메뉴 건너뛰기




Volumn 581, Issue 25, 2007, Pages 4972-4976

Corrigendum to "Ligand-transporter interaction in the AcrB multidrug efflux pump determined by fluorescence polarization assay" [FEBS Lett. 581 (2007) 4972-4976] (DOI:10.1016/j.febslet.2007.09.035);Ligand-transporter interaction in the AcrB multidrug efflux pump determined by fluorescence polarization assay

Author keywords

AcrB; Membrane protein; Multidrug resistance; Multidrug transporter; Protein ligand interaction

Indexed keywords

ACRB PROTEIN; GLYCOPROTEIN P; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 34948849834     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.11.001     Document Type: Erratum
Times cited : (51)

References (31)
  • 2
    • 0346694551 scopus 로고    scopus 로고
    • Efflux as a mechanism of resistance to antimicrobials in Pseudomonas aeruginosa and related bacteria: unanswered questions
    • Schweizer H.P. Efflux as a mechanism of resistance to antimicrobials in Pseudomonas aeruginosa and related bacteria: unanswered questions. Genet. Mol. Res. 31 (2003) 48-62
    • (2003) Genet. Mol. Res. , vol.31 , pp. 48-62
    • Schweizer, H.P.1
  • 3
    • 0027508337 scopus 로고
    • Molecular cloning and characterization of acrA and acrE genes of Escherichia coli
    • Ma D., Cook D.A., Alberti M., Pon N.G., Nikaido H., and Hearst J.E. Molecular cloning and characterization of acrA and acrE genes of Escherichia coli. J. Bacteriol. 175 (1993) 6299-6313
    • (1993) J. Bacteriol. , vol.175 , pp. 6299-6313
    • Ma, D.1    Cook, D.A.2    Alberti, M.3    Pon, N.G.4    Nikaido, H.5    Hearst, J.E.6
  • 4
    • 0029129966 scopus 로고
    • Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa
    • Li X.-Z., Nikaido H., and Poole K. Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 39 (1995) 1948-1953
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1948-1953
    • Li, X.-Z.1    Nikaido, H.2    Poole, K.3
  • 5
    • 0028926676 scopus 로고
    • Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli
    • Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., and Hearst J.E. Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli. Mol. Microbiol. 16 (1995) 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
  • 6
    • 0029845913 scopus 로고    scopus 로고
    • Multidrug efflux pumps of Gram-negative bacteria
    • Nikaido H. Multidrug efflux pumps of Gram-negative bacteria. J. Bacteriol. 178 (1996) 5853-5859
    • (1996) J. Bacteriol. , vol.178 , pp. 5853-5859
    • Nikaido, H.1
  • 7
    • 0033940002 scopus 로고    scopus 로고
    • Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli
    • Zgurskaya H.I., and Nikaido H. Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli. J. Bacteriol. 182 (2000) 4264-4267
    • (2000) J. Bacteriol. , vol.182 , pp. 4264-4267
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 8
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis V., Sharff A., Koronakis E., Luisi B., and Hughes C. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405 (2000) 914-919
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 9
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S., Nakashima R., Yamashita E., and Yamaguchi A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419 (2002) 587-593
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 10
    • 0038670226 scopus 로고    scopus 로고
    • Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump
    • Yu E.W., McDermott G., Zgurskaya H.I., Nikaido H., and Koshland Jr. D.E. Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump. Science 300 (2003) 976-980
    • (2003) Science , vol.300 , pp. 976-980
    • Yu, E.W.1    McDermott, G.2    Zgurskaya, H.I.3    Nikaido, H.4    Koshland Jr., D.E.5
  • 11
    • 25144504245 scopus 로고    scopus 로고
    • A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study
    • Yu E.W., Aires J.R., McDermott G., and Nikaido H. A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study. J. Bacteriol. 187 (2005) 6804-6815
    • (2005) J. Bacteriol. , vol.187 , pp. 6804-6815
    • Yu, E.W.1    Aires, J.R.2    McDermott, G.3    Nikaido, H.4
  • 12
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • Murakami S., Nakashima R., Yamashita E., Matsumoto T., and Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443 (2006) 173-179
    • (2006) Nature , vol.443 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 13
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • Seeger M.A., Schiefner A., Eicher T., Verrey F., Dietrichs K., and Pos K.M. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313 (2006) 1295-1298
    • (2006) Science , vol.313 , pp. 1295-1298
    • Seeger, M.A.1    Schiefner, A.2    Eicher, T.3    Verrey, F.4    Dietrichs, K.5    Pos, K.M.6
  • 14
    • 33749632749 scopus 로고    scopus 로고
    • Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway
    • Su C.-C., Li M., Gu R., Takatsuka Y., Mcdermott G., Nikaido H., and Yu E.W. Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway. J. Bacteriol. 188 (2006) 7290-7296
    • (2006) J. Bacteriol. , vol.188 , pp. 7290-7296
    • Su, C.-C.1    Li, M.2    Gu, R.3    Takatsuka, Y.4    Mcdermott, G.5    Nikaido, H.6    Yu, E.W.7
  • 16
    • 34248572735 scopus 로고    scopus 로고
    • Crystal structure of the multidrug efflux transporter AcrB at 3.1 Å resolution reveals the N-terminal region with conserved amino acids
    • Das D., Xu Q.S., Lee J.Y., Ankoudinova I., Huang C., Lou Y., Degiovanni A., Kim R., and Kim S.H. Crystal structure of the multidrug efflux transporter AcrB at 3.1 Å resolution reveals the N-terminal region with conserved amino acids. J. Struct. Biol. 158 (2006) 494-502
    • (2006) J. Struct. Biol. , vol.158 , pp. 494-502
    • Das, D.1    Xu, Q.S.2    Lee, J.Y.3    Ankoudinova, I.4    Huang, C.5    Lou, Y.6    Degiovanni, A.7    Kim, R.8    Kim, S.H.9
  • 17
    • 33749630424 scopus 로고    scopus 로고
    • Threonine-978 in the transmember segment of the multidrug efflux pump AcrB of Escherichia coli is crucial for drug transport as a probable component of the proton relay network
    • Takatsuka Y., and Nikaido H. Threonine-978 in the transmember segment of the multidrug efflux pump AcrB of Escherichia coli is crucial for drug transport as a probable component of the proton relay network. J. Bacteriol. 188 (2006) 7284-7289
    • (2006) J. Bacteriol. , vol.188 , pp. 7284-7289
    • Takatsuka, Y.1    Nikaido, H.2
  • 18
    • 0033594886 scopus 로고    scopus 로고
    • Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli
    • Zgurskaya H.I., and Nikaido H. Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli. Proc. Natl. Acad. Sci. USA 96 (1999) 7190-7196
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7190-7196
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 19
    • 0027214299 scopus 로고
    • Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA binding
    • LeTilly V., and Royer C.A. Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA binding. Biochemistry 32 (1993) 7753-7758
    • (1993) Biochemistry , vol.32 , pp. 7753-7758
    • LeTilly, V.1    Royer, C.A.2
  • 20
    • 0025261344 scopus 로고
    • Application of fluorescence energy transfer and polarization to monitor Escherichia coli camp receptor protein lac promoter interaction
    • Heyduk T., and Lee J.C. Application of fluorescence energy transfer and polarization to monitor Escherichia coli camp receptor protein lac promoter interaction. Proc. Natl. Acad. Sci. USA 87 (1990) 1744-1748
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1744-1748
    • Heyduk, T.1    Lee, J.C.2
  • 21
    • 34948813274 scopus 로고    scopus 로고
    • ORIGIN Ver. 7.5. OriginLab Corporation, Northampton, MA, USA.
  • 22
    • 0033517728 scopus 로고    scopus 로고
    • Kinetics and consequences of binding of nona- and dodecapeptides to the oligopeptide binding protein (OppA) of Lactococcus lactis
    • Lanfermeijer F.C., Picon A., Konings W.N., and Poolman B. Kinetics and consequences of binding of nona- and dodecapeptides to the oligopeptide binding protein (OppA) of Lactococcus lactis. Biochemistry 38 (1999) 14440-14450
    • (1999) Biochemistry , vol.38 , pp. 14440-14450
    • Lanfermeijer, F.C.1    Picon, A.2    Konings, W.N.3    Poolman, B.4
  • 23
    • 0035940473 scopus 로고    scopus 로고
    • Evidence for simultaneous binding of dissimilar substrates by the Escherichia coli multidrug transporter MdfA
    • Lewinson O., and Bibi E. Evidence for simultaneous binding of dissimilar substrates by the Escherichia coli multidrug transporter MdfA. Biochemistry 40 (2001) 12612-12618
    • (2001) Biochemistry , vol.40 , pp. 12612-12618
    • Lewinson, O.1    Bibi, E.2
  • 24
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • Muth T.R., and Schuldiner S. A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE. EMBO J. 19 (2000) 234-240
    • (2000) EMBO J. , vol.19 , pp. 234-240
    • Muth, T.R.1    Schuldiner, S.2
  • 25
    • 11244254913 scopus 로고    scopus 로고
    • Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry
    • Sikora C., and Turner R. Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry. Biophys. J. 88 (2005) 475-482
    • (2005) Biophys. J. , vol.88 , pp. 475-482
    • Sikora, C.1    Turner, R.2
  • 26
    • 3542992044 scopus 로고    scopus 로고
    • Weak base permeability characteristics influence the intracellular sequestration site in the multidrug-resistant human leukemic cell line HL-60
    • Duvvuri M., Gong Y., Chatterji D., and Krise J.P. Weak base permeability characteristics influence the intracellular sequestration site in the multidrug-resistant human leukemic cell line HL-60. J. Biol. Chem. 297 (2004) 32367-32372
    • (2004) J. Biol. Chem. , vol.297 , pp. 32367-32372
    • Duvvuri, M.1    Gong, Y.2    Chatterji, D.3    Krise, J.P.4
  • 27
    • 34948846844 scopus 로고    scopus 로고
    • .
  • 28
    • 21844452398 scopus 로고    scopus 로고
    • Characterization of the multiple transferable resistance repressor, MtrR, from Neisseria gonorrhoeae.
    • Hoffmann K.M., Williams D., Shafer W.M., and Brennan R.G. Characterization of the multiple transferable resistance repressor, MtrR, from Neisseria gonorrhoeae. J. Bacteriol. 187 (2005) 5008-5012
    • (2005) J. Bacteriol. , vol.187 , pp. 5008-5012
    • Hoffmann, K.M.1    Williams, D.2    Shafer, W.M.3    Brennan, R.G.4
  • 29
    • 34547124088 scopus 로고    scopus 로고
    • Characterization of the multidrug efflux regulator AcrR from Escherichia coli
    • Su C.-C., Rutherford D.J., and Yu E.W. Characterization of the multidrug efflux regulator AcrR from Escherichia coli. Biochem. Biophys. Res. Commun. 361 (2007) 85-90
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , pp. 85-90
    • Su, C.-C.1    Rutherford, D.J.2    Yu, E.W.3
  • 30
    • 4143103793 scopus 로고    scopus 로고
    • Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein
    • Schumacher M.A., Miller M.C., and Brennan R.G. Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein. EMBO J. 23 (2004) 2923-2930
    • (2004) EMBO J. , vol.23 , pp. 2923-2930
    • Schumacher, M.A.1    Miller, M.C.2    Brennan, R.G.3
  • 31
    • 34447119668 scopus 로고    scopus 로고
    • Multidrug-binding transcription factor QacR binds the bivalent aromatic diamidines DB75 and DB359 in multiple positions
    • Brooks B.E., Piro K.M., and Brennan R.G. Multidrug-binding transcription factor QacR binds the bivalent aromatic diamidines DB75 and DB359 in multiple positions. J. Am. Chem. Soc. 129 (2007) 8389-8395
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 8389-8395
    • Brooks, B.E.1    Piro, K.M.2    Brennan, R.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.