메뉴 건너뛰기




Volumn 25, Issue 2, 2000, Pages 39-43

A structure-based mechanism for drug binding by multidrug transporters

Author keywords

[No Author keywords available]

Indexed keywords

CHLORAMPHENICOL; ETHIDIUM BROMIDE; GLYCOPROTEIN P; RHODAMINE 6G; TETRAPHENYLPHOSPHONIUM;

EID: 0033984186     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(99)01514-5     Document Type: Note
Times cited : (74)

References (42)
  • 1
    • 0031455482 scopus 로고    scopus 로고
    • The P-glycoprotein efflux pump: How does it transport drugs?
    • Sharom F.J. The P-glycoprotein efflux pump: how does it transport drugs? J. Membr. Biol. 160:1997;161-175.
    • (1997) J. Membr. Biol. , vol.160 , pp. 161-175
    • Sharom, F.J.1
  • 2
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman M.M., Pastan I. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu. Rev. Biochem. 62:1993;385-427.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 3
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido H. Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science. 264:1994;382-388.
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 4
    • 0029845047 scopus 로고    scopus 로고
    • Proton-dependent multidrug efflux systems
    • Paulsen I.T.et al. Proton-dependent multidrug efflux systems. Microbiol. Rev. 60:1996;575-608.
    • (1996) Microbiol. Rev. , vol.60 , pp. 575-608
    • Paulsen, I.T.1
  • 5
    • 0031020837 scopus 로고    scopus 로고
    • Multidrug-resistant transport proteins in yeast: Complete inventory and phylogenetic characterization of yeast open reading frames with the major facilitator superfamily
    • Goffeau A.et al. Multidrug-resistant transport proteins in yeast: complete inventory and phylogenetic characterization of yeast open reading frames with the major facilitator superfamily. Yeast. 13:1997;43-54.
    • (1997) Yeast , vol.13 , pp. 43-54
    • Goffeau, A.1
  • 6
    • 0028829125 scopus 로고
    • The minimal gene complement of Mycoplasma genitalium
    • Fraser C.M.et al. The minimal gene complement of Mycoplasma genitalium. Science. 270:1995;397-403.
    • (1995) Science , vol.270 , pp. 397-403
    • Fraser, C.M.1
  • 7
    • 0029190287 scopus 로고
    • The role of the MDR protein in altered drug translocation across tumor cell membranes
    • Roepe P.D. The role of the MDR protein in altered drug translocation across tumor cell membranes. Biochim. Biophys. Acta. 1241:1995;385-405.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 385-405
    • Roepe, P.D.1
  • 8
    • 0029781640 scopus 로고    scopus 로고
    • Multidrug resistance in Lactococcus lactis: Evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane
    • Bolhuis H.et al. Multidrug resistance in Lactococcus lactis: evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane. EMBO J. 15:1996;4239-4245.
    • (1996) EMBO J. , vol.15 , pp. 4239-4245
    • Bolhuis, H.1
  • 9
    • 0030822996 scopus 로고    scopus 로고
    • P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer
    • Shapiro A.B.et al. P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer. Eur. J. Biochem. 250:1997;115-121.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 115-121
    • Shapiro, A.B.1
  • 11
    • 0027303904 scopus 로고
    • The nitrogen of the acetamido group of colchicine modulates P-glycoprotein-mediated multidrug resistance
    • Tang-Wai D.F.et al. The nitrogen of the acetamido group of colchicine modulates P-glycoprotein-mediated multidrug resistance. Biochemistry. 32:1993;6470-6476.
    • (1993) Biochemistry , vol.32 , pp. 6470-6476
    • Tang-Wai, D.F.1
  • 12
    • 0029954843 scopus 로고    scopus 로고
    • P-glycoprotein - A mediator of multidrug resistance in tumour cells
    • Germann U.A. P-glycoprotein - a mediator of multidrug resistance in tumour cells. Eur. J. Cancer. 32A:1996;927-944.
    • (1996) Eur. J. Cancer , vol.32 , pp. 927-944
    • Germann, U.A.1
  • 13
    • 0029879199 scopus 로고    scopus 로고
    • Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning
    • Hanna M.et al. Mutagenesis of transmembrane domain 11 of P-glycoprotein by alanine scanning. Biochemistry. 35:1996;3625-3635.
    • (1996) Biochemistry , vol.35 , pp. 3625-3635
    • Hanna, M.1
  • 14
    • 0027160409 scopus 로고
    • Mutants of the Bacillus subtilis multidrug transporter Bmr with altered sensitivity to the antihypertensive alkaloid reserpine
    • Ahmed M.et al. Mutants of the Bacillus subtilis multidrug transporter Bmr with altered sensitivity to the antihypertensive alkaloid reserpine. J. Biol. Chem. 268:1993;11086-11089.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11086-11089
    • Ahmed, M.1
  • 15
    • 0029925159 scopus 로고    scopus 로고
    • The SMR family: A novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs
    • Paulsen I.T.et al. The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs. Mol. Microbiol. 19:1996;1167-1175.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1167-1175
    • Paulsen, I.T.1
  • 16
    • 0029872148 scopus 로고    scopus 로고
    • Multidrug resistance proteins QacA and QacB from Staphylococcus aureus: Membrane topology and identification of residues involved in substrate specificity
    • Paulsen I.T.et al. Multidrug resistance proteins QacA and QacB from Staphylococcus aureus: membrane topology and identification of residues involved in substrate specificity. Proc. Natl. Acad. Sci. U. S. A. 93:1996;3630-3635.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3630-3635
    • Paulsen, I.T.1
  • 17
    • 0030949566 scopus 로고    scopus 로고
    • Mutations affecting substrate specificity of the Bacillus subtilis multidrug transporter Bmr
    • Klyachko K.A.et al. Mutations affecting substrate specificity of the Bacillus subtilis multidrug transporter Bmr. J. Bacteriol. 179:1997;2189-2193.
    • (1997) J. Bacteriol. , vol.179 , pp. 2189-2193
    • Klyachko, K.A.1
  • 18
    • 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., Bibi E. A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug resistance protein MdfA. EMBO J. 18:1999;822-832.
    • (1999) EMBO J. , vol.18 , pp. 822-832
    • Edgar, R.1    Bibi, E.2
  • 19
    • 0001463656 scopus 로고
    • Membrane vesicles from multidrug-resistant human cancer cells contain a specific 150- To 170-kDa protein detected by photoaffinity labeling
    • Cornwell M.M.et al. Membrane vesicles from multidrug-resistant human cancer cells contain a specific 150- to 170-kDa protein detected by photoaffinity labeling. Proc. Natl. Acad. Sci. U. S. A. 83:1986;3847-3850.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 3847-3850
    • Cornwell, M.M.1
  • 20
    • 0025951663 scopus 로고
    • Interaction of forskolin with the P-glycoprotein multidrug transporter
    • Morris D.I.et al. Interaction of forskolin with the P-glycoprotein multidrug transporter. Biochemistry. 30:1991;8371-8379.
    • (1991) Biochemistry , vol.30 , pp. 8371-8379
    • Morris, D.I.1
  • 21
    • 0026669363 scopus 로고
    • Characterization of the azidopine and vinblastine binding site of P-glycoprotein
    • Bruggemann E.P.et al. Characterization of the azidopine and vinblastine binding site of P-glycoprotein. J. Biol. Chem. 267:1992;21020-21026.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21020-21026
    • Bruggemann, E.P.1
  • 22
    • 0028104421 scopus 로고
    • A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates
    • Ahmed M.et al. A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates. J. Biol. Chem. 269:1994;28506-28513.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28506-28513
    • Ahmed, M.1
  • 23
    • 0026734859 scopus 로고
    • Untwist and shout: A heavy metal-responsive transcriptional regulator
    • Summers A.O. Untwist and shout: a heavy metal-responsive transcriptional regulator. J. Bacteriol. 174:1992;3097-3101.
    • (1992) J. Bacteriol. , vol.174 , pp. 3097-3101
    • Summers, A.O.1
  • 24
    • 0031561388 scopus 로고    scopus 로고
    • Broad ligand specificity of the transcriptional regulator of the Bacillus subtilis multidrug transporter Bmr
    • Markham P.N.et al. Broad ligand specificity of the transcriptional regulator of the Bacillus subtilis multidrug transporter Bmr. Biochem. Biophys. Res. Commun. 239:1997;269-272.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 269-272
    • Markham, P.N.1
  • 25
    • 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.et al. The drug-binding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain. J. Bacteriol. 178:1996;473-475.
    • (1996) J. Bacteriol. , vol.178 , pp. 473-475
    • Markham, P.N.1
  • 26
    • 0033525105 scopus 로고    scopus 로고
    • Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter
    • Zheleznova E.E.et al. Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter. Cell. 96:1999;353-362.
    • (1999) Cell , vol.96 , pp. 353-362
    • Zheleznova, E.E.1
  • 27
    • 0026686805 scopus 로고
    • Emr, an Escherichia coli locus for multidrug resistance
    • Lomovskaya O., Lewis K. Emr, an Escherichia coli locus for multidrug resistance. Proc. Natl. Acad. Sci. U. S. A. 89:1992;8938-8942.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 8938-8942
    • Lomovskaya, O.1    Lewis, K.2
  • 28
    • 0030956372 scopus 로고    scopus 로고
    • MdfA, an Escherichia coli multidrug resistance protein with an extraordinarily broad spectrum of drug recognition
    • Edgar R., Bibi E. MdfA, an Escherichia coli multidrug resistance protein with an extraordinarily broad spectrum of drug recognition. J. Bacteriol. 179:1997;2274-2280.
    • (1997) J. Bacteriol. , vol.179 , pp. 2274-2280
    • Edgar, R.1    Bibi, E.2
  • 29
    • 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., Skurray R.A. Topology, structure and evolution of two families of proteins involved in antibiotic and antiseptic resistance in eukaryotes and prokaryotes - an analysis. Gene. 124:1993;1-11.
    • (1993) Gene , vol.124 , pp. 1-11
    • Paulsen, I.T.1    Skurray, R.A.2
  • 30
    • 0029583203 scopus 로고
    • The pharmacological profile of the vesicular monoamine transporter resembles that of multidrug transporters
    • Yelin R., Schuldiner S. The pharmacological profile of the vesicular monoamine transporter resembles that of multidrug transporters. FEBS Lett. 377:1995;201-207.
    • (1995) FEBS Lett. , vol.377 , pp. 201-207
    • Yelin, R.1    Schuldiner, S.2
  • 31
    • 0030845301 scopus 로고    scopus 로고
    • Use of fluorescence probes to monitor function of the subunit proteins of the MexA-MexB-oprM drug extrusion machinery in Pseudomonas aeruginosa
    • Ocaktan A.et al. Use of fluorescence probes to monitor function of the subunit proteins of the MexA-MexB-oprM drug extrusion machinery in Pseudomonas aeruginosa. J. Biol. Chem. 272:1997;21964-21969.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21964-21969
    • Ocaktan, A.1
  • 32
    • 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.et al. Bioenergetics of the staphylococcal multidrug export protein QacA. Identification of distinct binding sites for monovalent and divalent cations. J. Biol. Chem. 274:1999;3541-3548.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3541-3548
    • Mitchell, B.A.1
  • 33
    • 0027432409 scopus 로고
    • Fluorescent cellular indicators are extruded by the multidrug resistance protein
    • Homolya L.et al. Fluorescent cellular indicators are extruded by the multidrug resistance protein. J. Biol. Chem. 268:1993;21493-21496.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21493-21496
    • Homolya, L.1
  • 35
    • 0033602840 scopus 로고    scopus 로고
    • The membrane lipid environment modulates drug interactions with the P-glycoprotein multidrug transporter
    • Romsicki Y., Sharom F.J. The membrane lipid environment modulates drug interactions with the P-glycoprotein multidrug transporter. Biochemistry. 38:1999;6887-6896.
    • (1999) Biochemistry , vol.38 , pp. 6887-6896
    • Romsicki, Y.1    Sharom, F.J.2
  • 36
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty D.A. Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science. 271:1996;163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 37
    • 0032509102 scopus 로고    scopus 로고
    • Proline-induced disruption of a transmembrane alpha-helix in its natural environment
    • Nilsson I.et al. Proline-induced disruption of a transmembrane alpha-helix in its natural environment. J. Mol. Biol. 284:1998;1165-1175.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1165-1175
    • Nilsson, I.1
  • 38
    • 0032512754 scopus 로고    scopus 로고
    • Multiple residues contribute independently to differences in ligand recognition between vesicular monoamine transporters 1 and 2
    • Finn J.P. III, Edwards R.H. Multiple residues contribute independently to differences in ligand recognition between vesicular monoamine transporters 1 and 2. J. Biol. Chem. 273:1998;3943-3947.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3943-3947
    • Finn J.P. III1    Edwards, R.H.2
  • 39
    • 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.et al. Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone. Evidence for a third drug-binding site. Eur. J. Biochem. 259:1999;841-850.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 841-850
    • Shapiro, A.B.1
  • 40
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo T.W., Clarke D.M. Membrane topology of a cysteine-less mutant of human P-glycoprotein. J. Biol. Chem. 270:1995;843-848.
    • (1995) J. Biol. Chem. , vol.270 , pp. 843-848
    • Loo, T.W.1    Clarke, D.M.2
  • 41
    • 0029048812 scopus 로고
    • Multidrug resistance protein (Mdr)-alkaline phosphatase hybrids in Escherichia coli suggest a major revision in the topology of the C-terminal half of Mdr
    • Beja O., Bibi E. Multidrug resistance protein (Mdr)-alkaline phosphatase hybrids in Escherichia coli suggest a major revision in the topology of the C-terminal half of Mdr. J. Biol. Chem. 270:1995;12351-12354.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12351-12354
    • Beja, O.1    Bibi, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.