메뉴 건너뛰기




Volumn 293, Issue 2, 1999, Pages 381-399

ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans

Author keywords

ABC ATPase; ATP hydrolysis; CFTR; Multidrug resistance; Type I secretion

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; GLYCOPROTEIN P; MEMBRANE PROTEIN; MULTIDRUG RESISTANCE PROTEIN; POLYPEPTIDE;

EID: 0032698874     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2993     Document Type: Article
Times cited : (508)

References (118)
  • 2
    • 0028307625 scopus 로고
    • Covalent inhibitors of P-glycoprotein ATPase activity
    • Al-Shawi M. K., Urbatsch I. L., Senior A. F. Covalent inhibitors of P-glycoprotein ATPase activity. J. Biol. Chem. 269:1994;8986-8992.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8986-8992
    • Al-Shawi, M.K.1    Urbatsch, I.L.2    Senior, A.F.3
  • 3
    • 0026638255 scopus 로고
    • ATP-dependent bacterial transporters and cystic fibrosis: Analogy between channels and transporters
    • Ames G. F-L., Lecar H. ATP-dependent bacterial transporters and cystic fibrosis: analogy between channels and transporters. FASEB J. 6:1992;2660-2666.
    • (1992) FASEB J. , vol.6 , pp. 2660-2666
    • Ames, G.F.-L.1    Lecar, H.2
  • 4
    • 0025033814 scopus 로고
    • Bacterial periplasmic permeases belong to a family of transport proteins operating from E. coli to humans: Traffic ATPases
    • Ames G. F-L., Mimura C., Shyamalo V. Bacterial periplasmic permeases belong to a family of transport proteins operating from E. coli to humans: traffic ATPases. FEMS Microbiol. Rev. 75:1990;429-446.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 429-446
    • Ames, G.F.-L.1    Mimura, C.2    Shyamalo, V.3
  • 6
    • 0002431486 scopus 로고    scopus 로고
    • Powering the ABC transporter: The 2.5 Å crystallographic structure of the ABC domain of RBSA
    • Armstrong S., Tabernero L., Zhang H., Hermodsen M., Stauffacher C. Powering the ABC transporter: the 2.5 Å crystallographic structure of the ABC domain of RBSA. Pediat. Pulmonol. 17:1998;91-92.
    • (1998) Pediat. Pulmonol. , vol.17 , pp. 91-92
    • Armstrong, S.1    Tabernero, L.2    Zhang, H.3    Hermodsen, M.4    Stauffacher, C.5
  • 7
    • 0027475808 scopus 로고
    • The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface
    • Baichwal V., Liu D., Ames G. F-L. The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface. Proc. Natl Acad. Sci. USA. 90:1993;620-624.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 620-624
    • Baichwal, V.1    Liu, D.2    Ames, G.F.-L.3
  • 8
    • 0026532895 scopus 로고
    • Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Bear C. E., Canhui L., Kartner N., Bridges R. J., Jensen T. J. Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR). Cell. 68:1992;809-818.
    • (1992) Cell , vol.68 , pp. 809-818
    • Bear, C.E.1    Canhui, L.2    Kartner, N.3    Bridges, R.J.4    Jensen, T.J.5
  • 9
    • 0031036630 scopus 로고    scopus 로고
    • ABC1, an ATP binding cassette transporter required for phagocytosis of apoptotic cells, generates a regulated anion flux after expression in Xenopus laevis oocytes
    • Becq F., Hamon Y., Bajetto A., Gola M., Verrier B., Chimini G. ABC1, an ATP binding cassette transporter required for phagocytosis of apoptotic cells, generates a regulated anion flux after expression in Xenopus laevis oocytes. J. Biol. Chem. 272:1997;2695-2699.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2695-2699
    • Becq, F.1    Hamon, Y.2    Bajetto, A.3    Gola, M.4    Verrier, B.5    Chimini, G.6
  • 10
    • 0029056415 scopus 로고
    • Protein secretion by hybrid bacterial ABC-transporters:specific functions of the membrane ATPase and the membrane fusion protein
    • Binet R., Wandersman C. Protein secretion by hybrid bacterial ABC-transporters:specific functions of the membrane ATPase and the membrane fusion protein. EMBO J. 14:1995;2298-2306.
    • (1995) EMBO J. , vol.14 , pp. 2298-2306
    • Binet, R.1    Wandersman, C.2
  • 11
    • 0024726144 scopus 로고
    • Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport
    • Bishop L., Agbayani R. Jr, Ambudkar S., Maloney P. C., Ames G. F. Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport. Proc. Natl Acad. Sci. USA. 86:1989;6953-6957.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6953-6957
    • Bishop, L.1    Agbayani R., Jr.2    Ambudkar, S.3    Maloney, P.C.4    Ames, G.F.5
  • 12
    • 0025193254 scopus 로고
    • Structure and function of haemolysin B, P-glycoprotein and other members of a novel family of membrane translocators
    • Blight M., Holland I. B. Structure and function of haemolysin B, P-glycoprotein and other members of a novel family of membrane translocators. Mol. Microbiol. 4:1990;873-880.
    • (1990) Mol. Microbiol. , vol.4 , pp. 873-880
    • Blight, M.1    Holland, I.B.2
  • 13
    • 0027945133 scopus 로고
    • Identification and preliminary characterization of temperature sensitive and other sec-mutations affecting HlyB, responsible for the secretion of Haemolysin (HlyA) from E. coli
    • Blight M. A., Pimenta A. L., Lazzaroni J.-C., Dando C., Kotevelets L., Séror S. J., Holland I. B. Identification and preliminary characterization of temperature sensitive and other sec-mutations affecting HlyB, responsible for the secretion of Haemolysin (HlyA) from E. coli. Mol. Gen. Genet. 245:1994;431-440.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 431-440
    • Blight, M.A.1    Pimenta, A.L.2    Lazzaroni, J.-C.3    Dando, C.4    Kotevelets, L.5    Séror, S.J.6    Holland, I.B.7
  • 14
    • 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., van Veen H. W., Molenaar D., Poolman. B., Driessen A. J. M., Konings W. N. 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    Van Veen, H.W.2    Molenaar, D.3    Poolman., B.4    Driessen, A.J.M.5    Konings, W.N.6
  • 15
    • 0027509460 scopus 로고
    • Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions
    • Boyd D., Traxler B., Beckwith J. Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions. J. Bacteriol. 175:1993;553-556.
    • (1993) J. Bacteriol. , vol.175 , pp. 553-556
    • Boyd, D.1    Traxler, B.2    Beckwith, J.3
  • 16
    • 0028241858 scopus 로고
    • Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion
    • Chang X-B., Hou Y-X., Jensen R. J., Riordan J. R. Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion. J. Biol. Chem. 269:1994;18572-18575.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18572-18575
    • Chang, X.-B.1    Hou, Y.-X.2    Jensen, R.J.3    Riordan, J.R.4
  • 17
    • 0030060225 scopus 로고    scopus 로고
    • Random and directed mutagenesis to elucidate the functional importance of helix II and F989 in the C-terminal secretion signal of E. coli haemolysin
    • Chervaux C., Holland I. B. Random and directed mutagenesis to elucidate the functional importance of helix II and F989 in the C-terminal secretion signal of E. coli haemolysin. J. Bacteriol. 178:1996;1232-1236.
    • (1996) J. Bacteriol. , vol.178 , pp. 1232-1236
    • Chervaux, C.1    Holland, I.B.2
  • 18
    • 0030893916 scopus 로고    scopus 로고
    • Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel
    • Cheung M., Akabas M. H. Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel. J. Gen. Physiol. 109:1997;289-299.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 289-299
    • Cheung, M.1    Akabas, M.H.2
  • 19
    • 0032211417 scopus 로고    scopus 로고
    • Multidrug resistance mediated by the ATP-binding cassette transporter protein MRP
    • Cole S., Deeley G. Multidrug resistance mediated by the ATP-binding cassette transporter protein MRP. Bioessays. 20:1998;931-940.
    • (1998) Bioessays , vol.20 , pp. 931-940
    • Cole, S.1    Deeley, G.2
  • 21
    • 0027960078 scopus 로고
    • Pharmacological characterisation of multidrug resistant MRP-transfected human tumor cells
    • Cole S. P. C., Sparks K. E., Fraser K., Loe D., Grant C. E., Wilson G. M., Deeley R. G. Pharmacological characterisation of multidrug resistant MRP-transfected human tumor cells. Cancer Res. 54:1994;5902-5910.
    • (1994) Cancer Res. , vol.54 , pp. 5902-5910
    • Cole, S.P.C.1    Sparks, K.E.2    Fraser, K.3    Loe, D.4    Grant, C.E.5    Wilson, G.M.6    Deeley, R.G.7
  • 22
    • 0022058315 scopus 로고
    • Homologies entre les protéines de membrane interne de systèmes de transports à protéine affine chez les entérobactéries
    • Dassa E., Hofnung M. Homologies entre les protéines de membrane interne de systèmes de transports à protéine affine chez les entérobactéries. Ann. Inst. Pasteur, Microbiol. 136A:1985;281-288.
    • (1985) Ann. Inst. Pasteur, Microbiol. , vol.136 , pp. 281-288
    • Dassa, E.1    Hofnung, M.2
  • 23
    • 0025214263 scopus 로고
    • Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli
    • Davidson A. L., Nikaido H. Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli. J. Biol. Chem. 265:1990;4254-4260.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4254-4260
    • Davidson, A.L.1    Nikaido, H.2
  • 25
    • 0031056684 scopus 로고    scopus 로고
    • Complete inventory of the yeast ABC proteins
    • Decottignies A., Goffeau A. Complete inventory of the yeast ABC proteins. Nature Genet. 15:1997;137-145.
    • (1997) Nature Genet. , vol.15 , pp. 137-145
    • Decottignies, A.1    Goffeau, A.2
  • 26
    • 0030052748 scopus 로고    scopus 로고
    • P-glycoprotein confers methotrexate resistance in 3T6 cells with deficient carrier-mediated methotrexate uptake
    • de Graaf D., Sharma R. C., Mechetner E. B., Schimke R. T., Roninson I. B. P-glycoprotein confers methotrexate resistance in 3T6 cells with deficient carrier-mediated methotrexate uptake. Proc. Natl Acad. Sci. USA. 93:1996;1238-1242.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1238-1242
    • De Graaf, D.1    Sharma, R.C.2    Mechetner, E.B.3    Schimke, R.T.4    Roninson, I.B.5
  • 28
    • 0026768856 scopus 로고
    • Transport properties of P-glycoprotein in plasma membrane vesicles from multidrug resistant chinese hamster ovary cells
    • Doige C. A., Sharom F. J. Transport properties of P-glycoprotein in plasma membrane vesicles from multidrug resistant chinese hamster ovary cells. Biochem. Biophys. Acta. 1109:1992;161-171.
    • (1992) Biochem. Biophys. Acta , vol.1109 , pp. 161-171
    • Doige, C.A.1    Sharom, F.J.2
  • 29
    • 77956776810 scopus 로고    scopus 로고
    • Translocation of proteins across the bacterial cytoplasmic membrane
    • W. N. Konings, H. R. Kaback, & J. S. Lolkema. North Holland, Elsevier
    • Driessen A. J. M. Translocation of proteins across the bacterial cytoplasmic membrane. Konings W. N., Kaback H. R., Lolkema J. S. Handbook of Biological Physics. 1996;759-790 North Holland, Elsevier.
    • (1996) Handbook of Biological Physics , pp. 759-790
    • Driessen, A.J.M.1
  • 32
    • 0032936619 scopus 로고    scopus 로고
    • Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis
    • Gadsby D. C., Nairn A. C. Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis. Physiol Rev. 79:1999;S77-S107.
    • (1999) Physiol Rev. , vol.79
    • Gadsby, D.C.1    Nairn, A.C.2
  • 33
    • 0029985152 scopus 로고    scopus 로고
    • Reconstitution of ATP-dependent LTC transport by co-expression of both half-molecules of human MRP in insect cell
    • Gao M., Loe D. W., Grant C. E., Cole S. P. C., Deeley R. G. Reconstitution of ATP-dependent LTC transport by co-expression of both half-molecules of human MRP in insect cell. J. Biol. Chem. 271:1996;27782-27787.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27782-27787
    • Gao, M.1    Loe, D.W.2    Grant, C.E.3    Cole, S.P.C.4    Deeley, R.G.5
  • 35
    • 0026575486 scopus 로고
    • Topological and functional studies on HlyB of Escherichia coli
    • Gentschev I., Goebel W. Topological and functional studies on HlyB of Escherichia coli. Mol. Gen. Genet. 232:1992;40-48.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 40-48
    • Gentschev, I.1    Goebel, W.2
  • 36
    • 0027391633 scopus 로고
    • Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody
    • Georges E., Tsuro T., Ling V. Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody. J. Biol. Chem. 25:1993;1792-1798.
    • (1993) J. Biol. Chem. , vol.25 , pp. 1792-1798
    • Georges, E.1    Tsuro, T.2    Ling, V.3
  • 37
    • 0030744062 scopus 로고    scopus 로고
    • The nucleotide binding folds of the cystic fibrosis transmembrane conductance regulator are extracellularly accessible
    • Gruis D. B., Price E. M. The nucleotide binding folds of the cystic fibrosis transmembrane conductance regulator are extracellularly accessible. Biochemistry. 36:1997;7739-7745.
    • (1997) Biochemistry , vol.36 , pp. 7739-7745
    • Gruis, D.B.1    Price, E.M.2
  • 38
    • 0030250311 scopus 로고    scopus 로고
    • ATP transport and ABC proteins
    • Guidotti G. ATP transport and ABC proteins. Curr. Biol. 3:1996;703-706.
    • (1996) Curr. Biol. , vol.3 , pp. 703-706
    • Guidotti, G.1
  • 39
    • 0028876622 scopus 로고
    • Protein kinase C-mediated phosphorylation of the human multidrug resistance P-glycoprotein regulates cell volume activated chloride channels
    • Hardy S. P., Goodfellow H. R., Valverde M. A., Gill D. R., Sepulveda F. V., Higgins C. F. Protein kinase C-mediated phosphorylation of the human multidrug resistance P-glycoprotein regulates cell volume activated chloride channels. EMBO J. 14:1995;68-75.
    • (1995) EMBO J. , vol.14 , pp. 68-75
    • Hardy, S.P.1    Goodfellow, H.R.2    Valverde, M.A.3    Gill, D.R.4    Sepulveda, F.V.5    Higgins, C.F.6
  • 40
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins C. F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:1992;67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 42
    • 0344195661 scopus 로고    scopus 로고
    • Structure and function of HlyB, the ABC-transporter essential for haemolysin secretion from Escherichia coli
    • W. N. Konings, H. R. Kaback, & J. S. Lolkema. Elsevier
    • Holland I. B., Blight M. A. Structure and function of HlyB, the ABC-transporter essential for haemolysin secretion from Escherichia coli. Konings W. N., Kaback H. R., Lolkema J. S. Handbook of Biological Physics. 1996;111-135 Elsevier.
    • (1996) Handbook of Biological Physics , pp. 111-135
    • Holland, I.B.1    Blight, M.A.2
  • 47
    • 0028001416 scopus 로고
    • ATP-dependent transport of glutathione S-conjugates by the multidrug resistance-associated protein
    • Jedlitschky G., Leier I., Buchholz U., Center M., Keppler D. ATP-dependent transport of glutathione S-conjugates by the multidrug resistance-associated protein. Cancer Res. 54:1994;4833-4836.
    • (1994) Cancer Res. , vol.54 , pp. 4833-4836
    • Jedlitschky, G.1    Leier, I.2    Buchholz, U.3    Center, M.4    Keppler, D.5
  • 48
    • 0033515434 scopus 로고    scopus 로고
    • Alignment and structure prediction of divergent protein families: Periplasmic and outer membrane proteins of bacterial efflux pumps
    • Johnson J. M., Church G. M. Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps. J. Mol. Biol. 287:1999;695-715.
    • (1999) J. Mol. Biol. , vol.287 , pp. 695-715
    • Johnson, J.M.1    Church, G.M.2
  • 49
    • 0029918133 scopus 로고    scopus 로고
    • Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence
    • Kast C., Canfield V., Levenson R., Gros P. Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence. J. Biol. Chem. 271:1996;9240-9248.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9240-9248
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 50
    • 0026683501 scopus 로고
    • Identification of individual amino acids required for secretion within the haemolysin (HlyA), C-terminal targeting region
    • Kenny B., Taylor S., Holland I. B. Identification of individual amino acids required for secretion within the haemolysin (HlyA), C-terminal targeting region. Mol. Microbiol. 6:1992;1477-1489.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1477-1489
    • Kenny, B.1    Taylor, S.2    Holland, I.B.3
  • 51
    • 0028308070 scopus 로고
    • Evidence that residues -15 to -46 of the haemolysin secretion signal are involved in early steps in secretion, leading to recognition of the translocator
    • Kenny B., Chervaux C., Holland I. B. Evidence that residues -15 to -46 of the haemolysin secretion signal are involved in early steps in secretion, leading to recognition of the translocator. Mol. Microbiol. 11:1994;99-109.
    • (1994) Mol. Microbiol. , vol.11 , pp. 99-109
    • Kenny, B.1    Chervaux, C.2    Holland, I.B.3
  • 52
    • 0029113976 scopus 로고
    • The first nucleoide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase
    • Ko Y. H., Pedersen P. L. The first nucleoide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase. J. Biol. Chem. 270:1993;22093-22096.
    • (1993) J. Biol. Chem. , vol.270 , pp. 22093-22096
    • Ko, Y.H.1    Pedersen, P.L.2
  • 53
    • 0027190678 scopus 로고
    • ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator HlyB
    • Koronakis V., Hughes C., Koronakis E. ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator HlyB. Mol. Microbiol. 8:1993;1163-1175.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1163-1175
    • Koronakis, V.1    Hughes, C.2    Koronakis, E.3
  • 54
    • 0028915106 scopus 로고
    • Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB
    • Koronakis E., Hughes C., Milisav I., Koronakis V. Protein exporter function and in vitro ATPase activity are correlated in ABC-domain mutants of HlyB. Mol. Microbiol. 16:1995;87-96.
    • (1995) Mol. Microbiol. , vol.16 , pp. 87-96
    • Koronakis, E.1    Hughes, C.2    Milisav, I.3    Koronakis, V.4
  • 55
    • 0025935023 scopus 로고
    • Iron (III) hydroxamate transport across the cytoplasmic membrane of Escherichia coli
    • Köster W. Iron (III) hydroxamate transport across the cytoplasmic membrane of Escherichia coli. Biol. Metals. 4:1991;23-32.
    • (1991) Biol. Metals , vol.4 , pp. 23-32
    • Köster, W.1
  • 56
    • 0030775546 scopus 로고    scopus 로고
    • Induction by antitumoral drugs of proteins that functionally complement CFTR: A novel therapy for cystic fibrosis?
    • Lallemand J. Y., Stoven V., Annereau J. P., Boucher J., Blanquet S., Barthe J., Lenoir G. Induction by antitumoral drugs of proteins that functionally complement CFTR: a novel therapy for cystic fibrosis? Lancet. 350:1997;711-712.
    • (1997) Lancet. , vol.350 , pp. 711-712
    • Lallemand, J.Y.1    Stoven, V.2    Annereau, J.P.3    Boucher, J.4    Blanquet, S.5    Barthe, J.6    Lenoir, G.7
  • 58
    • 0031851457 scopus 로고    scopus 로고
    • Glutathione permeability of CFTR
    • Linsdell P., Hannrahan J. W. Glutathione permeability of CFTR. Am. J. Physiol. 275:1998a;323-326.
    • (1998) Am. J. Physiol. , vol.275 , pp. 323-326
    • Linsdell, P.1    Hannrahan, J.W.2
  • 59
    • 0031954021 scopus 로고    scopus 로고
    • Adenosine triphosphate-dependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Linsdell P., Hannrahan J. W. Adenosine triphosphate-dependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Gen. Physiol. 111:1998b;601-614.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 601-614
    • Linsdell, P.1    Hannrahan, J.W.2
  • 60
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton K., Higgins C. F. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28:1998;5-13.
    • (1998) Mol. Microbiol. , vol.28 , pp. 5-13
    • Linton, K.1    Higgins, C.F.2
  • 61
    • 0031021530 scopus 로고    scopus 로고
    • Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis
    • Liu C. E., Ames G. F.-L. Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis. J. Biol. Chem. 272:1997;859-866.
    • (1997) J. Biol. Chem. , vol.272 , pp. 859-866
    • Liu, C.E.1    Ames, G.F.-L.2
  • 62
    • 0032584131 scopus 로고    scopus 로고
    • In vitro disassembly and reassembly of an ABC transporter, the histidine permease
    • Liu P.-Q., Ames G. F.-L. In vitro disassembly and reassembly of an ABC transporter, the histidine permease. Proc. Natl Acad. Sci. USA. 95:1998;3495-3500.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3495-3500
    • Liu, P.-Q.1    Ames, G.F.-L.2
  • 63
    • 0029840320 scopus 로고    scopus 로고
    • Site directed fluorescence labeling of P-glyprotein on cysteine residues in the nucleotide binding domains
    • Liu R., Sharom F. J. Site directed fluorescence labeling of P-glyprotein on cysteine residues in the nucleotide binding domains. Biochemistry. 35:1996;11865-11873.
    • (1996) Biochemistry , vol.35 , pp. 11865-11873
    • Liu, R.1    Sharom, F.J.2
  • 64
    • 0030973613 scopus 로고    scopus 로고
    • Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter
    • Liu R., Sharom F. J. Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter. Biochemistry. 36:1997;2836-2843.
    • (1997) Biochemistry , vol.36 , pp. 2836-2843
    • Liu, R.1    Sharom, F.J.2
  • 65
    • 0028229881 scopus 로고
    • Reconstitution of drug-stimulated ATPase activity following co-expression of each half of humanP-glycoprotein as separate polypeptides
    • Loo T. W., Clarke D. M. Reconstitution of drug-stimulated ATPase activity following co-expression of each half of humanP-glycoprotein as separate polypeptides. J. Biol. Chem. 269:1994;7750-7755.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7750-7755
    • Loo, T.W.1    Clarke, D.M.2
  • 66
    • 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
  • 67
    • 0029909604 scopus 로고    scopus 로고
    • Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates
    • Loo T. W., Clarke D. M. Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates. J. Biol. Chem. 271:1996;27482-27487.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27482-27487
    • Loo, T.W.1    Clarke, D.M.2
  • 68
    • 0030779102 scopus 로고    scopus 로고
    • Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12
    • Loo T. W., Clarke D. M. Drug-stimulated ATPase activity of human P-glycoprotein requires movement between transmembrane segments 6 and 12. J. Biol. Chem. 272:1997a;20986-20989.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20986-20989
    • Loo, T.W.1    Clarke, D.M.2
  • 69
    • 0031434236 scopus 로고    scopus 로고
    • Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate
    • Loo T. W., Clarke D. M. Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrate. J. Biol. Chem. 272:1997b;31945-31948.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31945-31948
    • Loo, T.W.1    Clarke, D.M.2
  • 70
    • 0030662644 scopus 로고    scopus 로고
    • ATP-dependent ferric hydroxamate transport system in Escherichia coli: Periplasmic FhuD interacts with a periplasmic and with a transmembrane/cytoplasmic region of the integral membrane protein FhuB, as revealed by competitive peptide mapping
    • Mademidis A., Killmann H., Kraas W., Flechsler I., Jung G., Braun V. ATP-dependent ferric hydroxamate transport system in Escherichia coli: periplasmic FhuD interacts with a periplasmic and with a transmembrane/cytoplasmic region of the integral membrane protein FhuB, as revealed by competitive peptide mapping. Mol. Microbiol. 26:1997;1109-1123.
    • (1997) Mol. Microbiol. , vol.26 , pp. 1109-1123
    • Mademidis, A.1    Killmann, H.2    Kraas, W.3    Flechsler, I.4    Jung, G.5    Braun, V.6
  • 72
    • 0024853842 scopus 로고
    • Energy coupling to periplasmic binding protein-dependent transport systems: Stoichiometry of ATP hydrolysis during transport in vivo
    • Mimmack M. L., Gallagher M. P., Pearce S. R., Hyde S. C., Booth I. R., Higgins C. F. Energy coupling to periplasmic binding protein-dependent transport systems: stoichiometry of ATP hydrolysis during transport in vivo. Proc. Natl Acad. Sci. USA. 86:1989;8257-8261.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 8257-8261
    • Mimmack, M.L.1    Gallagher, M.P.2    Pearce, S.R.3    Hyde, S.C.4    Booth, I.R.5    Higgins, C.F.6
  • 73
    • 0027272354 scopus 로고
    • The ATP-binding cassette (ABC) transporter for maltose/maltodextrins of Salmonella typhimurium. Characterization of the ATPase activity associated with the purified MalK subunit
    • Morbach S., Tebbe S., Schneider E. The ATP-binding cassette (ABC) transporter for maltose/maltodextrins of Salmonella typhimurium. Characterization of the ATPase activity associated with the purified MalK subunit. J. Biol. Mol. 268:1993;18617-18621.
    • (1993) J. Biol. Mol. , vol.268 , pp. 18617-18621
    • Morbach, S.1    Tebbe, S.2    Schneider, E.3
  • 74
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez M., Hofnung M., Dassa E. Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 16:1997;3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 75
    • 0031756353 scopus 로고    scopus 로고
    • In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: Modulation by ATP
    • Mourez M., Jéhanno M., Schneider E., Dassa E. In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP. Mol. Microbiol. 30:1998;353-363.
    • (1998) Mol. Microbiol. , vol.30 , pp. 353-363
    • Mourez, M.1    Jéhanno, M.2    Schneider, E.3    Dassa, E.4
  • 76
    • 0028578004 scopus 로고
    • Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport
    • Müller M., Meijer C., Zaman G. J. R., Borst P., Scheper R. J., Mulder N. H., de Vries E. G. E., Jansen P. L. M. Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport. Proc. Natl Acad. Sci. USA. 91:1994;13033-13037.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 13033-13037
    • Müller, M.1    Meijer, C.2    Zaman, G.J.R.3    Borst, P.4    Scheper, R.J.5    Mulder, N.H.6    De Vries, E.G.E.7    Jansen, P.L.M.8
  • 77
    • 0030822352 scopus 로고    scopus 로고
    • Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium
    • Nikaido K., Liu P.-Q., Ames G. F.-L. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. J. Biol. Chem. 272:1997;27745-27752.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27745-27752
    • Nikaido, K.1    Liu, P.-Q.2    Ames, G.F.-L.3
  • 78
    • 0027934102 scopus 로고
    • A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium
    • Parra-Lopez C., Lin R., Aspedon A., Groisman E. A. A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium. EMBO J. 13:1994;3964-3972.
    • (1994) EMBO J. , vol.13 , pp. 3964-3972
    • Parra-Lopez, C.1    Lin, R.2    Aspedon, A.3    Groisman, E.A.4
  • 79
    • 0029979819 scopus 로고    scopus 로고
    • ATP-dependent uptake of natural product cytotoxic drugs by membrane vesicles establishes MRP as a broad specificity transporter
    • Paul S., Breuninger L. M., Tew K. D., Shen H., Druh G. D. ATP-dependent uptake of natural product cytotoxic drugs by membrane vesicles establishes MRP as a broad specificity transporter. Proc. Natl Acad. Sci. USA. 93:1996;6929-6934.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6929-6934
    • Paul, S.1    Breuninger, L.M.2    Tew, K.D.3    Shen, H.4    Druh, G.D.5
  • 80
    • 0000887546 scopus 로고
    • Essential features of the P-glycoprotein pharmacophore as defined by a series of reserpine analogs that modulate multidrug resistance
    • Pearce H. L., Safa A. R., Bach N. J., Winter M. A., Cirtain M. C., Beck W. T. Essential features of the P-glycoprotein pharmacophore as defined by a series of reserpine analogs that modulate multidrug resistance. Proc. Natl Acad. Sci. USA. 86:1989;5128-5131.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5128-5131
    • Pearce, H.L.1    Safa, A.R.2    Bach, N.J.3    Winter, M.A.4    Cirtain, M.C.5    Beck, W.T.6
  • 81
    • 0026047738 scopus 로고
    • Binding protein-independent histidine permease mutants. Uncoupling of ATP hydrolysis from transmembrane signalling
    • Petronilli V., Ames G. F.-L. Binding protein-independent histidine permease mutants. Uncoupling of ATP hydrolysis from transmembrane signalling. J. Biol. Chem. 266:1991;16293-16296.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16293-16296
    • Petronilli, V.1    Ames, G.F.-L.2
  • 82
    • 0030032951 scopus 로고    scopus 로고
    • The Gram-negative cell envelope "springs" to life: Coiled-coil trans-envelope proteins
    • Pimenta A., Blight M. A., Clarke D., Holland I. B. The Gram-negative cell envelope "springs" to life: coiled-coil trans-envelope proteins. Mol. Microbiol. 19:1996;643-645.
    • (1996) Mol. Microbiol. , vol.19 , pp. 643-645
    • Pimenta, A.1    Blight, M.A.2    Clarke, D.3    Holland, I.B.4
  • 83
    • 0033515437 scopus 로고    scopus 로고
    • Inventory, assembly and analysis of Bacillus subtilis ABC transport systems
    • Quentin Y., Fichant G., Denizot F. Inventory, assembly and analysis of Bacillus subtilis ABC transport systems. J. Mol. Biol. 287:1999;467-484.
    • (1999) J. Mol. Biol. , vol.287 , pp. 467-484
    • Quentin, Y.1    Fichant, G.2    Denizot, F.3
  • 84
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Raviv Y., Pollard H. B., Bruggemann E. P., Pastan I., Gottesman M. M. Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells. J. Biol. Chem. 265:1990;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
  • 86
    • 0030971840 scopus 로고    scopus 로고
    • Structure of the multidrug resistance P-glycoprotein to 2.5 mm resolution determined by electron microscopy and image analysis
    • Rosenberg M. F., Callaghan R., Ford R. C., Higgins C. F. Structure of the multidrug resistance P-glycoprotein to 2.5 mm resolution determined by electron microscopy and image analysis. J. Biol. Chem. 272:1997;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
  • 87
    • 0032951188 scopus 로고    scopus 로고
    • Getting in or out: Early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters
    • Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 48:1999;22-41.
    • (1999) J. Mol. Evol. , vol.48 , pp. 22-41
    • Saurin, W.1    Hofnung, M.2    Dassa, E.3
  • 88
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolysing subunits/domains
    • Schneider E., Hunke S. ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolysing subunits/domains. FEMS Microbiol. Rev. 22:1998;1-20.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 89
    • 0028109264 scopus 로고
    • Nucleotide-induced conformational changes of MalK, a bacterial ATP binding cassette transporter protein
    • Schneider E., Wilken S., Schmid R. Nucleotide-induced conformational changes of MalK, a bacterial ATP binding cassette transporter protein. J. Biol. Chem. 269:1994;20456-20461.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20456-20461
    • Schneider, E.1    Wilken, S.2    Schmid, R.3
  • 90
    • 0029092262 scopus 로고
    • The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible from the periplasmic side of the membrane
    • Schneider E., Hunke S., Tebbe S. The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible from the periplasmic side of the membrane. J. Bacteriol. 177:1995;5364-5367.
    • (1995) J. Bacteriol. , vol.177 , pp. 5364-5367
    • Schneider, E.1    Hunke, S.2    Tebbe, S.3
  • 92
    • 0028980536 scopus 로고
    • CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP
    • Schweibert E. M., Egan M. E., Hwang T.-H., Fulmer S. B., Allen S. S., Cutting G. R., Guggino W. B. CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP. Cell. 81:1995;1063-1073.
    • (1995) Cell , vol.81 , pp. 1063-1073
    • Schweibert, E.M.1    Egan, M.E.2    Hwang, T.-H.3    Fulmer, S.B.4    Allen, S.S.5    Cutting, G.R.6    Guggino, W.B.7
  • 93
    • 0032478144 scopus 로고    scopus 로고
    • Chloride channel and chloride conductance regulator domains of CFTR, the cystic fibrosis transmembrane conductance regulator
    • Schweibert E. M., Morolas M. M., Devidas S., Egan M. E., Guggino W. B. Chloride channel and chloride conductance regulator domains of CFTR, the cystic fibrosis transmembrane conductance regulator. Proc. Natl Acad. Sci. USA. 95:1998;2674-2679.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2674-2679
    • Schweibert, E.M.1    Morolas, M.M.2    Devidas, S.3    Egan, M.E.4    Guggino, W.B.5
  • 95
    • 0027937143 scopus 로고
    • ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells
    • Shapiro A. B., Ling V. ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells. J. Biol. Chem. 269:1994;3745-3754.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3745-3754
    • Shapiro, A.B.1    Ling, V.2
  • 96
    • 0029061103 scopus 로고
    • Reconstitution of drug transport by purified P-glyprotein
    • Shapiro A. B., Ling V. Reconstitution of drug transport by purified P-glyprotein. J. Biol. Chem. 270:1995;16167-16175.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16167-16175
    • Shapiro, A.B.1    Ling, V.2
  • 97
    • 0030784559 scopus 로고    scopus 로고
    • Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membrane by P-glycoprotein
    • Shapiro A. B., Ling V. Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membrane by P-glycoprotein. Eur. J. Biochem. 259:1997;122-129.
    • (1997) Eur. J. Biochem. , vol.259 , pp. 122-129
    • Shapiro, A.B.1    Ling, V.2
  • 98
    • 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., Ling V. Transport of LDS-751 from the cytoplasmic leaflet of the plasma membrane by the rhodamine-123-selective site of P-glycoprotein. Eur. J. Biochem. 254:1998;181-188.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 181-188
    • Shapiro, A.B.1    Ling, V.2
  • 99
    • 0032461892 scopus 로고    scopus 로고
    • Spectroscopic and biophysical approaches for studying the structure and function of the P-glycoprotein multidrug transporter
    • Sharom F. J., Liu R., Romsicki Y. Spectroscopic and biophysical approaches for studying the structure and function of the P-glycoprotein multidrug transporter. Biochem. Cell Biol. 76:1998;695-708.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 695-708
    • Sharom, F.J.1    Liu, R.2    Romsicki, Y.3
  • 100
    • 0029043806 scopus 로고
    • Hemolysin transport in Escherichia coli. Point mutants in HlyB compensate for a deletion in the predicted amphiphilic helix region of the HlyA signal
    • Sheps J. A., Cheung I., Ling V. Hemolysin transport in Escherichia coli. Point mutants in HlyB compensate for a deletion in the predicted amphiphilic helix region of the HlyA signal. J. Biol. Chem. 270:1995;14829-14834.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14829-14834
    • Sheps, J.A.1    Cheung, I.2    Ling, V.3
  • 101
    • 0029784872 scopus 로고    scopus 로고
    • Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis
    • Sonveaux N., Shapiro A. B., Goormaghtigh E., Ling V., Ruysschaert J. M. Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis. J. Biol. Chem. 271:1996;24617-24624.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24617-24624
    • Sonveaux, N.1    Shapiro, A.B.2    Goormaghtigh, E.3    Ling, V.4    Ruysschaert, J.M.5
  • 102
    • 0025972404 scopus 로고
    • Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins
    • Speiser D. M., Ames G. F. Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins. J. Bacteriol. 173:1991;1444-1451.
    • (1991) J. Bacteriol. , vol.173 , pp. 1444-1451
    • Speiser, D.M.1    Ames, G.F.2
  • 103
    • 0026009429 scopus 로고
    • Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin
    • Stanley P., Koronakis V., Hughes C. Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin. Mol. Microbiol. 5:1991;2391-2403.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2391-2403
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 106
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E. coli: Reversible bridging of an inner-membrane translocase to an outer membrane exit pore
    • Thanabalu T., Koronakis E., Hughes C., Koronakis V. Substrate-induced assembly of a contiguous channel for protein export from E. coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore. EMBO J. 17:1998;6487-6496.
    • (1998) EMBO J. , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 108
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch I. L., Sankaran B., Weber J., Senior A. E. P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J. Biol. Chem. 270:1995a;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
  • 109
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch I. L., Sankaran B., Bhagat S., Senior A. E. Both P-glycoprotein nucleotide-binding sites are catalytically active. J. Mol. Biol. 270:1995b;26956-26961.
    • (1995) J. Mol. Biol. , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 111
    • 0001607723 scopus 로고
    • Distantly related sequences in the α and β subunits of the ATP synthase, myosin, kinases and other ATP requiring enzymes and a common nucleotide binding fold
    • Walker J. E., Saraste M., Rumswick M. J., Gay N. J. Distantly related sequences in the α and β subunits of the ATP synthase, myosin, kinases and other ATP requiring enzymes and a common nucleotide binding fold. EMBO J. 1:1982;945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Rumswick, M.J.3    Gay, N.J.4
  • 112
    • 0026012975 scopus 로고
    • Analysis of the membrane organisation of an E. coli protein translocator, HlyB, a member of a large family of pro-and eukaryote surface transport proteins
    • Wang R., Séror S. J., Blight M., Pratt J. M., Broome-Smith J. K., Holland I. B. Analysis of the membrane organisation of an E. coli protein translocator, HlyB, a member of a large family of pro-and eukaryote surface transport proteins. J. Mol. Biol. 217:1991;441-454.
    • (1991) J. Mol. Biol. , vol.217 , pp. 441-454
    • Wang, R.1    Séror, S.J.2    Blight, M.3    Pratt, J.M.4    Broome-Smith, J.K.5    Holland, I.B.6
  • 113
    • 0029161044 scopus 로고
    • Overexpression of the cystic fibrosis transmembrane conductance regulator in NIH 3T3 cells lowers membrane potential and intracellular pH and confers a mutidrug resistance phenotype
    • Wei L. Y., Stutts M. J., Hoffman M. M., Roepe P. D. Overexpression of the cystic fibrosis transmembrane conductance regulator in NIH 3T3 cells lowers membrane potential and intracellular pH and confers a mutidrug resistance phenotype. Biophys. J. 69:1995;883-895.
    • (1995) Biophys. J. , vol.69 , pp. 883-895
    • Wei, L.Y.1    Stutts, M.J.2    Hoffman, M.M.3    Roepe, P.D.4
  • 114
    • 0029830549 scopus 로고    scopus 로고
    • A putative helical domain in the MalK subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool
    • Wilken S., Schmees G;., Schneider E. A putative helical domain in the MalK subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool. Mol. Microbiol. 22:1996;655-666.
    • (1996) Mol. Microbiol. , vol.22 , pp. 655-666
    • Wilken, S.1    Schmees, G.2    Schneider, E.3
  • 116
    • 0027171205 scopus 로고
    • Complementation of transport-deficient mutants of Escherichia coli alpha-hemolysin by second-site mutations in the transporter hemolysin B
    • Zhang F., Sheps J. A., Ling V. Complementation of transport-deficient mutants of Escherichia coli alpha-hemolysin by second-site mutations in the transporter hemolysin B. J. Biol. Chem. 268:1993;19889-19895.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19889-19895
    • Zhang, F.1    Sheps, J.A.2    Ling, V.3
  • 117
    • 0025951859 scopus 로고
    • Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation
    • Zhang J.-T., Ling V. Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation. J. Biol. Chem. 266:1991;18224-18232.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18224-18232
    • Zhang, J.-T.1    Ling, V.2
  • 118
    • 0033525105 scopus 로고    scopus 로고
    • Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter
    • Zheleznova E. E., Markham P. N., Neyfakh A. A., Brennan R. G. Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter. Cell. 96:1999;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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.