메뉴 건너뛰기




Volumn 64, Issue 4, 2000, Pages 672-693

Molecular properties of bacterial multidrug transporters

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; ANTIBIOTIC AGENT; BETA LACTAM ANTIBIOTIC; CARBAPENEM; CEPHALOSPORIN DERIVATIVE; CHLORAMPHENICOL; GLYCOPEPTIDE; GLYCOPROTEIN P; LINCOSAMIDE; LIPOSOME; MACROLIDE; NOVOBIOCIN; PENICILLIN DERIVATIVE; PROTEIN BMRR; QUINOLONE DERIVATIVE; REGULATOR PROTEIN; RIFAMPICIN; SULFONAMIDE; TETRACYCLINE DERIVATIVE; TRIMETHOPRIM; UNCLASSIFIED DRUG;

EID: 0034445202     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.64.4.672-693.2000     Document Type: Review
Times cited : (671)

References (286)
  • 1
    • 0033040998 scopus 로고    scopus 로고
    • Effects of NorA inhibitors on in vitro antibacterial activities and postantibiotic effects of levofloxacin, ciprofloxacin, and norfloxacin in genetically related strains of Staphylococcus aureus
    • Aeschlimann, J. R., L. D. Dresser, G. W. Kaatz, and M. J. Rybak. 1999. Effects of NorA inhibitors on in vitro antibacterial activities and postantibiotic effects of levofloxacin, ciprofloxacin, and norfloxacin in genetically related strains of Staphylococcus aureus. Antimicrob. Agents Chemother. 43:335-340.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 335-340
    • Aeschlimann, J.R.1    Dresser, L.D.2    Kaatz, G.W.3    Rybak, M.J.4
  • 2
    • 0027160409 scopus 로고
    • Mutants of the Bacillus subtilis multidrug transporter Bmr with altered sensitivity to the antihypertensitive alkaloid reserpine
    • Ahmed, M., C. M. Borsch, A. A. Neyfakh, and S. Schuldiner. 1993. Mutants of the Bacillus subtilis multidrug transporter Bmr with altered sensitivity to the antihypertensitive alkaloid reserpine. J. Biol. Chem. 268:11086-11089.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11086-11089
    • Ahmed, M.1    Borsch, C.M.2    Neyfakh, A.A.3    Schuldiner, S.4
  • 3
    • 0028104421 scopus 로고
    • A protein that activates expression of a multidrug transporter upon binding the transporter substrates
    • Ahmed, M., C. M. Borsch, S. S. Taylor, N. Vásquez-Laslop, and A. A. Neyfakh. 1994. A protein that activates expression of a multidrug transporter upon binding the transporter substrates. J. Biol. Chem. 269:28506-25813.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28506-125813
    • Ahmed, M.1    Borsch, C.M.2    Taylor, S.S.3    Vásquez-Laslop, N.4    Neyfakh, A.A.5
  • 4
    • 0029013337 scopus 로고
    • Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated
    • Ahmed, M., L. Lyass, P. N. Markham, S. S. Taylor, N. Vásquez-Laslop, and A. A. Neyfakh. 1995. Two highly similar multidrug transporters of Bacillus subtilis whose expression is differentially regulated. J. Bacteriol. 177:3904-3910.
    • (1995) J. Bacteriol. , vol.177 , pp. 3904-3910
    • Ahmed, M.1    Lyass, L.2    Markham, P.N.3    Taylor, S.S.4    Vásquez-Laslop, N.5    Neyfakh, A.A.6
  • 5
    • 0031793411 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Tap, a putative multidrug efflux pump present in Mycobacterium fortuitum and Mycobacterium tuberculosis
    • Aínsa, J. A., M. C. J. Blokpoel, I. Otal, D. B. Young, K. A. L. De Smet, and C. Martín. 1998. Molecular cloning and characterization of Tap, a putative multidrug efflux pump present in Mycobacterium fortuitum and Mycobacterium tuberculosis. J. Bacteriol. 180:5836-5843.
    • (1998) J. Bacteriol. , vol.180 , pp. 5836-5843
    • Aínsa, J.A.1    Blokpoel, M.C.J.2    Otal, I.3    Young, D.B.4    De Smet, K.A.L.5    Martín, C.6
  • 6
    • 0345466364 scopus 로고    scopus 로고
    • Involvement of an active efflux system in the natural resistance of Pseudomonas aeruginosa to aminoglycosides
    • Aires, J. R., T. Köhler, H. Nikaido, and P. Plésiat. 1999. Involvement of an active efflux system in the natural resistance of Pseudomonas aeruginosa to aminoglycosides. Antimicrob. Agents Chemother. 43:2624-2628.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 2624-2628
    • Aires, J.R.1    Köhler, T.2    Nikaido, H.3    Plésiat, P.4
  • 7
    • 0028342805 scopus 로고
    • Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: Evidence against direct drug extrusion from the plasma membrane
    • USA
    • Altenberg, G. A., C. G. Vanoye, J. K. Horton, and L. Reuss. 1994. Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: evidence against direct drug extrusion from the plasma membrane. Proc. Natl. Acad. Sci. USA 91:4654-4657.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 4654-4657
    • Altenberg, G.A.1    Vanoye, C.G.2    Horton, J.K.3    Reuss, L.4
  • 8
    • 0025033814 scopus 로고
    • Bacterial periplasmic permeases belong to a family of transport proteins operating from E. coli to human: Traffic ATPases
    • Ames, G. F.-L., C. S. Mimura, and V. Shyamala. 1990. Bacterial periplasmic permeases belong to a family of transport proteins operating from E. coli to human: traffic ATPases. FEMS Microbiol. Rev. 75:429-446.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 429-446
    • Ames, G.F.-L.1    Mimura, C.S.2    Shyamala, V.3
  • 9
    • 0027954601 scopus 로고
    • Repressor mutations in the marRAB operon that activate oxidative stress genes and multiple antibiotic resistance in Escherichia coli
    • Ariza, R. R., S. P. Cohen, N. Bachhawat, S. B. Levy, and B. Demple. 1994. Repressor mutations in the marRAB operon that activate oxidative stress genes and multiple antibiotic resistance in Escherichia coli. J. Bacteriol. 176:143-148.
    • (1994) J. Bacteriol. , vol.176 , pp. 143-148
    • Ariza, R.R.1    Cohen, S.P.2    Bachhawat, N.3    Levy, S.B.4    Demple, B.5
  • 10
    • 0028924091 scopus 로고
    • Activation of multiple antibiotic resistance and binding of stress-inducible promoters by Escherichia coli Rob protein
    • Ariza, R. R., Z. Li, N. Ringstad, and B. Demple. 1995. Activation of multiple antibiotic resistance and binding of stress-inducible promoters by Escherichia coli Rob protein. J. Bacteriol. 177:1655-1661.
    • (1995) J. Bacteriol. , vol.177 , pp. 1655-1661
    • Ariza, R.R.1    Li, Z.2    Ringstad, N.3    Demple, B.4
  • 11
    • 0029999396 scopus 로고    scopus 로고
    • Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle
    • Arkin, I. T., W. P. Russ, M. Lebendiker, and S. Schuldiner. 1996. Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle. Biochemistry 35:7233-7238.
    • (1996) Biochemistry , vol.35 , pp. 7233-7238
    • Arkin, I.T.1    Russ, W.P.2    Lebendiker, M.3    Schuldiner, S.4
  • 12
    • 0033514493 scopus 로고    scopus 로고
    • The relationship between the volume of antimicrobial consumption in human communities and the frequency of resistance
    • USA
    • Austin, D. J., K. G. Kristinsson, and R. M. Anderson. 1999. The relationship between the volume of antimicrobial consumption in human communities and the frequency of resistance. Proc. Natl. Acad. Sci. USA 96:1152-1156.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 1152-1156
    • Austin, D.J.1    Kristinsson, K.G.2    Anderson, R.M.3
  • 13
    • 0030004763 scopus 로고    scopus 로고
    • Co-operative, competitive and non-competitive interactions between modulators of P-glycoprotein
    • Ayesh, S., Y.-M. Shao, and W. D. Stein. 1996. Co-operative, competitive and non-competitive interactions between modulators of P-glycoprotein. Biochim. Biophys. Acta 1316:8-18.
    • (1996) Biochim. Biophys. Acta , vol.1316 , pp. 8-18
    • Ayesh, S.1    Shao, Y.-M.2    Stein, W.D.3
  • 14
    • 0039229975 scopus 로고    scopus 로고
    • Evolution of antibiotic resistance
    • Baquero, F., and J. Blázquez. 1997. Evolution of antibiotic resistance. TREE 12:482-487.
    • (1997) TREE , vol.12 , pp. 482-487
    • Baquero, F.1    Blázquez, J.2
  • 15
    • 0030918973 scopus 로고    scopus 로고
    • Apparent involvement of a multidrug transporter in the fluoroquinolone resistance of Streptococcus pneumoniae
    • Baranova, N. N., and A. A. Neyfakh. 1997. Apparent involvement of a multidrug transporter in the fluoroquinolone resistance of Streptococcus pneumoniae. Antimicrob. Agents Chemother. 41:1396-1398.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1396-1398
    • Baranova, N.N.1    Neyfakh, A.A.2
  • 16
    • 0033023361 scopus 로고    scopus 로고
    • Mta, a global MerR-type regulator of the Bacillus subtilis multidrug-efflux transporters
    • Baranova, N. N., A. Danchin, and A. A. Neyfakh. 1999. Mta, a global MerR-type regulator of the Bacillus subtilis multidrug-efflux transporters. Mol. Microbiol. 31:1549-1559.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1549-1559
    • Baranova, N.N.1    Danchin, A.2    Neyfakh, A.A.3
  • 17
    • 0028936040 scopus 로고
    • The ard1 gene from Streptomyces capreolus encodes a polypeptide of the ABC-transporters superfamily which confers resistance to the aminonucleoside antibiotic A201A
    • Barrasa, M. I., J. A. Tercero, R. A. Lacalle, and A. Jimenez. 1995. The ard1 gene from Streptomyces capreolus encodes a polypeptide of the ABC-transporters superfamily which confers resistance to the aminonucleoside antibiotic A201A. Eur. J. Biochem. 228:562-569.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 562-569
    • Barrasa, M.I.1    Tercero, J.A.2    Lacalle, R.A.3    Jimenez, A.4
  • 18
    • 0027324803 scopus 로고
    • Cloning and sequence analysis of an Escherichia coli gene conferring bicyclomycin resistance
    • Bentley, J., L. S. Hyatt, K. Ainley, J. H. Parish, R. B. Herbert, and G. R. White. 1993. Cloning and sequence analysis of an Escherichia coli gene conferring bicyclomycin resistance. Gene 127:117-120.
    • (1993) Gene , vol.127 , pp. 117-120
    • Bentley, J.1    Hyatt, L.S.2    Ainley, K.3    Parish, J.H.4    Herbert, R.B.5    White, G.R.6
  • 19
    • 0031734033 scopus 로고    scopus 로고
    • The Escherichia coli cmlA gene encodes the multidrug efflux pump Cmr/MdfA and is responsible for isopropyl-β-D-thiogalactopyranoside exclusion and spectinomycin sensitivity
    • Bohn, C., and P. Bouloc. 1998. The Escherichia coli cmlA gene encodes the multidrug efflux pump Cmr/MdfA and is responsible for isopropyl-β-D-thiogalactopyranoside exclusion and spectinomycin sensitivity. J. Bacteriol. 190:6072-6075.
    • (1998) J. Bacteriol. , vol.190 , pp. 6072-6075
    • Bohn, C.1    Bouloc, P.2
  • 20
  • 23
    • 0029781640 scopus 로고    scopus 로고
    • Multidrug resistance in Lactacoccus lactis: Evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane
    • Bolhuis, H., H. W. van Veen, D. Molenaar, B. Poolman, A. J. M. Driessen, and W. N. Konings. 1996. Multidrug resistance in Lactacoccus lactis: Evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane. EMBO J. 15:4239-4245.
    • (1996) EMBO J. , vol.15 , pp. 4239-4245
    • Bolhuis, H.1    Van Veen, H.W.2    Molenaar, D.3    Poolman, B.4    Driessen, A.J.M.5    Konings, W.N.6
  • 24
    • 0030977145 scopus 로고    scopus 로고
    • Phosphatidylcholine and phosphatidylethanolamine behave as substrates of the human MDR1 P-glycoprotein
    • Bosch, I., K. Dunussi-Joannopoulos, R.-L. Wu, S. Furlong, and J. Croop. 1997. Phosphatidylcholine and phosphatidylethanolamine behave as substrates of the human MDR1 P-glycoprotein. Biochemistry 36:5685-5694.
    • (1997) Biochemistry , vol.36 , pp. 5685-5694
    • Bosch, I.1    Dunussi-Joannopoulos, K.2    Wu, R.-L.3    Furlong, S.4    Croop, J.5
  • 25
    • 0030770318 scopus 로고    scopus 로고
    • The effect of reserpine, an inhibitor of multi-drug efflux pumps, on the in-vitro susceptibilities of fluoroquinolone-resistant strains of Streptococcus pneumoniae to norfloxacin
    • Brenwald, N. P., M. J. Gill, and R. Wise. 1997. The effect of reserpine, an inhibitor of multi-drug efflux pumps, on the in-vitro susceptibilities of fluoroquinolone-resistant strains of Streptococcus pneumoniae to norfloxacin. J. Antimicrob. Chemother. 40:458-460.
    • (1997) J. Antimicrob. Chemother. , vol.40 , pp. 458-460
    • Brenwald, N.P.1    Gill, M.J.2    Wise, R.3
  • 26
    • 0031927418 scopus 로고    scopus 로고
    • Prevalence of a putative efflux mechanism among fluoroquinolone-resistant clinical isolates of Streptococcus pneumonias
    • Brenwald, N. P., M. J. Gill, and R. Wise. 1998. Prevalence of a putative efflux mechanism among fluoroquinolone-resistant clinical isolates of Streptococcus pneumonias. Antimicrob. Agents Chemother. 42:2032-2035.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2032-2035
    • Brenwald, N.P.1    Gill, M.J.2    Wise, R.3
  • 27
    • 0032839007 scopus 로고    scopus 로고
    • Purification and ligand binding of EmrE, a regulator of a multidrug transporter
    • Brooun, A., J. J. Tomashek, and K. Lewis. 1999. Purification and ligand binding of EmrE, a regulator of a multidrug transporter. J. Bacteriol. 181:5131-5133.
    • (1999) J. Bacteriol. , vol.181 , pp. 5131-5133
    • Brooun, A.1    Tomashek, J.J.2    Lewis, K.3
  • 28
    • 0032949426 scopus 로고    scopus 로고
    • The multidrug efflux protein NorM is a prototype of a new family of transporters
    • Brown, M. H., I. T. Paulsen, and R. A. Skurray. 1999. The multidrug efflux protein NorM is a prototype of a new family of transporters. Mol. Microbiol. 31:394-395.
    • (1999) Mol. Microbiol. , vol.31 , pp. 394-395
    • Brown, M.H.1    Paulsen, I.T.2    Skurray, R.A.3
  • 29
    • 0029071785 scopus 로고
    • A functional classification scheme for β-lactamases and its correlation with molecular structure
    • Bush, K., G. A. Jacoby, and A. A. Medeiros. 1995. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 30
    • 0033214124 scopus 로고    scopus 로고
    • Co-operative binding sites for transported substrates in the multiple drug resistance transporter Mdrl
    • Buxbaum, E. 1999. Co-operative binding sites for transported substrates in the multiple drug resistance transporter Mdrl. Eur. J. Biochem. 265:64-70.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 64-70
    • Buxbaum, E.1
  • 31
    • 0027506202 scopus 로고
    • Induction of multidrug resistance in human cells by transient exposure to different chemotherapeutic drugs
    • Chaudhary, P. M., and I. B. Roninson. 1993. Induction of multidrug resistance in human cells by transient exposure to different chemotherapeutic drugs. J. Natl. Cancer Inst. 85:632-639.
    • (1993) J. Natl. Cancer Inst. , vol.85 , pp. 632-639
    • Chaudhary, P.M.1    Roninson, I.B.2
  • 32
    • 0026705492 scopus 로고
    • Epidemiology of drug resistance: Implications for a postantimicrobial era
    • Cohen, M. L. 1992. Epidemiology of drug resistance: implications for a postantimicrobial era. Science 257:1050-1055.
    • (1992) Science , vol.257 , pp. 1050-1055
    • Cohen, M.L.1
  • 33
    • 0024235788 scopus 로고
    • MarA locus causes decreased expression of OmpF porin in multiple-antibiotic-resistant (Mar) mutants of Escherichia coli
    • Cohen, S. P., L. M. McMurry, and S. B. Levy. 1988. marA locus causes decreased expression of OmpF porin in multiple-antibiotic-resistant (Mar) mutants of Escherichia coli. J. Bacteriol. 170:5416-5422.
    • (1988) J. Bacteriol. , vol.170 , pp. 5416-5422
    • Cohen, S.P.1    McMurry, L.M.2    Levy, S.B.3
  • 34
    • 0027419613 scopus 로고
    • Genetic and functional analysis of the multiple antibiotic resistance (mar) locus in Escherichia coli
    • Cohen, S. P., H. Hächler, and S. B. Levy. 1993. Genetic and functional analysis of the multiple antibiotic resistance (mar) locus in Escherichia coli. J. Bacteriol. 175:1484-1492.
    • (1993) . J. Bacteriol. , vol.175 , pp. 1484-1492
    • Cohen, S.P.1    Hächler, H.2    Levy, S.B.3
  • 35
    • 0027131605 scopus 로고
    • Salicylate induction of antibiotic resistance in Escherichia coli: Activation of the mar operon and a mar-independent pathway
    • Cohen, S. P., S. B. Levy, J. Foulds, and J. L. Rosner. 1993. Salicylate induction of antibiotic resistance in Escherichia coli: activation of the mar operon and a mar-independent pathway. J. Bacteriol. 175:7856-7862.
    • (1993) J. Bacteriol. , vol.175 , pp. 7856-7862
    • Cohen, S.P.1    Levy, S.B.2    Foulds, J.3    Rosner, J.L.4
  • 36
    • 0027171048 scopus 로고
    • A multidrug resistance regulatory chromosomal locus is widespread among enteric bacteria
    • Cohen, S. P., W. Yan, and S. B. Levy. 1993. A multidrug resistance regulatory chromosomal locus is widespread among enteric bacteria. J. Infect. Dis. 168:484-488.
    • (1993) J. Infect. Dis. , vol.168 , pp. 484-488
    • Cohen, S.P.1    Yan, W.2    Levy, S.B.3
  • 37
    • 0031983410 scopus 로고    scopus 로고
    • Isolation and characterization of a putative multidrug resistance pump from Vibrio cholerae
    • Colmer, J. A., J. A. Fralick, and A. N. Hamood. 1998. Isolation and characterization of a putative multidrug resistance pump from Vibrio cholerae. Mol. Microbiol. 27:63-72.
    • (1998) Mol. Microbiol. , vol.27 , pp. 63-72
    • Colmer, J.A.1    Fralick, J.A.2    Hamood, A.N.3
  • 38
    • 0026559854 scopus 로고
    • Drug-resistant TB may bring epidemic
    • Culliton, B. J. 1992. Drug-resistant TB may bring epidemic. Nature 356: 473.
    • (1992) Nature , vol.356 , pp. 473
    • Culliton, B.J.1
  • 39
    • 0026473238 scopus 로고
    • Identification of residues in the first cyloplasmic loop of P-glycoprotein involved in the function of chimeric human MDR1-MDR2 transporters
    • Currier, S. J., S. E. Kane, M. C. Willingham, C. O. Cardarelli, I. Pastan, and M. M. Gottesman. 1992. Identification of residues in the first cyloplasmic loop of P-glycoprotein involved in the function of chimeric human MDR1-MDR2 transporters. J. Biol. Chem. 267:25153-25159.
    • (1992) J. Biol. Chem. , vol.267 , 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
  • 40
    • 23444440823 scopus 로고
    • Inactivation of antibiotics and the dissemination of resistance genes
    • Davies, J. 1994. Inactivation of antibiotics and the dissemination of resistance genes. Science 264:375-382.
    • (1994) Science , vol.264 , pp. 375-382
    • Davies, J.1
  • 41
    • 0030788246 scopus 로고    scopus 로고
    • Involvement of the gonococcal MtrE protein in the resistance of Neisseria gonorrhoeae to toxic hydrophobic agents
    • Delahay, R. M., B. D. Robertson, J. T. Balthazar, W. M. Shafer, and C. A. Ison. 1997. Involvement of the gonococcal MtrE protein in the resistance of Neisseria gonorrhoeae to toxic hydrophobic agents. Microbiology 143:2127-2133.
    • (1997) Microbiology , vol.143 , pp. 2127-2133
    • Delahay, R.M.1    Robertson, B.D.2    Balthazar, J.T.3    Shafer, W.M.4    Ison, C.A.5
  • 42
    • 0031733415 scopus 로고    scopus 로고
    • Mmr, a Mycobacterium tuberculosis gene conferring resistance to small cationic dyes and inhibitors
    • De Rossi, E., M. Branzoni, R. Cantoni, A. Milano, G. Riccardi, and O. Ciferri. 1998. mmr, a Mycobacterium tuberculosis gene conferring resistance to small cationic dyes and inhibitors. J. Bacteriol. 180:6068-6071.
    • (1998) J. Bacteriol. , vol.180 , pp. 6068-6071
    • De Rossi, E.1    Branzoni, M.2    Cantoni, R.3    Milano, A.4    Riccardi, G.5    Ciferri, O.6
  • 43
    • 0026556302 scopus 로고
    • Amino acid substitutions in the sixth transmembrane domain of P-glycoprotein alter multidrug resistance
    • USA
    • Devine, S. E., V. Ling, and P. W. Melera. 1992. Amino acid substitutions in the sixth transmembrane domain of P-glycoprotein alter multidrug resistance. Proc. Natl. Acad. Sci. USA 89:4564-4568.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 4564-4568
    • Devine, S.E.1    Ling, V.2    Melera, P.W.3
  • 44
    • 0030924052 scopus 로고    scopus 로고
    • Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein
    • USA
    • Dey, S., M. Ramachandra, I. Pastan, M. M. Gottesman, and S. V. Ambudkar. 1997. Evidence for two nonidentical drug-interaction sites in the human P-glycoprotein. Proc. Natl. Acad. Sci. USA 94:10594-10599.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 10594-10599
    • Dey, S.1    Ramachandra, M.2    Pastan, I.3    Gottesman, M.M.4    Ambudkar, S.V.5
  • 45
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria
    • Dinh, T., I. T. Paulsen, and M. H. Saier. 1994. A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria. J. Bacteriol. 176:3825-3831.
    • (1994) J. Bacteriol. , vol.176 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier, M.H.3
  • 46
    • 0027509809 scopus 로고
    • The effect of lipids and detergents on ATPase-active P-glycoprotein
    • Doige, C. A., X. Yu, and F. J. Sharom. 1993. The effect of lipids and detergents on ATPase-active P-glycoprotein. Biochim. Biophys. Acta 1146: 65-72.
    • (1993) Biochim. Biophys. Acta , vol.1146 , pp. 65-72
    • Doige, C.A.1    Yu, X.2    Sharom, F.J.3
  • 47
    • 0030043489 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D. A. 1996. Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 271:163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 48
    • 0024409463 scopus 로고
    • Overproduction of transposon Tn10-encoded tetracycline resistance protein results in cell death and loss of membrane potential
    • Eckert, B., and C. F. Beck. 1989. Overproduction of transposon Tn10-encoded tetracycline resistance protein results in cell death and loss of membrane potential. J. Bacteriol. 171:3557-3559.
    • (1989) J. Bacteriol. , vol.171 , pp. 3557-3559
    • Eckert, B.1    Beck, C.F.2
  • 49
    • 0030956372 scopus 로고    scopus 로고
    • MdfA, an Escherichia coli multidrug resistance protein with an extraordinarily broad spectrum of drug recognition
    • Edgar, R., and E. Bibi. 1997. MdfA, an Escherichia coli multidrug resistance protein with an extraordinarily broad spectrum of drug recognition. J. Bacteriol. 179:2274-2280.
    • (1997) J. Bacteriol. , vol.179 , pp. 2274-2280
    • Edgar, R.1    Bibi, E.2
  • 50
    • 0033558105 scopus 로고    scopus 로고
    • A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug resistance protein MdfA
    • Edgar, R., and E. Bibi. 1999. A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug resistance protein MdfA. EMBO J. 18:822-832.
    • (1999) EMBO J. , vol.18 , pp. 822-832
    • Edgar, R.1    Bibi, E.2
  • 51
    • 0032460712 scopus 로고    scopus 로고
    • Alpha-periodicity analysis of small multidrug resistance (SMR) efflux transporters
    • Edwards, R. A., and R. J. Turner. 1998. Alpha-periodicity analysis of small multidrug resistance (SMR) efflux transporters. Biochem. Cell Biol. 76:791-797.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 791-797
    • Edwards, R.A.1    Turner, R.J.2
  • 52
    • 0031661594 scopus 로고    scopus 로고
    • Influence of the MexAB-OprM multidrug efflux system on quorum sensing in Pseudoinonas aeruginosa
    • Evans, K., I. Passador, R. Srikumar, E. Tsang, J. Nezezon, and K. Poole. 1998. Influence of the MexAB-OprM multidrug efflux system on quorum sensing in Pseudoinonas aeruginosa. J. Bacteriol. 180:5443-5447.
    • (1998) J. Bacteriol. , vol.180 , pp. 5443-5447
    • Evans, K.1    Passador, I.2    Srikumar, R.3    Tsang, E.4    Nezezon, J.5    Poole, K.6
  • 53
    • 0033002701 scopus 로고    scopus 로고
    • The MexA-MexB-OprM multidrug efflux system of Pseudomonas aeruginosa is growth-phase regulated
    • Evans, K., an K. Poole. 1999. The MexA-MexB-OprM multidrug efflux system of Pseudomonas aeruginosa is growth-phase regulated. FEMS Microbiol. Lett. 173:35-39.
    • (1999) FEMS Microbiol. Lett. , vol.173 , pp. 35-39
    • Evans, K.1    Poole, K.2
  • 54
    • 0028020549 scopus 로고
    • Transport of polypeptide ionophores into proteoliposomes reconstituted with rat liver P-glycoprotein
    • Eytan, G. D., M. J. Borgnia, R. Regev, and Y. G. Assaraf. 1994. Transport of polypeptide ionophores into proteoliposomes reconstituted with rat liver P-glycoprotein. J. Biol. Chem. 269:26058-26065.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26058-26065
    • Eytan, G.D.1    Borgnia, M.J.2    Regev, R.3    Assaraf, Y.G.4
  • 55
    • 0027132575 scopus 로고
    • ABC transporters: Bacterial exporters
    • Fath, M. J., and R. Kolter. 1993. ABC transporters: bacterial exporters. Microbiol. Rev. 57:995-1017.
    • (1993) Microbiol. Rev. , vol.57 , pp. 995-1017
    • Fath, M.J.1    Kolter, R.2
  • 56
    • 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., M. A. Russell, and M. H. Cullen. 1992. 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. 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
  • 58
    • 0029796966 scopus 로고    scopus 로고
    • Evidence that ToIC is required for functioning of the Mar/AcrAB efflux pump of Escherichia coli
    • Fralick, J. A. 1996. Evidence that ToIC is required for functioning of the Mar/AcrAB efflux pump of Escherichia coli. J. Bacteriol. 178:5803-5805.
    • (1996) J. Bacteriol. , vol.178 , pp. 5803-5805
    • Fralick, J.A.1
  • 59
    • 0027204547 scopus 로고
    • Thiolactomycin resistance in Escherichia coli is associated with the multidrug resistance efflux pump encoded by emrAB
    • Furukawa, H., J.-T. Tsay, S. Jackowski, Y. Takamura, and C. O. Rock. 1993. Thiolactomycin resistance in Escherichia coli is associated with the multidrug resistance efflux pump encoded by emrAB. J. Bacteriol. 175:3723-3729.
    • (1993) J. Bacteriol. , vol.175 , pp. 3723-3729
    • Furukawa, H.1    Tsay, J.-T.2    Jackowski, S.3    Takamura, Y.4    Rock, C.O.5
  • 60
    • 0027287346 scopus 로고
    • Overexpression of the MarA positive regulator is sufficient to confer multiple antibiotic resistance in Escherichia coli
    • Gambino, L., S. J. Gracheck, and P. F. Miller. 1993. Overexpression of the MarA positive regulator is sufficient to confer multiple antibiotic resistance in Escherichia coli. J. Bacteriol. 175:2888-2894.
    • (1993) J. Bacteriol. , vol.175 , pp. 2888-2894
    • Gambino, L.1    Gracheck, S.J.2    Miller, P.F.3
  • 61
    • 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., L. M. Mir, and S. Orlowski. 1997. Competitive and non-competitive inhibition of the multidrug-resistance-associated P-glycoprotein ATPase; further experimental evidence for a multisite model. Eur. J. Biochem. 244:664-673.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 664-673
    • Garrigos, M.1    Mir, L.M.2    Orlowski, S.3
  • 62
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • USA
    • Gaudu, P., and B. Weiss. 1996. SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc. Natl. Acad. Sci. USA 93:10094-10098.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 63
    • 0032907704 scopus 로고    scopus 로고
    • Identification of an efflux pump gene, pmrA, associated with fluoroquinolone resistance in Streptococcus pneumoniae
    • Gill, M. J., N. P. Brenwald, and R. Wise. 1999. Identification of an efflux pump gene, pmrA, associated with fluoroquinolone resistance in Streptococcus pneumoniae. Antimicrob. Agents Chemother. 43:187-189.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 187-189
    • Gill, M.J.1    Brenwald, N.P.2    Wise, R.3
  • 64
    • 0028894850 scopus 로고
    • The outer membrane protein OprM of Pseudomonas aeruginosa is encoded by oprK of the mexA-mexB-oprK multidrug resistance operon
    • Gotoh, N., H. Tsujimoto, K. Poole, J.-I. Yamagishi, and T. Nishino. 1995. The outer membrane protein OprM of Pseudomonas aeruginosa is encoded by oprK of the mexA-mexB-oprK multidrug resistance operon. Antimicrob. Agents Chemother. 39:2567-2569.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2567-2569
    • Gotoh, N.1    Tsujimoto, H.2    Poole, K.3    Yamagishi, J.-I.4    Nishino, T.5
  • 66
    • 0032146271 scopus 로고    scopus 로고
    • Functional replacement of OprJ by OprM in the MexCD-OprJ multidrug efflux system of Pseudomonas aeruginosa
    • Gotoh, N., H. Tsujimoto, A. Nomura, K. Okamoto, M. Tsuda, and T. Nishino. 1998. Functional replacement of OprJ by OprM in the MexCD-OprJ multidrug efflux system of Pseudomonas aeruginosa. FEMS Microbiol. Lett. 165:21-27.
    • (1998) FEMS Microbiol. Lett. , vol.165 , pp. 21-27
    • Gotoh, N.1    Tsujimoto, H.2    Nomura, A.3    Okamoto, K.4    Tsuda, M.5    Nishino, T.6
  • 67
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman, M. M., and I. Pastan. 1993. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu. Rev. Biochem. 62:335-427.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 335-427
    • Gottesman, M.M.1    Pastan, I.2
  • 69
    • 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. 1993. 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. 268:11417-11425.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11417-11425
    • Greenberger, L.M.1
  • 71
    • 0026553163 scopus 로고
    • A staphylococcal multidrug resistance gene product is a member of a new protein family
    • Grinius, L., G. Dreguniene, E. B. Goldberg, C.-H. Liao, and S. J. Projan. 1992. A staphylococcal multidrug resistance gene product is a member of a new protein family. Gene 27:119-129.
    • (1992) Gene , vol.27 , pp. 119-129
    • Grinius, L.1    Dreguniene, G.2    Goldberg, E.B.3    Liao, C.-H.4    Projan, S.J.5
  • 72
    • 0027970086 scopus 로고
    • Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump
    • Grinius, L., and E. B. Goldberg. 1994. Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump. J. Biol. Chem. 269:29998-30004.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29998-30004
    • Grinius, L.1    Goldberg, E.B.2
  • 73
    • 33750106248 scopus 로고    scopus 로고
    • Quinolone efflux protein Nora is a proton-driven drug pump
    • Grinius, L. L., R. J. Siehnel, and C. M. Morris. 1997. Quinolone efflux protein NorA is a proton-driven drug pump. FASEB J. 11:A958.
    • (1997) FASEB J. , vol.11
    • Grinius, L.L.1    Siehnel, R.J.2    Morris, C.M.3
  • 74
    • 0032541162 scopus 로고    scopus 로고
    • QacR is a repressor protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA
    • Grkovic, S., M. H. Brown, N. J. Roberts, I. T. Paulsen, and R. A. Skurray. 1998. QacR is a repressor protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA. J. Biol. Chem. 273:18665-18673.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18665-18673
    • Grkovic, S.1    Brown, M.H.2    Roberts, N.J.3    Paulsen, I.T.4    Skurray, R.A.5
  • 75
    • 0033538028 scopus 로고    scopus 로고
    • Membrane topology of the xenobiotic-exporting subunit, MexB, of the MexA,B-OprM Extrusion pump in Pseudomonas aeruginosa
    • Guan, L., M. Ehrmann, H. Yoneyama, and T. Nakae. 1999. Membrane topology of the xenobiotic-exporting subunit, MexB, of the MexA,B-OprM Extrusion pump in Pseudomonas aeruginosa. J. Biol. Chem. 274:10517-10522.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10517-10522
    • Guan, L.1    Ehrmann, M.2    Yoneyama, H.3    Nakae, T.4
  • 76
    • 0025999987 scopus 로고
    • A bacteriol analog of the indigene of mammalian tumor cells is present in Streptomyces peucetius, the producer of daunorubicin and doxorubicin
    • USA
    • Guilfoile, P. G., and C. R. Hutchinson. 1991. A bacteriol analog of the indigene of mammalian tumor cells is present in Streptomyces peucetius, the producer of daunorubicin and doxorubicin. Proc. Natl. Acad. Sci. USA 88:8553-8557.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 8553-8557
    • Guilfoile, P.G.1    Hutchinson, C.R.2
  • 77
    • 0021990551 scopus 로고
    • Cross-resistance to nalidixic acid, trimethoprim, and chloramphenicol associated with alterations in outer mem0 brane proteins of Klebsiella, Enterobacter, and Serratia
    • Gutmann, L., R. Williamson, N. Moreau, M.-D. Kitzis, E. Collatz, J. F. Acar, and F. W. Goldstein. 1985. Cross-resistance to nalidixic acid, trimethoprim, and chloramphenicol associated with alterations in outer mem0 brane proteins of Klebsiella, Enterobacter, and Serratia. J. Infect. Dis. 151: 501-507.
    • (1985) J. Infect. Dis. , vol.151 , pp. 501-507
    • Gutmann, L.1    Williamson, R.2    Moreau, N.3    Kitzis, M.-D.4    Collatz, E.5    Acar, J.F.6    Goldstein, F.W.7
  • 78
    • 0026095607 scopus 로고
    • A, a regulated locus which controls expression of chromosomal multiple antibiotic resistance in Escherichia coli
    • Hächler, H., S. P. Cohen, and S. B. Levy. 1991. marA, a regulated locus which controls expression of chromosomal multiple antibiotic resistance in Escherichia coli. J. Bacteriol. 173:5532-5538.
    • (1991) J. Bacteriol. , vol.173 , pp. 5532-5538
    • Hächler, H.1    Cohen, S.P.2    Levy, S.B.3
  • 79
    • 0029078189 scopus 로고
    • Transcriptional control of the mtr efflux system of Neisseria gonorrhoeae
    • Hagman, K. E., and W. M. Shafer. 1995. Transcriptional control of the mtr efflux system of Neisseria gonorrhoeae. J. Bacteriol. 177:4162-4165.
    • (1995) J. Bacteriol. , vol.177 , pp. 4162-4165
    • Hagman, K.E.1    Shafer, W.M.2
  • 80
    • 0028906903 scopus 로고
    • Resistance of Neisseria gonorrhoeae to antimicrobial hydrophobic agents is modulated by the mtrRCDE efflux system
    • Hagman, K. E., W. Pan, B. G. Spratt, J. T. Balthazar, R. C. Judd, and W. M. Shafer. 1995. Resistance of Neisseria gonorrhoeae to antimicrobial hydrophobic agents is modulated by the mtrRCDE efflux system. Microbiology 141:611-622.
    • (1995) Microbiology , vol.141 , pp. 611-622
    • Hagman, K.E.1    Pan, W.2    Spratt, B.G.3    Balthazar, J.T.4    Judd, R.C.5    Shafer, W.M.6
  • 81
    • 0030788726 scopus 로고    scopus 로고
    • The MtrD protein of Neisseria gonorrhoeae is a member of the resistance/nodulation/division protein family constituting part of an efflux system
    • Hagman, K. E., C. E. Lucas, J. T. Balthazar, L. Snyder, M. Nilles, R. C. Judd, and W. M. Shafer. 1997. The MtrD protein of Neisseria gonorrhoeae is a member of the resistance/nodulation/division protein family constituting part of an efflux system. Microbiology 143:2117-2125.
    • (1997) Microbiology , vol.143 , pp. 2117-2125
    • Hagman, K.E.1    Lucas, C.E.2    Balthazar, J.T.3    Snyder, L.4    Nilles, M.5    Judd, R.C.6    Shafer, W.M.7
  • 82
    • 0029879199 scopus 로고    scopus 로고
    • Mutagenesis of transmembrane domain 11 of P-glyeoprotein by alaninc scanning
    • Hanna, M., M. Brault, T. Kwan, C. Kast, and P. Gros. 1996. Mutagenesis of transmembrane domain 11 of P-glyeoprotein by alaninc scanning. Biochemistry 35:3625-3635.
    • (1996) Biochemistry , vol.35 , pp. 3625-3635
    • Hanna, M.1    Brault, M.2    Kwan, T.3    Kast, C.4    Gros, P.5
  • 83
    • 0025612231 scopus 로고
    • Molecular mechanisms of drug resistance
    • Hayes, J. D., and C. R. Wolf. 1990. Molecular mechanisms of drug resistance. Biochem. J. 272:281-295.
    • (1990) Biochem. J. , vol.272 , pp. 281-295
    • Hayes, J.D.1    Wolf, C.R.2
  • 84
    • 0032101923 scopus 로고    scopus 로고
    • The Staphylococcus aureus qacH gene product: A new member of the SMR family encoding multidrug resistance
    • Heir, E., G. Sundheim, and A. L. Holck. 1998. The Staphylococcus aureus qacH gene product: a new member of the SMR family encoding multidrug resistance. FEMS Microbiol. Lett. 163:49-56.
    • (1998) FEMS Microbiol. Lett. , vol.163 , pp. 49-56
    • Heir, E.1    Sundheim, G.2    Holck, A.L.3
  • 85
    • 0033001706 scopus 로고    scopus 로고
    • The qacG gene on plasmid pST94 confers resistance to quarternary ammonium compounds in staphylococci isolated from the food industry
    • Heir, E., G. Sundheim, and A. L. Holck. 1999. The qacG gene on plasmid pST94 confers resistance to quarternary ammonium compounds in staphylococci isolated from the food industry. J. Appl. Microbiol. 86:378-388.
    • (1999) J. Appl. Microbiol. , vol.86 , pp. 378-388
    • Heir, E.1    Sundheim, G.2    Holck, A.L.3
  • 86
    • 0343472846 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 87
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 88
  • 89
    • 0028332661 scopus 로고
    • Calcein accumulation as a fluorometric functional assay of the multidrug transporter
    • Holló, Z., L. Homolya, C. W. Davis, and B. Sarkadi. 1994. Calcein accumulation as a fluorometric functional assay of the multidrug transporter. Biochim. Biophys. Acta 1191:384-388.
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 384-388
    • Holló, Z.1    Homolya, L.2    Davis, C.W.3    Sarkadi, B.4
  • 90
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-hearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje, J.-V. 1998. Growth of the stress-hearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62:181-203.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 181-203
    • Höltje, J.-V.1
  • 91
  • 92
    • 0007630205 scopus 로고
    • ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells
    • USA
    • Horio, M., M. M. Gottesman, and I. Pastan. 1988. ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells. Proc. Natl. Acad. Sci. USA 85:3580-3584.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 3580-3584
    • Horio, M.1    Gottesman, M.M.2    Pastan, I.3
  • 93
    • 0032479280 scopus 로고    scopus 로고
    • Mechanism of action of human P-glycoprotein ATPase activity; photochemical cleavage during a catalytic transition state using orthovanadate reveals cross-talk between the two ATP sites
    • Hrycyna, C. A., M. Ramachandra, S. V. Ambudkar, Y. Hee Ko, P. L. Pedersen, I. Pastan, and M. M. Gottesman. 1998. Mechanism of action of human P-glycoprotein ATPase activity; photochemical cleavage during a catalytic transition state using orthovanadate reveals cross-talk between the two ATP sites. J. Biol. Chem. 273:16631-16634.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16631-16634
    • Hrycyna, C.A.1    Ramachandra, M.2    Ambudkar, S.V.3    Hee Ko, Y.4    Pedersen, P.L.5    Pastan, I.6    Gottesman, M.M.7
  • 94
    • 0032499778 scopus 로고    scopus 로고
    • Bacteria lacking a multidrug pump: A sensitive tool for drug discovery
    • USA
    • Hsieh, P.-C., S. A. Siegel, B. Rogers, D. Davis, and K. Lewis. 1998. Bacteria lacking a multidrug pump: a sensitive tool for drug discovery. Proc. Natl. Acad. Sci. USA 95:6602-6606.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 6602-6606
    • Hsieh, P.-C.1    Siegel, S.A.2    Rogers, B.3    Davis, D.4    Lewis, K.5
  • 97
    • 0034087478 scopus 로고    scopus 로고
    • A broad-specificity multidrug efflux pump requiring a pair of homologous SMR-type proteins
    • Jack, D. L., M. L. Storms, J. H. Tchieu, I. T. Paulsen, and M. H. Saier, Jr. 2000. A broad-specificity multidrug efflux pump requiring a pair of homologous SMR-type proteins. J. Bacteriol. 182:2311-2313.
    • (2000) J. Bacteriol. , vol.182 , pp. 2311-2313
    • Jack, D.L.1    Storms, M.L.2    Tchieu, J.H.3    Paulsen, I.T.4    Saier M.H., Jr.5
  • 98
    • 0030938155 scopus 로고    scopus 로고
    • A Corynebacterium glutamicum gene conferring multidrug resistance in the heterologous host Escherichia coli
    • Jäger, W., J. Kalinowski, and A. Pühler. 1997. A Corynebacterium glutamicum gene conferring multidrug resistance in the heterologous host Escherichia coli. J. Bacteriol. 179:2449-2451.
    • (1997) J. Bacteriol. , vol.179 , pp. 2449-2451
    • Jäger, W.1    Kalinowski, J.2    Pühler, A.3
  • 99
    • 0028879546 scopus 로고
    • Purification and regulatory properties of Mara protein, a transcriptional activator of Escherichia coli multiple antibiotic and superoxide resistance promoters
    • Jair, K.-W., R. G. Martin, J. L. Rosner, N. Fujita, A. Ishihama, and R. E. Wolf, Jr. 1995. Purification and regulatory properties of MarA protein, a transcriptional activator of Escherichia coli multiple antibiotic and superoxide resistance promoters. J. Bacteriol. 177:7100-7104.
    • (1995) J. Bacteriol. , vol.177 , pp. 7100-7104
    • Jair, K.-W.1    Martin, R.G.2    Rosner, J.L.3    Fujita, N.4    Ishihama, A.5    Wolf R.E., Jr.6
  • 100
    • 0029863748 scopus 로고    scopus 로고
    • Transcriptional activation of promoters of the superoxide and multiple antibiotic resistance regulons by Rob, a binding protein of the Escherichia coli origin of chromosomal replication
    • Jair, K.-W., X. Yu, K. Skarstad, B. Thöny, N. Fujita, A. Ishihama, and R. E. Wolf, Jr. 1996. Transcriptional activation of promoters of the superoxide and multiple antibiotic resistance regulons by Rob, a binding protein of the Escherichia coli origin of chromosomal replication. J. Bacteriol. 178:2507-2513.
    • (1996) J. Bacteriol. , vol.178 , pp. 2507-2513
    • Jair, K.-W.1    Yu, X.2    Skarstad, K.3    Thöny, B.4    Fujita, N.5    Ishihama, A.6    Wolf R.E., Jr.7
  • 101
    • 0028061607 scopus 로고
    • Mycobacterial cell wall: Structure and role in natural resistance to antibiotics
    • Jarlier, V., and H. Nikaido. 1994. Mycobacterial cell wall: structure and role in natural resistance to antibiotics. FEMS Microbiol. Lett. 123:11-18.
    • (1994) FEMS Microbiol. Lett. , vol.123 , pp. 11-18
    • Jarlier, V.1    Nikaido, H.2
  • 102
    • 0028999357 scopus 로고
    • The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K.), in hydrophilic loop 2/3 of the lactose permease
    • Jessen-Marshall, A. E., N. J. Paul, and R. J. Brooker. 1995. The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K.), in hydrophilic loop 2/3 of the lactose permease. J. Biol. Chem. 27:16251-16257.
    • (1995) J. Biol. Chem. , vol.27 , pp. 16251-16257
    • Jessen-Marshall, A.E.1    Paul, N.J.2    Brooker, R.J.3
  • 103
    • 0027270540 scopus 로고
    • Efflux-mediated fluoroquinolone resistance in Staphylococcus aureus
    • Kaatz, G. W., S. M. Seo, and C. A. Ruble. 1993. Efflux-mediated fluoroquinolone resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 37:1086-1094.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1086-1094
    • Kaatz, G.W.1    Seo, S.M.2    Ruble, C.A.3
  • 104
    • 0028859486 scopus 로고
    • Inducible NorA-mediated multidrug resistance in Staphylococcus aureus
    • Kaatz, G. W., and S. M. Seo. 1995. Inducible NorA-mediated multidrug resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 39: 2650-2655.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2650-2655
    • Kaatz, G.W.1    Seo, S.M.2
  • 105
    • 0030063395 scopus 로고    scopus 로고
    • Rhodamine 123 efflux transporter in Haloferax volcanii is induced when cultured under 'metabolic stress' by amino acids: The efflux system resembles that in a doxorubicin-resistant mutant
    • Kaidoh, K., S. Miyauchi, A. Abe, S. Tanabu, T. Nara, and N. Kamo. 1996. Rhodamine 123 efflux transporter in Haloferax volcanii is induced when cultured under 'metabolic stress' by amino acids: the efflux system resembles that in a doxorubicin-resistant mutant. Biochem. J. 314:355-359.
    • (1996) Biochem. J. , vol.314 , pp. 355-359
    • Kaidoh, K.1    Miyauchi, S.2    Abe, A.3    Tanabu, S.4    Nara, T.5    Kamo, N.6
  • 106
    • 0027215242 scopus 로고
    • Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain 11 as a putative drug binding site
    • Kajiji, S., F. Talbot, K. Grizzuti, V. Van Dyke-Phillips, M. Agresti, A. R. Safa, and P. Gros. 1993. Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain 11 as a putative drug binding site. Biochemistry 32:4185-4194.
    • (1993) Biochemistry , vol.32 , 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
  • 107
    • 0026663641 scopus 로고
    • Modulation of expression of multidrug resistance gene (mdr-1) by adriamycin
    • Kato, S., J. Nishimura, Y. Yufu, H. Ideguchi, T. Umemura, and H. Nawata. 1992. Modulation of expression of multidrug resistance gene (mdr-1) by adriamycin. FEBS Lett. 308:175-178.
    • (1992) FEBS Lett. , vol.308 , pp. 175-178
    • Kato, S.1    Nishimura, J.2    Yufu, Y.3    Ideguchi, H.4    Umemura, T.5    Nawata, H.6
  • 108
    • 0032519958 scopus 로고    scopus 로고
    • Distribution of the antiseptic-resistance genes qacE and qacEΔ1 in Gram-negative bacteria
    • Kazama, H., H. Hamashima, M. Sasatsu, and T. Arai. 1998. Distribution of the antiseptic-resistance genes qacE and qacEΔ1 in Gram-negative bacteria. FEMS Microbiol. Lett. 159:173-178.
    • (1998) FEMS Microbiol. Lett. , vol.159 , pp. 173-178
    • Kazama, H.1    Hamashima, H.2    Sasatsu, M.3    Arai, T.4
  • 109
    • 0032460882 scopus 로고    scopus 로고
    • Distribution of the antiseptic-resistance gene qacEΔ1 in Gram-positive bacteria
    • Kazama, H., H. Hamashima, M. Sasatsu, and T. Arai. 1998. Distribution of the antiseptic-resistance gene qacEΔ1 in Gram-positive bacteria. FEMS Microbiol. Lett. 165:295-299.
    • (1998) FEMS Microbiol. Lett. , vol.165 , pp. 295-299
    • Kazama, H.1    Hamashima, H.2    Sasatsu, M.3    Arai, T.4
  • 110
    • 0025996531 scopus 로고
    • Molecular analysis and nucleotide sequence of the envCD operon of Escherichia coli
    • Klein, J. R., B. Henrich, and R. Plapp. 1991. Molecular analysis and nucleotide sequence of the envCD operon of Escherichia coli. Mol. Gen. Genet. 230:230-240.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 230-240
    • Klein, J.R.1    Henrich, B.2    Plapp, R.3
  • 111
    • 0030949566 scopus 로고    scopus 로고
    • Mutations affecting substrate specificity of the Bacillus subtilis multidrug transporter Bmr
    • Klyachko, K. A., S. Schuldiner, and A. A. Neyfakh. 1997. Mutations affecting substrate specificity of the Bacillus subtilis multidrug transporter Bmr. J. Bacteriol. 179:2189-2193.
    • (1997) J. Bacteriol. , vol.179 , pp. 2189-2193
    • Klyachko, K.A.1    Schuldiner, S.2    Neyfakh, A.A.3
  • 112
    • 0032469004 scopus 로고    scopus 로고
    • Paradoxical enhancement of the activity of a bacterial multidrug transporter caused by substitutions of a conserved residue
    • Klyachko, K. A., and A. A. Neyfakh. 1998. Paradoxical enhancement of the activity of a bacterial multidrug transporter caused by substitutions of a conserved residue. J. Bacteriol. 180:2817-2821.
    • (1998) J. Bacteriol. , vol.180 , pp. 2817-2821
    • Klyachko, K.A.1    Neyfakh, A.A.2
  • 113
    • 0029897240 scopus 로고    scopus 로고
    • Unidirectional reconstitution into detergent destabilized liposomes of the purified lactose transport systems of Streptococcus thermophilus
    • Knol, J., L. Veenhoff, W.-J. Liang, P. J. F. Henderson, G. Leblanc, and B. Poolman. 1996. Unidirectional reconstitution into detergent destabilized liposomes of the purified lactose transport systems of Streptococcus thermophilus. J. Biol. Chem. 271:15358-15366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15358-15366
    • Knol, J.1    Veenhoff, L.2    Liang, W.-J.3    Henderson, P.J.F.4    Leblanc, G.5    Poolman, B.6
  • 114
    • 0343472845 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 116
    • 0344131941 scopus 로고    scopus 로고
    • Characterization of MexT, the regulator of the MexE-MexF-OprN multidrug efflux system of Pseudomonas aeruginosa
    • Köhler, T., S. F. Epp, L. Kocjancic Curty, and J.-C. Pechère. 1999. Characterization of MexT, the regulator of the MexE-MexF-OprN multidrug efflux system of Pseudomonas aeruginosa. J. Bacteriol. 181:6300-6305.
    • (1999) J. Bacteriol. , vol.181 , pp. 6300-6305
    • Köhler, T.1    Epp, S.F.2    Kocjancic Curty, L.3    Pechère, J.-C.4
  • 118
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Kronakis, V., A. Sharff, E. Koronakis, B. Luisi, and C. Hughes. 2000. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405:914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Kronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 119
    • 0030016417 scopus 로고    scopus 로고
    • Bacterial growth inhibition by over-production of protein
    • Kurland, C. G., and H. Dong. 1996. Bacterial growth inhibition by over-production of protein. Mol. Microbiol. 21:1-4.
    • (1996) Mol. Microbiol. , vol.21 , pp. 1-4
    • Kurland, C.G.1    Dong, H.2
  • 120
  • 121
    • 0029118321 scopus 로고
    • Multidrug resistance plasmid pSK108 from coagulase-negative staphylococci: Relationships to Staphylococcus aureus qacC plasmids
    • Leelaporn, A., N. Firth, I. T. Paulsen, A. Hettiaratchi, and R. A. Skurray. 1995. Multidrug resistance plasmid pSK108 from coagulase-negative staphylococci: relationships to Staphylococcus aureus qacC plasmids. Plasmid 34:62-67.
    • (1995) Plasmid , vol.34 , pp. 62-67
    • Leelaporn, A.1    Firth, N.2    Paulsen, I.T.3    Hettiaratchi, A.4    Skurray, R.A.5
  • 122
    • 0026588343 scopus 로고
    • Active efflux mechanisms for antibiotic resistance
    • Levy, S. 1992. Active efflux mechanisms for antibiotic resistance. Antimicrob. Agents Chemother. 36:695-703.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 695-703
    • Levy, S.1
  • 123
    • 0032014842 scopus 로고    scopus 로고
    • The challenge of antibiotic resistance
    • Levy, S. 1998. The challenge of antibiotic resistance. Sci. Am. 278:32-39.
    • (1998) Sci. Am. , vol.278 , pp. 32-39
    • Levy, S.1
  • 124
    • 0032493114 scopus 로고    scopus 로고
    • Multidrug resistance - A sign of the times
    • Levy, S. 1998. Multidrug resistance - a sign of the times. N. Engl. J. Med. 338:1376-1378.
    • (1998) N. Engl. J. Med. , vol.338 , pp. 1376-1378
    • Levy, S.1
  • 125
    • 0032226553 scopus 로고    scopus 로고
    • Reversing tetracycline resistance: A renaissance for the tetracycline family of antibiotics
    • B. P. Rosen and S. Mobashery (ed.). Kluwer Academic/ Plenum Publishers, New York, N.Y.
    • Levy, S., and M. Nelson. 1998. Reversing tetracycline resistance: a renaissance for the tetracycline family of antibiotics, p. 17-25. In B. P. Rosen and S. Mobashery (ed.). Resolving the antibiotic paradox. Kluwer Academic/ Plenum Publishers, New York, N.Y.
    • (1998) Resolving the Antibiotic Paradox , pp. 17-25
    • Levy, S.1    Nelson, M.2
  • 126
    • 0028314541 scopus 로고
    • Multidrug resistance pumps in bacteria: Variations on a theme
    • Lewis, K. 1994. Multidrug resistance pumps in bacteria: variations on a theme. Trends Biochem. Sci. 19:119-123.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 119-123
    • Lewis, K.1
  • 127
    • 0000686395 scopus 로고    scopus 로고
    • Multidrug resistance pumps provide broad defense
    • Lewis, K-, D. C. Hooper, and M. Ouellette. 1997. Multidrug resistance pumps provide broad defense. ASM News 63:605-610.
    • (1997) ASM News , vol.63 , pp. 605-610
    • Lewis, K.1    Hooper, D.C.2    Ouellette, M.3
  • 128
    • 0028067837 scopus 로고
    • Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: Resistance to tetracycline, chloramphenicol, and norfloxacin
    • Li, X.-Z., D. M. Livermore, and H. Nikaido. 1994. Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: resistance to tetracycline, chloramphenicol, and norfloxacin. Antimicrob. Agents Chemother. 38:1732-1741.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1732-1741
    • Li, X.-Z.1    Livermore, D.M.2    Nikaido, H.3
  • 129
    • 0029129966 scopus 로고
    • Role of MexA-MexB-OprM in antibiotic efflux in Pseudomonas aeruginosa
    • Li, X.-Z., H. Nikaido, and K. Poole. 1995. Role of MexA-MexB-OprM in antibiotic efflux in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 39:1948-1953.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1948-1953
    • Li, X.-Z.1    Nikaido, H.2    Poole, K.3
  • 130
    • 0028180409 scopus 로고
    • An ABC-transporter from Streptomyces longisporoflavus confers resistance to the polyether-ionophore antibiotic tetronasin
    • Linton, K. J., H. N. Cooper, I. S. Hunter, and P. F. Leadleay. 1994. An ABC-transporter from Streptomyces longisporoflavus confers resistance to the polyether-ionophore antibiotic tetronasin. Mol. Microbiol. 11:777-785.
    • (1994) Mol. Microbiol. , vol.11 , pp. 777-785
    • Linton, K.J.1    Cooper, H.N.2    Hunter, I.S.3    Leadleay, P.F.4
  • 131
    • 0030743356 scopus 로고    scopus 로고
    • Competitive, non-competitive and cooperative ineractions between substrates of P-glycoprotein as measured by its ATPase activity
    • Litman, T., T. Zeuthen, T. Skovsgaard, and W. D. Stein. 1997. Competitive, non-competitive and cooperative ineractions between substrates of P-glycoprotein as measured by its ATPase activity. Biochim. Biophys. Acta 1361:169-176.
    • (1997) Biochim. Biophys. Acta , vol.1361 , pp. 169-176
    • Litman, T.1    Zeuthen, T.2    Skovsgaard, T.3    Stein, W.D.4
  • 132
    • 0025731481 scopus 로고
    • Structure and evolution of a family of genes encoding antiseptic and disinfectant resistance in Staphylococcus aureus
    • Littlejohn, T. G., D. DiBerardino, L. J. Messerotti, S. J. Spiers, and R. A. Skurray. 1991. Structure and evolution of a family of genes encoding antiseptic and disinfectant resistance in Staphylococcus aureus. Gene 101: 59-66.
    • (1991) Gene , vol.101 , pp. 59-66
    • Littlejohn, T.G.1    Diberardino, D.2    Messerotti, L.J.3    Spiers, S.J.4    Skurray, R.A.5
  • 134
    • 0030013072 scopus 로고    scopus 로고
    • Active efflux of fluoroquinolones in Mycobacterium smegmatis mediated by LfrA, a multidrug efflux pump
    • Liu, J., H. E. Takiff, and H. Nikaido. 1996. Active efflux of fluoroquinolones in Mycobacterium smegmatis mediated by LfrA, a multidrug efflux pump. J. Bacteriol. 178:3791-3795.
    • (1996) J. Bacteriol. , vol.178 , pp. 3791-3795
    • Liu, J.1    Takiff, H.E.2    Nikaido, H.3
  • 135
    • 0026686805 scopus 로고
    • Emr, an Escherichia coli locus for multidrug resistance
    • USA
    • Lomovskaya, O., and K. Lewis. 1992. emr, an Escherichia coli locus for multidrug resistance. Proc. Natl. Acad. Sci. USA 89:8938-8942.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 8938-8942
    • Lomovskaya, O.1    Lewis, K.2
  • 136
    • 0028999706 scopus 로고
    • EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB
    • Lomovskaya, O., K. Lewis, and A. Matin. 1995. EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB. J. Bacteriol. 177:2328-2334.
    • (1995) J. Bacteriol. , vol.177 , pp. 2328-2334
    • Lomovskaya, O.1    Lewis, K.2    Matin, A.3
  • 137
    • 0027260959 scopus 로고
    • Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein
    • Loo, T. W., and D. M. Clarke. 1993. Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein. J. Biol. Chem. 268:19965-19972.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19965-19972
    • Loo, T.W.1    Clarke, D.M.2
  • 138
    • 0028229881 scopus 로고
    • Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides
    • Loo, T. W., and D. M. Clarke. 1994. Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides. J. Biol. Chem. 269:7750-7755.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7750-7755
    • Loo, T.W.1    Clarke, D.M.2
  • 139
    • 0027997698 scopus 로고
    • Mutation of amino acids located in predicted transmembrane domain segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein
    • Loo, T. W., and D. M. Clarke. 1994. Mutation of amino acids located in predicted transmembrane domain segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein. Biochemistry 33:14049-14057.
    • (1994) Biochemistry , vol.33 , pp. 14049-14057
    • Loo, T.W.1    Clarke, D.M.2
  • 140
    • 0342602774 scopus 로고    scopus 로고
    • Cyclosporins and related fungal products in the reversal of P-glycoprotein-mediated multidrug resistance
    • S. Gupta and T. Tsuruo (ed.), John Wiley & Sons Ltd, Chichester, U.K.
    • Loor, F. 1996. Cyclosporins and related fungal products in the reversal of P-glycoprotein-mediated multidrug resistance, p. 385-412. In S. Gupta and T. Tsuruo (ed.), Multidrug resistance in cancer cells: cellular, biochemical and biological aspects. John Wiley & Sons Ltd, Chichester, U.K.
    • (1996) Multidrug Resistance in Cancer Cells: Cellular, Biochemical and Biological Aspects , pp. 385-412
    • Loor, F.1
  • 141
    • 0027508337 scopus 로고
    • Molecular cloning and characterization of acrA and acrE genes Escherichia coli
    • Ma, D., D. N. Cook., M. Alberti, N. G. Pon, H. Nikaido, and J. E. Hearst. 1993. Molecular cloning and characterization of acrA and acrE genes Escherichia coli. J. Bacteriol. 175:6299-6313.
    • (1993) J. Bacteriol. , vol.175 , pp. 6299-6313
    • Ma, D.1    Cook, D.N.2    Alberti, M.3    Pon, N.G.4    Nikaido, H.5    Hearst, J.E.6
  • 142
    • 0027959315 scopus 로고
    • Efflux pumps and drug resistance in Gram-negative bacteria
    • Ma, D., D. N. Cook, J. E. Hearst, and H. Nikaido. 1994. Efflux pumps and drug resistance in Gram-negative bacteria. Trends Microbiol. 2:489-493.
    • (1994) Trends Microbiol. , vol.2 , pp. 489-493
    • Ma, D.1    Cook, D.N.2    Hearst, J.E.3    Nikaido, H.4
  • 143
    • 0028926676 scopus 로고
    • Genes acra and acrB encode a stress-induced efflux system of Escherichia coli
    • Ma, D., D. N. Cook, M. Alberti, N. G. Pon, H. Nikaido, and J. E. Hearst. 1995. Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli. Mol. Microbiol. 16:45-55.
    • (1995) Mol. Microbiol. , vol.16 , pp. 45-55
    • Ma, D.1    Cook, D.N.2    Alberti, M.3    Pon, N.G.4    Nikaido, H.5    Hearst, J.E.6
  • 144
    • 0030023489 scopus 로고    scopus 로고
    • The local repressor AcrR plays a modulating role in the regulation of acrAB genes of Escherichia coli by global stress signals
    • Ma, D., M. Alberti, C. Lynch, H. Nikaido, and J. E. Hearst. 1996. The local repressor AcrR plays a modulating role in the regulation of acrAB genes of Escherichia coli by global stress signals. Mol. Microbiol. 19:101-112.
    • (1996) Mol. Microbiol. , vol.19 , pp. 101-112
    • Ma, D.1    Alberti, M.2    Lynch, C.3    Nikaido, H.4    Hearst, J.E.5
  • 146
    • 0027507306 scopus 로고
    • A major superfamily of transmembrane facilitators that can catalyze uniport, symport and antiport
    • Marger, M., and M. H. Saier, Jr. 1993. A major superfamily of transmembrane facilitators that can catalyze uniport, symport and antiport. Trends Biochem. Sci. 18:13-20.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 13-20
    • Marger, M.1    Saier M.H., Jr.2
  • 147
    • 0033534178 scopus 로고    scopus 로고
    • The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids
    • Margolles, A., M. Putman, H. W. van Veen, and W. N. Konings. 1999. The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids. Biochemistry 38:16298-16306.
    • (1999) Biochemistry , vol.38 , pp. 16298-16306
    • Margolles, A.1    Putman, M.2    Van Veen, H.W.3    Konings, W.N.4
  • 148
    • 0029990932 scopus 로고    scopus 로고
    • The drug-binding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain
    • Markham, P. N., M. Ahmed, and A. A. Neyfakh. 1996. The drug-binding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain. J. Bacteriol. 178:1473-1475.
    • (1996) J. Bacteriol. , vol.178 , pp. 1473-1475
    • Markham, P.N.1    Ahmed, M.2    Neyfakh, A.A.3
  • 149
    • 0029973621 scopus 로고    scopus 로고
    • Inhibition of the multidrug transporter NorA prevents emergence of norfloxacin resistance in Staphylococcus aureus
    • Markham, P. N., and A. A. Neyfakh. 1996. Inhibition of the multidrug transporter NorA prevents emergence of norfloxacin resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 40:2673-2674.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2673-2674
    • Markham, P.N.1    Neyfakh, A.A.2
  • 150
    • 0031561388 scopus 로고    scopus 로고
    • Broad ligand specificity of the transcriptional regulator of the Bacillus subtilis multidrug transporter Bmr
    • Markham, P. N., J. LoGuidice, and A. A. Neyfakh. 1997. Broad ligand specificity of the transcriptional regulator of the Bacillus subtilis multidrug transporter Bmr. Biochem. Biophys. Res. Commun. 239:269-272.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 269-272
    • Markham, P.N.1    Loguidice, J.2    Neyfakh, A.A.3
  • 151
    • 0032942964 scopus 로고    scopus 로고
    • Inhibition of the emergence of ciprofloxacin resistance in Streptococcus pneumoniae by the multidrug inhibitor reserpine
    • Markham, P. N. 1999. Inhibition of the emergence of ciprofloxacin resistance in Streptococcus pneumoniae by the multidrug inhibitor reserpine. Antimicrob. Agents Chemother. 43:988-989.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 988-989
    • Markham, P.N.1
  • 153
    • 0030697879 scopus 로고    scopus 로고
    • The multidrug resistance reversal agent SR33557 and modulation of vinca alkaloid binding to P-glycoprotein by an allosteric interaction
    • Martin, C., G. Berridge, C. F. Higgins, and R. Callaghan. 1997. The multidrug resistance reversal agent SR33557 and modulation of vinca alkaloid binding to P-glycoprotein by an allosteric interaction. Br. J. Pharmacol. 122:765-771.
    • (1997) Br. J. Pharmacol. , vol.122 , pp. 765-771
    • Martin, C.1    Berridge, G.2    Higgins, C.F.3    Callaghan, R.4
  • 155
    • 0033994786 scopus 로고    scopus 로고
    • Assignment of the substrate-selective subunits of the MexEF-OprN multidrug efflux pump of Pseudomonas aeruginosa
    • Maseda, H., H. Yoneyama, and T. Nakae. 2000. Assignment of the substrate-selective subunits of the MexEF-OprN multidrug efflux pump of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 44:658-664.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 658-664
    • Maseda, H.1    Yoneyama, H.2    Nakae, T.3
  • 156
    • 0032462726 scopus 로고    scopus 로고
    • Multidrug resistance following expression of the Escherichia coli marA gene in Mycobacterium smegmatis
    • McDermott, P. F., D. G. White, I. Podglajen, M. N. Aleksun, and S. B. Levy. 1998. Multidrug resistance following expression of the Escherichia coli marA gene in Mycobacterium smegmatis. J. Bacteriol. 180:2992-2998.
    • (1998) J. Bacteriol. , vol.180 , pp. 2992-2998
    • McDermott, P.F.1    White, D.G.2    Podglajen, I.3    Aleksun, M.N.4    Levy, S.B.5
  • 157
    • 0023619948 scopus 로고
    • Loss of OmpC porin in a strain of Salmonella typhimurium causes increased resistance to cephalosporins during therapy
    • Medeiros, A. A., T. F. O'Brien, E. Y. Rosenberg, and H. Nikaido. 1987. Loss of OmpC porin in a strain of Salmonella typhimurium causes increased resistance to cephalosporins during therapy. J. Infect. Dis. 156:751-757.
    • (1987) J. Infect. Dis. , vol.156 , pp. 751-757
    • Medeiros, A.A.1    O'Brien, T.F.2    Rosenberg, E.Y.3    Nikaido, H.4
  • 158
    • 0032994954 scopus 로고    scopus 로고
    • Expression in Escherichia coli of a new efflux pump, MexXY, from Pseudomonas aeruginosa
    • Mine, T., Y. Morita, A. Kataoka, T. Mizushima, and T. Tsuchiya. 1999. Expression in Escherichia coli of a new efflux pump, MexXY, from Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 43:415-417.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 415-417
    • Mine, T.1    Morita, Y.2    Kataoka, A.3    Mizushima, T.4    Tsuchiya, T.5
  • 159
    • 0033524927 scopus 로고    scopus 로고
    • Bioenergetics of the staphylococcal multidrug export protein QacA: Identification of distinct binding sites for monovalent and divalent cations
    • Mitchell, B. A., I. T. Paulsen, M. H. Brown, and R. A. Skurray. 1999. Bioenergetics of the staphylococcal multidrug export protein QacA: identification of distinct binding sites for monovalent and divalent cations. J. Biol. Chem. 274:3541-3548.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3541-3548
    • Mitchell, B.A.1    Paulsen, I.T.2    Brown, M.H.3    Skurray, R.A.4
  • 160
    • 0032063955 scopus 로고    scopus 로고
    • Introduction: Problems with antimicrobial resistance in Gram-positive cocci
    • Moellering, R. C., Jr. 1998. Introduction: problems with antimicrobial resistance in Gram-positive cocci. Clin. Infect. Dis. 16:1177-1178.
    • (1998) Clin. Infect. Dis. , vol.16 , pp. 1177-1178
    • Moellering R.C., Jr.1
  • 162
    • 0026653589 scopus 로고
    • Cloning and characterization of the mvrC gene of Escherichia coli K-12 which confers resistance against methyl viologen toxicity
    • Morimyo, M., E. Hongo, H. Hama-Inaba, and I. Machida. 1992. Cloning and characterization of the mvrC gene of Escherichia coli K-12 which confers resistance against methyl viologen toxicity. Nucleic Acids Res. 20: 3159-3165.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3159-3165
    • Morimyo, M.1    Hongo, E.2    Hama-Inaba, H.3    Machida, I.4
  • 164
    • 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., L. M. Greenberger, E. P. Bruggemann, C. Cardarelli, M. M. Gottesman, I. Pastan, and K. B. Seamon. 1994. Localization of the forskolin labeling sites to both halves of P-glycoprotein: similarity of the sites labeled by forskolin and prazosin. Mol. Pharmacol. 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
  • 165
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • Muth, T. R., and S. Schuldiner. 2000. A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE. EMBO J. 19:232-240.
    • (2000) EMBO J. , vol.19 , pp. 232-240
    • Muth, T.R.1    Schuldiner, S.2
  • 166
    • 0002269404 scopus 로고
    • Gene-controlled resistance to acriflavine and other basic dyes in Escherichia coli
    • Nakamura, H. 1965. Gene-controlled resistance to acriflavine and other basic dyes in Escherichia coli. J. Bacteriol. 90:8-14.
    • (1965) J. Bacteriol. , vol.90 , pp. 8-14
    • Nakamura, H.1
  • 167
    • 0014348023 scopus 로고
    • Genetic determination of resistance to acriflavine, phenethyl alcohol, and sodium dodecyl sulfate in Escherichia coli
    • Nakamura, H. 1968. Genetic determination of resistance to acriflavine, phenethyl alcohol, and sodium dodecyl sulfate in Escherichia coli. J. Bacteriol. 96:987-996.
    • (1968) J. Bacteriol. , vol.96 , pp. 987-996
    • Nakamura, H.1
  • 169
    • 0026760182 scopus 로고
    • The crisis in antibiotic resistance
    • Neu, H. C. 1992. The crisis in antibiotic resistance. Science 257:1064-1073.
    • (1992) Science , vol.257 , pp. 1064-1073
    • Neu, H.C.1
  • 170
    • 0025864903 scopus 로고
    • Efflux-mediated multidrug resistance in Bacillus subtilis: Similarities and dissimilarities with the mammalian system
    • USA
    • Neyfakh, A. A., V. E. Bidnenko, and L. B. Chen. 1991. Efflux-mediated multidrug resistance in Bacillus subtilis: similarities and dissimilarities with the mammalian system. Proc. Natl. Acad. Sci. USA 88:4781-4785.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 4781-4785
    • Neyfakh, A.A.1    Bidnenko, V.E.2    Chen, L.B.3
  • 171
    • 0026569448 scopus 로고
    • The multidrug efflux transporter of Bacillus subtilis is a structural and functional homolog of the Staphylococcus Nora protein
    • Neyfakh, A. A. 1992. The multidrug efflux transporter of Bacillus subtilis is a structural and functional homolog of the Staphylococcus NorA protein. Antimicrob. Agents Chemother. 36:484-485.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 484-485
    • Neyfakh, A.A.1
  • 172
    • 0027514765 scopus 로고
    • Fluoroquinolone resistance protein Nora of Staphylococcus aureus is a multidrug efflux protein
    • Neyfakh, A. A., C. M. Borsch, and G. W. Kaatz. 1993. Fluoroquinolone resistance protein NorA of Staphylococcus aureus is a multidrug efflux protein. Antimicrob. Agents Chemother. 37:128-129.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 128-129
    • Neyfakh, A.A.1    Borsch, C.M.2    Kaatz, G.W.3
  • 173
    • 0030756063 scopus 로고    scopus 로고
    • Natural functions of bacterial multidrug transporters
    • Neyfakh, A. A. 1997. Natural functions of bacterial multidrug transporters. Trends Microbiol. 8:309-313.
    • (1997) Trends Microbiol. , vol.8 , pp. 309-313
    • Neyfakh, A.A.1
  • 174
    • 0028217509 scopus 로고
    • Quinolone resistance mediated by norA: Physiologic characterization and relationship to flqB, a quinolone resistance locus on the Staphylococcus aureus chromosome
    • Ng, E. Y. W., M. Trucksis, and D. C. Hooper. 1994. Quinolone resistance mediated by norA: physiologic characterization and relationship to flqB, a quinolone resistance locus on the Staphylococcus aureus chromosome. Antimicrob. Agents Chemother. 38:1345-1355.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1345-1355
    • Ng, E.Y.W.1    Trucksis, M.2    Hooper, D.C.3
  • 175
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and M. Vaara. 1985. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49:1-32.
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 176
    • 0024467106 scopus 로고
    • Outer membrane barrier as a mechanism of antimicrobial resistance
    • Nikaido, H. 1989. Outer membrane barrier as a mechanism of antimicrobial resistance. Antimicrob. Agents Chemother. 33:1831-1836.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1831-1836
    • Nikaido, H.1
  • 177
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido, H. 1994. Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science 264:382-388.
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 178
    • 0029845913 scopus 로고    scopus 로고
    • Multidrug efflux pumps of gram-negative bacteria
    • Nikaido, H. 1996. Multidrug efflux pumps of gram-negative bacteria. J. Bacteriol. 178:5853-5859.
    • (1996) J. Bacteriol. , vol.178 , pp. 5853-5859
    • Nikaido, H.1
  • 179
    • 0029980852 scopus 로고    scopus 로고
    • Isolation of cmr, a novel Escherichia coli chloramphenicol resistance gene encoding a putative efflux pump
    • Nilsen, I. W., I. Bakke, A. Vader, Ø. Olsvik, and M. R. El-Gewely. 1996. Isolation of cmr, a novel Escherichia coli chloramphenicol resistance gene encoding a putative efflux pump. J. Bacteriol. 178:3188-3193.
    • (1996) J. Bacteriol. , vol.178 , pp. 3188-3193
    • Nilsen, I.W.1    Bakke, I.2    Vader, A.3    Olsvik, Ø.4    El-Gewely, M.R.5
  • 180
    • 0030845301 scopus 로고    scopus 로고
    • Use of fluorescent probes to monitor the subunit proteins of the MexA-MexB-OprM drug extrusion machinery in Pseudomonas aeruginosa
    • Ocaktan, A., H. Yoneyama, and T. Nakae. 1997. Use of fluorescent probes to monitor the subunit proteins of the MexA-MexB-OprM drug extrusion machinery in Pseudomonas aeruginosa. J. Biol. Chem. 272:21964-21969.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21964-21969
    • Ocaktan, A.1    Yoneyama, H.2    Nakae, T.3
  • 181
    • 0031053662 scopus 로고    scopus 로고
    • Bmr3, a third multidrug transporter gene of Bacillus subtilis
    • Ohki, R., and M. Murata. 1997. bmr3, a third multidrug transporter gene of Bacillus subtilis. J. Bacteriol. 179:1423-1427.
    • (1997) J. Bacteriol. , vol.179 , pp. 1423-1427
    • Ohki, R.1    Murata, M.2
  • 182
    • 0030029513 scopus 로고    scopus 로고
    • AcrAB efflux pump plays a major role in the antibiotic resistance phenotype of Escherichia coli multiple antibiotic resistance (Mar) mutants
    • Okusu, H., D. Ma, and H. Nikaido. 1996. AcrAB efflux pump plays a major role in the antibiotic resistance phenotype of Escherichia coli multiple antibiotic resistance (Mar) mutants. J. Bacteriol. 178:306-308.
    • (1996) J. Bacteriol. , vol.178 , pp. 306-308
    • Okusu, H.1    Ma, D.2    Nikaido, H.3
  • 183
    • 0029010093 scopus 로고
    • A second ABC transporter is involved in oleandomycin resistance and its secretion by Streptomyces antibioticus
    • Olano, C., A. M. Rodríguez, C. Méndez, and J. A. Salas. 1995. A second ABC transporter is involved in oleandomycin resistance and its secretion by Streptomyces antibioticus. Mol. Microbiol. 16:333-343.
    • (1995) Mol. Microbiol. , vol.16 , pp. 333-343
    • Olano, C.1    Rodríguez, A.M.2    Méndez, C.3    Salas, J.A.4
  • 184
    • 0025203013 scopus 로고
    • A point mutation in the norA gene is responsible for quinolone resistance in Staphylococcus aureus
    • Oshita, Y., K. Hiramatsu, and T. Yokota. 1990. A point mutation in the norA gene is responsible for quinolone resistance in Staphylococcus aureus. Biochem. Biophys. Res. Commun. 172:1028-1034.
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 1028-1034
    • Oshita, Y.1    Hiramatsu, K.2    Yokota, T.3
  • 185
    • 0028364451 scopus 로고
    • Regulation of the permeability of the gonococcal cell envelope by the mtr system
    • Pan, W., and B. G. Spratt. 1994. Regulation of the permeability of the gonococcal cell envelope by the mtr system. Mol. Microbiol. 11:769-775.
    • (1994) Mol. Microbiol. , vol.11 , pp. 769-775
    • Pan, W.1    Spratt, B.G.2
  • 186
    • 0032528254 scopus 로고    scopus 로고
    • Multidrug resistance transporter P-glycoprotein has distinct but interacting binding sites tor cytotoxic drugs and reversing agents
    • Pascaud, C., M. Garrigos, and S. Orlowski. 1998. Multidrug resistance transporter P-glycoprotein has distinct but interacting binding sites tor cytotoxic drugs and reversing agents. Biochem. J. 333:351-358.
    • (1998) Biochem. J. , vol.333 , pp. 351-358
    • Pascaud, C.1    Garrigos, M.2    Orlowski, S.3
  • 188
    • 0027408932 scopus 로고
    • Topology, structure and evolution of two families of proteins involved in antibiotic and antiseptic resistance in eukaryotes and prokaryotes - An analysis
    • Paulsen, I. T., and R. A. Skurray. 1993. Topology, structure and evolution of two families of proteins involved in antibiotic and antiseptic resistance in eukaryotes and prokaryotes - an analysis. Gene 124:1-11.
    • (1993) Gene , vol.124 , pp. 1-11
    • Paulsen, I.T.1    Skurray, R.A.2
  • 189
    • 0029034869 scopus 로고
    • Molecular characterization of the staphylococcal multidrug resistance export protein QacC
    • Paulsen, I. T., M. H. Brown, S. J. Dunstan, and R. A. Skurray. 1995. Molecular characterization of the staphylococcal multidrug resistance export protein QacC. J. Bacteriol. 177:2827-2833.
    • (1995) J. Bacteriol. , vol.177 , pp. 2827-2833
    • Paulsen, I.T.1    Brown, M.H.2    Dunstan, S.J.3    Skurray, R.A.4
  • 190
  • 192
    • 0029872148 scopus 로고    scopus 로고
    • Multidrug resistance proteins QacA and QacB from Staphylococcus aureus: Membrane topology and identification of residues involved in substrate specificity
    • USA
    • Paulsen, I. T., M. H. Brown, T. G. Littlejohn, B. A. Mitchell, and R. A. Skurray. 1996c. Multidrug resistance proteins QacA and QacB from Staphylococcus aureus: membrane topology and identification of residues involved in substrate specificity. Proc. Natl. Acad. Sci. USA 93:3630-3635.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 3630-3635
    • Paulsen, I.T.1    Brown, M.H.2    Littlejohn, T.G.3    Mitchell, B.A.4    Skurray, R.A.5
  • 193
    • 0031749891 scopus 로고    scopus 로고
    • Characterization of the earliest known Staphylococcus aureus plasmid encoding a multidrug efflux system
    • Paulsen, I. T., M. H. Brown, and R. A. Skurray. 1998. Characterization of the earliest known Staphylococcus aureus plasmid encoding a multidrug efflux system. J. Bacteriol. 180:3477-3479.
    • (1998) J. Bacteriol. , vol.180 , pp. 3477-3479
    • Paulsen, I.T.1    Brown, M.H.2    Skurray, R.A.3
  • 194
    • 0032478498 scopus 로고    scopus 로고
    • Microbial genome analyses: Global comparisons of transport capabilities based on phytogenies, bioenergetics and substrate specificities
    • Paulsen, I. T., M. K. Sliwinski, and M. H. Saier, Jr. 1998. Microbial genome analyses: global comparisons of transport capabilities based on phytogenies, bioenergetics and substrate specificities. J. Mol. Biol. 277:573-592.
    • (1998) J. Mol. Biol. , vol.277 , pp. 573-592
    • Paulsen, I.T.1    Sliwinski, M.K.2    Saier, M.H.3    Jr4
  • 195
    • 0028097634 scopus 로고
    • Transmembrane aromatic amino acid distribution in P-glycoprotein: A functional role in broad substrate specificity
    • Pawagi, A. B., J. Wang, M. Silverman, R. A. F. Reithmeier, and C. M. Deber. 1994. Transmembrane aromatic amino acid distribution in P-glycoprotein: a functional role in broad substrate specificity. J. Mol. Biol. 235: 554-564.
    • (1994) J. Mol. Biol. , vol.235 , pp. 554-564
    • Pawagi, A.B.1    Wang, J.2    Silverman, M.3    Reithmeier, R.A.F.4    Deber, C.M.5
  • 196
    • 0027952904 scopus 로고
    • Non-competitive inhibition of P-glycoprotein-associated efflux of THP-adriamycin by verapamil in living K562 leukemia cells
    • Pereira, E., M. N. Borrel, M. Fiallo, and A. Garnier-Suillerot. 1994. Non-competitive inhibition of P-glycoprotein-associated efflux of THP-adriamycin by verapamil in living K562 leukemia cells. Biochim. Biophys. Acta 1225:209-216.
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 209-216
    • Pereira, E.1    Borrel, M.N.2    Fiallo, M.3    Garnier-Suillerot, A.4
  • 197
    • 0029132858 scopus 로고
    • Bacillus licheniformis bacitracin-resistance ABC transporter: Relationship to mammalian multidrug resistance
    • Podlesek, Z., A. Comino, B. Herzog-Velikonja, D. Zgur-Bertok, R. Komel, and M. Grabnar. 1995. Bacillus licheniformis bacitracin-resistance ABC transporter: relationship to mammalian multidrug resistance. Mol. Microbiol. 16:969-976.
    • (1995) Mol. Microbiol. , vol.16 , pp. 969-976
    • Podlesek, Z.1    Comino, A.2    Herzog-Velikonja, B.3    Zgur-Bertok, D.4    Komel, R.5    Grabnar, M.6
  • 198
    • 0027367171 scopus 로고
    • Cloning and sequence analysis of an EnvCD homologue in Pseudomonas aeruginosa: Regulation by iron and possible involvement in the secretion of the siderophore pyoverdine
    • Poole, K., D. E. Heinrichs, and S. Neshat. 1993. Cloning and sequence analysis of an EnvCD homologue in Pseudomonas aeruginosa: regulation by iron and possible involvement in the secretion of the siderophore pyoverdine. Mol. Microbiol. 10:529-544.
    • (1993) Mol. Microbiol. , vol.10 , pp. 529-544
    • Poole, K.1    Heinrichs, D.E.2    Neshat, S.3
  • 199
    • 0027494050 scopus 로고
    • Multiple antibiotic resistance in Pseudomonas aeruginosa: Evidence for involvement of an efflux operon
    • Poole, K., K. Krebes, C. McNally, and S. Neshat. 1993. Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for involvement of an efflux operon. J. Bacteriol. 175:7363-7372.
    • (1993) J. Bacteriol. , vol.175 , pp. 7363-7372
    • Poole, K.1    Krebes, K.2    McNally, C.3    Neshat, S.4
  • 201
    • 0029815432 scopus 로고    scopus 로고
    • Expression of the multidrug resistance operon mexA-mexB-oprM in Pseudomonas aeruginosa: MexR encodes a regulator of operon expression
    • Poole, K., K. Tetro, Q. Zhao, S. Neshat, D. E. Heinrichs, and N. Bianco. 1996. Expression of the multidrug resistance operon mexA-mexB-oprM in Pseudomonas aeruginosa: mexR encodes a regulator of operon expression. Antimicrob. Agents Chemother. 40:2021-2028.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 2021-2028
    • Poole, K.1    Tetro, K.2    Zhao, Q.3    Neshat, S.4    Heinrichs, D.E.5    Bianco, N.6
  • 202
    • 0025916414 scopus 로고
    • Nucleotide sequence of the ethidium efflux gene from Escherichia coli
    • Purewal., A. S. 1991. Nucleotide sequence of the ethidium efflux gene from Escherichia coli. FEMS Microbiol. Lett. 82:229-232.
    • (1991) FEMS Microbiol. Lett. , vol.82 , pp. 229-232
    • Purewal, A.S.1
  • 203
    • 0033579808 scopus 로고    scopus 로고
    • Restrictive use of detergents in the functional reconstitution of the secondary multidrug transporter LmrP
    • Putman, M., H. W. van Veen, B. Poolman, and W. N. Konings. 1999. Restrictive use of detergents in the functional reconstitution of the secondary multidrug transporter LmrP. Biochemistry 38:1002-1008.
    • (1999) Biochemistry , vol.38 , pp. 1002-1008
    • Putman, M.1    Van Veen, H.W.2    Poolman, B.3    Konings, W.N.4
  • 204
    • 0345035518 scopus 로고    scopus 로고
    • The secondary multidrug transporter LmrP contains multiple drug interaction sites
    • Putman, M., L. A. Koole, H. W. van Veen, and W. N. Konings. 1999. The secondary multidrug transporter LmrP contains multiple drug interaction sites. Biochemistry 38:13900-13905.
    • (1999) Biochemistry , vol.38 , pp. 13900-13905
    • Putman, M.1    Koole, L.A.2    Van Veen, H.W.3    Konings, W.N.4
  • 207
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Raviv, Y., H. B. Pollard, E. P. Bruggemann, I. Pastan, and M. M. Gottesman. 1990. Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells. J. Biol. Chem. 265:3975-3980.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3975-3980
    • Raviv, Y.1    Pollard, H.B.2    Bruggemann, E.P.3    Pastan, I.4    Gottesman, M.M.5
  • 208
    • 0014252498 scopus 로고
    • Chromosomal location of a mutation causing chloramphenicol resistance in Escherichia coli K 12
    • Reeve, E. C., and D. R. Suttie. 1968. Chromosomal location of a mutation causing chloramphenicol resistance in Escherichia coli K 12. Genet. Res. 11:97-104.
    • (1968) Genet. Res. , vol.11 , pp. 97-104
    • Reeve, E.C.1    Suttie, D.R.2
  • 209
    • 0030273002 scopus 로고    scopus 로고
    • Tetracycline resistance determinants: Mechanisms of action, regulation of expression, genetic mobility, and distribution
    • Roberts, M. C. 1996. Tetracycline resistance determinants: mechanisms of action, regulation of expression, genetic mobility, and distribution. FEMS Microbiol. Rev. 19:1-24.
    • (1996) FEMS Microbiol. Rev. , vol.19 , pp. 1-24
    • Roberts, M.C.1
  • 210
    • 0027214965 scopus 로고
    • Streptomyces antibioticus contains at least three oleandomycin-resistance determinants, one of which shows similarity with proteins of the ABC-transporter superfamily
    • Rodríguez, A. M., C. Olano, C. Vilches, C. Méndez, and J. A. Salas. 1993. Streptomyces antibioticus contains at least three oleandomycin-resistance determinants, one of which shows similarity with proteins of the ABC-transporter superfamily. Mol. Microbiol. 8:571-582.
    • (1993) Mol. Microbiol. , vol.8 , pp. 571-582
    • Rodríguez, A.M.1    Olano, C.2    Vilches, C.3    Méndez, C.4    Salas, J.A.5
  • 211
    • 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., R. Callaghan, R. C. Ford, and C. F. Higgins. 1997. Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J. Biol. Chem. 272:10685-10694.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10685-10694
    • Rosenberg, M.F.1    Callaghan, R.2    Ford, R.C.3    Higgins, C.F.4
  • 212
    • 0025456967 scopus 로고
    • Inducible erythromycin resistance in staphylococci is encoded by a member of the ATP-binding transport super-gene family
    • Ross, J. I., E. A. Eady, J. H. Cove, W. J. Cunliffe, S. Baumberg, and J. C. Wootton. 1990. Inducible erythromycin resistance in staphylococci is encoded by a member of the ATP-binding transport super-gene family. Mol. Microbiol. 4:1207-1214.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1207-1214
    • Ross, J.I.1    Eady, E.A.2    Cove, J.H.3    Cunliffe, W.J.4    Baumberg, S.5    Wootton, J.C.6
  • 213
    • 0025695158 scopus 로고
    • Efflux-mediated antiseptic resistance gene qacA from Staphylococcus aureus: Common ancestry with tetracycline- And sugar-transport proteins
    • Rouch, D. A., D. S. Cram, D. DiBerardino, T. G. Littlejohn, and R. A. Skurray. 1990. Efflux-mediated antiseptic resistance gene qacA from Staphylococcus aureus: common ancestry with tetracycline- and sugar-transport proteins. Mol. Microbiol. 4:2051-2062.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2051-2062
    • Rouch, D.A.1    Cram, D.S.2    Diberardino, D.3    Littlejohn, T.G.4    Skurray, R.A.5
  • 214
    • 0032767010 scopus 로고    scopus 로고
    • Induction of the mrrCDE-encoded efflux pump system of Neisseria gonorrhoeae requires MtrA, an AraC-like protein
    • Rouquette, C., J. B. Harmon, and W. F. Shafer. 1999. Induction of the mrrCDE-encoded efflux pump system of Neisseria gonorrhoeae requires MtrA, an AraC-like protein. Mol. Microbiol. 33:651-658.
    • (1999) Mol. Microbiol. , vol.33 , pp. 651-658
    • Rouquette, C.1    Harmon, J.B.2    Shafer, W.F.3
  • 215
    • 0025269098 scopus 로고
    • Gene duplication in the evolution of the two complementing domains of Gramnegative bacterial tetracyclin efflux proteins
    • Rubin, R. A., S. B. Levy, R. L. Heinrikson, and F. J. Kétzy. 1990. Gene duplication in the evolution of the two complementing domains of Gramnegative bacterial tetracyclin efflux proteins. Gene 87:7-13.
    • (1990) Gene , vol.87 , pp. 7-13
    • Rubin, R.A.1    Levy, S.B.2    Heinrikson, R.L.3    Kétzy, F.J.4
  • 216
    • 0028365952 scopus 로고
    • Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport
    • Saier, M. H., Jr., R. Tam, A. Reizer, and J. Reizer. 1994. Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Mol. Microbiol. 11:841-847.
    • (1994) Mol. Microbiol. , vol.11 , pp. 841-847
    • Saier M.H., Jr.1    Tam, R.2    Reizer, A.3    Reizer, J.4
  • 218
  • 220
    • 0030663047 scopus 로고    scopus 로고
    • The acrAB homolog of Haemophilus influenzae codes for a functional multidrug efflux pump
    • Sánchez, L., W. Pan, M. Viñas, and H. Nikaido. 1997. The acrAB homolog of Haemophilus influenzae codes for a functional multidrug efflux pump. J. Bacteriol. 179:6855-6857.
    • (1997) J. Bacteriol. , vol.179 , pp. 6855-6857
    • Sánchez, L.1    Pan, W.2    Viñas, M.3    Nikaido, H.4
  • 221
    • 0024804865 scopus 로고
    • Nucleotide sequence of a gene that encodes resistance to ethidium bromide from a transferable plasmid in Staphylococcus aureus
    • Sasatsu, M., K. Shima, Y. Shibata, and M. Kono. 1989. Nucleotide sequence of a gene that encodes resistance to ethidium bromide from a transferable plasmid in Staphylococcus aureus. Nucleic Acids Res. 17:10103.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10103
    • Sasatsu, M.1    Shima, K.2    Shibata, Y.3    Kono, M.4
  • 223
    • 0029559159 scopus 로고
    • The catalytic cycle of P-glycoprotein
    • Senior, A. E., M. Al-Shawi, and I. L. Urbatsch. 1995. The catalytic cycle of P-glycoprotein. FEBS Lett. 377:285-289.
    • (1995) FEBS Lett. , vol.377 , pp. 285-289
    • Senior, A.E.1    Al-Shawi, M.2    Urbatsch, I.L.3
  • 224
    • 0032548468 scopus 로고    scopus 로고
    • P-glycoprotein shows strong catalytic cooperativity between the two nucleotide sites
    • Senior, A. E., and S. Bhagat. 1998. P-glycoprotein shows strong catalytic cooperativity between the two nucleotide sites. Biochemistry 37:831-836.
    • (1998) Biochemistry , vol.37 , pp. 831-836
    • Senior, A.E.1    Bhagat, S.2
  • 225
    • 0029025536 scopus 로고
    • Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli
    • Seoane, A. S., and S. B. Levy. 1995. Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli. J. Bacteriol. 177:3414-3419.
    • (1995) J. Bacteriol. , vol.177 , pp. 3414-3419
    • Seoane, A.S.1    Levy, S.B.2
  • 226
    • 0028961635 scopus 로고
    • Identification of new genes regulated by the marRAB operon in Escherichia coli
    • Seoane, A. S., and S. B. Levy. 1995. Identification of new genes regulated by the marRAB operon in Escherichia coli. J. Bacteriol. 177:530-535.
    • (1995) J. Bacteriol. , vol.177 , pp. 530-535
    • Seoane, A.S.1    Levy, S.B.2
  • 227
    • 0029061103 scopus 로고
    • Reconstitution of drug transport by purified P-glycoprotein
    • Shapiro, A. B., and V. Ling. 1995. Reconstitution of drug transport by purified P-glycoprotein. J. Biol. Chem. 270:16167-16175.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16167-16175
    • Shapiro, A.B.1    Ling, V.2
  • 228
    • 0030822996 scopus 로고    scopus 로고
    • P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer
    • Shapiro, A. B., A. B. Corder, and V. Ling. 1997. P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer. Eur. J. Biochem 250:115-121.
    • (1997) Eur. J. Biochem , vol.250 , pp. 115-121
    • Shapiro, A.B.1    Corder, A.B.2    Ling, V.3
  • 229
    • 0030784559 scopus 로고    scopus 로고
    • Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membrane by P-glycoprotein
    • Shapiro, A. B., and V. Ling. 1997. Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membrane by P-glycoprotein. Eur. J. Biochem. 250:122-129.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 122-129
    • Shapiro, A.B.1    Ling, V.2
  • 230
    • 0030782511 scopus 로고    scopus 로고
    • Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities
    • Shapiro, A. B., and V. Ling. 1997. Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities. Eur. J. Biochem 250:130-137.
    • (1997) Eur. J. Biochem , vol.250 , pp. 130-137
    • Shapiro, A.B.1    Ling, V.2
  • 231
    • 0032523929 scopus 로고    scopus 로고
    • Transport of LDS-751 from the cytoplasmic leaflet of the plasma membrane by the rhodamine-123-selective site of P-glycoprotein
    • Shapiro, A. B., and V. Ling. 1998. Transport of LDS-751 from the cytoplasmic leaflet of the plasma membrane by the rhodamine-123-selective site of P-glycoprotein. Eur. J. Biochem. 254:181-188.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 181-188
    • Shapiro, A.B.1    Ling, V.2
  • 232
    • 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., K. Fox, P. Lam, and V. Ling. 1999. Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone: evidence for a third drug-binding site. Eur. J. Biochem. 259:841-850.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 841-850
    • Shapiro, A.B.1    Fox, K.2    Lam, P.3    Ling, V.4
  • 233
    • 0028920219 scopus 로고
    • Interaction of the P-glycoprotein multidrug transporter with peptides and ionophores
    • Sharotn, F. J., G. DiDiodato, X. Yu, and K. J. D. Ashbourne. 1995. Interaction of the P-glycoprotein multidrug transporter with peptides and ionophores. J. Biol. Chem. 270:10334-10341.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10334-10341
    • Sharotn, F.J.1    Didiodato, G.2    Yu, X.3    Ashbourne, K.J.D.4
  • 234
    • 0027478123 scopus 로고
    • Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes
    • Shaw, K. J., P. N. Rather, R. S. Hare, and G. H. Miller. 1993. Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes. Microbiol. Rev. 57:138-163.
    • (1993) Microbiol. Rev. , vol.57 , pp. 138-163
    • Shaw, K.J.1    Rather, P.N.2    Hare, R.S.3    Miller, G.H.4
  • 235
    • 0027419803 scopus 로고
    • A novel binding protein of the origin of the Escherichia coli chromosome
    • Skarstad, K., B. Thöny, D. Hwang, and A. Kornberg. 1993. A novel binding protein of the origin of the Escherichia coli chromosome. J. Biol. Chem 268:5365-5370.
    • (1993) J. Biol. Chem , vol.268 , pp. 5365-5370
    • Skarstad, K.1    Thöny, B.2    Hwang, D.3    Kornberg, A.4
  • 237
    • 0026768854 scopus 로고
    • Bacterial resistance to tetracycline: Mechanisms, transfer, and clinical significance
    • Speer, B. S., N. B. Shoemaker, and A. A. Salyers. 1992. Bacterial resistance to tetracycline: mechanisms, transfer, and clinical significance. Clin. Microbiol. Rev. 5:387-399.
    • (1992) Clin. Microbiol. Rev. , vol.5 , pp. 387-399
    • Speer, B.S.1    Shoemaker, N.B.2    Salyers, A.A.3
  • 238
    • 0028264893 scopus 로고
    • The multidrug-resistance-reverser verapamil interferes with cellular P-glycoprotein-mediated pumping of daunomycin as a non-competitive substrate
    • Spoelstra, E. C., H. V. Westerhoff, H. M. Pinedo, H. Dekker, and J. Lankelma. 1994. The multidrug-resistance-reverser verapamil interferes with cellular P-glycoprotein-mediated pumping of daunomycin as a non-competitive substrate. Eur. J. Biochem. 221:363-373.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 363-373
    • Spoelstra, E.C.1    Westerhoff, H.V.2    Pinedo, H.M.3    Dekker, H.4    Lankelma, J.5
  • 239
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • Spratt, B. G. 1994. Resistance to antibiotics mediated by target alterations. Science 264:388-393.
    • (1994) Science , vol.264 , pp. 388-393
    • Spratt, B.G.1
  • 240
    • 0030735455 scopus 로고    scopus 로고
    • Inner membrane efflux components are responsible for β-lactam specificity of multidrug efflux pumps in Pseudomonas aeruginosa
    • Srikumar, R., X.-Z. Li, and K. Poole. 1997. Inner membrane efflux components are responsible for β-lactam specificity of multidrug efflux pumps in Pseudomonas aeruginosa. J. Bacteriol. 179:7875-7881.
    • (1997) J. Bacteriol. , vol.179 , pp. 7875-7881
    • Srikumar, R.1    Li, X.-Z.2    Poole, K.3
  • 241
    • 0031962577 scopus 로고    scopus 로고
    • Expression of Pseudomonas aeruinosa multidrug efflux pumps MexA-MexB-OprM and McxC-MexD-OprJ in a multidrug-sensitive Escherichia coli strain
    • Srikumar, R., T. Kon, N. Gotoh, and K. Poole. 1998. Expression of Pseudomonas aeruinosa multidrug efflux pumps MexA-MexB-OprM and McxC-MexD-OprJ in a multidrug-sensitive Escherichia coli strain. Antimicrob. Agents Chemother. 42:65-71.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 65-71
    • Srikumar, R.1    Kon, T.2    Gotoh, N.3    Poole, K.4
  • 243
    • 0029950955 scopus 로고    scopus 로고
    • NorA plasmid resistance to fluoroquinolones: Role of copy number and norA frameshift mutations
    • Sun, L., S. Sreedharan, K. Plummer, and L. M. Fisher. 1996. NorA plasmid resistance to fluoroquinolones: role of copy number and norA frameshift mutations. Antimicrob. Agents Chemother. 40:1665-1669.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 1665-1669
    • Sun, L.1    Sreedharan, S.2    Plummer, K.3    Fisher, L.M.4
  • 245
    • 0025991731 scopus 로고
    • Azidopine noncompetitively interacts with vinblastine and cyclosporin a binding to P-glycoprotein in multidrug-resistant cells
    • Tamai, I. and A. R. Safa. 1991. Azidopine noncompetitively interacts with vinblastine and cyclosporin A binding to P-glycoprotein in multidrug-resistant cells. J. Biol. Chem. 266:16796-16800.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16796-16800
    • Tamai, I.1    Safa, A.R.2
  • 247
    • 0028270396 scopus 로고
    • Location of a potassium tellurite resistance operon (teha tehB) within the terminus of Escherichia coli K-12
    • Taylor, D. E., Y. Hou, R. J. Turner, and J. H. Weiner. 1994. Location of a potassium tellurite resistance operon (tehA tehB) within the terminus of Escherichia coli K-12. J. Bacteriol. 166:2740-2742.
    • (1994) J. Bacteriol. , vol.166 , pp. 2740-2742
    • Taylor, D.E.1    Hou, Y.2    Turner, R.J.3    Weiner, J.H.4
  • 248
    • 0024552014 scopus 로고
    • Physical and biochemical characterization of the qacA gene encoding antiseptic and disinfectant resistance in Staphylococcus aureus
    • Tennent, J. M., B. R. Lyon, M. Midgley, G. Jones, A. S. Purewal, and R. A. Skurray. 1989. Physical and biochemical characterization of the qacA gene encoding antiseptic and disinfectant resistance in Staphylococcus aureus. J. Gen. Microbiol. 135:1-10.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1-10
    • Tennent, J.M.1    Lyon, B.R.2    Midgley, M.3    Jones, G.4    Purewal, A.S.5    Skurray, R.A.6
  • 249
    • 0030934759 scopus 로고    scopus 로고
    • Active efflux of bile salts by Escherichia coli
    • Thanassi, D. G., L. W. Cheng, and H. Nikaido. 1997. Active efflux of bile salts by Escherichia coli. J. Bacteriol. 179:2512-2518.
    • (1997) J. Bacteriol. , vol.179 , pp. 2512-2518
    • Thanassi, D.G.1    Cheng, L.W.2    Nikaido, H.3
  • 250
    • 0031053884 scopus 로고    scopus 로고
    • Expression of Escherichia coli TehA gives resistance to antiseptics and disinfectants similar to that conferred by multidrug efflux pumps
    • Turner, R. J., D. E. Taylor, and J. H. Weiner. 1997. Expression of Escherichia coli TehA gives resistance to antiseptics and disinfectants similar to that conferred by multidrug efflux pumps. Antimicrob. Agents Chemother. 41:440-444.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 440-444
    • Turner, R.J.1    Taylor, D.E.2    Weiner, J.H.3
  • 251
    • 0024435169 scopus 로고
    • Cloning and expression of the norA gene for fluoroquinolone resistance in Staphylococcus aureus
    • Ubukata, K., N.-Y. Itoh, and M. Konno. 1989. Cloning and expression of the norA gene for fluoroquinolone resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 33:1535-1539.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1535-1539
    • Ubukata, K.1    Itoh, N.-Y.2    Konno, M.3
  • 252
    • 0031156390 scopus 로고    scopus 로고
    • How does P-glycoprotein recognize its substrates? Semin
    • Ueda, K., Y. Taguchi, and M. Morishima. 1997. How does P-glycoprotein recognize its substrates? Semin. Cancer Biol. 8:151-159.
    • (1997) Cancer Biol. , vol.8 , pp. 151-159
    • Ueda, K.1    Taguchi, Y.2    Morishima, M.3
  • 253
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch, I. L., B. Sankaran, J. Weber, and A. E. Senior. 1995. P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J. Biol. Chem. 270:19383-19390.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 254
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch, I. L., B. Sankaran, S. Bhagat, and A. E. Senior. 1995. Both P-glycoprotein nucleotide-binding sites are catalytically active. J. Biol. Chem. 270:26956-26961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 255
    • 0007544439 scopus 로고    scopus 로고
    • MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine
    • A. H., P. Borst
    • 254a.van Helvoort, A., A. J. Smith, H. Sprang, I. Fritzsche, A. H. Schinkel, A. H., P. Borst, and G. Vermeer. 1996. MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. Cell 87:507-517.
    • (1996) Cell , vol.87 , pp. 507-517
    • Van Helvoort, A.1    Smith, A.J.2    Sprang, H.3    Fritzsche, I.4    Schinkel, A.H.5    Vermeer, G.6
  • 256
    • 0031160937 scopus 로고    scopus 로고
    • Multidrug transporters from bacteria to man: Similarities in structure and function
    • van Veen, H. W., and W. N. Konings. 1997. Multidrug transporters from bacteria to man: similarities in structure and function. Semin. Cancer Biol. 8:183-191.
    • (1997) Semin. Cancer Biol. , vol.8 , pp. 183-191
    • Van Veen, H.W.1    Konings, W.N.2
  • 258
    • 0032518394 scopus 로고    scopus 로고
    • A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene
    • van Veen, H. W., R. Callaghan, L. Soceneantu, A. Sardini, W. N. Konings, and C. F. Higgins. 1998. A bacterial antibiotic-resistance gene that complements the human multidrug-resistance P-glycoprotein gene. Nature 391: 291-295.
    • (1998) Nature , vol.391 , 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
  • 259
    • 0034212332 scopus 로고    scopus 로고
    • The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
    • van Veen, H. W., A. Margolles, M. Müller, C. F. Higgins, and W. N. Konings. 2000. The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism. EMBO J. 19:2503-2514.
    • (2000) EMBO J. , vol.19 , pp. 2503-2514
    • Van Veen, H.W.1    Margolles, A.2    Müller, M.3    Higgins, C.F.4    Konings, W.N.5
  • 260
    • 0032321699 scopus 로고    scopus 로고
    • The ABC family of multidrug transporters in microorganisms
    • van Veen, H. W., and W. N. Konings. 1998. The ABC family of multidrug transporters in microorganisms. Biochim. Biophys. Acta 1365:31-36.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 31-36
    • Van Veen, H.W.1    Konings, W.N.2
  • 261
    • 0029382408 scopus 로고
    • Mutational analysis and molecular modelling of an amino acid sequence motif conserved in antiporters but not symporters in a transporter superfamily
    • Varela, M. F., C. E. Sansom, and J. K. Griffith. 1995. Mutational analysis and molecular modelling of an amino acid sequence motif conserved in antiporters but not symporters in a transporter superfamily. Mol. Membr. Biol. 12:313151-159.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 313151-313159
    • Varela, M.F.1    Sansom, C.E.2    Griffith, J.K.3
  • 263
    • 0034646645 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted Lmra induced by nucleotide binding or hydrolysis; a Fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis
    • Vigano, C., A. Margolles, H. W. van Veen, W. N. Konings, and J.-M. Ruysschaert. 2000. Secondary and tertiary structure changes of reconstituted LmrA induced by nucleotide binding or hydrolysis; a Fourier transform attenuated total reflection infrared spectroscopy and tryptophan fluorescence quenching analysis. J. Biol. Chem. 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
  • 264
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- And β-subunits of ATP synthase, myosin, kinases and other ATP requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 265
    • 0032528075 scopus 로고    scopus 로고
    • Dissection of drug-binding-induced conformational changes in P-glycoprotein
    • Wang, G., R. Pincheira, and J.-T. Zhang. 1998. Dissection of drug-binding-induced conformational changes in P-glycoprotein. Eur. J. Biochem. 255: 383-390.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 383-390
    • Wang, G.1    Pincheira, R.2    Zhang, J.-T.3
  • 266
    • 0028963496 scopus 로고
    • Erythromycin resistance by ribosome modification
    • Weisblum, B. 1995. Erythromycin resistance by ribosome modification. Antimicrob. Agents Chemother. 39:577-585.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 577-585
    • Weisblum, B.1
  • 267
    • 0030983818 scopus 로고    scopus 로고
    • Role of the acrAB locus in organic solvent tolerance mediated by expression of marA, saxS, or robA in Escherichia coli
    • White, D. G., J. D. Goldman, B. Demple, and S. B. Levy. 1997. Role of the acrAB locus in organic solvent tolerance mediated by expression of marA, saxS, or robA in Escherichia coli. J. Bacteriol. 179:6122-6126.
    • (1997) J. Bacteriol. , vol.179 , pp. 6122-6126
    • White, D.G.1    Goldman, J.D.2    Demple, B.3    Levy, S.B.4
  • 268
    • 0032549098 scopus 로고    scopus 로고
    • Containment of antibiotic resistance
    • Williams, R. J., and D. L. Heymann. 1998. Containment of antibiotic resistance. Science 279:1153-1154.
    • (1998) Science , vol.279 , pp. 1153-1154
    • Williams, R.J.1    Heymann, D.L.2
  • 270
    • 0030910587 scopus 로고    scopus 로고
    • Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Bit
    • Woolridge, D. P., N. Vasquez-Laslop, P. N. Markham, M. S. Chevalier, E. W. Gerner, and A. A. Neyfakh. 1997. Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Bit. J. Biol. Chem. 272:8864-8866.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8864-8866
    • Woolridge, D.P.1    Vasquez-Laslop, N.2    Markham, P.N.3    Chevalier, M.S.4    Gerner, E.W.5    Neyfakh, A.A.6
  • 271
    • 0025809949 scopus 로고
    • Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli
    • Wu, J., and B. Weiss. 1991. Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli. J. Bacteriol. 173:2864-2871.
    • (1991) J. Bacteriol. , vol.173 , pp. 2864-2871
    • Wu, J.1    Weiss, B.2
  • 274
    • 0026657365 scopus 로고
    • + antiporter encoded by transposon Tn10 of Escherichia coli
    • + antiporter encoded by transposon Tn10 of Escherichia coli. Biochemistry 31:8344-8348.
    • (1992) Biochemistry , vol.31 , pp. 8344-8348
    • Yamaguchi, A.1    Nakatani, M.2    Sawai, T.3
  • 275
    • 0027460297 scopus 로고
    • + antiporter of Escherichia coli encoded by transposon Tn10: The structural resemblance and functional difference in the role of the duplicated sequence motif between hydrophobic segments 2 and 3 and segments 8 and 9
    • + antiporter of Escherichia coli encoded by transposon Tn10: the structural resemblance and functional difference in the role of the duplicated sequence motif between hydrophobic segments 2 and 3 and segments 8 and 9. J. Biol. Chem. 268:6496-6504.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6496-6504
    • Yamaguchi, A.1    Kimura, T.2    Someya, Y.3    Sawai, T.4
  • 277
    • 0029856981 scopus 로고    scopus 로고
    • Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli
    • Yerushalmi, H., M. Lebendiker, and S. Schuldiner. 1996. Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli. J. Biol. Chem. 271:31044-31048.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31044-31048
    • Yerushalmi, H.1    Lebendiker, M.2    Schuldiner, S.3
  • 278
    • 0025282176 scopus 로고
    • Quinolone resistance-determining region in the DNA gyrase gyrA gene of Escherichia coli
    • Yoshida, H., M. Bogaki, M. Nakamura, and S. Nakamura. 1990. Quinolone resistance-determining region in the DNA gyrase gyrA gene of Escherichia coli. Antimicrob. Agents Chemother. 34:1271-1272.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 1271-1272
    • Yoshida, H.1    Bogaki, M.2    Nakamura, M.3    Nakamura, S.4
  • 279
    • 0025688065 scopus 로고
    • Nucleotide sequence and characterization of the Staphylococcus aureus norA gene, which confers resistance to quinolones
    • Yoshida, H., M. Bogaki, S. Nakamura, K. Ubukata, and M. Konno. 1990. Nucleotide sequence and characterization of the Staphylococcus aureus norA gene, which confers resistance to quinolones. J. Bacteriol. 172:6942-6949.
    • (1990) J. Bacteriol. , vol.172 , pp. 6942-6949
    • Yoshida, H.1    Bogaki, M.2    Nakamura, S.3    Ubukata, K.4    Konno, M.5
  • 280
    • 0030805166 scopus 로고    scopus 로고
    • Active efflux as a mechanism of resistance to ciprofloxacin in Streptococcus pneumoniae
    • Zeller, V., C. Janoir, M. Kitzis, L. Gutmann, and N. J. Moreau. 1997. Active efflux as a mechanism of resistance to ciprofloxacin in Streptococcus pneumoniae. Antimicrob. Agents Chemother. 41:1973-1978.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1973-1978
    • Zeller, V.1    Janoir, C.2    Kitzis, M.3    Gutmann, L.4    Moreau, N.J.5
  • 281
    • 0033594886 scopus 로고    scopus 로고
    • Bypassing the periplasm: Reconstitution of the AcrAB multidrug efflux pump of Escherichia coli
    • USA
    • Zgurskaya, H. I., and H. Nikaido. 1999. Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli. Proc. Natl. Acad. Sci. USA 96:7190-7195.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 7190-7195
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 282
    • 0033534373 scopus 로고    scopus 로고
    • Acra is a highly asymmetric protein capable of spanning the periplasm
    • Zgurskaya, H. I., and H. Nikaido. 1999. AcrA is a highly asymmetric protein capable of spanning the periplasm. J. Mol. Biol. 285:409-420.
    • (1999) J. Mol. Biol. , vol.285 , pp. 409-420
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 283
    • 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., K. I. Collins, and L. M. Greenberger. 1995. 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. 270:5441-5448.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5441-5448
    • Zhang, X.1    Collins, K.I.2    Greenberger, L.M.3
  • 284
    • 0031835556 scopus 로고    scopus 로고
    • Contribution of outer membrane protein OprM to antibiotic resistance in Pseudomonas aeruginosa independent of MexAB
    • Zhao, Q., X.-Z. Li, R. Srikumar, and K. Poole. 1998. Contribution of outer membrane protein OprM to antibiotic resistance in Pseudomonas aeruginosa independent of MexAB. Antimicrob. Agents Chemother. 42:1682-1688.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1682-1688
    • Zhao, Q.1    Li, X.-Z.2    Srikumar, R.3    Poole, K.4
  • 285
    • 0033525105 scopus 로고    scopus 로고
    • Structural basis of multidrug recognition by BmrR, a transcriptional activator of a multidrug transporter
    • Zheleznova, E. E., P. N. Markham, A. A. Neyfakh, and R. G. Brennan. 1999. Structural basis of multidrug recognition by BmrR, a transcriptional activator of a multidrug transporter. Cell 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
  • 286
    • 0032524302 scopus 로고    scopus 로고
    • Function of Escherichia coli MsbA, an essential ABC transporter, in lipid a and phospholipid biosynthesis
    • Zhou, Z., K. A. White, A. Polissi, C. Georgopoulos, and C. R. H. Raetz. 1998. Function of Escherichia coli MsbA, an essential ABC transporter, in lipid A and phospholipid biosynthesis. J. Biol. Chem. 273:12466-12475.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12466-12475
    • Zhou, Z.1    White, K.A.2    Polissi, A.3    Georgopoulos, C.4    Raetz, C.R.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.