, J. M., Daskiewicz, J. B., Barron, D., and Di Pietro, A. (2001) Sequence requirements of the ATP-binding site within the C-terminal nucleotide-binding domain of mouse P-glycoprotein: structure-activity relationships for flavonoid binding. Biochemistry 40, 10382-10391. (Pubitemid 32800145)
    • (2001) Biochemistry , vol.40 , Issue.34 , pp. 10382-10391
    • De Wet, H.1    McIntosh, D.B.2    Conseil, G.3    Baubichon-Cortay, H.4    Krell, T.5    Jault, J.-M.6    Daskiewicz, J.-B.7    Barron, D.8    Di Pietro, A.9
  • 31
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • DOI 10.1038/sj.emboj.7600657
    • Zaitseva, J., Jenewein, S., Jumpertz, T., Holland, I. B., and Schmitt, L. (2005) H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24, 1901-1910. (Pubitemid 40896162)
    • (2005) EMBO Journal , vol.24 , Issue.11 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 33
    • 0034941969 scopus 로고    scopus 로고
    • Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter
    • DOI 10.1016/S0969-2126(01)00617-7, PII S0969212601006177
    • Karpowich, N., Martsinkevich, O., Millen, L., Yuan, Y. R., Dai, P. L., MacVey, K., Thomas, P. J., and Hunt, J. F. (2001) Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Structure (Cambridge) 9, 571-586. (Pubitemid 32695582)
    • (2001) Structure , vol.9 , Issue.7 , pp. 571-586
    • Karpowich, N.1    Martsinkevich, O.2    Millen, L.3    Yuan, Y.-R.4    Dai, P.L.5    MacVey, K.6    Thomas, P.J.7    Hunt, J.F.8
  • 34
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of Malk, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs, K., Diez, J., Greller, G., Muller, C., Breed, J., Schnell, C., Vonrhein, C., Boos, W., and Welte, W. (2000) Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J. 19, 5951-5961. (Pubitemid 30943321)
    • (2000) EMBO Journal , vol.19 , Issue.22 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3    Muller, C.4    Breed, J.5    Schnell, C.6    Vonrhein, C.7    Boos, W.8    Welte, W.9
  • 35
    • 27844467773 scopus 로고    scopus 로고
    • A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva, J., Jenewein, S., Oswald, C., Jumpertz, T., Holland, I. B., and Schmitt, L. (2005) A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB. Biochem. Soc. Trans. 33, 990-995.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 990-995
    • Zaitseva, J.1    Jenewein, S.2    Oswald, C.3    Jumpertz, T.4    Holland, I.B.5    Schmitt, L.6
  • 36
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer
    • DOI 10.1038/sj.emboj.7601208, PII 7601208
    • Zaitseva, J., Oswald, C., Jumpertz, T., Jenewein, S., Wiedenmann, A., Holland, I. B., and Schmitt, L. (2006) A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer. EMBO J. 25, 3432-3443. (Pubitemid 44141799)
    • (2006) EMBO Journal , vol.25 , Issue.14 , pp. 3432-3443
    • Zaitseva, J.1    Oswald, C.2    Jumpertz, T.3    Jenewein, S.4    Wiedenmann, A.5    Holland, I.B.6    Schmitt, L.7
  • 37
    • 34447311648 scopus 로고    scopus 로고
    • Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism
    • Dawson, R. J., Hollenstein, K., and Locher, K. P. (2007) Uptake or extrusion: crystal structures of full ABC transporters suggest a common mechanism. Mol. Microbiol. 65, 250-257.
    • (2007) Mol. Microbiol. , vol.65 , pp. 250-257
    • Dawson, R.J.1    Hollenstein, K.2    Locher, K.P.3
  • 39
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • DOI 10.1126/science.1133488
    • Pinkett, H. W., Lee, A. T., Lum, P., Locher, K. P., and Rees, D. C. (2007) An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315, 373-377. (Pubitemid 46175517)
    • (2007) Science , vol.315 , Issue.5810 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 40
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak, M. (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44, 283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 41
    • 0023669148 scopus 로고
    • Cell lineage ablation in transgenic mice by cell-specific expression of a toxin gene
    • erratum: (1990) Cell 62, 608
    • Palmiter, R. D., Behringer, R. R., Quaife, C. J., Maxwell, F., Maxwell, I. H., and Brinster, R. L. (1987) Cell lineage ablation in transgenic mice by cell-specific expression of a toxin gene. Cell 50, 435-443 [erratum: (1990) Cell 62, 608].
    • (1987) Cell , vol.50 , pp. 435-443
    • Palmiter, R.D.1    Behringer, R.R.2    Quaife, C.J.3    Maxwell, F.4    Maxwell, I.H.5    Brinster, R.L.6
  • 42
    • 0027311276 scopus 로고
    • Protein kinase a (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites
    • Chang, X. B., Tabcharani, J. A., Hou, Y. X., Jensen, T. J., Kartner, N., Alon, N., Hanrahan, J. W., and Riordan, J. R. (1993) Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites. J. Biol. Chem. 268, 11304-11311.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11304-11311
    • Chang, X.B.1    Tabcharani, J.A.2    Hou, Y.X.3    Jensen, T.J.4    Kartner, N.5    Alon, N.6    Hanrahan, J.W.7    Riordan, J.R.8
  • 43
    • 0030689692 scopus 로고    scopus 로고
    • ATPase activity of purified multidrug resistance-associated protein
    • erratum: (1998) J. Biol. Chem. 273, 7782
    • Chang, X. B., Hou, Y. X., and Riordan, J. R. (1997) ATPase activity of purified multidrug resistance-associated protein. J. Biol. Chem. 272, 30962-30968 [erratum: (1998) J. Biol. Chem. 273, 7782].
    • (1997) J. Biol. Chem. , vol.272 , pp. 30962-30968
    • Chang, X.B.1    Hou, Y.X.2    Riordan, J.R.3
  • 44
    • 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., and Chang, X. B. (2000) Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1. J. Biol. Chem. 275, 20280-20287.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20280-20287
    • Hou, Y.1    Cui, L.2    Riordan, J.R.3    Chang, X.B.4
  • 46
    • 3142766112 scopus 로고    scopus 로고
    • Visualization of G protein betagamma dimers using bimolecular fluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting
    • Hynes, T. R., Tang, L., Mervine, S. M., Sabo, J. L., Yost, E. A., Devreotes, P. N., and Berlot, C. H. (2004) Visualization of G protein betagamma dimers using bimolecular fluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting. J. Biol. Chem. 279, 30279-30286.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30279-30286
    • Hynes, T.R.1    Tang, L.2    Mervine, S.M.3    Sabo, J.L.4    Yost, E.A.5    Devreotes, P.N.6    Berlot, C.H.7
  • 47
    • 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., and Chang, X. B. (2001) Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation. Arch. Biochem. Biophys. 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
  • 48
    • 0028347079 scopus 로고
    • Characterization of the ATP-dependent leukotriene C4 export carrier in mastocytoma cells
    • Leier, I., Jedlitschky, G., Buchholz, U., and Keppler, D. (1994) Characterization of the ATP-dependent leukotriene C4 export carrier in mastocytoma cells. Eur. J. Biochem. 220, 599-606.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 599-606
    • Leier, I.1    Jedlitschky, G.2    Buchholz, U.3    Keppler, D.4
  • 49
    • 0030009305 scopus 로고    scopus 로고
    • Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transport
    • Loe, D. W., Almquist, K. C., Deeley, R. G., and Cole, S. P. (1996) Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transport. J. Biol. Chem. 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
  • 51
    • 0042068263 scopus 로고    scopus 로고
    • A functional study on polymorphism of the ATP-binding cassette transporter ABCG2: Critical role of arginine-482 in methotrexate transport
    • DOI 10.1042/BJ20030150
    • Mitomo, H., Kato, R., Ito, A., Kasamatsu, S., Ikegami, Y., Kii, I., Kudo, A., Kobatake, E., Sumino, Y., and Ishikawa, T. (2003) A functional study on polymorphism of the ATP-binding cassette transporter ABCG2: critical role of arginine-482 in methotrexate transport. Biochem. J. 373, 767-774. (Pubitemid 36981086)
    • (2003) Biochemical Journal , vol.373 , Issue.3 , pp. 767-774
    • Mitomo, H.1    Kato, R.2    Ito, A.3    Kasamatsu, S.4    Ikegami, Y.5    Kii, I.6    Kudos, A.7    Kobatake, E.8    Sumino, Y.9    Ishikawa, T.10
  • 52
    • 85009628144 scopus 로고    scopus 로고
    • Expression and functional characterization of human ABC transporter ABCG2 variants in insect cells
    • Ishikawa, T., Kasamatsu, S., Hagiwara, Y., Mitomo, H., Kato, R., and Sumino, Y. (2003) Expression and functional characterization of human ABC transporter ABCG2 variants in insect cells. Drug Metab. Pharmacokinet. 18, 194-202.
    • (2003) Drug Metab. Pharmacokinet. , vol.18 , pp. 194-202
    • Ishikawa, T.1    Kasamatsu, S.2    Hagiwara, Y.3    Mitomo, H.4    Kato, R.5    Sumino, Y.6
  • 53
    • 2442520293 scopus 로고    scopus 로고
    • Characterization of oligomeric human half-ABC transporter ATP-binding cassette G2
    • Xu, J., Liu, Y., Yang, Y., Bates, S., and Zhang, J. T. (2004) Characterization of oligomeric human half-ABC transporter ATP-binding cassette G2. J. Biol. Chem. 279, 19781-19789.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19781-19789
    • Xu, J.1    Liu, Y.2    Yang, Y.3    Bates, S.4    Zhang, J.T.5
  • 54
    • 17844405072 scopus 로고    scopus 로고
    • Effect of Walker a mutation (K86M) on oligomerization and surface targeting of the multidrug resistance transporter ABCG2
    • Henriksen, U., Gether, U., and Litman, T. (2005) Effect of Walker A mutation (K86M) on oligomerization and surface targeting of the multidrug resistance transporter ABCG2. J. Cell. Sci. 118, 1417-1426.
    • (2005) J. Cell. Sci. , vol.118 , pp. 1417-1426
    • Henriksen, U.1    Gether, U.2    Litman, T.3
  • 55
    • 0141815941 scopus 로고    scopus 로고
    • Wild-type breast cancer resistance protein (BCRP/ABCG2) is a methotrexate polyglutamate transporter
    • Volk, E. L., and Schneider, E. (2003) Wild-type breast cancer resistance protein (BCRP/ABCG2) is a methotrexate polyglutamate transporter. Cancer Res. 63, 5538-5543.
    • (2003) Cancer Res. , vol.63 , pp. 5538-5543
    • Volk, E.L.1    Schneider, E.2
  • 56
    • 0042354831 scopus 로고    scopus 로고
    • Transport of methotrexate, methotrexate polyglutamates, and 17beta-estradiol 17-(beta-D-glucuronide) by ABCG2: Effects of acquired mutations at R482 on methotrexate transport
    • Chen, Z. S., Robey, R. W., Belinsky, M. G., Shchaveleva, I., Ren, X. Q., Sugimoto, Y., Ross, D. D., Bates, S. E., and Kruh, G. D. (2003) Transport of methotrexate, methotrexate polyglutamates, and 17beta-estradiol 17-(beta-D-glucuronide) by ABCG2: effects of acquired mutations at R482 on methotrexate transport. Cancer Res. 63, 4048-4054. (Pubitemid 36917926)
    • (2003) Cancer Research , vol.63 , Issue.14 , pp. 4048-4054
    • Chen, Z.-S.1    Robey, R.W.2    Belinsky, M.G.3    Shchaveleva, I.4    Ren, X.-Q.5    Sugimoto, Y.6    Ross, D.D.7    Bates, S.E.8    Kruh, G.D.9
  • 57
    • 0034700265 scopus 로고    scopus 로고
    • Mutational analysis of conserved carboxylate residues in the nucleotide binding sites of P-glycoprotein
    • DOI 10.1021/bi001128w
    • Urbatsch, I. L., Julien, M., Carrier, I., Rousseau, M. E., Cayrol, R., and Gros, P. (2000) Mutational analysis of conserved carboxylate residues in the nucleotide binding sites of P-glycoprotein. Biochemistry 39, 14138-14149. (Pubitemid 30842324)
    • (2000) Biochemistry , vol.39 , Issue.46 , pp. 14138-14149
    • Urbatsch, I.L.1    Julien, M.2    Carrier, I.3    Rousseau, M.-E.4    Cayrol, R.5    Gros, P.6
  • 58
    • 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)
    • DOI 10.1074/jbc.M305786200
    • Payen, L. F., Gao, M., Westlake, C. J., Cole, S. P., and Deeley, R. G. (2003) 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. 278, 38537-38547. (Pubitemid 37221749)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 38537-38547
    • Payen, L.F.1    Gao, M.2    Westlake, C.J.3    Cole, S.P.C.4    Deeley, R.G.5
  • 59
    • 14544295691 scopus 로고    scopus 로고
    • Nucleotide dissociation from NBD1 promotes solute transport by MRP1
    • Yang, R., McBride, A., Hou, Y. X., Goldberg, A., and Chang, X. B. (2005) Nucleotide dissociation from NBD1 promotes solute transport by MRP1. Biochim. Biophys. Acta 1668, 248-261.
    • (2005) Biochim. Biophys. Acta , vol.1668 , pp. 248-261
    • Yang, R.1    McBride, A.2    Hou, Y.X.3    Goldberg, A.4    Chang, X.B.5
  • 60
    • 67349103361 scopus 로고    scopus 로고
    • Becatecarin (rebeccamycin analog, NSC 655649) is a transport substrate and induces expression of theATP-binding cassette transporter, ABCG2, in lung carcinoma cells
    • in press
    • Robey, R. W., Obrzut, T., Shukla, S., Polgar, O., Macalou, S., Bahr, J. C., Di Pietro, A., Ambudkar, S. V., and Bates, S. E. (2009) Becatecarin (rebeccamycin analog, NSC 655649) is a transport substrate and induces expression of theATP-binding cassette transporter, ABCG2, in lung carcinoma cells. Cancer Chemother. Pharmacol. (in press).
    • (2009) Cancer Chemother. Pharmacol.
    • Robey, R.W.1    Obrzut, T.2    Shukla, S.3    Polgar, O.4    Macalou, S.5    Bahr, J.C.6    Di Pietro, A.7    Ambudkar, S.V.8    Bates, S.E.9
  • 62
    • 3042765579 scopus 로고    scopus 로고
    • Functional expression of the human breast cancer resistance protein in Pichia pastoris
    • Mao, Q., Conseil, G., Gupta, A., Cole, S. P., and Unadkat, J. D. (2004) Functional expression of the human breast cancer resistance protein in Pichia pastoris. Biochem. Biophys. Res. Commun. 320, 730-737.
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 730-737
    • Mao, Q.1    Conseil, G.2    Gupta, A.3    Cole, S.P.4    Unadkat, J.D.5
  • 63
    • 0038757689 scopus 로고    scopus 로고
    • Sterol transport by the human breast cancer resistance protein (ABCG2) expressed in Lactococcus lactis
    • Janvilisri, T., Venter, H., Shahi, S., Reuter, G., Balakrishnan, L., and van Veen, H. W. (2003) Sterol transport by the human breast cancer resistance protein (ABCG2) expressed in Lactococcus lactis. J. Biol. Chem. 278, 20645-20651.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20645-20651
    • Janvilisri, T.1    Venter, H.2    Shahi, S.3    Reuter, G.4    Balakrishnan, L.5    Van Veen, H.W.6
  • 64
    • 23844530574 scopus 로고    scopus 로고
    • Oligomerization of the human ABC transporter ABCG2: Evaluation of the native protein and chimeric dimers
    • DOI 10.1021/bi0503807
    • Bhatia, A., Schafer, H. J., and Hrycyna, C. A. (2005) Oligomerization of the human ABC transporter ABCG2: evaluation of the native protein and chimeric dimers. Biochemistry 44, 10893-10904. (Pubitemid 41153650)
    • (2005) Biochemistry , vol.44 , Issue.32 , pp. 10893-10904
    • Bhatia, A.1    Schafer, H.-J.2    Hrycyna, C.A.3
  • 65
    • 49349089223 scopus 로고    scopus 로고
    • Is ATP binding responsible for initiating drug translocation by the multidrug transporter ABCG2?
    • McDevitt, C. A., Crowley, E., Hobbs, G., Starr, K. J., Kerr, I. D., and Callaghan, R. (2008) Is ATP binding responsible for initiating drug translocation by the multidrug transporter ABCG2? FEBS J. 275, 4354-4362.
    • (2008) FEBS J. , vol.275 , pp. 4354-4362
    • McDevitt, C.A.1    Crowley, E.2    Hobbs, G.3    Starr, K.J.4    Kerr, I.D.5    Callaghan, R.6
  • 66
    • 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., and Deeley, R. G. (2000) Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1. J. Biol. Chem. 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
  • 67
    • 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
    • DOI 10.1042/BJ20051363
    • Buyse, F., Hou, Y. X., Vigano, C., Zhao, Q., Ruysschaert, J. M., and Chang, X. B. (2006) 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. 397, 121-130. (Pubitemid 44032843)
    • (2006) Biochemical Journal , vol.397 , Issue.1 , pp. 121-130
    • Buyse, F.1    Hou, Y.-X.2    Vigano, C.3    Zhao, Q.4    Ruysschaert, J.-M.5    Chang, X.-B.6
  • 68
    • 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., and Chang, X. B. (2008) 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 1778, 454-465.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 454-465
    • Yang, R.1    Scavetta, R.2    Chang, X.B.3
  • 69
    • 21744431708 scopus 로고    scopus 로고
    • 4 binding sites of multidrug resistance protein 1 (ABCC1)
    • DOI 10.1124/mol.104.007708
    • Payen, L., Gao, M., Westlake, C., Theis, A., Cole, S. P., and Deeley, R. G. (2005) Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1). Mol. Pharmacol. 67, 1944-1953. (Pubitemid 41007776)
    • (2005) Molecular Pharmacology , vol.67 , Issue.6 , pp. 1944-1953
    • Payen, L.1    Gao, M.2    Westlake, C.3    Theis, A.4    Cole, S.P.C.5    Deeley, R.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.