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Volumn 8, Issue , 2012, Pages 145-173

Molecular aspects of the translocation process by ABC proteins

Author keywords

ABC proteins; ATP hydrolysis; Bioenergetic coupling; Drug binding site; Drug translocation; Export protein; Import protein; Membrane protein structure; Membrane transport; Multidrug resistance; Nucleotide binding domain; Periplasmic binding protein; Transport mechanism; Uptake

Indexed keywords


EID: 84882787424     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374920-8.00812-2     Document Type: Chapter
Times cited : (14)

References (341)
  • 1
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson A.L., Dassa E., Orelle C., Chen J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 2008, 72(2):317-364.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , Issue.2 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 2
    • 25844487733 scopus 로고    scopus 로고
    • Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates
    • Dean M., Annilo T. Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates. Annu. Rev. Genom. Hum. Genet. 2005, 6(1):123-142.
    • (2005) Annu. Rev. Genom. Hum. Genet. , vol.6 , Issue.1 , pp. 123-142
    • Dean, M.1    Annilo, T.2
  • 3
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • Schneider E., Hunke S. ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains. FEMS Microbiol. Rev. 1998, 22(1):1-20.
    • (1998) FEMS Microbiol. Rev. , vol.22 , Issue.1 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 5
    • 0035010486 scopus 로고    scopus 로고
    • Translational regulation by ABC systems
    • Chakraburtty K. Translational regulation by ABC systems. Res. Microbiol. 2001, 152(3-4):391-399.
    • (2001) Res. Microbiol. , vol.152 , Issue.3-4 , pp. 391-399
    • Chakraburtty, K.1
  • 6
    • 0035001894 scopus 로고    scopus 로고
    • Role of ATP hydrolysis by UvrA and UvrB during nucleotide excision repair
    • Goosen N., Moolenaar G.F. Role of ATP hydrolysis by UvrA and UvrB during nucleotide excision repair. Res. Microbiol. 2001, 152(3-4):401-409.
    • (2001) Res. Microbiol. , vol.152 , Issue.3-4 , pp. 401-409
    • Goosen, N.1    Moolenaar, G.F.2
  • 7
    • 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(5570):1091-1098.
    • (2002) Science , vol.296 , Issue.5570 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 8
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. coli methionine ABC transporter: Structure and allosteric regulation
    • Kadaba N.S., Kaiser J.T., Johnson E., Lee A., Rees D.C. The high-affinity E. coli methionine ABC transporter: Structure and allosteric regulation. Science 2008, 321(5886):250-253.
    • (2008) Science , vol.321 , Issue.5886 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 10
    • 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(10):520-531.
    • (2009) Trends Biochem. Sci. , vol.34 , Issue.10 , pp. 520-531
    • Jones, P.M.1    O'Mara, M.L.2    George, A.M.3
  • 11
  • 12
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen J., Lu G., Lin J., Davidson A.L., Quiocho F.A. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 2003, 12(3):651-661.
    • (2003) Mol. 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
  • 13
    • 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., Tainer J.A. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 2000, 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
  • 14
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung L.W., Wang I.X., Nikaido K., Liu P.Q., Ames G.F., Kim S.H. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 1998, 396(6712):703-707.
    • (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.5    Kim, S.H.6
  • 15
    • 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
    • Karpowich N., Martsinkevich O., Millen L., Yuan Y.R., Dai P.L., MacVey K., Thomas P.J., Hunt J.F. Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Structure (Cambridge) 2001, 9(7):571-586.
    • (2001) Structure (Cambridge) , 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
  • 16
    • 0037424465 scopus 로고    scopus 로고
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding. J. Biol. Chem. 2003, 278(10):8429-8434.
    • (2003) J. Biol. Chem. , vol.278 , Issue.10 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 17
    • 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., Schmitt L. A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB. Biochem. Soc. Trans. 2005, 33(Pt 5):990-995.
    • (2005) Biochem. Soc. Trans. , vol.33 , Issue.PT 5 , pp. 990-995
    • Zaitseva, J.1    Jenewein, S.2    Oswald, C.3    Jumpertz, T.4    Holland, I.B.5    Schmitt, L.6
  • 18
    • 0035801375 scopus 로고    scopus 로고
    • Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing
    • Gaudet R., Wiley D.C. Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing. EMBO J. 2001, 20(17):4964-4972.
    • (2001) EMBO J. , vol.20 , Issue.17 , pp. 4964-4972
    • Gaudet, R.1    Wiley, D.C.2
  • 21
    • 65749102092 scopus 로고    scopus 로고
    • - channel by ATP-driven nucleotide-binding domain dimerisation
    • - channel by ATP-driven nucleotide-binding domain dimerisation. J. Physiol. 2009, 587(Pt 10):2151-2161.
    • (2009) J. Physiol. , vol.587 , Issue.PT 10 , pp. 2151-2161
    • Hwang, T.C.1    Sheppard, D.N.2
  • 22
    • 0025987020 scopus 로고
    • Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
    • Cheng S.H., Rich D.P., Marshall J., Gregory R.J., Welsh M.J., Smith A.E. Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel. Cell 1991, 66(5):1027-1036.
    • (1991) Cell , vol.66 , Issue.5 , pp. 1027-1036
    • Cheng, S.H.1    Rich, D.P.2    Marshall, J.3    Gregory, R.J.4    Welsh, M.J.5    Smith, A.E.6
  • 23
    • 0028328645 scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase causes a conformational change in the R domain of the cystic fibrosis transmembrane conductance regulator
    • Dulhanty A.M., Riordan J.R. Phosphorylation by cAMP-dependent protein kinase causes a conformational change in the R domain of the cystic fibrosis transmembrane conductance regulator. Biochemistry 1994, 33(13):4072-4079.
    • (1994) Biochemistry , vol.33 , Issue.13 , pp. 4072-4079
    • Dulhanty, A.M.1    Riordan, J.R.2
  • 25
    • 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., Riordan J.R. Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites. J. Biol. Chem. 1993, 268(15):11304-11311.
    • (1993) J. Biol. Chem. , vol.268 , Issue.15 , 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
  • 26
    • 33750222000 scopus 로고    scopus 로고
    • In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer
    • Mense M., Vergani P., White D.M., Altberg G., Nairn A.C., Gadsby D.C. In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer. EMBO J. 2006, 25(20):4728-4739.
    • (2006) EMBO J. , vol.25 , Issue.20 , pp. 4728-4739
    • Mense, M.1    Vergani, P.2    White, D.M.3    Altberg, G.4    Nairn, A.C.5    Gadsby, D.C.6
  • 27
    • 0026031479 scopus 로고
    • A 45-kDa protein antigenically related to band 3 is selectively expressed in kidney mitochondria
    • Ostedgaard L.S., Jennings M.L., Karniski L.P., Schuster V.L. A 45-kDa protein antigenically related to band 3 is selectively expressed in kidney mitochondria. Proc. Natl. Acad. Sci. USA 1991, 88(3):981-985.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.3 , pp. 981-985
    • Ostedgaard, L.S.1    Jennings, M.L.2    Karniski, L.P.3    Schuster, V.L.4
  • 28
    • 33846678695 scopus 로고    scopus 로고
    • The ABCA subfamily - Gene and protein structures, functions and associated hereditary diseases
    • Albrecht C., Viturro E. The ABCA subfamily - Gene and protein structures, functions and associated hereditary diseases. Pflugers Arch. 2007, 453(5):581-589.
    • (2007) Pflugers Arch. , vol.453 , Issue.5 , pp. 581-589
    • Albrecht, C.1    Viturro, E.2
  • 30
    • 72749113531 scopus 로고    scopus 로고
    • Small discoidal pre-beta1 HDL particles are efficient acceptors of cell cholesterol via ABCA1 and ABCG1
    • Favari E., Calabresi L., Adorni M.P., Jessup W., Simonelli S., Franceschini G., Bernini F. Small discoidal pre-beta1 HDL particles are efficient acceptors of cell cholesterol via ABCA1 and ABCG1. Biochemistry 2009, 48(46):11067-11074.
    • (2009) Biochemistry , vol.48 , Issue.46 , pp. 11067-11074
    • Favari, E.1    Calabresi, L.2    Adorni, M.P.3    Jessup, W.4    Simonelli, S.5    Franceschini, G.6    Bernini, F.7
  • 31
    • 14744302026 scopus 로고    scopus 로고
    • ATP-binding cassette transporter AI and its role in HDL formation
    • Lee J.Y., Parks J.S. ATP-binding cassette transporter AI and its role in HDL formation. Curr. Opin. Lipidol. 2005, 16(1):19-25.
    • (2005) Curr. Opin. Lipidol. , vol.16 , Issue.1 , pp. 19-25
    • Lee, J.Y.1    Parks, J.S.2
  • 32
    • 0038448097 scopus 로고    scopus 로고
    • Regulation and mechanisms of ATP-binding cassette transporter A1-mediated cellular cholesterol efflux
    • Wang N., Tall A.R. Regulation and mechanisms of ATP-binding cassette transporter A1-mediated cellular cholesterol efflux. Arterioscler. Thromb. Vasc. Biol. 2003, 23(7):1178-1184.
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , Issue.7 , pp. 1178-1184
    • Wang, N.1    Tall, A.R.2
  • 37
    • 0027034365 scopus 로고
    • Mutations and sequence variations detected in the cystic fibrosis transmembrane conductance regulator (CFTR) gene: A report from the Cystic Fibrosis Genetic Analysis Consortium
    • Tsui L.C. Mutations and sequence variations detected in the cystic fibrosis transmembrane conductance regulator (CFTR) gene: A report from the Cystic Fibrosis Genetic Analysis Consortium. Hum. Mutat. 1992, 1(3):197-203.
    • (1992) Hum. Mutat. , vol.1 , Issue.3 , pp. 197-203
    • Tsui, L.C.1
  • 38
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen T.J., Loo M.A., Pind S., Williams D.B., Goldberg A.L., Riordan J.R. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 1995, 83(1):129-135.
    • (1995) Cell , vol.83 , Issue.1 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 40
    • 0033361889 scopus 로고    scopus 로고
    • Cystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoprotein
    • Riordan J.R. Cystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoprotein. Am. J. Hum. Genet. 1999, 64(6):1499-1504.
    • (1999) Am. J. Hum. Genet. , vol.64 , Issue.6 , pp. 1499-1504
    • Riordan, J.R.1
  • 41
    • 34047166052 scopus 로고    scopus 로고
    • Airway surface dehydration in cystic fibrosis: Pathogenesis and therapy
    • Boucher R.C. Airway surface dehydration in cystic fibrosis: Pathogenesis and therapy. Annu. Rev. Med. 2007, 58:157-170.
    • (2007) Annu. Rev. Med. , vol.58 , pp. 157-170
    • Boucher, R.C.1
  • 43
    • 75849161721 scopus 로고    scopus 로고
    • Cystic fibrosis lung disease starts in the small airways: Can we treat it more effectively?
    • Tiddens H.A., Donaldson S.H., Rosenfeld M., Pare P.D. Cystic fibrosis lung disease starts in the small airways: Can we treat it more effectively?. Pediatr. Pulmonol. 2010, 45(2):107-117.
    • (2010) Pediatr. Pulmonol. , vol.45 , Issue.2 , pp. 107-117
    • Tiddens, H.A.1    Donaldson, S.H.2    Rosenfeld, M.3    Pare, P.D.4
  • 44
    • 54049150505 scopus 로고    scopus 로고
    • Patterns of gastrointestinal disease associated with mutations of CFTR
    • Wilschanski M. Patterns of gastrointestinal disease associated with mutations of CFTR. Curr. Gastroenterol. Rep. 2008, 10(3):316-323.
    • (2008) Curr. Gastroenterol. Rep. , vol.10 , Issue.3 , pp. 316-323
    • Wilschanski, M.1
  • 45
    • 0033859128 scopus 로고    scopus 로고
    • Further evidence for an association of ABCR alleles with age-related macular degeneration. The International ABCR Screening Consortium
    • Allikmets R. Further evidence for an association of ABCR alleles with age-related macular degeneration. The International ABCR Screening Consortium. Am. J. Hum. Genet. 2000, 67(2):487-491.
    • (2000) Am. J. Hum. Genet. , vol.67 , Issue.2 , pp. 487-491
    • Allikmets, R.1
  • 53
    • 0034691089 scopus 로고    scopus 로고
    • Biosynthesis of a major lipofuscin fluorophore in mice and humans with ABCR-mediated retinal and macular degeneration
    • Mata N.L., Weng J., Travis G.H. Biosynthesis of a major lipofuscin fluorophore in mice and humans with ABCR-mediated retinal and macular degeneration. Proc. Natl. Acad. Sci. USA 2000, 97(13):7154-7159.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.13 , pp. 7154-7159
    • Mata, N.L.1    Weng, J.2    Travis, G.H.3
  • 54
    • 0033538438 scopus 로고    scopus 로고
    • Insights into the function of Rim protein in photoreceptors and etiology of Stargardt's disease from the phenotype in abcr knockout mice
    • Weng J., Mata N.L., Azarian S.M., Tzekov R.T., Birch D.G., Travis G.H. Insights into the function of Rim protein in photoreceptors and etiology of Stargardt's disease from the phenotype in abcr knockout mice. Cell 1999, 98(1):13-23.
    • (1999) Cell , vol.98 , Issue.1 , pp. 13-23
    • Weng, J.1    Mata, N.L.2    Azarian, S.M.3    Tzekov, R.T.4    Birch, D.G.5    Travis, G.H.6
  • 55
    • 11144240503 scopus 로고    scopus 로고
    • N-retinylidene-phosphatidylethanolamine is the preferred retinoid substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR)
    • Beharry S., Zhong M., Molday R.S. N-retinylidene-phosphatidylethanolamine is the preferred retinoid substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR). J. Biol. Chem. 2004, M405216200.
    • (2004) J. Biol. Chem.
    • Beharry, S.1    Zhong, M.2    Molday, R.S.3
  • 56
    • 0000761427 scopus 로고    scopus 로고
    • Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt disease
    • Sun H., Molday R.S., Nathans J. Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt disease. J. Biol. Chem. 1999, 274(12):8269-8281.
    • (1999) J. Biol. Chem. , vol.274 , Issue.12 , pp. 8269-8281
    • Sun, H.1    Molday, R.S.2    Nathans, J.3
  • 57
  • 62
    • 33846419807 scopus 로고    scopus 로고
    • How can we best use structural information on P-glycoprotein to design inhibitors?
    • McDevitt C., Callaghan R. How can we best use structural information on P-glycoprotein to design inhibitors?. Pharmacol. Ther. 2007, 113:429-441.
    • (2007) Pharmacol. Ther. , vol.113 , pp. 429-441
    • McDevitt, C.1    Callaghan, R.2
  • 64
    • 0029028792 scopus 로고
    • Overlapping substrate specificities and tissue distribution of cytochrome P450 3A and P-glycoprotein: Implications for drug delivery and activity in cancer chemotherapy
    • Wacher V.J., Wu C.Y., Benet L.Z. Overlapping substrate specificities and tissue distribution of cytochrome P450 3A and P-glycoprotein: Implications for drug delivery and activity in cancer chemotherapy. Mol. Carcinog. 1995, 13(3):129-134.
    • (1995) Mol. Carcinog. , vol.13 , Issue.3 , pp. 129-134
    • Wacher, V.J.1    Wu, C.Y.2    Benet, L.Z.3
  • 65
    • 0035054725 scopus 로고    scopus 로고
    • The gut as a barrier to drug absorption: Combined role of cytochrome P450 3A and P-glycoprotein
    • Zhang Y., Benet L.Z. The gut as a barrier to drug absorption: Combined role of cytochrome P450 3A and P-glycoprotein. Clin. Pharmacokinet. 2001, 40(3):159-168.
    • (2001) Clin. Pharmacokinet. , vol.40 , Issue.3 , pp. 159-168
    • Zhang, Y.1    Benet, L.Z.2
  • 66
    • 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(1):48-58.
    • (2002) Nat. Rev. Cancer , vol.2 , Issue.1 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 67
    • 0141888537 scopus 로고    scopus 로고
    • The role of ABC transporters in clinical practice
    • Leonard G.D., Fojo T., Bates S.E. The role of ABC transporters in clinical practice. Oncologist 2003, 8(5):411-424.
    • (2003) Oncologist , vol.8 , Issue.5 , pp. 411-424
    • Leonard, G.D.1    Fojo, T.2    Bates, S.E.3
  • 68
    • 33745852782 scopus 로고    scopus 로고
    • Modulation of multidrug resistance efflux pump activity to overcome chemoresistance in cancer
    • Modok S., Mellor H.R., Callaghan R. Modulation of multidrug resistance efflux pump activity to overcome chemoresistance in cancer. Curr. Opin. Pharmacol. 2006, 6(4):350-354.
    • (2006) Curr. Opin. Pharmacol. , vol.6 , Issue.4 , pp. 350-354
    • Modok, S.1    Mellor, H.R.2    Callaghan, R.3
  • 69
    • 36148972767 scopus 로고    scopus 로고
    • Nrf2-dependent and -independent induction of ABC transporters ABCC1, ABCC2, and ABCG2 in HepG2 cells under oxidative stress
    • Adachi T., Nakagawa H., Chung I., Hagiya Y., Hoshijima K., Noguchi N., Kuo M.T., Ishikawa T. Nrf2-dependent and -independent induction of ABC transporters ABCC1, ABCC2, and ABCG2 in HepG2 cells under oxidative stress. J. Exp. Ther. Oncol. 2007, 6(4):335-348.
    • (2007) J. Exp. Ther. Oncol. , vol.6 , Issue.4 , pp. 335-348
    • Adachi, T.1    Nakagawa, H.2    Chung, I.3    Hagiya, Y.4    Hoshijima, K.5    Noguchi, N.6    Kuo, M.T.7    Ishikawa, T.8
  • 71
    • 0033764825 scopus 로고    scopus 로고
    • The human multidrug resistance-associated protein (MRP) gene family: From biological function to drug molecular design
    • Ishikawa T., Kuo M.T., Furuta K., Suzuki M. The human multidrug resistance-associated protein (MRP) gene family: From biological function to drug molecular design. Clin. Chem. Lab. Med. 2000, 38(9):893-897.
    • (2000) Clin. Chem. Lab. Med. , vol.38 , Issue.9 , pp. 893-897
    • Ishikawa, T.1    Kuo, M.T.2    Furuta, K.3    Suzuki, M.4
  • 72
    • 25144494203 scopus 로고    scopus 로고
    • Redundancy of biological regulation as the basis of emergence of multidrug resistance
    • Shtil A.A., Azare J. Redundancy of biological regulation as the basis of emergence of multidrug resistance. Int. Rev. Cytol. 2005, 246:1-29.
    • (2005) Int. Rev. Cytol. , vol.246 , pp. 1-29
    • Shtil, A.A.1    Azare, J.2
  • 73
    • 0346814102 scopus 로고    scopus 로고
    • Phylogenetic and functional classification of ABC (ATP-binding cassette) systems
    • Elsevier, London, I.B. Holland, S.P.C. Cole, K. Kuchler, C.F. Higgins (Eds.)
    • Dassa E. Phylogenetic and functional classification of ABC (ATP-binding cassette) systems. ABC Proteins: From Bacteria to Man 2003, 81-106. Elsevier, London. I.B. Holland, S.P.C. Cole, K. Kuchler, C.F. Higgins (Eds.).
    • (2003) ABC Proteins: From Bacteria to Man , pp. 81-106
    • Dassa, E.1
  • 74
    • 0029899662 scopus 로고    scopus 로고
    • Mutational analysis and properties of the msbA gene of Escherichia coli, coding for an essential ABC family transporter
    • Polissi A., Georgopoulos C. Mutational analysis and properties of the msbA gene of Escherichia coli, coding for an essential ABC family transporter. Mol. Microbiol. 1996, 20(6):1221-1233.
    • (1996) Mol. Microbiol. , vol.20 , Issue.6 , pp. 1221-1233
    • Polissi, A.1    Georgopoulos, C.2
  • 75
    • 0032524302 scopus 로고    scopus 로고
    • Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis
    • Zhou Z., White K.A., Polissi A., Georgopoulos C., Raetz C.R.H. Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis. J. Biol. Chem. 1998, 273(20):12466-12475.
    • (1998) J. Biol. Chem. , vol.273 , Issue.20 , pp. 12466-12475
    • Zhou, Z.1    White, K.A.2    Polissi, A.3    Georgopoulos, C.4    Raetz, C.R.H.5
  • 77
    • 0037184103 scopus 로고    scopus 로고
    • ATPase activity of the MsbA lipid flippase of Escherichia coli
    • Doerrler W.T., Raetz C.R.H. ATPase activity of the MsbA lipid flippase of Escherichia coli. J. Biol. Chem. 2002, 277(39):36697-36705.
    • (2002) J. Biol. Chem. , vol.277 , Issue.39 , pp. 36697-36705
    • Doerrler, W.T.1    Raetz, C.R.H.2
  • 78
    • 0035853703 scopus 로고    scopus 로고
    • An Escherichia coli mutant defective in lipid export
    • Doerrler W.T., Reedy M.C., Raetz C.R.H. An Escherichia coli mutant defective in lipid export. J. Biol. Chem. 2001, 276(15):11461-11464.
    • (2001) J. Biol. Chem. , vol.276 , Issue.15 , pp. 11461-11464
    • Doerrler, W.T.1    Reedy, M.C.2    Raetz, C.R.H.3
  • 79
    • 45149113880 scopus 로고    scopus 로고
    • Functional characterization of Escherichia coli MsbA: Interaction with nucleotides and substrates
    • Eckford P.D.W., Sharom F.J. Functional characterization of Escherichia coli MsbA: Interaction with nucleotides and substrates. J. Biol. Chem. 2008, 283(19):12840-12850.
    • (2008) J. Biol. Chem. , vol.283 , Issue.19 , pp. 12840-12850
    • Eckford, P.D.W.1    Sharom, F.J.2
  • 80
    • 0042818111 scopus 로고    scopus 로고
    • The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities
    • Reuter G., Janvilisri T., Venter H., Shahi S., Balakrishnan L., van Veen H.W. The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities. J. Biol. Chem. 2003, 278(37):35193-35198.
    • (2003) J. Biol. Chem. , vol.278 , Issue.37 , pp. 35193-35198
    • Reuter, G.1    Janvilisri, T.2    Venter, H.3    Shahi, S.4    Balakrishnan, L.5    van Veen, H.W.6
  • 81
    • 34548724460 scopus 로고    scopus 로고
    • Distribution and physiology of ABC-type transporters contributing to multidrug resistance in bacteria
    • Lubelski J., Konings W.N., Driessen A.J. Distribution and physiology of ABC-type transporters contributing to multidrug resistance in bacteria. Microbiol. Mol. Biol. Rev. 2007, 71(3):463-476.
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , Issue.3 , pp. 463-476
    • Lubelski, J.1    Konings, W.N.2    Driessen, A.J.3
  • 82
    • 17144426125 scopus 로고    scopus 로고
    • Multidrug resistance in parasites: ABC transporters, P-glycoproteins and molecular modelling
    • Jones P.M., George A.M. Multidrug resistance in parasites: ABC transporters, P-glycoproteins and molecular modelling. Int. J. Parasitol. 2005, 35(5):555-566.
    • (2005) Int. J. Parasitol. , vol.35 , Issue.5 , pp. 555-566
    • Jones, P.M.1    George, A.M.2
  • 83
    • 77955895736 scopus 로고    scopus 로고
    • ABC proteins in antigen translocation and viral inhibition
    • Parcej D., Tampe R. ABC proteins in antigen translocation and viral inhibition. Nat. Chem. Biol. 2010, 6(8):572-580.
    • (2010) Nat. Chem. Biol. , vol.6 , Issue.8 , pp. 572-580
    • Parcej, D.1    Tampe, R.2
  • 84
    • 0026532895 scopus 로고
    • Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Bear C.E., Li C.H., Kartner N., Bridges R.J., Jensen T.J., Ramjeesingh M., Riordan J.R. Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR). Cell 1992, 68(4):809-818.
    • (1992) Cell , vol.68 , Issue.4 , pp. 809-818
    • Bear, C.E.1    Li, C.H.2    Kartner, N.3    Bridges, R.J.4    Jensen, T.J.5    Ramjeesingh, M.6    Riordan, J.R.7
  • 85
    • 0020596438 scopus 로고
    • Relative ion permeability of normal and cystic fibrosis nasal epithelium
    • Knowles M., Gatzy J., Boucher R. Relative ion permeability of normal and cystic fibrosis nasal epithelium. J. Clin. Invest. 1983, 71(5):1410-1417.
    • (1983) J. Clin. Invest. , vol.71 , Issue.5 , pp. 1410-1417
    • Knowles, M.1    Gatzy, J.2    Boucher, R.3
  • 86
    • 77953808359 scopus 로고    scopus 로고
    • CLC channels and transporters: Proteins with borderline personalities
    • Accardi A., Picollo A. CLC channels and transporters: Proteins with borderline personalities. Biochim. Biophys. Acta 2010, 1798(8):1457-1464.
    • (2010) Biochim. Biophys. Acta , vol.1798 , Issue.8 , pp. 1457-1464
    • Accardi, A.1    Picollo, A.2
  • 90
    • 23644442552 scopus 로고    scopus 로고
    • ATP-sensitive potassium channelopathies: Focus on insulin secretion
    • Ashcroft F.M. ATP-sensitive potassium channelopathies: Focus on insulin secretion. J. Clin. Invest. 2005, 115(8):2047-2058.
    • (2005) J. Clin. Invest. , vol.115 , Issue.8 , pp. 2047-2058
    • Ashcroft, F.M.1
  • 91
    • 33645221787 scopus 로고    scopus 로고
    • Mutations in the genes encoding the pancreatic beta-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 beta-cell KATP channel subunits Kir6.2 (KCNJ11) and SUR1 (ABCC8) in diabetes mellitus and hyperinsulinism. Hum. Mutat. 2006, 27(3):220-231.
    • (2006) Hum. Mutat. , vol.27 , Issue.3 , pp. 220-231
    • Gloyn, A.L.1    Siddiqui, J.2    Ellard, S.3
  • 92
    • 24144467758 scopus 로고    scopus 로고
    • Activating mutations in Kir6.2 and neonatal diabetes: New clinical syndromes, new scientific insights, and new therapy
    • Hattersley A.T., Ashcroft F.M. Activating mutations in Kir6.2 and neonatal diabetes: New clinical syndromes, new scientific insights, and new therapy. Diabetes 2005, 54(9):2503-2513.
    • (2005) Diabetes , vol.54 , Issue.9 , pp. 2503-2513
    • Hattersley, A.T.1    Ashcroft, F.M.2
  • 93
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O. Simple allosteric model for membrane pumps. Nature 1966, 211(5052):969-970.
    • (1966) Nature , vol.211 , Issue.5052 , pp. 969-970
    • Jardetzky, O.1
  • 95
    • 0025991731 scopus 로고
    • Azidopine noncompetitively interacts with vinblastine and cyclosporin A binding to P-glycoprotein in multidrug resistant cells
    • Tamai I., Safa A.R. Azidopine noncompetitively interacts with vinblastine and cyclosporin A binding to P-glycoprotein in multidrug resistant cells. J. Biol. Chem. 1991, 266:16796-16800.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16796-16800
    • Tamai, I.1    Safa, A.R.2
  • 97
    • 0026475310 scopus 로고
    • P-glycoprotein possesses a 1,4-dihydropyridine selective drug acceptor site which is allosterically coupled to a vinca alkaloid selective binding site
    • Ferry D.R., Russell M.A., Cullen M.H. P-glycoprotein possesses a 1,4-dihydropyridine selective drug acceptor site which is allosterically coupled to a vinca alkaloid selective binding site. Biochem. Biophys. Res. Commun. 1992, 188:440-445.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 440-445
    • Ferry, D.R.1    Russell, M.A.2    Cullen, M.H.3
  • 98
    • 0030782511 scopus 로고    scopus 로고
    • Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities
    • Shapiro A.B., Ling V. Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities. Eur. J. Biochem. 1997, 250(1):130-137.
    • (1997) Eur. J. Biochem. , vol.250 , Issue.1 , pp. 130-137
    • Shapiro, A.B.1    Ling, V.2
  • 99
    • 0033083015 scopus 로고    scopus 로고
    • Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site
    • Shapiro A.B., Fox K., Lam P., Ling V. Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site. Eur. J. Biochem. 1999, 259(3):841-850.
    • (1999) Eur. J. Biochem. , vol.259 , Issue.3 , pp. 841-850
    • Shapiro, A.B.1    Fox, K.2    Lam, P.3    Ling, V.4
  • 100
    • 0030697879 scopus 로고    scopus 로고
    • The multi-drug resistance reversal agent SR33557 and modulation of vinca alkaloid binding to P-glycoprotein by an allosteric interaction
    • Martin C., Berridge G., Higgins C.F., Callaghan R. The multi-drug resistance reversal agent SR33557 and modulation of vinca alkaloid binding to P-glycoprotein by an allosteric interaction. Br. J. Pharmacol. 1997, 122(4):765-771.
    • (1997) Br. J. Pharmacol. , vol.122 , Issue.4 , pp. 765-771
    • Martin, C.1    Berridge, G.2    Higgins, C.F.3    Callaghan, R.4
  • 102
    • 0032881342 scopus 로고    scopus 로고
    • The molecular interaction of the high affinity reversal agent XR9576 with P-glycoprotein
    • Martin C., Berridge G., Mistry P., Higgins C., Charlton P., Callaghan R. The molecular interaction of the high affinity reversal agent XR9576 with P-glycoprotein. Br. J. Pharmacol. 1999, 128(2):403-411.
    • (1999) Br. J. Pharmacol. , vol.128 , Issue.2 , pp. 403-411
    • Martin, C.1    Berridge, G.2    Mistry, P.3    Higgins, C.4    Charlton, P.5    Callaghan, R.6
  • 104
    • 0034739274 scopus 로고    scopus 로고
    • Two transport binding sites of P-glycoprotein are unequal yet contingent: Initial rate kinetic analysis by ATP hydrolysis demonstrates intersite dependence
    • Wang E.J., Casciano C.N., Clement R.P., Johnson W.W. Two transport binding sites of P-glycoprotein are unequal yet contingent: Initial rate kinetic analysis by ATP hydrolysis demonstrates intersite dependence. Biochim. Biophys. Acta 2000, 1481(1):63-74.
    • (2000) Biochim. Biophys. Acta , vol.1481 , Issue.1 , pp. 63-74
    • Wang, E.J.1    Casciano, C.N.2    Clement, R.P.3    Johnson, W.W.4
  • 105
    • 0034326834 scopus 로고    scopus 로고
    • Cooperativity in the inhibition of P-glycoprotein-mediated daunorubicin transport: Evidence for half-of-the-sites reactivity
    • Wang E.J., Casciano C.N., Clement R.P., Johnson W.W. Cooperativity in the inhibition of P-glycoprotein-mediated daunorubicin transport: Evidence for half-of-the-sites reactivity. Arch. Biochem. Biophys. 2000, 383(1):91-98.
    • (2000) Arch. Biochem. Biophys. , vol.383 , Issue.1 , pp. 91-98
    • Wang, E.J.1    Casciano, C.N.2    Clement, R.P.3    Johnson, W.W.4
  • 106
    • 0030035535 scopus 로고    scopus 로고
    • Effects of steroids and verapamil on P-glycoprotein ATPase activity: Progesterone, desoxycorticosterone and verapamil are mutually non-exclusive modulators
    • Orlowski S., Mir L.M., Belehradek J., Garrigos M. Effects of steroids and verapamil on P-glycoprotein ATPase activity: Progesterone, desoxycorticosterone and verapamil are mutually non-exclusive modulators. Biochem. J. 1996, 317:515-522.
    • (1996) Biochem. J. , vol.317 , pp. 515-522
    • Orlowski, S.1    Mir, L.M.2    Belehradek, J.3    Garrigos, M.4
  • 107
    • 0030921564 scopus 로고    scopus 로고
    • The functional purification of P-glycoprotein is dependent on maintenance of a lipid-protein interface
    • Callaghan R., Berridge G., Ferry D.R., Higgins C.F. The functional purification of P-glycoprotein is dependent on maintenance of a lipid-protein interface. Biochim. Biophys. Acta 1997, 1328(2):109-124.
    • (1997) Biochim. Biophys. Acta , vol.1328 , Issue.2 , pp. 109-124
    • Callaghan, R.1    Berridge, G.2    Ferry, D.R.3    Higgins, C.F.4
  • 108
    • 0029027674 scopus 로고
    • Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Sharom F.J., Yu X., Chu J.W., Doige C.A. Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochem. J. 1995, 308(Pt 2):381-390.
    • (1995) Biochem. J. , vol.308 , Issue.PT 2 , pp. 381-390
    • Sharom, F.J.1    Yu, X.2    Chu, J.W.3    Doige, C.A.4
  • 109
    • 0028362501 scopus 로고
    • Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch I.L., Al-Shawi M.K., Senior A.E. Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein. Biochemistry 1994, 33:7069-7076.
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Urbatsch, I.L.1    Al-Shawi, M.K.2    Senior, A.E.3
  • 110
    • 0346732289 scopus 로고    scopus 로고
    • Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein
    • Al-Shawi M.K., Polar M.K., Omote H., Figler R.A. Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein. J. Biol. Chem. 2003, 278(52):52629-52640.
    • (2003) J. Biol. Chem. , vol.278 , Issue.52 , pp. 52629-52640
    • Al-Shawi, M.K.1    Polar, M.K.2    Omote, H.3    Figler, R.A.4
  • 111
    • 0032716822 scopus 로고    scopus 로고
    • Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR transporters
    • Krupka R.M. Uncoupled active transport mechanisms accounting for low selectivity in multidrug carriers: P-glycoprotein and SMR transporters. J. Membr. Biol. 1999, 172:129-143.
    • (1999) J. Membr. Biol. , vol.172 , pp. 129-143
    • Krupka, R.M.1
  • 112
    • 0031039693 scopus 로고    scopus 로고
    • Competitive and non-competitive inhibition of the multidrug-resistance-associated P-glycoprotein ATPase: Further experimental evidence for a multisite model
    • Garrigos M., Mir L.M., Orlowski S. Competitive and non-competitive inhibition of the multidrug-resistance-associated P-glycoprotein ATPase: Further experimental evidence for a multisite model. Eur. J. Biochem. 1997, 244:664-673.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 664-673
    • Garrigos, M.1    Mir, L.M.2    Orlowski, S.3
  • 113
    • 0032518394 scopus 로고    scopus 로고
    • A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene
    • van Veen H.W., Callaghan R., Soceneantu L., Sardini A., Konings W.N., Higgins C.F. A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene. Nature 1998, 391(6664):291-295.
    • (1998) Nature , vol.391 , Issue.6664 , pp. 291-295
    • van Veen, H.W.1    Callaghan, R.2    Soceneantu, L.3    Sardini, A.4    Konings, W.N.5    Higgins, C.F.6
  • 114
    • 33750478648 scopus 로고    scopus 로고
    • Multiple drug binding sites on the R482G isoform of the ABCG2 transporter
    • Clark R., Kerr I.D., Callaghan R. Multiple drug binding sites on the R482G isoform of the ABCG2 transporter. Br. J. Pharmacol. 2006, 149:506-515.
    • (2006) Br. J. Pharmacol. , vol.149 , pp. 506-515
    • Clark, R.1    Kerr, I.D.2    Callaghan, R.3
  • 116
    • 61449121173 scopus 로고    scopus 로고
    • Substrate-dependent breast cancer resistance protein (Bcrp1/Abcg2)-mediated interactions: Consideration of multiple binding sites in in vitro assay design
    • Giri N., Agarwal S., Shaik N., Pan G., Chen Y., Elmquist W.F. Substrate-dependent breast cancer resistance protein (Bcrp1/Abcg2)-mediated interactions: Consideration of multiple binding sites in in vitro assay design. Drug Metab. Dispos. 2009, 37(3):560-570.
    • (2009) Drug Metab. Dispos. , vol.37 , Issue.3 , pp. 560-570
    • Giri, N.1    Agarwal, S.2    Shaik, N.3    Pan, G.4    Chen, Y.5    Elmquist, W.F.6
  • 117
    • 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(4):1103-1111.
    • (2006) FEBS Lett. , vol.580 , Issue.4 , pp. 1103-1111
    • Deeley, R.G.1    Cole, S.P.2
  • 118
    • 0035813012 scopus 로고    scopus 로고
    • Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters
    • Leslie E.M., Deeley R.G., Cole S.P. Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters. Toxicology 2001, 167(1):3-23.
    • (2001) Toxicology , vol.167 , Issue.1 , pp. 3-23
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.3
  • 119
    • 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., Cole S.P. Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles: Demonstration of glutathione-dependent vincristine transport. J. Biol. Chem. 1996, 271(16):9675-9682.
    • (1996) J. Biol. Chem. , vol.271 , Issue.16 , pp. 9675-9682
    • Loe, D.W.1    Almquist, K.C.2    Deeley, R.G.3    Cole, S.P.4
  • 120
    • 0032534064 scopus 로고    scopus 로고
    • Characterization of vincristine transport by the M(r) 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 M(r) 190,000 multidrug resistance protein (MRP): Evidence for cotransport with reduced glutathione. Cancer Res. 1998, 58(22):5130-5136.
    • (1998) Cancer Res. , vol.58 , Issue.22 , pp. 5130-5136
    • Loe, D.W.1    Deeley, R.G.2    Cole, S.P.3
  • 121
    • 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(20):13906-13914.
    • (2006) J. Biol. Chem. , vol.281 , Issue.20 , pp. 13906-13914
    • Rothnie, A.1    Callaghan, R.2    Deeley, R.G.3    Cole, S.P.4
  • 122
    • 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(6):1375-1385.
    • (2004) Mol. Pharmacol. , vol.65 , Issue.6 , pp. 1375-1385
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.4
  • 123
    • 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(7):1411-1420.
    • (2009) Drug Metab. Dispos. , vol.37 , Issue.7 , pp. 1411-1420
    • Maeno, K.1    Nakajima, A.2    Conseil, G.3    Rothnie, A.4    Deeley, R.G.5    Cole, S.P.6
  • 124
    • 0026580336 scopus 로고
    • Is the multidrug transporter a flippase?
    • Higgins C.F., Gottesman M.M. Is the multidrug transporter a flippase?. Trends Biochem. Sci. 1992, 17(1):18-21.
    • (1992) Trends Biochem. Sci. , vol.17 , Issue.1 , pp. 18-21
    • Higgins, C.F.1    Gottesman, M.M.2
  • 125
    • 0027432409 scopus 로고
    • Fluorescent cellular indicators are extruded by the multidrug resistance protein
    • Homolya L., Hollo Z., Germann U.A., Pastan I., Gottesman M.M., Sarkadi B. Fluorescent cellular indicators are extruded by the multidrug resistance protein. J. Biol. Chem. 1993, 268(29):21493-21496.
    • (1993) J. Biol. Chem. , vol.268 , Issue.29 , pp. 21493-21496
    • Homolya, L.1    Hollo, Z.2    Germann, U.A.3    Pastan, I.4    Gottesman, M.M.5    Sarkadi, B.6
  • 126
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Raviv Y., Pollard H.B., Bruggemann E.P., Pastan I., Gottesman M.M. Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells. J. Biol. Chem. 1990, 265(7):3975-3980.
    • (1990) J. Biol. Chem. , vol.265 , Issue.7 , pp. 3975-3980
    • Raviv, Y.1    Pollard, H.B.2    Bruggemann, E.P.3    Pastan, I.4    Gottesman, M.M.5
  • 127
    • 0000887546 scopus 로고
    • Essential features of the P-glycoprotein pharmacophore as defined by a series of reserpine analogs that modulate multidrug resistance
    • Pearce H.L., Safa A.R., Bach N.J., Winter M.A., Cirtain M.C., Beck W.T. Essential features of the P-glycoprotein pharmacophore as defined by a series of reserpine analogs that modulate multidrug resistance. Proc. Natl. Acad. Sci. USA 1989, 86:5128-5132.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5128-5132
    • Pearce, H.L.1    Safa, A.R.2    Bach, N.J.3    Winter, M.A.4    Cirtain, M.C.5    Beck, W.T.6
  • 128
    • 0035083243 scopus 로고    scopus 로고
    • The ostensible paradox of multidrug recognition
    • Neyfakh A.A. The ostensible paradox of multidrug recognition. J. Mol. Microbiol. Biotechnol. 2001, 3(2):151-154.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , Issue.2 , pp. 151-154
    • Neyfakh, A.A.1
  • 129
    • 77955981791 scopus 로고    scopus 로고
    • MD recognition by MDR gene regulators
    • Wade H. MD recognition by MDR gene regulators. Curr. Opin. Struct. Biol. 2010, 20(4):489-496.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , Issue.4 , pp. 489-496
    • Wade, H.1
  • 130
    • 3242812945 scopus 로고    scopus 로고
    • Crystal structure of the TetR/CamR family repressor Mycobacterium tuberculosis EthR implicated in ethionamide resistance
    • Dover L.G., Corsino P.E., Daniels I.R., Cocklin S.L., Tatituri V., Besra G.S., Futterer K. Crystal structure of the TetR/CamR family repressor Mycobacterium tuberculosis EthR implicated in ethionamide resistance. J. Mol. Biol. 2004, 340(5):1095-1105.
    • (2004) J. Mol. Biol. , vol.340 , Issue.5 , pp. 1095-1105
    • Dover, L.G.1    Corsino, P.E.2    Daniels, I.R.3    Cocklin, S.L.4    Tatituri, V.5    Besra, G.S.6    Futterer, K.7
  • 132
    • 0033525105 scopus 로고    scopus 로고
    • Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter
    • Zheleznova E.E., Markham P.N., Neyfakh A.A., Brennan R.G. Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter. Cell 1999, 96:353-362.
    • (1999) Cell , vol.96 , pp. 353-362
    • Zheleznova, E.E.1    Markham, P.N.2    Neyfakh, A.A.3    Brennan, R.G.4
  • 134
    • 0032518454 scopus 로고    scopus 로고
    • A general pattern for substrate recognition by P-glycoprotein
    • Seelig A. A general pattern for substrate recognition by P-glycoprotein. Eur. J. Biochem. 1998, 251:252-261.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 252-261
    • Seelig, A.1
  • 135
    • 0033739115 scopus 로고    scopus 로고
    • Structure-activity relationship of P-glycoprotein substrates and modifiers
    • Seelig A., Landwojtowicz E. Structure-activity relationship of P-glycoprotein substrates and modifiers. Eur. J. Pharm. Sci. 2000, 12:31-40.
    • (2000) Eur. J. Pharm. Sci. , vol.12 , pp. 31-40
    • Seelig, A.1    Landwojtowicz, E.2
  • 136
    • 0034055630 scopus 로고    scopus 로고
    • Substrate recognition by P-glycoprotein and the multidrug resistance-associated protein MRP1: A comparison
    • Seelig A., Blatter X.L., Wohnsland F. Substrate recognition by P-glycoprotein and the multidrug resistance-associated protein MRP1: A comparison. Int. J. Clin. Pharmacol. Ther. 2000, 38(3):111-121.
    • (2000) Int. J. Clin. Pharmacol. Ther. , vol.38 , Issue.3 , pp. 111-121
    • Seelig, A.1    Blatter, X.L.2    Wohnsland, F.3
  • 137
    • 0027215242 scopus 로고
    • Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain 11 as a putative drug binding site
    • Kajiji S., Talbot F., Grizzuti K., Van Dyke-Phillips V., Agresti M., Safa A.R., Gros P. Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain 11 as a putative drug binding site. Biochemistry 1993, 32(16):4185-4194.
    • (1993) Biochemistry , vol.32 , Issue.16 , pp. 4185-4194
    • Kajiji, S.1    Talbot, F.2    Grizzuti, K.3    Van Dyke-Phillips, V.4    Agresti, M.5    Safa, A.R.6    Gros, P.7
  • 138
    • 0027260959 scopus 로고
    • Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein
    • Loo T.W., Clarke D.M. Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein. J. Biol. Chem. 1993, 268(27):19965-19972.
    • (1993) J. Biol. Chem. , vol.268 , Issue.27 , pp. 19965-19972
    • Loo, T.W.1    Clarke, D.M.2
  • 139
    • 0028097634 scopus 로고
    • Transmembrane aromatic amino acid distribution in P-glycoprotein: A functional role in broad substrate specificity
    • Pawagi A.B., Wang J., Silverman M., Reithmeier R.A., Deber C.M. Transmembrane aromatic amino acid distribution in P-glycoprotein: A functional role in broad substrate specificity. J. Mol. Biol. 1994, 235(2):554-564.
    • (1994) J. Mol. Biol. , vol.235 , Issue.2 , pp. 554-564
    • Pawagi, A.B.1    Wang, J.2    Silverman, M.3    Reithmeier, R.A.4    Deber, C.M.5
  • 140
    • 33644692007 scopus 로고    scopus 로고
    • P-glycoprotein recognition of substrates and circumvention through rational drug design
    • Raub T.J. P-glycoprotein recognition of substrates and circumvention through rational drug design. Mol. Pharm. 2006, 3(1):3-25.
    • (2006) Mol. Pharm. , vol.3 , Issue.1 , pp. 3-25
    • Raub, T.J.1
  • 141
    • 0036774002 scopus 로고    scopus 로고
    • Transporters: One, two or four extracytoplasmic substrate-binding sites?
    • van der Heide T., Poolman B.ABC transporters: One, two or four extracytoplasmic substrate-binding sites?. EMBO Rep. 2002, 3(10):938-943.
    • (2002) EMBO Rep. , vol.3 , Issue.10 , pp. 938-943
    • van der Heide, T.1    Poolman, B.A.B.C.2
  • 142
    • 0025362726 scopus 로고
    • The role of ATP in binding-protein-dependent transport systems
    • Higgins C.F. The role of ATP in binding-protein-dependent transport systems. Res. Microbiol. 1990, 141(3):353-360.
    • (1990) Res. Microbiol. , vol.141 , Issue.3 , pp. 353-360
    • Higgins, C.F.1
  • 143
    • 0023644827 scopus 로고
    • Molecular characterization of the oligopeptide permease of Salmonella typhimurium
    • Hiles I.D., Gallagher M.P., Jamieson D.J., Higgins C.F. Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J. Mol. Biol. 1987, 195(1):125-142.
    • (1987) J. Mol. Biol. , vol.195 , Issue.1 , pp. 125-142
    • Hiles, I.D.1    Gallagher, M.P.2    Jamieson, D.J.3    Higgins, C.F.4
  • 146
    • 0023038504 scopus 로고
    • Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli
    • Guyer C.A., Morgan D.G., Staros J.V. Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli. J. Bacteriol. 1986, 168(2):775-779.
    • (1986) J. Bacteriol. , vol.168 , Issue.2 , pp. 775-779
    • Guyer, C.A.1    Morgan, D.G.2    Staros, J.V.3
  • 147
    • 15844389112 scopus 로고    scopus 로고
    • Identification of a gene cluster encoding an arginine ATP-binding-cassette transporter in the genome of the thermophilic Gram-positive bacterium Geobacillus stearothermophilus strain DSMZ 13240
    • Fleischer R., Wengner A., Scheffel F., Landmesser H., Schneider E. Identification of a gene cluster encoding an arginine ATP-binding-cassette transporter in the genome of the thermophilic Gram-positive bacterium Geobacillus stearothermophilus strain DSMZ 13240. Microbiology 2005, 151(Pt 3):835-840.
    • (2005) Microbiology , vol.151 , Issue.PT 3 , pp. 835-840
    • Fleischer, R.1    Wengner, A.2    Scheffel, F.3    Landmesser, H.4    Schneider, E.5
  • 148
    • 0026630610 scopus 로고
    • Purification and characterization of the periplasmic lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium
    • Nikaido K., Ames G.F. Purification and characterization of the periplasmic lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium. J. Biol. Chem. 1992, 267(29):20706-20712.
    • (1992) J. Biol. Chem. , vol.267 , Issue.29 , pp. 20706-20712
    • Nikaido, K.1    Ames, G.F.2
  • 149
    • 36549063540 scopus 로고    scopus 로고
    • Crystal structures and mutational analysis of the arginine-, lysine-, histidine-binding protein ArtJ from Geobacillus stearothermophilus: Implications for interactions of ArtJ with its cognate ATP-binding cassette transporter, Art(MP)2
    • Vahedi-Faridi A., Eckey V., Scheffel F., Alings C., Landmesser H., Schneider E., Saenger W. Crystal structures and mutational analysis of the arginine-, lysine-, histidine-binding protein ArtJ from Geobacillus stearothermophilus: Implications for interactions of ArtJ with its cognate ATP-binding cassette transporter, Art(MP)2. J. Mol. Biol. 2008, 375(2):448-459.
    • (2008) J. Mol. Biol. , vol.375 , Issue.2 , pp. 448-459
    • Vahedi-Faridi, A.1    Eckey, V.2    Scheffel, F.3    Alings, C.4    Landmesser, H.5    Schneider, E.6    Saenger, W.7
  • 151
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
    • Hvorup R.N., Goetz B.A., Niederer M., Hollenstein K., Perozo E., Locher K.P. Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 2007, 317(5843):1387-1390.
    • (2007) Science , vol.317 , Issue.5843 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 152
    • 0037168666 scopus 로고    scopus 로고
    • The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter
    • Borths E.L., Locher K.P., Lee A.T., Rees D.C. The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proc. Natl. Acad. Sci. USA 2002, 99(26):16642-16647.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.26 , pp. 16642-16647
    • Borths, E.L.1    Locher, K.P.2    Lee, A.T.3    Rees, D.C.4
  • 156
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham M.L., Khare D., Quiocho F.A., Davidson A.L., Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 2007, 450(7169):515-521.
    • (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
  • 157
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho F.A., Spurlino J.C., Rodseth L.E. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure 1997, 5(8):997-1015.
    • (1997) Structure , vol.5 , Issue.8 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 158
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • Sharff A.J., Rodseth L.E., Spurlino J.C., Quiocho F.A. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 1992, 31(44):10657-10663.
    • (1992) Biochemistry , vol.31 , Issue.44 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 159
    • 0025754301 scopus 로고
    • The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino J.C., Lu G.Y., Quiocho F.A. The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 1991, 266(8):5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , Issue.8 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.Y.2    Quiocho, F.A.3
  • 160
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D., Oldham M.L., Orelle C., Davidson A.L., Chen J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell 2009, 33(4):528-536.
    • (2009) Mol. Cell , vol.33 , Issue.4 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 161
    • 67650546951 scopus 로고    scopus 로고
    • Transmembrane signaling in the maltose ABC transporter MalFGK2-E: Periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer
    • Grote M., Polyhach Y., Jeschke G., Steinhoff H.J., Schneider E., Bordignon E. Transmembrane signaling in the maltose ABC transporter MalFGK2-E: Periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer. J. Biol. Chem. 2009, 284(26):17521-17526.
    • (2009) J. Biol. Chem. , vol.284 , Issue.26 , pp. 17521-17526
    • Grote, M.1    Polyhach, Y.2    Jeschke, G.3    Steinhoff, H.J.4    Schneider, E.5    Bordignon, E.6
  • 163
    • 0035190570 scopus 로고    scopus 로고
    • Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis
    • Steinke A., Grau S., Davidson A., Hofmann E., Ehrmann M. Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis. J. Bacteriol. 2001, 183(1):375-381.
    • (2001) J. Bacteriol. , vol.183 , Issue.1 , pp. 375-381
    • Steinke, A.1    Grau, S.2    Davidson, A.3    Hofmann, E.4    Ehrmann, M.5
  • 164
    • 0026669363 scopus 로고
    • Characterization of the azidopine and vinblastine binding site of P-glycoprotein
    • Bruggemann E.P., Currier S.J., Gottesman M.M., Pastan I. Characterization of the azidopine and vinblastine binding site of P-glycoprotein. J. Biol. Chem. 1992, 267(29):21020-21026.
    • (1992) J. Biol. Chem. , vol.267 , Issue.29 , pp. 21020-21026
    • Bruggemann, E.P.1    Currier, S.J.2    Gottesman, M.M.3    Pastan, I.4
  • 165
    • 0024971222 scopus 로고
    • Two different regions of P-glycoprotein [corrected] are photoaffinity-labeled by azidopine
    • Bruggemann E.P., Germann U.A., Gottesman M.M., Pastan I. Two different regions of P-glycoprotein [corrected] are photoaffinity-labeled by azidopine. J. Biol. Chem. 1989, 264(26):15483-15488.
    • (1989) J. Biol. Chem. , vol.264 , Issue.26 , pp. 15483-15488
    • Bruggemann, E.P.1    Germann, U.A.2    Gottesman, M.M.3    Pastan, I.4
  • 166
    • 0027216104 scopus 로고
    • Major photoaffinity drug labeling sites for iodoaryl azidoprazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domains 6 and 12
    • Greenberger L.M. Major photoaffinity drug labeling sites for iodoaryl azidoprazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domains 6 and 12. J. Biol. Chem. 1993, 268(15):11417-11425.
    • (1993) J. Biol. Chem. , vol.268 , Issue.15 , pp. 11417-11425
    • Greenberger, L.M.1
  • 167
    • 0025872032 scopus 로고
    • Domain mapping of the photoaffinity drug binding sites in P-glycoprotein encoded by mouse mdr1b
    • Greenberger L.M., Lisanti C.J., Silva J.T., Horwitz S.B. Domain mapping of the photoaffinity drug binding sites in P-glycoprotein encoded by mouse mdr1b. J. Biol. Chem. 1991, 266:20744-20751.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20744-20751
    • Greenberger, L.M.1    Lisanti, C.J.2    Silva, J.T.3    Horwitz, S.B.4
  • 168
    • 0034858151 scopus 로고    scopus 로고
    • Identification and localization of three photobinding sites of iodoarylazidoprazosin in hamster P-glycoprotein
    • Isenberg B., Thole H., Tummler B., Demmer A. Identification and localization of three photobinding sites of iodoarylazidoprazosin in hamster P-glycoprotein. Eur. J. Biochem. 2001, 268(9):2629-2634.
    • (2001) Eur. J. Biochem. , vol.268 , Issue.9 , pp. 2629-2634
    • Isenberg, B.1    Thole, H.2    Tummler, B.3    Demmer, A.4
  • 169
    • 0028128286 scopus 로고
    • Localization of the forskolin labeling sites to both halves of P-glycoprotein: Similarity of the sites labeled by forskolin and prazosin
    • Morris D.I., Greenberger L.M., Bruggemann E.P., Cardarelli C., Gottesman M.M., Pastan I., Seamon K.B. Localization of the forskolin labeling sites to both halves of P-glycoprotein: Similarity of the sites labeled by forskolin and prazosin. Mol. Pharmacol. 1994, 46:329-337.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 329-337
    • Morris, D.I.1    Greenberger, L.M.2    Bruggemann, E.P.3    Cardarelli, C.4    Gottesman, M.M.5    Pastan, I.6    Seamon, K.B.7
  • 170
    • 0028901538 scopus 로고
    • Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by MDR1
    • Zhang X., Collins K.I., Greenberger L.M. Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by MDR1. J. Biol. Chem. 1995, 270(10):5441-5448.
    • (1995) J. Biol. Chem. , vol.270 , Issue.10 , pp. 5441-5448
    • Zhang, X.1    Collins, K.I.2    Greenberger, L.M.3
  • 171
    • 0025766958 scopus 로고
    • A single amino acid substitution strongly modulates the activity and substrate specificity of the mouse mdr1 and mdr3 drug efflux pumps
    • Gros P., Dhir R., Croop J., Talbot F. A single amino acid substitution strongly modulates the activity and substrate specificity of the mouse mdr1 and mdr3 drug efflux pumps. Proc. Natl. Acad. Sci. USA 1991, 88(16):7289-7293.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.16 , pp. 7289-7293
    • Gros, P.1    Dhir, R.2    Croop, J.3    Talbot, F.4
  • 172
    • 0032541975 scopus 로고    scopus 로고
    • Contribution to substrate specificity and transport of nonconserved residues in transmembrane domain 12 of human P-glycoprotein
    • Hafkemeyer P., Dey S., Ambudkar S.V., Hrycyna C.A., Pastan I., Gottesman M.M. Contribution to substrate specificity and transport of nonconserved residues in transmembrane domain 12 of human P-glycoprotein. Biochemistry 1998, 37(46):16400-16409.
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16400-16409
    • Hafkemeyer, P.1    Dey, S.2    Ambudkar, S.V.3    Hrycyna, C.A.4    Pastan, I.5    Gottesman, M.M.6
  • 173
    • 0027512768 scopus 로고
    • Functional consequences of proline mutations in the predicted transmembrane domain of P-glycoprotein
    • Loo T.W., Clarke D.M. Functional consequences of proline mutations in the predicted transmembrane domain of P-glycoprotein. J. Biol. Chem. 1993, 268(5):3143-3149.
    • (1993) J. Biol. Chem. , vol.268 , Issue.5 , pp. 3143-3149
    • Loo, T.W.1    Clarke, D.M.2
  • 174
    • 0027997698 scopus 로고
    • Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein
    • Loo T.W., Clarke D.M. Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein. Biochemistry 1994, 33(47):14049-14057.
    • (1994) Biochemistry , vol.33 , Issue.47 , pp. 14049-14057
    • Loo, T.W.1    Clarke, D.M.2
  • 175
    • 0040700700 scopus 로고    scopus 로고
    • Mutations in the sixth transmembrane domain of P-glycoprotein that alter the pattern of cross-resistance also alter sensitivity to cyclosporin A reversal
    • Ma J.F., Grant G., Melera P.W. Mutations in the sixth transmembrane domain of P-glycoprotein that alter the pattern of cross-resistance also alter sensitivity to cyclosporin A reversal. Mol. Pharmacol. 1997, 51(6):922-930.
    • (1997) Mol. Pharmacol. , vol.51 , Issue.6 , pp. 922-930
    • Ma, J.F.1    Grant, G.2    Melera, P.W.3
  • 176
    • 0028914111 scopus 로고
    • Characterization and functional reconstitution of the multidrug transporter
    • Sharom F.J. Characterization and functional reconstitution of the multidrug transporter. J. Bioenerg. Biomembr. 1995, 27(1):15-22.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , Issue.1 , pp. 15-22
    • Sharom, F.J.1
  • 177
    • 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(16):10685-10694.
    • (1997) J. Biol. Chem. , vol.272 , Issue.16 , pp. 10685-10694
    • Rosenberg, M.F.1    Callaghan, R.2    Ford, R.C.3    Higgins, C.F.4
  • 178
    • 85016724399 scopus 로고    scopus 로고
    • 3-D structure of P-glycoprotein: The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state
    • Rosenberg M.F., Callaghan R., Modok S., Higgins C.F., Ford R.C. 3-D structure of P-glycoprotein: The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state. J. Biol. Chem. 2004, M410296200.
    • (2004) J. Biol. Chem.
    • Rosenberg, M.F.1    Callaghan, R.2    Modok, S.3    Higgins, C.F.4    Ford, R.C.5
  • 179
    • 13244292479 scopus 로고    scopus 로고
    • Three-dimensional structure of P-glycoprotein: The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state
    • Rosenberg M.F., Callaghan R., Modok S., Higgins C.F., Ford R.C. Three-dimensional structure of P-glycoprotein: The transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state. J. Biol. Chem. 2005, 280(4):2857-2862.
    • (2005) J. Biol. Chem. , vol.280 , Issue.4 , pp. 2857-2862
    • Rosenberg, M.F.1    Callaghan, R.2    Modok, S.3    Higgins, C.F.4    Ford, R.C.5
  • 181
    • 1542320036 scopus 로고    scopus 로고
    • Disulfide cross-linking analysis shows that transmembrane segments 5 and 8 of human P-glycoprotein are close together on the cytoplasmic side of the membrane
    • Loo T.W., Bartlett M.C., Clarke D.M. Disulfide cross-linking analysis shows that transmembrane segments 5 and 8 of human P-glycoprotein are close together on the cytoplasmic side of the membrane. J. Biol. Chem. 2004, 279(9):7692-7697.
    • (2004) J. Biol. Chem. , vol.279 , Issue.9 , pp. 7692-7697
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 182
    • 0029909604 scopus 로고    scopus 로고
    • Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates
    • Loo T.W., Clarke D.M. Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates. J. Biol. Chem. 1996, 271(44):27482-27487.
    • (1996) J. Biol. Chem. , vol.271 , Issue.44 , pp. 27482-27487
    • Loo, T.W.1    Clarke, D.M.2
  • 183
    • 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., Clarke D.M. 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. 1996, 271(26):15414-15419.
    • (1996) J. Biol. Chem. , vol.271 , Issue.26 , pp. 15414-15419
    • Loo, T.W.1    Clarke, D.M.2
  • 184
    • 0034671916 scopus 로고    scopus 로고
    • Identification of residues within the drug binding domain of the human multidrug resistance P-glycoprotein by cysteine-scanning mutagenesis and reaction with dibromobimane
    • Loo T.W., Clarke D.M. Identification of residues within the drug binding domain of the human multidrug resistance P-glycoprotein by cysteine-scanning mutagenesis and reaction with dibromobimane. J. Biol. Chem. 2000, 275:39272-39278.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39272-39278
    • Loo, T.W.1    Clarke, D.M.2
  • 185
    • 0034051662 scopus 로고    scopus 로고
    • The packing of the transmembrane segments of human multidrug resistance P-glycoprotein is revealed by disulfide cross-linking analysis
    • Loo T.W., Clarke D.M. The packing of the transmembrane segments of human multidrug resistance P-glycoprotein is revealed by disulfide cross-linking analysis. J. Biol. Chem. 2000, 275(8):5253-5256.
    • (2000) J. Biol. Chem. , vol.275 , Issue.8 , pp. 5253-5256
    • Loo, T.W.1    Clarke, D.M.2
  • 186
    • 0035943691 scopus 로고    scopus 로고
    • Cross-linking of human multidrug resistance P-glycoprotein by the substrate, tris-(2-maleimidoethyl)amine, is altered by ATP hydrolysis: Evidence for rotation of a transmembrane helix
    • Loo T.W., Clarke D.M. Cross-linking of human multidrug resistance P-glycoprotein by the substrate, tris-(2-maleimidoethyl)amine, is altered by ATP hydrolysis: Evidence for rotation of a transmembrane helix. J. Biol. Chem. 2001, 276(34):31800-31805.
    • (2001) J. Biol. Chem. , vol.276 , Issue.34 , pp. 31800-31805
    • Loo, T.W.1    Clarke, D.M.2
  • 187
    • 0035813143 scopus 로고    scopus 로고
    • Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers
    • Loo T.W., Clarke D.M. Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers. J. Biol. Chem. 2001, 276(40):36877-36880.
    • (2001) J. Biol. Chem. , vol.276 , Issue.40 , pp. 36877-36880
    • Loo, T.W.1    Clarke, D.M.2
  • 188
    • 32044453808 scopus 로고    scopus 로고
    • Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux
    • Loo T.W., Clarke D.M. Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux. J. Membr. Biol. 2005, 206(3):173-185.
    • (2005) J. Membr. Biol. , vol.206 , Issue.3 , pp. 173-185
    • Loo, T.W.1    Clarke, D.M.2
  • 189
    • 33749985062 scopus 로고    scopus 로고
    • Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket
    • Loo T.W., Bartlett M.C., Clarke D.M. Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket. Biochem. J. 2006, 399(2):351-359.
    • (2006) Biochem. J. , vol.399 , Issue.2 , pp. 351-359
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 190
    • 33745008903 scopus 로고    scopus 로고
    • Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket
    • Loo T.W., Bartlett M.C., Clarke D.M. Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket. Biochem. J. 2006, 396(3):537-545.
    • (2006) Biochem. J. , vol.396 , Issue.3 , pp. 537-545
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 191
    • 0037113961 scopus 로고    scopus 로고
    • Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein
    • Loo T.W., Clarke D.M. Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein. J. Biol. Chem. 2002, 277(46):44332-44338.
    • (2002) J. Biol. Chem. , vol.277 , Issue.46 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 192
    • 4644265234 scopus 로고    scopus 로고
    • The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium
    • Loo T.W., Bartlett M.C., Clarke D.M. The drug-binding pocket of the human multidrug resistance P-glycoprotein is accessible to the aqueous medium. Biochemistry 2004, 43(38):12081-12089.
    • (2004) Biochemistry , vol.43 , Issue.38 , pp. 12081-12089
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 193
    • 14644425991 scopus 로고    scopus 로고
    • Do drug substrates enter the common drug-binding pocket of P-glycoprotein through 'gates'?
    • Loo T.W., Clarke D.M. Do drug substrates enter the common drug-binding pocket of P-glycoprotein through 'gates'?. Biochem. Biophys. Res. Commun. 2005, 329(2):419-422.
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , Issue.2 , pp. 419-422
    • Loo, T.W.1    Clarke, D.M.2
  • 194
    • 0029898576 scopus 로고    scopus 로고
    • Structural requirements for activity of propafenone-type modulators in P-glycoprotein mediated multidrug resistance
    • Chiba P., Ecker G., Schmid D., Drach J., Tell B., Goldenberg S., Gekeler V. Structural requirements for activity of propafenone-type modulators in P-glycoprotein mediated multidrug resistance. Mol. Pharmacol. 1996, 49:1122-1130.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 1122-1130
    • Chiba, P.1    Ecker, G.2    Schmid, D.3    Drach, J.4    Tell, B.5    Goldenberg, S.6    Gekeler, V.7
  • 195
    • 0036176213 scopus 로고    scopus 로고
    • Identification of ligand-binding regions of P-glycoprotein by activated-pharmacophore photoaffinity labeling and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry
    • Ecker G.F., Csaszar E., Kopp S., Plagens B., Holzer W., Ernst W., Chiba P. Identification of ligand-binding regions of P-glycoprotein by activated-pharmacophore photoaffinity labeling and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry. Mol. Pharmacol. 2002, 61(3):637-648.
    • (2002) Mol. Pharmacol. , vol.61 , Issue.3 , pp. 637-648
    • Ecker, G.F.1    Csaszar, E.2    Kopp, S.3    Plagens, B.4    Holzer, W.5    Ernst, W.6    Chiba, P.7
  • 196
    • 13444266621 scopus 로고    scopus 로고
    • P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: A combined photoaffinity labeling-protein homology modeling approach
    • Pleban K., Kopp S., Csaszar E., Peer M., Hrebicek T., Rizzi A., Ecker G.F., Chiba P. P-glycoprotein substrate binding domains are located at the transmembrane domain/transmembrane domain interfaces: A combined photoaffinity labeling-protein homology modeling approach. Mol. Pharmacol. 2005, 67(2):365-374.
    • (2005) Mol. Pharmacol. , vol.67 , Issue.2 , pp. 365-374
    • Pleban, K.1    Kopp, S.2    Csaszar, E.3    Peer, M.4    Hrebicek, T.5    Rizzi, A.6    Ecker, G.F.7    Chiba, P.8
  • 197
    • 33645991819 scopus 로고    scopus 로고
    • Role of transmembrane domain/transmembrane domain interfaces of P-glycoprotein (ABCB1) in solute transport: Convergent information from photoaffinity labeling, site directed mutagenesis and in silico importance prediction
    • Chiba P., Mihalek I., Ecker G.F., Kopp S., Lichtarge O. Role of transmembrane domain/transmembrane domain interfaces of P-glycoprotein (ABCB1) in solute transport: Convergent information from photoaffinity labeling, site directed mutagenesis and in silico importance prediction. Curr. Med. Chem. 2006, 13(7):793-805.
    • (2006) Curr. Med. Chem. , vol.13 , Issue.7 , pp. 793-805
    • Chiba, P.1    Mihalek, I.2    Ecker, G.F.3    Kopp, S.4    Lichtarge, O.5
  • 198
    • 75149147634 scopus 로고    scopus 로고
    • Multidrug efflux pumps: Drug binding - Gates or cavity?
    • Crowley E., Callaghan R. Multidrug efflux pumps: Drug binding - Gates or cavity?. FEBS J. 2010, 277(3):530-539.
    • (2010) FEBS J. , vol.277 , Issue.3 , pp. 530-539
    • Crowley, E.1    Callaghan, R.2
  • 199
    • 0035951073 scopus 로고    scopus 로고
    • The vinblastine binding site adopts high- and low-affinity conformations during a transport cycle of P-glycoprotein
    • Martin C., Higgins C.F., Callaghan R. The vinblastine binding site adopts high- and low-affinity conformations during a transport cycle of P-glycoprotein. Biochemistry 2001, 40(51):15733-15742.
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15733-15742
    • Martin, C.1    Higgins, C.F.2    Callaghan, R.3
  • 201
    • 34548133239 scopus 로고    scopus 로고
    • P-glycoprotein models of the apo and ATP-bound states based on homology with Sav1866 and MalK
    • O'Mara M.L., Tieleman D.P. P-glycoprotein models of the apo and ATP-bound states based on homology with Sav1866 and MalK. FEBS Lett. 2007, 581(22):4217-4222.
    • (2007) FEBS Lett. , vol.581 , Issue.22 , pp. 4217-4222
    • O'Mara, M.L.1    Tieleman, D.P.2
  • 202
    • 70449713662 scopus 로고    scopus 로고
    • Comparison of the inward- and outward-open homology models and ligand binding of human P-glycoprotein
    • Pajeva I.K., Globisch C., Wiese M. Comparison of the inward- and outward-open homology models and ligand binding of human P-glycoprotein. FEBS J. 2009, 276(23):7016-7026.
    • (2009) FEBS J. , vol.276 , Issue.23 , pp. 7016-7026
    • Pajeva, I.K.1    Globisch, C.2    Wiese, M.3
  • 203
    • 0042531543 scopus 로고    scopus 로고
    • A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure
    • Seigneuret M., Garnier-Suillerot A. A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure. J. Biol. Chem. 2003, 278(32):30115-30124.
    • (2003) J. Biol. Chem. , vol.278 , Issue.32 , pp. 30115-30124
    • Seigneuret, M.1    Garnier-Suillerot, A.2
  • 204
    • 0642272487 scopus 로고    scopus 로고
    • An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling
    • Stenham D.R., Campbell J.D., Sansom M.S., Higgins C.F., Kerr I.D., Linton K.J. An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling. FASEB J. 2003, 17(15):2287-2289.
    • (2003) FASEB J. , vol.17 , Issue.15 , pp. 2287-2289
    • Stenham, D.R.1    Campbell, J.D.2    Sansom, M.S.3    Higgins, C.F.4    Kerr, I.D.5    Linton, K.J.6
  • 207
    • 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(7132):213-216.
    • (2007) Nature , vol.446 , Issue.7132 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 208
    • 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. USA 2007, 104(48):19005-19010.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.48 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 209
    • 70349785109 scopus 로고    scopus 로고
    • Conformational cycle of the ABC transporter MsbA in liposomes: Detailed analysis using double electron-electron resonance spectroscopy
    • Zou P., Bortolus M., McHaourab H.S. Conformational cycle of the ABC transporter MsbA in liposomes: Detailed analysis using double electron-electron resonance spectroscopy. J. Mol. Biol. 2009, 393(3):586-597.
    • (2009) J. Mol. Biol. , vol.393 , Issue.3 , pp. 586-597
    • Zou, P.1    Bortolus, M.2    McHaourab, H.S.3
  • 210
    • 70349785154 scopus 로고    scopus 로고
    • Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA
    • Zou P., McHaourab H.S. Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA. J. Mol. Biol. 2009, 393(3):574-585.
    • (2009) J. Mol. Biol. , vol.393 , Issue.3 , pp. 574-585
    • Zou, P.1    McHaourab, H.S.2
  • 211
    • 4544284056 scopus 로고    scopus 로고
    • The topography of transmembrane segment six is altered during the catalytic cycle of P-glycoprotein
    • Rothnie A., Storm J., Campbell J., Linton K.J., Kerr I.D., Callaghan R. The topography of transmembrane segment six is altered during the catalytic cycle of P-glycoprotein. J. Biol. Chem. 2004, 279(33):34913-34921.
    • (2004) J. Biol. Chem. , vol.279 , Issue.33 , pp. 34913-34921
    • Rothnie, A.1    Storm, J.2    Campbell, J.3    Linton, K.J.4    Kerr, I.D.5    Callaghan, R.6
  • 212
    • 21844451868 scopus 로고    scopus 로고
    • The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment
    • Rothnie A., Storm J., McMahon R., Taylor A.M., Kerr I.D., Callaghan R. The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment. FEBS Lett. 2005, 579:3984-3990.
    • (2005) FEBS Lett. , vol.579 , pp. 3984-3990
    • Rothnie, A.1    Storm, J.2    McMahon, R.3    Taylor, A.M.4    Kerr, I.D.5    Callaghan, R.6
  • 213
    • 41149140334 scopus 로고    scopus 로고
    • Cytosolic region of TM6 in P-glycoprotein: Topographical analysis and functional perturbation by site directed labeling
    • Storm J., Modok S., O'Mara M.L., Tieleman D.P., Kerr I.D., Callaghan R. Cytosolic region of TM6 in P-glycoprotein: Topographical analysis and functional perturbation by site directed labeling. Biochemistry 2008, 47(12):3615-3624.
    • (2008) Biochemistry , vol.47 , Issue.12 , pp. 3615-3624
    • Storm, J.1    Modok, S.2    O'Mara, M.L.3    Tieleman, D.P.4    Kerr, I.D.5    Callaghan, R.6
  • 214
    • 34548507482 scopus 로고    scopus 로고
    • Residue G346 in transmembrane segment six is involved in inter-domain communication in P-glycoprotein
    • Storm J., O'Mara M.L., Crowley E.H., Peall J., Tieleman D.P., Kerr I.D., Callaghan R. Residue G346 in transmembrane segment six is involved in inter-domain communication in P-glycoprotein. Biochemistry 2007, 46(35):9899-9910.
    • (2007) Biochemistry , vol.46 , Issue.35 , pp. 9899-9910
    • Storm, J.1    O'Mara, M.L.2    Crowley, E.H.3    Peall, J.4    Tieleman, D.P.5    Kerr, I.D.6    Callaghan, R.7
  • 216
    • 77956635483 scopus 로고    scopus 로고
    • Transmembrane helix 12 plays a pivotal role in coupling energy provision and drug binding in ABCB1
    • Crowley E., O'Mara M.L., Kerr I.D., Callaghan R. Transmembrane helix 12 plays a pivotal role in coupling energy provision and drug binding in ABCB1. FEBS J. 2010, 277(19):3974-3985.
    • (2010) FEBS J. , vol.277 , Issue.19 , pp. 3974-3985
    • Crowley, E.1    O'Mara, M.L.2    Kerr, I.D.3    Callaghan, R.4
  • 217
    • 0037687304 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein: Direct evidence for the substrate-induced fit mechanism for drug binding
    • Loo T.W., Bartlett M.C., Clarke D.M. Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein: Direct evidence for the substrate-induced fit mechanism for drug binding. J. Biol. Chem. 2003, 278(16):13603-13606.
    • (2003) J. Biol. Chem. , vol.278 , Issue.16 , pp. 13603-13606
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 218
    • 0037449746 scopus 로고    scopus 로고
    • Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains
    • Loo T.W., Bartlett M.C., Clarke D.M. Drug binding in human P-glycoprotein causes conformational changes in both nucleotide-binding domains. J. Biol. Chem. 2003, 278(3):1575-1578.
    • (2003) J. Biol. Chem. , vol.278 , Issue.3 , pp. 1575-1578
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 219
    • 23044503311 scopus 로고    scopus 로고
    • ATP hydrolysis promotes interactions between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein
    • Loo T.W., Bartlett M.C., Clarke D.M. ATP hydrolysis promotes interactions between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein. Biochemistry 2005, 44(30):10250-10258.
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10250-10258
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 220
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson R.J.P., Locher K.P. Structure of a bacterial multidrug ABC transporter. Nature 2006, 443(7108):180-185.
    • (2006) Nature , vol.443 , Issue.7108 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 222
    • 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, 61:1-18.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1-18
    • Jones, P.M.1    George, A.M.2
  • 223
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982, 1(8):945-951.
    • (1982) EMBO J. , vol.1 , Issue.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 224
    • 0033511228 scopus 로고    scopus 로고
    • Nucleoside triphosphate-binding proteins: Different scaffolds to achieve phosphoryl transfer
    • Vetter I.R., Wittinghofer A. Nucleoside triphosphate-binding proteins: Different scaffolds to achieve phosphoryl transfer. Q. Rev. Biophys. 1999, 32(1):1-56.
    • (1999) Q. Rev. Biophys. , vol.32 , Issue.1 , pp. 1-56
    • Vetter, I.R.1    Wittinghofer, A.2
  • 225
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • Jones P.M., George A.M. Subunit interactions in ABC transporters: Towards a functional architecture. FEMS Microbiol. Lett. 1999, 179(2):187-202.
    • (1999) FEMS Microbiol. Lett. , vol.179 , Issue.2 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 226
    • 0034641947 scopus 로고    scopus 로고
    • The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch
    • Lamers M.H., Perrakis A., Enzlin J.H., Winterwerp H.H., de Wind N., Sixma T.K. The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch. Nature 2000, 407(6805):711-717.
    • (2000) Nature , vol.407 , Issue.6805 , pp. 711-717
    • Lamers, M.H.1    Perrakis, A.2    Enzlin, J.H.3    Winterwerp, H.H.4    de Wind, N.5    Sixma, T.K.6
  • 228
    • 0034641938 scopus 로고    scopus 로고
    • Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
    • Obmolova G., Ban C., Hsieh P., Yang W. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature 2000, 407(6805):703-710.
    • (2000) Nature , vol.407 , Issue.6805 , pp. 703-710
    • Obmolova, G.1    Ban, C.2    Hsieh, P.3    Yang, W.4
  • 229
    • 38349057357 scopus 로고    scopus 로고
    • Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding
    • Pakotiprapha D., Inuzuka Y., Bowman B.R., Moolenaar G.F., Goosen N., Jeruzalmi D., Verdine G.L. Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding. Mol. Cell 2008, 29(1):122-133.
    • (2008) Mol. Cell , vol.29 , Issue.1 , pp. 122-133
    • Pakotiprapha, D.1    Inuzuka, Y.2    Bowman, B.R.3    Moolenaar, G.F.4    Goosen, N.5    Jeruzalmi, D.6    Verdine, G.L.7
  • 230
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., Thomas P.J., Hunt J.F. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 2002, 10(1):139-149.
    • (2002) Mol. 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
  • 231
    • 47249110343 scopus 로고    scopus 로고
    • Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter
    • Gerber S., Comellas-Bigler M., Goetz B.A., Locher K.P. Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 2008, 321(5886):246-250.
    • (2008) Science , vol.321 , Issue.5886 , pp. 246-250
    • Gerber, S.1    Comellas-Bigler, M.2    Goetz, B.A.3    Locher, K.P.4
  • 232
    • 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(5810):373-377.
    • (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
  • 233
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen J., Sharma S., Quiocho F.A., Davidson A.L. Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport. Proc. Natl. Acad. Sci. USA 2001, 98(4):1525-1530.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.4 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 234
    • 0038711772 scopus 로고    scopus 로고
    • The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p
    • Janas E., Hofacker M., Chen M., Gompf S., van der Does C., Tampe R. The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J. Biol. Chem. 2003, 278(29):26862-26869.
    • (2003) J. Biol. Chem. , vol.278 , Issue.29 , pp. 26862-26869
    • Janas, E.1    Hofacker, M.2    Chen, M.3    Gompf, S.4    van der Does, C.5    Tampe, R.6
  • 235
    • 0036829647 scopus 로고    scopus 로고
    • The 'LSGGQ' motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence
    • Loo T.W., Bartlett M.C., Clarke D.M. The 'LSGGQ' motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence. J. Biol. Chem. 2002, 277(44):41303-41306.
    • (2002) J. Biol. Chem. , vol.277 , Issue.44 , pp. 41303-41306
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 236
    • 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., Thomas P.J. Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters. J. Biol. Chem. 2002, 277(24):21111-21114.
    • (2002) J. Biol. Chem. , vol.277 , Issue.24 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 237
    • 33746537716 scopus 로고    scopus 로고
    • A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer
    • Zaitseva J., Oswald C., Jumpertz T., Jenewein S., Wiedenmann A., Holland I.B., Schmitt L. A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer. EMBO J. 2006, 25(14):3432-3443.
    • (2006) EMBO J. , 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
  • 238
    • 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(7):2989-3011.
    • (2009) Chem. Rev. , vol.109 , Issue.7 , pp. 2989-3011
    • Eckford, P.D.1    Sharom, F.J.2
  • 239
    • 75149135645 scopus 로고    scopus 로고
    • Multidrug efflux pumps: The structures of prokaryotic ATP-binding cassette transporter efflux pumps and implications for our understanding of eukaryotic P-glycoproteins and homologues
    • Kerr I.D., Jones P.M., George A.M. Multidrug efflux pumps: The structures of prokaryotic ATP-binding cassette transporter efflux pumps and implications for our understanding of eukaryotic P-glycoproteins and homologues. FEBS J. 2010, 277(3):550-563.
    • (2010) FEBS J. , vol.277 , Issue.3 , pp. 550-563
    • Kerr, I.D.1    Jones, P.M.2    George, A.M.3
  • 240
    • 70349312287 scopus 로고    scopus 로고
    • The ATP-binding cassette family: A structural perspective
    • Kos V., Ford R.C. The ATP-binding cassette family: A structural perspective. Cell. Mol. Life Sci. 2009, 66(19):3111-3126.
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.19 , pp. 3111-3126
    • Kos, V.1    Ford, R.C.2
  • 241
    • 70349333637 scopus 로고    scopus 로고
    • The mechanism of ABC transporters: General lessons from structural and functional studies of an antigenic peptide transporter
    • Procko E., O'Mara M.L., Bennett W.F., Tieleman D.P., Gaudet R. The mechanism of ABC transporters: General lessons from structural and functional studies of an antigenic peptide transporter. FASEB J. 2009, 23(5):1287-1302.
    • (2009) FASEB J. , vol.23 , Issue.5 , pp. 1287-1302
    • Procko, E.1    O'Mara, M.L.2    Bennett, W.F.3    Tieleman, D.P.4    Gaudet, R.5
  • 242
    • 0036909285 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Schmitt L., Tampe R. Structure and mechanism of ABC transporters. Curr. Opin. Struct. Biol. 2002, 12(6):754-760.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , Issue.6 , pp. 754-760
    • Schmitt, L.1    Tampe, R.2
  • 243
    • 10044244918 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in HisP: Molecular dynamics simulations of an ABC transporter nucleotide-binding domain
    • Campbell J.D., Deol S.S., Ashcroft F.M., Kerr I.D., Sansom M.S. Nucleotide-dependent conformational changes in HisP: Molecular dynamics simulations of an ABC transporter nucleotide-binding domain. Biophys. J. 2004, 87(6):3703-3715.
    • (2004) Biophys. J. , vol.87 , Issue.6 , pp. 3703-3715
    • Campbell, J.D.1    Deol, S.S.2    Ashcroft, F.M.3    Kerr, I.D.4    Sansom, M.S.5
  • 244
    • 22544453328 scopus 로고    scopus 로고
    • Nucleotide binding to the homodimeric MJ0796 protein: A computational study of a prokaryotic ABC transporter NBD dimer
    • Campbell J.D., Sansom M.S. Nucleotide binding to the homodimeric MJ0796 protein: A computational study of a prokaryotic ABC transporter NBD dimer. FEBS Lett. 2005, 579(19):4193-4199.
    • (2005) FEBS Lett. , vol.579 , Issue.19 , pp. 4193-4199
    • Campbell, J.D.1    Sansom, M.S.2
  • 245
    • 0036789902 scopus 로고    scopus 로고
    • Mechanism of ABC transporters: A molecular dynamics simulation of a well characterized nucleotide-binding subunit
    • Jones P.M., George A.M. Mechanism of ABC transporters: A molecular dynamics simulation of a well characterized nucleotide-binding subunit. Proc. Natl. Acad. Sci. USA 2002, 99(20):12639-12644.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.20 , pp. 12639-12644
    • Jones, P.M.1    George, A.M.2
  • 246
    • 34547943910 scopus 로고    scopus 로고
    • Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: A computational study of the MJ0796 dimer
    • Jones P.M., George A.M. Nucleotide-dependent allostery within the ABC transporter ATP-binding cassette: A computational study of the MJ0796 dimer. J. Biol. Chem. 2007, 282(31):22793-22803.
    • (2007) J. Biol. Chem. , vol.282 , Issue.31 , pp. 22793-22803
    • Jones, P.M.1    George, A.M.2
  • 247
    • 66149139241 scopus 로고    scopus 로고
    • Opening of the ADP-bound active site in the ABC transporter ATPase dimer: Evidence for a constant contact, alternating sites model for the catalytic cycle
    • Jones P.M., George A.M. Opening of the ADP-bound active site in the ABC transporter ATPase dimer: Evidence for a constant contact, alternating sites model for the catalytic cycle. Proteins 2009, 75(2):387-396.
    • (2009) Proteins , vol.75 , Issue.2 , pp. 387-396
    • Jones, P.M.1    George, A.M.2
  • 248
    • 7244240754 scopus 로고    scopus 로고
    • 12 ATP-binding cassette (ABC) transporter BtuCD
    • 12 ATP-binding cassette (ABC) transporter BtuCD. J. Biol. Chem. 2004, 279(43):45013-45019.
    • (2004) J. Biol. Chem. , vol.279 , Issue.43 , pp. 45013-45019
    • Oloo, E.O.1    Tieleman, D.P.2
  • 249
    • 77954613193 scopus 로고    scopus 로고
    • Asymmetric switching in a homodimeric ABC transporter: A simulation study
    • Aittoniemi J., de Wet H., Ashcroft F.M., Sansom M.S. Asymmetric switching in a homodimeric ABC transporter: A simulation study. PLoS Comput. Biol. 2010, 6(4):e1000762.
    • (2010) PLoS Comput. Biol. , vol.6 , Issue.4
    • Aittoniemi, J.1    de Wet, H.2    Ashcroft, F.M.3    Sansom, M.S.4
  • 250
    • 0037426344 scopus 로고    scopus 로고
    • Extending the structure of an ABC transporter to atomic resolution: Modeling and simulation studies of MsbA
    • Campbell J.D., Biggin P.C., Baaden M., Sansom M.S. Extending the structure of an ABC transporter to atomic resolution: Modeling and simulation studies of MsbA. Biochemistry 2003, 42(13):3666-3673.
    • (2003) Biochemistry , vol.42 , Issue.13 , pp. 3666-3673
    • Campbell, J.D.1    Biggin, P.C.2    Baaden, M.3    Sansom, M.S.4
  • 251
    • 34147168584 scopus 로고    scopus 로고
    • Simulation of the coupling between nucleotide binding and transmembrane domains in the ATP binding cassette transporter BtuCD
    • Sonne J., Kandt C., Peters G.H., Hansen F.Y., Jensen M.O., Tieleman D.P. Simulation of the coupling between nucleotide binding and transmembrane domains in the ATP binding cassette transporter BtuCD. Biophys. J. 2007, 92(8):2727-2734.
    • (2007) Biophys. J. , vol.92 , Issue.8 , pp. 2727-2734
    • Sonne, J.1    Kandt, C.2    Peters, G.H.3    Hansen, F.Y.4    Jensen, M.O.5    Tieleman, D.P.6
  • 252
    • 77449137874 scopus 로고    scopus 로고
    • The conformational transition pathway of ATP binding cassette transporter MsbA revealed by atomistic simulations
    • Weng J.W., Fan K.N., Wang W.N. The conformational transition pathway of ATP binding cassette transporter MsbA revealed by atomistic simulations. J. Biol. Chem. 2010, 285(5):3053-3063.
    • (2010) J. Biol. Chem. , vol.285 , Issue.5 , pp. 3053-3063
    • Weng, J.W.1    Fan, K.N.2    Wang, W.N.3
  • 253
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II)-ADP-vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution
    • Smith C.A., Rayment I. X-ray structure of the magnesium(II)-ADP-vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. Biochemistry 1996, 35(17):5404-5417.
    • (1996) Biochemistry , vol.35 , Issue.17 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 255
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva J., Jenewein S., Jumpertz T., Holland I.B., Schmitt L. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 2005, 24(11):1901-1910.
    • (2005) EMBO J. , vol.24 , Issue.11 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 256
    • 33646592576 scopus 로고    scopus 로고
    • Zooming in on ATP hydrolysis in F1
    • Dittrich M., Schulten K. Zooming in on ATP hydrolysis in F1. J. Bioenerg. Biomembr. 2005, 37(6):441-444.
    • (2005) J. Bioenerg. Biomembr. , vol.37 , Issue.6 , pp. 441-444
    • Dittrich, M.1    Schulten, K.2
  • 257
    • 0742270602 scopus 로고    scopus 로고
    • Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation
    • Nishizaka T., Oiwa K., Noji H., Kimura S., Muneyuki E., Yoshida M., Kinosita K. Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation. Nat. Struct. Mol. Biol. 2004, 11(2):142-148.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , Issue.2 , pp. 142-148
    • Nishizaka, T.1    Oiwa, K.2    Noji, H.3    Kimura, S.4    Muneyuki, E.5    Yoshida, M.6    Kinosita, K.7
  • 258
    • 0034738090 scopus 로고    scopus 로고
    • Reverse engineering a protein: The mechanochemistry of ATP synthase
    • Oster G., Wang H. Reverse engineering a protein: The mechanochemistry of ATP synthase. Biochim. Biophys. Acta 2000, 1458(2-3):482-510.
    • (2000) Biochim. Biophys. Acta , vol.1458 , Issue.2-3 , pp. 482-510
    • Oster, G.1    Wang, H.2
  • 259
    • 0345166868 scopus 로고    scopus 로고
    • Catalysis and rotation of F1 motor: Cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotation
    • Shimabukuro K., Yasuda R., Muneyuki E., Hara K.Y., Kinosita K., Yoshida M. Catalysis and rotation of F1 motor: Cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotation. Proc. Natl. Acad. Sci. USA 2003, 100(25):14731-14736.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.25 , pp. 14731-14736
    • Shimabukuro, K.1    Yasuda, R.2    Muneyuki, E.3    Hara, K.Y.4    Kinosita, K.5    Yoshida, M.6
  • 260
    • 30944465891 scopus 로고    scopus 로고
    • Phosphoryl transfer in Ras proteins, conclusive or elusive?
    • Wittinghofer A. Phosphoryl transfer in Ras proteins, conclusive or elusive?. Trends Biochem. Sci. 2006, 31(1):20-23.
    • (2006) Trends Biochem. Sci. , vol.31 , Issue.1 , pp. 20-23
    • Wittinghofer, A.1
  • 261
    • 2442669194 scopus 로고    scopus 로고
    • The GTPase-activating protein Rap1GAP uses a catalytic asparagine
    • Daumke O., Weyand M., Chakrabarti P.P., Vetter I.R., Wittinghofer A. The GTPase-activating protein Rap1GAP uses a catalytic asparagine. Nature 2004, 429(6988):197-201.
    • (2004) Nature , vol.429 , Issue.6988 , pp. 197-201
    • Daumke, O.1    Weyand, M.2    Chakrabarti, P.P.3    Vetter, I.R.4    Wittinghofer, A.5
  • 262
    • 33746356908 scopus 로고    scopus 로고
    • TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
    • Pan X., Eathiraj S., Munson M., Lambright D.G. TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism. Nature 2006, 442(7100):303-306.
    • (2006) Nature , vol.442 , Issue.7100 , pp. 303-306
    • Pan, X.1    Eathiraj, S.2    Munson, M.3    Lambright, D.G.4
  • 263
    • 77949318844 scopus 로고    scopus 로고
    • ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism
    • Parke C.L., Wojcik E.J., Kim S., Worthylake D.K. ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism. J. Biol. Chem. 2010, 285(8):5859-5867.
    • (2010) J. Biol. Chem. , vol.285 , Issue.8 , pp. 5859-5867
    • Parke, C.L.1    Wojcik, E.J.2    Kim, S.3    Worthylake, D.K.4
  • 264
    • 0142091405 scopus 로고    scopus 로고
    • The near attack conformation approach to the study of the chorismate to prephenate reaction
    • Hur S., Bruice T.C. The near attack conformation approach to the study of the chorismate to prephenate reaction. Proc. Natl. Acad. Sci. USA 2003, 100(21):12015-12020.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.21 , pp. 12015-12020
    • Hur, S.1    Bruice, T.C.2
  • 265
    • 0037180390 scopus 로고    scopus 로고
    • Importance of the conserved Walker B glutamate residues, 556 and 1201, for the completion of the catalytic cycle of ATP hydrolysis by human P-glycoprotein (ABCB1)
    • Sauna Z.E., Muller M., Peng X.H., Ambudkar S.V. Importance of the conserved Walker B glutamate residues, 556 and 1201, for the completion of the catalytic cycle of ATP hydrolysis by human P-glycoprotein (ABCB1). Biochemistry 2002, 41(47):13989-14000.
    • (2002) Biochemistry , vol.41 , Issue.47 , pp. 13989-14000
    • Sauna, Z.E.1    Muller, M.2    Peng, X.H.3    Ambudkar, S.V.4
  • 266
    • 3843140625 scopus 로고    scopus 로고
    • Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly
    • Tombline G., Bartholomew L.A., Urbatsch I.L., Senior A.E. Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly. J. Biol. Chem. 2004, 279(30):31212-31220.
    • (2004) J. Biol. Chem. , vol.279 , Issue.30 , pp. 31212-31220
    • Tombline, G.1    Bartholomew, L.A.2    Urbatsch, I.L.3    Senior, A.E.4
  • 267
    • 0034601811 scopus 로고    scopus 로고
    • Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein
    • Urbatsch I.L., Gimi K., Wilke-Mounts S., Senior A.E. Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein. Biochemistry 2000, 39(39):11921-11927.
    • (2000) Biochemistry , vol.39 , Issue.39 , pp. 11921-11927
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 268
    • 0030886132 scopus 로고    scopus 로고
    • Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli
    • Davidson A.L., Sharma S. Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli. J. Bacteriol. 1997, 179(17):5458-5464.
    • (1997) J. Bacteriol. , vol.179 , Issue.17 , pp. 5458-5464
    • Davidson, A.L.1    Sharma, S.2
  • 269
    • 0033578760 scopus 로고    scopus 로고
    • One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease
    • Nikaido K., Ames G.F. One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease. J. Biol. Chem. 1999, 274(38):26727-26735.
    • (1999) J. Biol. Chem. , vol.274 , Issue.38 , pp. 26727-26735
    • Nikaido, K.1    Ames, G.F.2
  • 271
    • 0022476864 scopus 로고
    • Structure of DNase I at 2.0 A resolution suggests a mechanism for binding to and cutting DNA
    • Suck D., Oefner C. Structure of DNase I at 2.0 A resolution suggests a mechanism for binding to and cutting DNA. Nature 1986, 321(6070):620-625.
    • (1986) Nature , vol.321 , Issue.6070 , pp. 620-625
    • Suck, D.1    Oefner, C.2
  • 273
    • 0033200322 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a carbon-carbon bond hydrolase
    • Timm D.E., Mueller H.A., Bhanumoorthy P., Harp J.M., Bunick G.J. Crystal structure and mechanism of a carbon-carbon bond hydrolase. Structure 1999, 7(9):1023-1033.
    • (1999) Structure , vol.7 , Issue.9 , pp. 1023-1033
    • Timm, D.E.1    Mueller, H.A.2    Bhanumoorthy, P.3    Harp, J.M.4    Bunick, G.J.5
  • 274
    • 0028925947 scopus 로고
    • Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins
    • Schweins T., Geyer M., Scheffzek K., Warshel A., Kalbitzer H.R., Wittinghofer A. Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins. Nat. Struct. Biol. 1995, 2(1):36-44.
    • (1995) Nat. Struct. Biol. , vol.2 , Issue.1 , pp. 36-44
    • Schweins, T.1    Geyer, M.2    Scheffzek, K.3    Warshel, A.4    Kalbitzer, H.R.5    Wittinghofer, A.6
  • 275
    • 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., Thunnissen A.M. Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: Nucleotide-free and nucleotide-bound conformations. J. Mol. Biol. 2003, 330(2):343-358.
    • (2003) J. Mol. Biol. , vol.330 , Issue.2 , pp. 343-358
    • Verdon, G.1    Albers, S.V.2    Dijkstra, B.W.3    Driessen, A.J.4    Thunnissen, A.M.5
  • 276
    • 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., Hunt J.F. 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. 2001, 276(34):32313-32321.
    • (2001) J. Biol. Chem. , vol.276 , Issue.34 , pp. 32313-32321
    • Yuan, Y.R.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas, P.J.5    Hunt, J.F.6
  • 277
    • 65249133460 scopus 로고    scopus 로고
    • Structural arrangement of the transmission interface in the antigen ABC transport complex TAP
    • Oancea G., O'Mara M.L., Bennett W.F., Tieleman D.P., Abele R., Tampe R. Structural arrangement of the transmission interface in the antigen ABC transport complex TAP. Proc. Natl. Acad. Sci. USA 2009, 106(14):5551-5556.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , Issue.14 , pp. 5551-5556
    • Oancea, G.1    O'Mara, M.L.2    Bennett, W.F.3    Tieleman, D.P.4    Abele, R.5    Tampe, R.6
  • 279
    • 0034460877 scopus 로고    scopus 로고
    • Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis
    • Sharma S., Davidson A.L. Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis. J. Bacteriol. 2000, 182(23):6570-6576.
    • (2000) J. Bacteriol. , vol.182 , Issue.23 , pp. 6570-6576
    • Sharma, S.1    Davidson, A.L.2
  • 280
    • 34447311648 scopus 로고    scopus 로고
    • Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism
    • Dawson R.J., Hollenstein K., Locher K.P. Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism. Mol. Microbiol. 2007, 65(2):250-257.
    • (2007) Mol. Microbiol. , vol.65 , Issue.2 , pp. 250-257
    • Dawson, R.J.1    Hollenstein, K.2    Locher, K.P.3
  • 281
    • 8344241152 scopus 로고    scopus 로고
    • How do ABC transporters drive transport?
    • van der Does C., Tampe R. How do ABC transporters drive transport?. Biol. Chem. 2004, 385(10):927-933.
    • (2004) Biol. Chem. , vol.385 , Issue.10 , pp. 927-933
    • van der Does, C.1    Tampe, R.2
  • 282
    • 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(10):918-926.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , Issue.10 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 283
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • Vergani P., Lockless S.W., Nairn A.C., Gadsby D.C. CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 2005, 433(7028):876-880.
    • (2005) Nature , vol.433 , Issue.7028 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 284
    • 36849067873 scopus 로고    scopus 로고
    • Catalytic cycle of ATP hydrolysis by P-glycoprotein: Evidence for formation of the E.S reaction intermediate with ATP-gamma-S, a nonhydrolyzable analogue of ATP
    • Sauna Z.E., Kim I.W., Nandigama K., Kopp S., Chiba P., Ambudkar S.V. Catalytic cycle of ATP hydrolysis by P-glycoprotein: Evidence for formation of the E.S reaction intermediate with ATP-gamma-S, a nonhydrolyzable analogue of ATP. Biochemistry 2007, 46(48):13787-13799.
    • (2007) Biochemistry , vol.46 , Issue.48 , pp. 13787-13799
    • Sauna, Z.E.1    Kim, I.W.2    Nandigama, K.3    Kopp, S.4    Chiba, P.5    Ambudkar, S.V.6
  • 285
    • 16844381206 scopus 로고    scopus 로고
    • Characterization of the Walker A motif of MsbA using site-directed spin labeling electron paramagnetic resonance spectroscopy
    • Buchaklian A.H., Klug C.S. Characterization of the Walker A motif of MsbA using site-directed spin labeling electron paramagnetic resonance spectroscopy. Biochemistry 2005, 44(14):5503-5509.
    • (2005) Biochemistry , vol.44 , Issue.14 , pp. 5503-5509
    • Buchaklian, A.H.1    Klug, C.S.2
  • 286
    • 33750038243 scopus 로고    scopus 로고
    • Characterization of the LSGGQ and H motifs from the Escherichia coli lipid A transporter MsbA
    • Buchaklian A.H., Klug C.S. Characterization of the LSGGQ and H motifs from the Escherichia coli lipid A transporter MsbA. Biochemistry 2006, 45(41):12539-12546.
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12539-12546
    • Buchaklian, A.H.1    Klug, C.S.2
  • 287
    • 55549133287 scopus 로고    scopus 로고
    • A comparative electron paramagnetic resonance study of the nucleotide-binding domains' catalytic cycle in the assembled maltose ATP-binding cassette importer
    • Grote M., Bordignon E., Polyhach Y., Jeschke G., Steinhoff H.J., Schneider E. A comparative electron paramagnetic resonance study of the nucleotide-binding domains' catalytic cycle in the assembled maltose ATP-binding cassette importer. Biophys. J. 2008, 95(6):2924-2938.
    • (2008) Biophys. J. , vol.95 , Issue.6 , pp. 2924-2938
    • Grote, M.1    Bordignon, E.2    Polyhach, Y.3    Jeschke, G.4    Steinhoff, H.J.5    Schneider, E.6
  • 288
    • 0037417765 scopus 로고    scopus 로고
    • Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle
    • Qu Q., Russell P.L., Sharom F.J. Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle. Biochemistry 2003, 42(4):1170-1177.
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 1170-1177
    • Qu, Q.1    Russell, P.L.2    Sharom, F.J.3
  • 289
    • 77951241376 scopus 로고    scopus 로고
    • Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: Implications for catalysis
    • Siarheyeva A., Liu R., Sharom F.J. Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: Implications for catalysis. J. Biol. Chem. 2010, 285(10):7575-7586.
    • (2010) J. Biol. Chem. , vol.285 , Issue.10 , pp. 7575-7586
    • Siarheyeva, A.1    Liu, R.2    Sharom, F.J.3
  • 290
    • 58849132410 scopus 로고    scopus 로고
    • Functionally important ATP binding and hydrolysis sites in Escherichia coli MsbA
    • Westfahl K.M., Merten J.A., Buchaklian A.H., Klug C.S. Functionally important ATP binding and hydrolysis sites in Escherichia coli MsbA. Biochemistry 2008, 47(52):13878-13886.
    • (2008) Biochemistry , vol.47 , Issue.52 , pp. 13878-13886
    • Westfahl, K.M.1    Merten, J.A.2    Buchaklian, A.H.3    Klug, C.S.4
  • 291
    • 36849079744 scopus 로고    scopus 로고
    • Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein
    • Zolnerciks J.K., Wooding C., Linton K.J. Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein. FASEB J. 2007, 21(14):3937-3948.
    • (2007) FASEB J. , vol.21 , Issue.14 , pp. 3937-3948
    • Zolnerciks, J.K.1    Wooding, C.2    Linton, K.J.3
  • 292
    • 0022125681 scopus 로고
    • Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems
    • Dassa E., Hofnung M. Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J. 1985, 4(9):2287-2293.
    • (1985) EMBO J. , vol.4 , Issue.9 , pp. 2287-2293
    • Dassa, E.1    Hofnung, M.2
  • 293
    • 0026786329 scopus 로고
    • Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease: Comparison with other members of the family
    • Kerppola R.E., Ames G.F. Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease: Comparison with other members of the family. J. Biol. Chem. 1992, 267(4):2329-2336.
    • (1992) J. Biol. Chem. , vol.267 , Issue.4 , pp. 2329-2336
    • Kerppola, R.E.1    Ames, G.F.2
  • 294
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez M., Hofnung M., Dassa E. Subunit interactions in ABC transporters: A conserved sequence of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 1997, 16:3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 295
    • 0034685825 scopus 로고    scopus 로고
    • ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking
    • Hunke S., Mourez M., Jehanno M., Dassa E., Schneider E. ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking. J. Biol. Chem. 2000, 275(20):15526-15534.
    • (2000) J. Biol. Chem. , vol.275 , Issue.20 , pp. 15526-15534
    • Hunke, S.1    Mourez, M.2    Jehanno, M.3    Dassa, E.4    Schneider, E.5
  • 296
    • 0024292717 scopus 로고
    • An altered pattern of cross-resistance in multidrug resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene
    • Choi K., Chen C.-J., Kriegler M., Roninson I.B. An altered pattern of cross-resistance in multidrug resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene. Cell 1988, 53:519-529.
    • (1988) Cell , vol.53 , pp. 519-529
    • Choi, K.1    Chen, C.-J.2    Kriegler, M.3    Roninson, I.B.4
  • 297
    • 0029100095 scopus 로고
    • Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug stimulated ATPase activities
    • Loo T.W., Clarke D.M. Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug stimulated ATPase activities. J. Biol. Chem. 1995, 270:21449-21452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21449-21452
    • Loo, T.W.1    Clarke, D.M.2
  • 298
    • 0028899422 scopus 로고
    • Mutation of glycine 185 to valine alters the ATPase function of the human P-glycoprotein expressed in Sf9 cells
    • Rao U.S. Mutation of glycine 185 to valine alters the ATPase function of the human P-glycoprotein expressed in Sf9 cells. J. Biol. Chem. 1995, 270:6686-6690.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6686-6690
    • Rao, U.S.1
  • 299
    • 0026473238 scopus 로고
    • Identification of residues in the first cytoplasmic loop of P-glycoprotein involved in the function of chimeric human MDR1-MDR2 transporters
    • Currier S.J., Kane S.E., Willingham M.C., Cardarelli C.O., Pastan I., Gottesman M.M. Identification of residues in the first cytoplasmic loop of P-glycoprotein involved in the function of chimeric human MDR1-MDR2 transporters. J. Biol. Chem. 1992, 267(35):25153-25159.
    • (1992) J. Biol. Chem. , vol.267 , Issue.35 , pp. 25153-25159
    • Currier, S.J.1    Kane, S.E.2    Willingham, M.C.3    Cardarelli, C.O.4    Pastan, I.5    Gottesman, M.M.6
  • 300
    • 0029835571 scopus 로고    scopus 로고
    • Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator
    • Cotten J.F., Ostedgaard L.S., Carson M.R., Welsh M.J. Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 1996, 271(35):21279-21284.
    • (1996) J. Biol. Chem. , vol.271 , Issue.35 , pp. 21279-21284
    • Cotten, J.F.1    Ostedgaard, L.S.2    Carson, M.R.3    Welsh, M.J.4
  • 301
    • 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
  • 302
    • 1842538878 scopus 로고    scopus 로고
    • Improved energy coupling of human P-glycoprotein by the glycine 185 to valine mutation
    • Omote H., Figler R.A., Polar M.K., Al-Shawi M.K. Improved energy coupling of human P-glycoprotein by the glycine 185 to valine mutation. Biochemistry 2004, 43(13):3917-3928.
    • (2004) Biochemistry , vol.43 , Issue.13 , pp. 3917-3928
    • Omote, H.1    Figler, R.A.2    Polar, M.K.3    Al-Shawi, M.K.4
  • 303
    • 21844451868 scopus 로고    scopus 로고
    • The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment
    • Rothnie A., Storm J., McMahon R., Taylor A., Kerr I.D., Callaghan R. The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment. FEBS Lett. 2005, 579(18):3984-3990.
    • (2005) FEBS Lett. , vol.579 , Issue.18 , pp. 3984-3990
    • Rothnie, A.1    Storm, J.2    McMahon, R.3    Taylor, A.4    Kerr, I.D.5    Callaghan, R.6
  • 304
    • 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(8):1659-1669.
    • (2008) Biochem. Pharmacol. , vol.75 , Issue.8 , pp. 1659-1669
    • Letourneau, I.J.1    Nakajima, A.2    Deeley, R.G.3    Cole, S.P.4
  • 305
    • 27744528467 scopus 로고    scopus 로고
    • The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA
    • Dalmas O., Orelle C., Foucher A.E., Geourjon C., Crouzy S., Di Pietro A., Jault J.M. The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA. J. Biol. Chem. 2005, 280(44):36857-36864.
    • (2005) J. Biol. Chem. , vol.280 , Issue.44 , pp. 36857-36864
    • Dalmas, O.1    Orelle, C.2    Foucher, A.E.3    Geourjon, C.4    Crouzy, S.5    Di Pietro, A.6    Jault, J.M.7
  • 306
    • 58049197842 scopus 로고    scopus 로고
    • Mutations define cross-talk between the N-terminal nucleotide-binding domain and transmembrane helix-2 of the yeast multidrug transporter Pdr5: Possible conservation of a signaling interface for coupling ATP hydrolysis to drug transport
    • Sauna Z.E., Bohn S.S., Rutledge R., Dougherty M.P., Cronin S., May L., Xia D., Ambudkar S.V., Golin J. Mutations define cross-talk between the N-terminal nucleotide-binding domain and transmembrane helix-2 of the yeast multidrug transporter Pdr5: Possible conservation of a signaling interface for coupling ATP hydrolysis to drug transport. J. Biol. Chem. 2008, 283(50):35010-35022.
    • (2008) J. Biol. Chem. , vol.283 , Issue.50 , pp. 35010-35022
    • Sauna, Z.E.1    Bohn, S.S.2    Rutledge, R.3    Dougherty, M.P.4    Cronin, S.5    May, L.6    Xia, D.7    Ambudkar, S.V.8    Golin, J.9
  • 307
    • 77956636052 scopus 로고    scopus 로고
    • The maltose ATP-binding cassette transporter in the 21st century - Towards a structural dynamic perspective on its mode of action
    • Bordignon E., Grote M., Schneider E. The maltose ATP-binding cassette transporter in the 21st century - Towards a structural dynamic perspective on its mode of action. Mol. Microbiol. 2010, 77(6):1354-1366.
    • (2010) Mol. Microbiol. , vol.77 , Issue.6 , pp. 1354-1366
    • Bordignon, E.1    Grote, M.2    Schneider, E.3
  • 308
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins
    • Davidson A.L., Shuman H.A., Nikaido H. Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins. Proc. Natl. Acad. Sci. USA 1992, 89:2360-2364.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 309
    • 0033534452 scopus 로고    scopus 로고
    • Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex: Effect of different ligands and consequences for the mechanism of action
    • Liu C.E., Liu P.Q., Wolf A., Lin E., Ames G.F. Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex: Effect of different ligands and consequences for the mechanism of action. J. Biol. Chem. 1999, 274(2):739-747.
    • (1999) J. Biol. Chem. , vol.274 , Issue.2 , pp. 739-747
    • Liu, C.E.1    Liu, P.Q.2    Wolf, A.3    Lin, E.4    Ames, G.F.5
  • 310
    • 0037144128 scopus 로고    scopus 로고
    • Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK(2)) of Salmonella typhimurium
    • Landmesser H., Stein A., Bluschke B., Brinkmann M., Hunke S., Schneider E. Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK(2)) of Salmonella typhimurium. Biochim. Biophys. Acta 2002, 1565(1):64.
    • (2002) Biochim. Biophys. Acta , vol.1565 , Issue.1 , pp. 64
    • Landmesser, H.1    Stein, A.2    Bluschke, B.3    Brinkmann, M.4    Hunke, S.5    Schneider, E.6
  • 311
    • 69049120910 scopus 로고    scopus 로고
    • Stimulation of the maltose transporter ATPase by unliganded maltose binding protein
    • Gould A.D., Telmer P.G., Shilton B.H. Stimulation of the maltose transporter ATPase by unliganded maltose binding protein. Biochemistry 2009, 48(33):8051-8061.
    • (2009) Biochemistry , vol.48 , Issue.33 , pp. 8051-8061
    • Gould, A.D.1    Telmer, P.G.2    Shilton, B.H.3
  • 312
    • 33645215647 scopus 로고    scopus 로고
    • ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter
    • Daus M.L., Landmesser H., Schlosser A., Muller P., Herrmann A., Schneider E. ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter. J. Biol. Chem. 2006, 281(7):3856-3865.
    • (2006) J. Biol. Chem. , vol.281 , Issue.7 , pp. 3856-3865
    • Daus, M.L.1    Landmesser, H.2    Schlosser, A.3    Muller, P.4    Herrmann, A.5    Schneider, E.6
  • 313
    • 63449123276 scopus 로고    scopus 로고
    • The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle
    • Daus M.L., Grote M., Schneider E. The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle. J. Bacteriol. 2009, 191(3):754-761.
    • (2009) J. Bacteriol. , vol.191 , Issue.3 , pp. 754-761
    • Daus, M.L.1    Grote, M.2    Schneider, E.3
  • 314
    • 58149512047 scopus 로고    scopus 로고
    • Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking
    • Goetz B.A., Perozo E., Locher K.P. Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking. FEBS Lett. 2009, 583(2):266-270.
    • (2009) FEBS Lett. , vol.583 , Issue.2 , pp. 266-270
    • Goetz, B.A.1    Perozo, E.2    Locher, K.P.3
  • 315
    • 37549043979 scopus 로고    scopus 로고
    • Distance determination in heterogeneous DNA model systems by pulsed EPR
    • Ward R., Keeble D.J., El-Mkami H., Norman D.G. Distance determination in heterogeneous DNA model systems by pulsed EPR. ChemBioChem 2007, 8(16):1957-1964.
    • (2007) ChemBioChem , vol.8 , Issue.16 , pp. 1957-1964
    • Ward, R.1    Keeble, D.J.2    El-Mkami, H.3    Norman, D.G.4
  • 316
    • 77949608570 scopus 로고    scopus 로고
    • Increased sensitivity and extended range of distance measurements in spin-labeled membrane proteins: Q-band double electron-electron resonance and nanoscale bilayers
    • Zou P., McHaourab H.S. Increased sensitivity and extended range of distance measurements in spin-labeled membrane proteins: Q-band double electron-electron resonance and nanoscale bilayers. Biophys. J. 2010, 98(6):L18-L20.
    • (2010) Biophys. J. , vol.98 , Issue.6
    • Zou, P.1    McHaourab, H.S.2
  • 317
    • 0031454955 scopus 로고    scopus 로고
    • Conformational changes of P-glycoprotein by nucleotide binding
    • Wang G., Pincheira R., Zhang M., Zhang J.-T. Conformational changes of P-glycoprotein by nucleotide binding. Biochem. J. 1997, 328:897-904.
    • (1997) Biochem. J. , vol.328 , pp. 897-904
    • Wang, G.1    Pincheira, R.2    Zhang, M.3    Zhang, J.-T.4
  • 318
    • 0032528075 scopus 로고    scopus 로고
    • Dissection of drug-binding-induced conformational changes in P-glycoprotein
    • Wang G., Pincheira R., Zhang J.T. Dissection of drug-binding-induced conformational changes in P-glycoprotein. Eur. J. Biochem. 1998, 255(2):383-390.
    • (1998) Eur. J. Biochem. , vol.255 , Issue.2 , pp. 383-390
    • Wang, G.1    Pincheira, R.2    Zhang, J.T.3
  • 319
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • Ramachandra M., Ambudkar S.V., Chen D., Hrycyna C.A., Dey S., Gottesman M.M., Pastan I. Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state. Biochemistry 1998, 37(14):5010-5019.
    • (1998) Biochemistry , vol.37 , Issue.14 , pp. 5010-5019
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6    Pastan, I.7
  • 320
    • 0034601776 scopus 로고    scopus 로고
    • Drug binding sites on P-glycoprotein are altered by ATP binding prior to nucleotide hydrolysis
    • Martin C., Berridge G., Mistry P., Higgins C.F., Charlton P., Callaghan R. Drug binding sites on P-glycoprotein are altered by ATP binding prior to nucleotide hydrolysis. Biochemistry 2000, 39:11901-11906.
    • (2000) Biochemistry , vol.39 , pp. 11901-11906
    • Martin, C.1    Berridge, G.2    Mistry, P.3    Higgins, C.F.4    Charlton, P.5    Callaghan, R.6
  • 321
    • 21744431708 scopus 로고    scopus 로고
    • Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1)
    • Payen L., Gao M., Westlake C., Theis A., Cole S.P., Deeley R.G. Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1). Mol. Pharmacol. 2005, 67(6):1944-1953.
    • (2005) Mol. Pharmacol. , vol.67 , Issue.6 , pp. 1944-1953
    • Payen, L.1    Gao, M.2    Westlake, C.3    Theis, A.4    Cole, S.P.5    Deeley, R.G.6
  • 322
    • 49349089223 scopus 로고    scopus 로고
    • Binding responsible for initiating drug translocation by the multidrug transporter ABCG2?
    • McDevitt C.A., Crowley E., Hobbs G., Starr K.J., Kerr I.D., Callaghan R., Is ATP binding responsible for initiating drug translocation by the multidrug transporter ABCG2?. FEBS J. 2008, 275(17):4354-4362.
    • (2008) FEBS J. , vol.275 , Issue.17 , pp. 4354-4362
    • McDevitt, C.A.1    Crowley, E.2    Hobbs, G.3    Starr, K.J.4    Kerr, I.D.5    Callaghan, R.6    Is, A.T.P.7
  • 323
    • 0033580854 scopus 로고    scopus 로고
    • Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein: A tryptophan fluorescence quenching analysis
    • Sonveaux N., Vigano C., Shapiro A.B., Ling V., Ruysschaert J.M. Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein: A tryptophan fluorescence quenching analysis. J. Biol. Chem. 1999, 274(25):17649-17654.
    • (1999) J. Biol. Chem. , vol.274 , Issue.25 , pp. 17649-17654
    • Sonveaux, N.1    Vigano, C.2    Shapiro, A.B.3    Ling, V.4    Ruysschaert, J.M.5
  • 324
    • 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(1):31-35.
    • (2001) FEBS Lett. , vol.493 , Issue.1 , pp. 31-35
    • Manciu, L.1    Chang, X.2    Riordan, J.R.3    Buyse, F.4    Ruysschaert, J.M.5
  • 325
    • 0034610402 scopus 로고    scopus 로고
    • Intrinsic fluorescence of the P-glycoprotein multidrug transporter: Sensitivity of tryptophan residues to binding of drugs and nucleotides
    • Liu R., Siemiarczuk A., Sharom F.J. Intrinsic fluorescence of the P-glycoprotein multidrug transporter: Sensitivity of tryptophan residues to binding of drugs and nucleotides. Biochemistry 2000, 39(48):14927-14938.
    • (2000) Biochemistry , vol.39 , Issue.48 , pp. 14927-14938
    • Liu, R.1    Siemiarczuk, A.2    Sharom, F.J.3
  • 326
    • 33749994338 scopus 로고    scopus 로고
    • Conformational and functional characterization of trapped complexes of the P-glycoprotein multidrug transporter
    • Russell P.L., Sharom F.J. Conformational and functional characterization of trapped complexes of the P-glycoprotein multidrug transporter. Biochem. J. 2006, 399(2):315-323.
    • (2006) Biochem. J. , vol.399 , Issue.2 , pp. 315-323
    • Russell, P.L.1    Sharom, F.J.2
  • 327
    • 77951651875 scopus 로고    scopus 로고
    • The human breast cancer resistance protein (BCRP/ABCG2) shows conformational changes with mitoxantrone
    • Rosenberg M.F., Bikadi Z., Chan J., Liu X., Ni Z., Cai X., Ford R.C., Mao Q. The human breast cancer resistance protein (BCRP/ABCG2) shows conformational changes with mitoxantrone. Structure 2010, 18(4):482-493.
    • (2010) Structure , vol.18 , Issue.4 , pp. 482-493
    • Rosenberg, M.F.1    Bikadi, Z.2    Chan, J.3    Liu, X.4    Ni, Z.5    Cai, X.6    Ford, R.C.7    Mao, Q.8
  • 328
    • 39749094439 scopus 로고    scopus 로고
    • Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA
    • Orelle C., Gubellini F., Durand A., Marco S., Levy D., Gros P., Di Pietro A., Jault J.M. Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA. Biochemistry 2008, 47(8):2404-2412.
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2404-2412
    • Orelle, C.1    Gubellini, F.2    Durand, A.3    Marco, S.4    Levy, D.5    Gros, P.6    Di Pietro, A.7    Jault, J.M.8
  • 329
    • 0038043182 scopus 로고    scopus 로고
    • Allosteric modulation of human P-glycoprotein: Inhibition of transport by preventing substrate translocation and dissociation
    • Maki N., Hafkemeyer P., Dey S. Allosteric modulation of human P-glycoprotein: Inhibition of transport by preventing substrate translocation and dissociation. J. Biol. Chem. 2003, 278(20):18132-18139.
    • (2003) J. Biol. Chem. , vol.278 , Issue.20 , pp. 18132-18139
    • Maki, N.1    Hafkemeyer, P.2    Dey, S.3
  • 330
    • 0035836477 scopus 로고    scopus 로고
    • Analysis of MDR1 P-glycoprotein conformational changes in permeabilized cells using differential immunoreactivity
    • Druley T.E., Stein W.D., Roninson I.B. Analysis of MDR1 P-glycoprotein conformational changes in permeabilized cells using differential immunoreactivity. Biochemistry 2001, 40(14):4312-4322.
    • (2001) Biochemistry , vol.40 , Issue.14 , pp. 4312-4322
    • Druley, T.E.1    Stein, W.D.2    Roninson, I.B.3
  • 331
    • 0035836495 scopus 로고    scopus 로고
    • Coordinate changes in drug resistance and drug-induced conformational transitions in altered-function mutants of the multidrug transporter P-glycoprotein
    • Ruth A., Stein W.D., Rose E., Roninson I.B. Coordinate changes in drug resistance and drug-induced conformational transitions in altered-function mutants of the multidrug transporter P-glycoprotein. Biochemistry 2001, 40(14):4332-4339.
    • (2001) Biochemistry , vol.40 , Issue.14 , pp. 4332-4339
    • Ruth, A.1    Stein, W.D.2    Rose, E.3    Roninson, I.B.4
  • 332
    • 0034646645 scopus 로고    scopus 로고
    • Secondary and tertiary structural changes of reconstituted LmrA induced by nucleotide binding or hydrolysis
    • Vigano C., Margolles A., van Veen H.W., Konings W.N., Ruysschaert J.-M. Secondary and tertiary structural changes of reconstituted LmrA induced by nucleotide binding or hydrolysis. J. Biol. Chem. 2000, 275:10962-10967.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10962-10967
    • Vigano, C.1    Margolles, A.2    van Veen, H.W.3    Konings, W.N.4    Ruysschaert, J.-M.5
  • 333
    • 33750499982 scopus 로고    scopus 로고
    • Thermodynamics of CFTR channel gating: A spreading conformational change initiates an irreversible gating cycle
    • Csanady L., Nairn A.C., Gadsby D.C. Thermodynamics of CFTR channel gating: A spreading conformational change initiates an irreversible gating cycle. J. Gen. Physiol. 2006, 128(5):523-533.
    • (2006) J. Gen. Physiol. , vol.128 , Issue.5 , pp. 523-533
    • Csanady, L.1    Nairn, A.C.2    Gadsby, D.C.3
  • 335
    • 18644362391 scopus 로고    scopus 로고
    • Structural basis of energy transduction in the transport cycle of MsbA
    • Dong J., Yang G., McHaourab H.S. Structural basis of energy transduction in the transport cycle of MsbA. Science 2005, 308(5724):1023-1028.
    • (2005) Science , vol.308 , Issue.5724 , pp. 1023-1028
    • Dong, J.1    Yang, G.2    McHaourab, H.S.3
  • 336
    • 38349035963 scopus 로고    scopus 로고
    • 12 ATP-binding cassette transporter BtuCD
    • 12 ATP-binding cassette transporter BtuCD. Biophys. J. 2008, 94(2):612-621.
    • (2008) Biophys. J. , vol.94 , Issue.2 , pp. 612-621
    • Weng, J.1    Ma, J.2    Fan, K.3    Wang, W.4
  • 337
    • 77949888931 scopus 로고    scopus 로고
    • 12 ABC transporter BtuCD
    • 12 ABC transporter BtuCD. Proteins 2010, 78(3):738-753.
    • (2010) Proteins , vol.78 , Issue.3 , pp. 738-753
    • Kandt, C.1    Tieleman, D.P.2
  • 338
    • 41949139811 scopus 로고    scopus 로고
    • Conformational changes in a pore-lining helix coupled to cystic fibrosis transmembrane conductance regulator channel gating
    • Beck E.J., Yang Y., Yaemsiri S., Raghuram V. Conformational changes in a pore-lining helix coupled to cystic fibrosis transmembrane conductance regulator channel gating. J. Biol. Chem. 2008, 283(8):4957-4966.
    • (2008) J. Biol. Chem. , vol.283 , Issue.8 , pp. 4957-4966
    • Beck, E.J.1    Yang, Y.2    Yaemsiri, S.3    Raghuram, V.4
  • 339
    • 40149088319 scopus 로고    scopus 로고
    • The Q-loop of DrrA is involved in producing the closed conformation of the nucleotide binding domains and in transduction of conformational changes between DrrA and DrrB
    • Rao D.K., Kaur P. The Q-loop of DrrA is involved in producing the closed conformation of the nucleotide binding domains and in transduction of conformational changes between DrrA and DrrB. Biochemistry 2008, 47(9):3038-3050.
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 3038-3050
    • Rao, D.K.1    Kaur, P.2
  • 340
    • 64349091310 scopus 로고    scopus 로고
    • Periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE
    • Jacso T., Grote M., Daus M.L., Schmieder P., Keller S., Schneider E., Reif B. Periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE. Biochemistry 2009, 48(10):2216-2225.
    • (2009) Biochemistry , vol.48 , Issue.10 , pp. 2216-2225
    • Jacso, T.1    Grote, M.2    Daus, M.L.3    Schmieder, P.4    Keller, S.5    Schneider, E.6    Reif, B.7
  • 341
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson R.J., Locher K.P. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 2007, 581(5):935-938.
    • (2007) FEBS Lett. , vol.581 , Issue.5 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.