메뉴 건너뛰기




Volumn 395, Issue 2, 2006, Pages 345-353

The ABC transporter BmrA from Bacillus subtilis is a functional dimer when in a detergent-solubilized state

Author keywords

ABC transporter (ATP binding cassette transporter); Analytical ultracentrifugation; Detergent; Multidrug resistance (MDR); Oligomeric state; Size exclusion chromatography (SEC)

Indexed keywords

ADENOSINETRIPHOSPHATE; CENTRIFUGATION; DETERGENTS; ESCHERICHIA COLI; LIPIDS; SIZE EXCLUSION CHROMATOGRAPHY;

EID: 33645775496     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051719     Document Type: Article
Times cited : (53)

References (52)
  • 2
    • 0346887115 scopus 로고    scopus 로고
    • Structure and function of efflux pumps that confer resistance to drugs
    • Borges-Walmsley, M. I., McKeegan, K. S. and Walmsley, A. R. (2003) Structure and function of efflux pumps that confer resistance to drugs. Biochem. J. 376, 313-338
    • (2003) Biochem. J. , vol.376 , pp. 313-338
    • Borges-Walmsley, M.I.1    McKeegan, K.S.2    Walmsley, A.R.3
  • 3
    • 0035014565 scopus 로고    scopus 로고
    • The ABC of ABCS: A phylogenetic and functional classification of ABC systems in living organisms
    • Dassa, E. and Bouige, P. (2001) The ABC of ABCS: a phylogenetic and functional classification of ABC systems in living organisms. Res. Microbiol. 152, 211-229
    • (2001) Res. Microbiol. , vol.152 , pp. 211-229
    • Dassa, E.1    Bouige, P.2
  • 4
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: Physiology, structure and mechanism - An overview
    • Higgins, C. F. (2001) ABC transporters: physiology, structure and mechanism-an overview. Res. Microbiol. 152, 205-210
    • (2001) Res. Microbiol. , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 5
    • 0028203332 scopus 로고
    • Detection of oligomeric and monomeric forms of P-glycoprotein in multidrug resistant cells
    • Poruchynsky, M. S. and Ling, V. (1994) Detection of oligomeric and monomeric forms of P-glycoprotein in multidrug resistant cells. Biochemistry 33, 4163-4174
    • (1994) Biochemistry , vol.33 , pp. 4163-4174
    • Poruchynsky, M.S.1    Ling, V.2
  • 7
    • 0030678505 scopus 로고    scopus 로고
    • P-glycoprotein is a dimer in the kidney and brain capillary membranes: Effect of cyclosporin a and SDZ-PSC 833
    • Jette, L., Potier, M. and Beliveau, R. (1997) P-glycoprotein is a dimer in the kidney and brain capillary membranes: effect of cyclosporin A and SDZ-PSC 833. Biochemistry 36, 13929-13937
    • (1997) Biochemistry , vol.36 , pp. 13929-13937
    • Jette, L.1    Potier, M.2    Beliveau, R.3
  • 8
    • 0032526848 scopus 로고    scopus 로고
    • Radiation inactivation suggests that human multidrug resistance- associated protein 1 occurs as a dimer in the human erythrocyte membrane
    • Soszynski, M., Kaluzna, A., Rychlik, B., Sokal, A. and Bartosz, G. (1998) Radiation inactivation suggests that human multidrug resistance-associated protein 1 occurs as a dimer in the human erythrocyte membrane. Arch. Biochim. Biophys. 354, 311-316
    • (1998) Arch. Biochim. Biophys. , vol.354 , pp. 311-316
    • Soszynski, M.1    Kaluzna, A.2    Rychlik, B.3    Sokal, A.4    Bartosz, G.5
  • 9
    • 0035844237 scopus 로고    scopus 로고
    • The structure of the multidrug resistance protein 1 (MRP1/ABCC1) crystallization and single-particle analysis
    • Rosenberg, M. F., Mao, Q., Holzenburg, A., Ford, R. C., Deeley, R. G. and Cole, S. P. (2001) The structure of the multidrug resistance protein 1 (MRP1/ABCC1) crystallization and single-particle analysis. J. Biol. Chem. 276, 16076-16082
    • (2001) J. Biol. Chem. , vol.276 , pp. 16076-16082
    • Rosenberg, M.F.1    Mao, Q.2    Holzenburg, A.3    Ford, R.C.4    Deeley, R.G.5    Cole, S.P.6
  • 10
    • 0038485609 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the Saccharomyces cerevisiae multidrug resistance protein Pdr5p
    • Ferreira-Pereira, A., Marco, S., Decottignies, A., Nader, J., Goffeau, A. and Rigaud, J. L. (2003) Three-dimensional reconstruction of the Saccharomyces cerevisiae multidrug resistance protein Pdr5p. J. Biol. Chem. 278, 11995-11999
    • (2003) J. Biol. Chem. , vol.278 , pp. 11995-11999
    • Ferreira-Pereira, A.1    Marco, S.2    Decottignies, A.3    Nader, J.4    Goffeau, A.5    Rigaud, J.L.6
  • 11
    • 2442520293 scopus 로고    scopus 로고
    • Characterization of oligomeric human half-ABC transporter ATP-binding cassette G2
    • Xu, J., Liu, Y., Yang, Y., Bates, S. and Zhang, J. T. (2004) Characterization of oligomeric human half-ABC transporter ATP-binding cassette G2. J. Biol. Chem. 279, 19781-19789
    • (2004) J. Biol. Chem. , vol.279 , pp. 19781-19789
    • Xu, J.1    Liu, Y.2    Yang, Y.3    Bates, S.4    Zhang, J.T.5
  • 12
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G. and Roth, C. B. (2001) Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science (Washington DC) 293, 1793-1800
    • (2001) Science (Washington DC) , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 13
    • 0038799725 scopus 로고    scopus 로고
    • Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation
    • Chang, G. (2003) Structure of MsbA from Vibrio cholera: a multidrug resistance ABC transporter homolog in a closed conformation. J. Mol. Biol. 330, 419-430
    • (2003) J. Mol. Biol. , vol.330 , pp. 419-430
    • Chang, G.1
  • 14
    • 18644363550 scopus 로고    scopus 로고
    • Structure of the ABC transporter MsbA in complex with ADP vanadate and lipopolysaccharide
    • Reyes, C. L. and Chang, G. (2005) Structure of the ABC transporter MsbA in complex with ADP vanadate and lipopolysaccharide. Science (Washington DC) 308, 1028-1031
    • (2005) Science (Washington DC) , vol.308 , pp. 1028-1031
    • Reyes, C.L.1    Chang, G.2
  • 15
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T. and Rees, D. C. (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science (Washington DC) 296, 1091-1098
    • (2002) Science (Washington DC) , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 16
    • 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. and Sansom, M. S. (2003) Extending the structure of an ABC transporter to atomic resolution: modeling and simulation studies of MsbA. Biochemistry 42, 3666-3673
    • (2003) Biochemistry , vol.42 , pp. 3666-3673
    • Campbell, J.D.1    Biggin, P.C.2    Baaden, M.3    Sansom, M.S.4
  • 17
    • 3142580842 scopus 로고    scopus 로고
    • Resting state conformation of the MsbA homodimer as studied by site-directed spin labeling
    • Buchaklian, A. H., Funk, A. L. and Klug, C. S. (2004) Resting state conformation of the MsbA homodimer as studied by site-directed spin labeling. Biochemistry 43, 8600-8606
    • (2004) Biochemistry , vol.43 , pp. 8600-8606
    • Buchaklian, A.H.1    Funk, A.L.2    Klug, C.S.3
  • 18
    • 0344875519 scopus 로고    scopus 로고
    • The conserved glutamate residue adjacent to the Walker-B motif is the catalytic base for ATP hydrolysis in the ATP-binding cassette transporter BmrA
    • Orelle, C. Dalmas, O., Gros, P., Di Pietro, A. and Jault, J. M. (2003) The conserved glutamate residue adjacent to the Walker-B motif is the catalytic base for ATP hydrolysis in the ATP-binding cassette transporter BmrA. J. Biol. Chem. 278, 47002-4708
    • (2003) J. Biol. Chem. , vol.278 , pp. 47002-54708
    • Orelle, C.1    Dalmas, O.2    Gros, P.3    Di Pietro, A.4    Jault, J.M.5
  • 20
    • 0037144131 scopus 로고    scopus 로고
    • Highly efficient over-production in E. coli of YvcC, a multidrug-like ATP-binding cassette transporter from Bacillus subtilis
    • Steinfels, F., Orelle, C., Dalmas, O., Penin, F., Miroux, B., Di Pietro, A. and Jault, J. M. (2002) Highly efficient over-production in E. coli of YvcC, a multidrug-like ATP-binding cassette transporter from Bacillus subtilis. Biochim. Biophys. Acta 1565, 1-5
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 1-5
    • Steinfels, F.1    Orelle, C.2    Dalmas, O.3    Penin, F.4    Miroux, B.5    Di Pietro, A.6    Jault, J.M.7
  • 21
    • 0036301010 scopus 로고    scopus 로고
    • Three-dimensional structure by cryo-electron microscopy of YvcC, an homodimeric ATP-binding cassette transporter from Bacillus subtilis
    • Chami, M., Steinfels, E., Orelle, C., Jault, J. M., Di Pietro, A., Rigaud, J. L. and Marco, S. (2002) Three-dimensional structure by cryo-electron microscopy of YvcC, an homodimeric ATP-binding cassette transporter from Bacillus subtilis. J. Mol. Biol. 315, 1075-1085
    • (2002) J. Mol. Biol. , vol.315 , pp. 1075-1085
    • Chami, M.1    Steinfels, E.2    Orelle, C.3    Jault, J.M.4    Di Pietro, A.5    Rigaud, J.L.6    Marco, S.7
  • 22
    • 15544365661 scopus 로고    scopus 로고
    • Time-resolved fluorescence resonance energy transfer shows that the bacterial multidrug ABC half-transporter BmrA functions as a homodimer
    • Dalmas, O., Do Cao, M. A., Lugo, M. R., Sharom, F. J., Di Pietro, A. and Jault, J. M. (2005) Time-resolved fluorescence resonance energy transfer shows that the bacterial multidrug ABC half-transporter BmrA functions as a homodimer. Biochemistry 44, 4312-4321
    • (2005) Biochemistry , vol.44 , pp. 4312-4321
    • Dalmas, O.1    Do Cao, M.A.2    Lugo, M.R.3    Sharom, F.J.4    Di Pietro, A.5    Jault, J.M.6
  • 25
    • 2942511249 scopus 로고    scopus 로고
    • Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli
    • Ma, C. and Chang, G. (2004) Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 101, 2852-2857
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2852-2857
    • Ma, C.1    Chang, G.2
  • 27
    • 0027477920 scopus 로고
    • Transitional steps in the solubilization of protein-containing membranes and liposomes by nonionic detergent
    • Kragh-Hansen, U., le Maire, M., Noel, J. P., Gulik-Krzywicki, T. and Møller, J. V. (1993) Transitional steps in the solubilization of protein-containing membranes and liposomes by nonionic detergent. Biochemistry 32, 1648-1656
    • (1993) Biochemistry , vol.32 , pp. 1648-1656
    • Kragh-Hansen, U.1    Le Maire, M.2    Noel, J.P.3    Gulik-Krzywicki, T.4    Møller, J.V.5
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriopnage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriopnage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A. and Weinstein, D. (1976) Assay of proteins in the presence of interfering materials. Anal. Biochem. 70, 241-250
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 30
    • 0022453762 scopus 로고
    • The use of high-performance liquid chromatography for the determination of size and molecular weight of proteins: A caution and a list of membrane proteins suitable as standards
    • Le Maire, M., Aggerbeck, L. P., Monteilhet, C., Andersen, J. P. and Møller, J. V. (1986) The use of high-performance liquid chromatography for the determination of size and molecular weight of proteins: a caution and a list of membrane proteins suitable as standards. Anal. Biochem. 154, 525-535
    • (1986) Anal. Biochem. , vol.154 , pp. 525-535
    • Le Maire, M.1    Aggerbeck, L.P.2    Monteilhet, C.3    Andersen, J.P.4    Møller, J.V.5
  • 32
    • 0027283560 scopus 로고
    • Detergent binding as a measure of hydrophobic surface area of integral membrane proteins
    • Møller, J. V. and le Maire, M. (1993) Detergent binding as a measure of hydrophobic surface area of integral membrane proteins. J. Biol. Chem. 268, 18659-18672
    • (1993) J. Biol. Chem. , vol.268 , pp. 18659-18672
    • Møller, J.V.1    Le Maire, M.2
  • 33
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • Chen, P. S., Toribara, T. Y. and Warner, H. (1956) Microdetermination of phosphorus. Anal. Chem. 28, 1756-1758
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 34
    • 0025775976 scopus 로고
    • Alteration of apparent negative cooperativity of ATPase activity by alpha-subunit glutamine 173 mutation in yeast mitochondriai F1. Correlation with impaired nucleotide interaction at a regulatory site
    • Jault, J. M., Di Pietro, A., Falson, P. and Gautheron, D. C. (1991) Alteration of apparent negative cooperativity of ATPase activity by alpha-subunit glutamine 173 mutation in yeast mitochondriai F1. Correlation with impaired nucleotide interaction at a regulatory site. J. Biol. Chem. 266, 8073-8078
    • (1991) J. Biol. Chem. , vol.266 , pp. 8073-8078
    • Jault, J.M.1    Di Pietro, A.2    Falson, P.3    Gautheron, D.C.4
  • 35
    • 3342922088 scopus 로고
    • A microcolorimetric method for the determination of inorganic phosphorus
    • Taussky, H. H. and Shorr, E. (1953) A microcolorimetric method for the determination of inorganic phosphorus. J. Biol. Chem. 202, 675-685
    • (1953) J. Biol. Chem. , vol.202 , pp. 675-685
    • Taussky, H.H.1    Shorr, E.2
  • 36
    • 0016218601 scopus 로고
    • Molecular characterization of proteins in detergent solutions
    • Tanford, C., Nozaki, Y., Reynolds, J. A. and Makino, S. (1974) Molecular characterization of proteins in detergent solutions. Biochemistry 13, 2369-2376
    • (1974) Biochemistry , vol.13 , pp. 2369-2376
    • Tanford, C.1    Nozaki, Y.2    Reynolds, J.A.3    Makino, S.4
  • 37
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 38
    • 0025208204 scopus 로고
    • Maintaining protein stability
    • (Deutcher, M.P., ed.), Academic Press, San Diego, U.S.A.
    • Deutcher, M. P. (1990) Maintaining protein stability. In Methods in Enzymology (Deutcher, M.P., ed.), pp. 83-89, Academic Press, San Diego, U.S.A.
    • (1990) Methods in Enzymology , pp. 83-89
    • Deutcher, M.P.1
  • 39
    • 0030845293 scopus 로고    scopus 로고
    • Dimer to monomer conversion of the cytochrome b6 f complex. Causes and consequences
    • Breyton, C., Tribet, C., Olive, J., Dubacq, J. P. and Popot, J. L. (1997) Dimer to monomer conversion of the cytochrome b6 f complex. Causes and consequences. J. Biol. Chem. 272, 21892-21900
    • (1997) J. Biol. Chem. , vol.272 , pp. 21892-21900
    • Breyton, C.1    Tribet, C.2    Olive, J.3    Dubacq, J.P.4    Popot, J.L.5
  • 40
    • 0034711042 scopus 로고    scopus 로고
    • Detergent-solubilized bovine cytochrome c oxidase: Dimerization depends on the amphiphilic environment
    • Musatov, A., Ortega-Lopez, J. and Robinson, N. C. (2000) Detergent-solubilized bovine cytochrome c oxidase: dimerization depends on the amphiphilic environment. Biochemistry 39, 12996-3004
    • (2000) Biochemistry , vol.39 , pp. 12996-13004
    • Musatov, A.1    Ortega-Lopez, J.2    Robinson, N.C.3
  • 42
    • 0036427425 scopus 로고    scopus 로고
    • Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain
    • Lemieux, M. J., Reithmeier, R. A. and Wang, D. N. (2002) Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain. J. Struct. Biol. 137, 322-332
    • (2002) J. Struct. Biol. , vol.137 , pp. 322-332
    • Lemieux, M.J.1    Reithmeier, R.A.2    Wang, D.N.3
  • 43
    • 3042561938 scopus 로고    scopus 로고
    • The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state
    • Butler, P. J., Ubarretxena-Belandia, I., Warne, T. and Tate, C. G. (2004) The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state. J. Mol. Biol. 340, 797-808
    • (2004) J. Mol. Biol. , vol.340 , pp. 797-808
    • Butler, P.J.1    Ubarretxena-Belandia, I.2    Warne, T.3    Tate, C.G.4
  • 44
    • 0034721921 scopus 로고    scopus 로고
    • Quaternary structure of the lactose transport protein of Streptococcus thermophilus in the detergent-solubilized and membrane-reconstituted state
    • Friesen, R. H., Knol, J. and Poolman, B. (2000) Quaternary structure of the lactose transport protein of Streptococcus thermophilus in the detergent-solubilized and membrane-reconstituted state. J. Biol. Chem. 275, 33527-33535
    • (2000) J. Biol. Chem. , vol.275 , pp. 33527-33535
    • Friesen, R.H.1    Knol, J.2    Poolman, B.3
  • 45
    • 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. and Jault., J. M. (2005) The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA. J. Biol. Chem. 280, 36857-36864
    • (2005) J. Biol. Chem. , vol.280 , 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
  • 46
    • 0035943735 scopus 로고    scopus 로고
    • The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter
    • Yuan, Y. R., Blecker, S., Martsinkevich, O., Millen, L., Thomas, P. J. and Hunt, J. F. (2001) The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter. J. Biol. Chem. 276, 32313-32321
    • (2001) J. Biol. Chem. , vol.276 , pp. 32313-32321
    • Yuan, Y.R.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas, P.J.5    Hunt, J.F.6
  • 47
    • 0029868327 scopus 로고    scopus 로고
    • The maltose transport system of Escherichia coli displays positive cooperativity in ATP hydrolysis
    • Davidson, A. L., Laghaeian, S. S. and Mannering, D. E. (1996) The maltose transport system of Escherichia coli displays positive cooperativity in ATP hydrolysis. J. Biol. Chem. 271, 4858-4863
    • (1996) J. Biol. Chem. , vol.271 , pp. 4858-4863
    • Davidson, A.L.1    Laghaeian, S.S.2    Mannering, D.E.3
  • 48
    • 0030803791 scopus 로고    scopus 로고
    • Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter)
    • Liu, C. E., Liu, P. Q. and Ames, G. F. (1997) Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter). J. Biol. Chem. 272, 21883-21891
    • (1997) J. Biol. Chem. , vol.272 , pp. 21883-21891
    • Liu, C.E.1    Liu, P.Q.2    Ames, G.F.3
  • 49
    • 0030689692 scopus 로고    scopus 로고
    • ATPase activity of purified multidrug resistance-associated protein
    • Chang, X. B., Hou, Y. X. and Riordan, J. R. (1997) ATPase activity of purified multidrug resistance-associated protein. J. Biol. Chem. 272, 30962-30968
    • (1997) J. Biol. Chem. , vol.272 , pp. 30962-30968
    • Chang, X.B.1    Hou, Y.X.2    Riordan, J.R.3
  • 50
    • 0037163877 scopus 로고    scopus 로고
    • A new experimental approach to detect long-range conformational changes transmitted between the membrane and cytosolic domains of LmrA, a bacterial multidrug transporter
    • Vigano, C., Grimard, V., Margolles, A., Goormaghtigh, E., van Veen, H. W., Konings, W. N. and Ruysschaert, J. M. (2002) A new experimental approach to detect long-range conformational changes transmitted between the membrane and cytosolic domains of LmrA, a bacterial multidrug transporter. FEBS Lett. 530, 197-203
    • (2002) FEBS Lett. , vol.530 , pp. 197-203
    • Vigano, C.1    Grimard, V.2    Margolles, A.3    Goormaghtigh, E.4    Van Veen, H.W.5    Konings, W.N.6    Ruysschaert, J.M.7
  • 51
    • 0037184103 scopus 로고    scopus 로고
    • ATPase activity of the MsbA lipid flippase of Escherichia coli
    • Doerrler, W. T. and Raetz, C. R. (2002) ATPase activity of the MsbA lipid flippase of Escherichia coli. J. Biol. Chem. 277, 36697-36705
    • (2002) J. Biol. Chem. , vol.277 , pp. 36697-36705
    • Doerrler, W.T.1    Raetz, C.R.2
  • 52
    • 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. and Figler, R. A. (2003) Transition state analysis of the coupling of drug transport to ATP hydrolysis by P-glycoprotein. J. Biol. Chem. 278, 52629-52640
    • (2003) J. Biol. Chem. , vol.278 , pp. 52629-52640
    • Al-Shawi, M.K.1    Polar, M.K.2    Omote, H.3    Figler, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.