메뉴 건너뛰기




Volumn 400, Issue , 2005, Pages 429-459

Functional analysis of detergent-solubilized and membrane-reconstituted ATP-binding cassette transporters

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; BINDING PROTEIN; DETERGENT; PROTEIN;

EID: 28944449620     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)00025-X     Document Type: Review
Times cited : (31)

References (69)
  • 1
    • 0031806924 scopus 로고    scopus 로고
    • Formation of giant liposomes promoted by divalent cations: Critical role of electrostatic repulsion
    • Akashi K., Miyata H., Itoh H., and Kinosita K. Jr. Formation of giant liposomes promoted by divalent cations: Critical role of electrostatic repulsion Biophys. J. 74 1998 2973 2982
    • (1998) Biophys. J. , vol.74 , pp. 2973-2982
    • Akashi, K.1    Miyata, H.2    Itoh, H.3    Kinosita Jr., K.4
  • 2
    • 0032808951 scopus 로고    scopus 로고
    • Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein
    • Albers S.V., Elferink M.G., Charlebois R.L., Sensen C.W., Driessen A.J., and Konings W.N. Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein J. Bacteriol. 181 1999 4285 4291
    • (1999) J. Bacteriol. , vol.181 , pp. 4285-4291
    • Albers, S.V.1    Elferink, M.G.2    Charlebois, R.L.3    Sensen, C.W.4    Driessen, A.J.5    Konings, W.N.6
  • 3
    • 0242493209 scopus 로고    scopus 로고
    • Photoaffinity labeling under non-energized conditions of a specific drug-binding site of the ABC multidrug transporter LmrA from Lactococcus lactis
    • Alqawi O., Poelarends G., Konings W.N., and Georges E. Photoaffinity labeling under non-energized conditions of a specific drug-binding site of the ABC multidrug transporter LmrA from Lactococcus lactis Biochem. Biophys. Res. Commun. 311 2003 696 701
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 696-701
    • Alqawi, O.1    Poelarends, G.2    Konings, W.N.3    Georges, E.4
  • 4
    • 0035004765 scopus 로고    scopus 로고
    • Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease
    • Ames G.F., Nikaido K., Wang I.X., Liu P.Q., Liu C.E., and Hu C. Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease J. Bioenerg. Biomem. 33 2001 79 92
    • (2001) J. Bioenerg. Biomem. , vol.33 , pp. 79-92
    • Ames, G.F.1    Nikaido, K.2    Wang, I.X.3    Liu, P.Q.4    Liu, C.E.5    Hu, C.6
  • 5
    • 0001029147 scopus 로고
    • Preparation of giant vesicles by external AC electric fields: Kinetics and applications
    • Angelova M.I., Soléau S. Ph., Méléard, Faucon J.F., and Bothorel P. Preparation of giant vesicles by external AC electric fields: Kinetics and applications Progr. Colloid Polym. Sci. 89 1992 127 131
    • (1992) Progr. Colloid Polym. Sci. , vol.89 , pp. 127-131
    • Angelova, M.I.1    Ph., S.S.2    Méléard3    Faucon, J.F.4    Bothorel, P.5
  • 6
    • 0344442852 scopus 로고    scopus 로고
    • On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA
    • Biemans-Oldehinkel E., and Poolman B. On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA EMBO J. 22 2003 5983 5993
    • (2003) EMBO J. , vol.22 , pp. 5983-5993
    • Biemans-oldehinkel, E.1    Poolman, B.2
  • 7
    • 0005824924 scopus 로고    scopus 로고
    • I.B. Holland S.P.C. Cole K. Kuchler C.F. Higgins Academic Press San Diego
    • Borst P. I.B. Holland S.P.C. Cole K. Kuchler C.F. Higgins "ABC Proteins: From Bacteria to Man" 2003 Academic Press San Diego
    • (2003) "aBC Proteins: From Bacteria to Man"
    • Borst, P.1
  • 8
    • 0038799725 scopus 로고    scopus 로고
    • Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation
    • Chang G. Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation J. Mol. Biol. 330 2003 419 430
    • (2003) J. Mol. Biol. , vol.330 , pp. 419-430
    • Chang, G.1
  • 9
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang G., and Roth C.B. Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters Science 293 2001 1793 1800
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 10
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen J., Sharma S., Quiocho F.A., and Davidson A.L. Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport Proc. Natl. Acad. Sci. USA 98 2001 1525 1530
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 11
    • 0036179213 scopus 로고    scopus 로고
    • Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters
    • Davidson A.L. Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters J. Bacteriol. 184 2002 1225 1233
    • (2002) J. Bacteriol. , vol.184 , pp. 1225-1233
    • Davidson, A.L.1
  • 12
    • 0025738363 scopus 로고
    • Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli
    • Davidson A.L., and Nikaido H. Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli J. Biol. Chem. 266 1991 8946 8951
    • (1991) J. Biol. Chem. , vol.266 , pp. 8946-8951
    • Davidson, A.L.1    Nikaido, H.2
  • 13
    • 0026744442 scopus 로고
    • Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli
    • Dean D.A., Hor L.I., Shuman H.A., and Nikaido H. Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli Mol. Microbiol. 6 1992 2033 2040
    • (1992) Mol. Microbiol. , vol.6 , pp. 2033-2040
    • Dean, D.A.1    Hor, L.I.2    Shuman, H.A.3    Nikaido, H.4
  • 14
    • 0033740174 scopus 로고    scopus 로고
    • Combinatorial peptide libraries reveal the ligand-binding mechanism of the oligopeptide receptor OppA of Lactococcus lactis
    • Detmers F.J., Lanfermeijer F.C., Abele R., Jack R.W., Tampe R., Konings W.N., and Poolman B. Combinatorial peptide libraries reveal the ligand-binding mechanism of the oligopeptide receptor OppA of Lactococcus lactis Proc. Natl. Acad. Sci. USA 97 2000 12487 12492
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12487-12492
    • Detmers, F.J.1    Lanfermeijer, F.C.2    Abele, R.3    Jack, R.W.4    Tampe, R.5    Konings, W.N.6    Poolman, B.7
  • 15
    • 3542996250 scopus 로고    scopus 로고
    • The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter
    • Doeven M.K., Abele R., Tampe R., and Poolman B. The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter J. Biol. Chem. 279 2004 32301 32307
    • (2004) J. Biol. Chem. , vol.279 , pp. 32301-32307
    • Doeven, M.K.1    Abele, R.2    Tampe, R.3    Poolman, B.4
  • 16
    • 21244447355 scopus 로고    scopus 로고
    • Distribution, lateral mobility and function of membrane proteins incorporated into giant unilamellar vesicles
    • Doeven M.K., Folgering J.H., Krasnikov V., Geertsma E.R., van den Bogaart G., and Poolman B. Distribution, lateral mobility and function of membrane proteins incorporated into giant unilamellar vesicles Biophys. J. 88 2005 1134 1142
    • (2005) Biophys. J. , vol.88 , pp. 1134-1142
    • Doeven, M.K.1    Folgering, J.H.2    Krasnikov, V.3    Geertsma, E.R.4    Van Den Bogaart, G.5    Poolman, B.6
  • 17
    • 4344599413 scopus 로고    scopus 로고
    • Lipid-mediated light activation of a mechanosensitive channel of large conductance
    • Folgering J.H., Kuiper J.M., de Vries A.H., Engberts J.B., and Poolman B. Lipid-mediated light activation of a mechanosensitive channel of large conductance Langmuir 20 2004 6985 6987
    • (2004) Langmuir , vol.20 , pp. 6985-6987
    • Folgering, J.H.1    Kuiper, J.M.2    De Vries, A.H.3    Engberts, J.B.4    Poolman, B.5
  • 18
    • 0034721921 scopus 로고    scopus 로고
    • Quaternary structure of the lactose transport protein of Streptococcus thermophilus in the detergent-solubilized and membrane-reconstituted state
    • Friesen R.H., Knol J., and Poolman B. Quaternary structure of the lactose transport protein of Streptococcus thermophilus in the detergent-solubilized and membrane-reconstituted state J. Biol. Chem. 275 2000 33527 33535
    • (2000) J. Biol. Chem. , vol.275 , pp. 33527-33535
    • Friesen, R.H.1    Knol, J.2    Poolman, B.3
  • 19
    • 3042733142 scopus 로고    scopus 로고
    • A new method for the reconstitution of membrane proteins into giant unilamellar vesicles
    • Girard P., Pecreaux J., Lenoir G., Falson P., Rigaud J.L., and Bassereau P. A new method for the reconstitution of membrane proteins into giant unilamellar vesicles Biophys. J. 87 2004 419 429
    • (2004) Biophys. J. , vol.87 , pp. 419-429
    • Girard, P.1    Pecreaux, J.2    Lenoir, G.3    Falson, P.4    Rigaud, J.L.5    Bassereau, P.6
  • 20
    • 0016631203 scopus 로고
    • Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range
    • Hess H.H., and Derr J.E. Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range Anal. Biochem. 63 1975 607 613
    • (1975) Anal. Biochem. , vol.63 , pp. 607-613
    • Hess, H.H.1    Derr, J.E.2
  • 21
    • 0036299012 scopus 로고    scopus 로고
    • Oligomeric state of membrane transport proteins analyzed with blue native electrophoresis and analytical ultracentrifugation
    • Heuberger E.H.M.L., Veenhoff L.M., Duurkens H.H., Friesen R.H.E., and Poolman B. Oligomeric state of membrane transport proteins analyzed with blue native electrophoresis and analytical ultracentrifugation J. Mol. Biol. 317 2002 617 626
    • (2002) J. Mol. Biol. , vol.317 , pp. 617-626
    • Heuberger, E.H.M.L.1    Veenhoff, L.M.2    Duurkens, H.H.3    Friesen, R.H.E.4    Poolman, B.5
  • 23
    • 0038392418 scopus 로고    scopus 로고
    • The preservation of liposomes by raffinose family oligosaccharides during drying is mediated by effects on fusion and lipid phase transitions
    • Hincha D.K., Zuther E., and Heyer A.G. The preservation of liposomes by raffinose family oligosaccharides during drying is mediated by effects on fusion and lipid phase transitions Biochim. Biophys. Acta 1612 2003 172 177
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 172-177
    • Hincha, D.K.1    Zuther, E.2    Heyer, A.G.3
  • 25
    • 0242494861 scopus 로고    scopus 로고
    • Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis
    • Horn C., Bremer E., and Schmitt L. Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis J. Mol. Biol. 334 2003 403 419
    • (2003) J. Mol. Biol. , vol.334 , pp. 403-419
    • Horn, C.1    Bremer, E.2    Schmitt, L.3
  • 26
    • 0034870954 scopus 로고    scopus 로고
    • Reconstitution of membrane proteins into giant unilamellar vesicles via peptide-induced fusion
    • Kahya N., Pecheur E.I., de Boeij W.P., Wiersma D.A., and Hoekstra D. Reconstitution of membrane proteins into giant unilamellar vesicles via peptide-induced fusion Biophys. J. 81 2001 1464 1474
    • (2001) Biophys. J. , vol.81 , pp. 1464-1474
    • Kahya, N.1    Pecheur, E.I.2    De Boeij, W.P.3    Wiersma, D.A.4    Hoekstra, D.5
  • 27
    • 0041461861 scopus 로고    scopus 로고
    • Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy
    • Kahya N., Scherfeld D., Bacia K., Poolman B., and Schwille P. Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy J. Biol. Chem. 278 2003 28109 28115
    • (2003) J. Biol. Chem. , vol.278 , pp. 28109-28115
    • Kahya, N.1    Scherfeld, D.2    Bacia, K.3    Poolman, B.4    Schwille, P.5
  • 28
    • 0037131368 scopus 로고    scopus 로고
    • Spatial organization of bacteriorhodopsin in model membranes: Light-induced mobility changes
    • Kahya N., Wiersma D.A., Poolman B., and Hoekstra D. Spatial organization of bacteriorhodopsin in model membranes: Light-induced mobility changes J. Biol. Chem. 277 2002 39304 39311
    • (2002) J. Biol. Chem. , vol.277 , pp. 39304-39311
    • Kahya, N.1    Wiersma, D.A.2    Poolman, B.3    Hoekstra, D.4
  • 29
    • 4744343547 scopus 로고    scopus 로고
    • A heteromeric complex of the two nucleotide binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) mediates ATPase activity
    • Kidd J.F., Ramjeesingh M., Stratford F., Huan L.J., and Bear C.E. A heteromeric complex of the two nucleotide binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) mediates ATPase activity J. Biol. Chem. 279 2004 41664 41669
    • (2004) J. Biol. Chem. , vol.279 , pp. 41664-41669
    • Kidd, J.F.1    Ramjeesingh, M.2    Stratford, F.3    Huan, L.J.4    Bear, C.E.5
  • 30
    • 0032541971 scopus 로고    scopus 로고
    • Detergent-mediated reconstitution of membrane proteins
    • Knol J., Sjollema K., and Poolman B. Detergent-mediated reconstitution of membrane proteins Biochemistry 37 1998 16410 16415
    • (1998) Biochemistry , vol.37 , pp. 16410-16415
    • Knol, J.1    Sjollema, K.2    Poolman, B.3
  • 31
    • 0029897240 scopus 로고    scopus 로고
    • Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus
    • Knol J., Veenhoff L., Liang W.J., Henderson P.J., Leblanc G., and Poolman B. Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus J. Biol. Chem. 271 1996 15358 15366
    • (1996) J. Biol. Chem. , vol.271 , pp. 15358-15366
    • Knol, J.1    Veenhoff, L.2    Liang, W.J.3    Henderson, P.J.4    Leblanc, G.5    Poolman, B.6
  • 32
    • 0034679818 scopus 로고    scopus 로고
    • On the binding mechanism of the peptide receptor of the oligopeptide transport system of Lactococcus lactis
    • Lanfermeijer F.C., Detmers F.J., Konings W.N., and Poolman B. On the binding mechanism of the peptide receptor of the oligopeptide transport system of Lactococcus lactis EMBO J. 19 2000 3649 3656
    • (2000) EMBO J. , vol.19 , pp. 3649-3656
    • Lanfermeijer, F.C.1    Detmers, F.J.2    Konings, W.N.3    Poolman, B.4
  • 33
    • 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
  • 34
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • LeMaire M., Champeil P., and Moller J.V. Interaction of membrane proteins and lipids with solubilizing detergents Biochim. Biophys. Acta 1508 2000 86 111
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Lemaire, M.1    Champeil, P.2    Moller, J.V.3
  • 35
    • 0022348630 scopus 로고
    • Characterization of the solubilization of lipid bilayers by surfactants
    • Lichtenberg D. Characterization of the solubilization of lipid bilayers by surfactants Biochim. Biophys. Acta 821 1985 470 478
    • (1985) Biochim. Biophys. Acta , vol.821 , pp. 470-478
    • Lichtenberg, D.1
  • 36
    • 0033534452 scopus 로고    scopus 로고
    • Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex: Effect of different ligands and consequences for the mechanism of action
    • Liu C.E., Liu P.Q., Wolf A., Lin E., and Ames G.F. Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex: Effect of different ligands and consequences for the mechanism of action J. Biol. Chem. 274 1999 739 747
    • (1999) J. Biol. Chem. , vol.274 , pp. 739-747
    • Liu, C.E.1    Liu, P.Q.2    Wolf, A.3    Lin, E.4    Ames, G.F.5
  • 37
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher K.P., Lee A.T., and Rees D.C. The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism Science 296 2002 1091 1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 38
    • 4544337748 scopus 로고    scopus 로고
    • YdaG and ydbA of Lactococcus lactis encode a heterodimeric ATP-binding cassette-type multidrug transporter
    • Lubelski J., Mazurkiewicz P., van Merkerk R., Konings W.N., and Driessen A.J. ydaG and ydbA of Lactococcus lactis encode a heterodimeric ATP-binding cassette-type multidrug transporter J. Biol. Chem. 279 2004 34449 34455
    • (2004) J. Biol. Chem. , vol.279 , pp. 34449-34455
    • Lubelski, J.1    Mazurkiewicz, P.2    Van Merkerk, R.3    Konings, W.N.4    Driessen, A.J.5
  • 39
    • 12144262818 scopus 로고    scopus 로고
    • Interaction of LDS-751 with P-glycoprotein and mapping of the location of the R drug binding site
    • Lugo M.R., and Sharom F.J. Interaction of LDS-751 with P-glycoprotein and mapping of the location of the R drug binding site Biochemistry 44 2005 643 655
    • (2005) Biochemistry , vol.44 , pp. 643-655
    • Lugo, M.R.1    Sharom, F.J.2
  • 40
    • 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., Putman M., van Veen H.W., and Konings W.N. The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids Biochemistry 38 1999 16298 16306
    • (1999) Biochemistry , vol.38 , pp. 16298-16306
    • Margolles, A.1    Putman, M.2    Van Veen, H.W.3    Konings, W.N.4
  • 41
    • 85190568395 scopus 로고    scopus 로고
    • University of Groningen The Netherlands
    • Mazurkiewicz P. 2004 University of Groningen The Netherlands
    • (2004)
    • Mazurkiewicz, P.1
  • 42
    • 0020768255 scopus 로고
    • Firefly and bacterial luminescence: Basic science and applications
    • McElroy W.D., and DeLuca M.A. Firefly and bacterial luminescence: Basic science and applications J. Appl. Biochem. 3 1983 197 209
    • (1983) J. Appl. Biochem. , vol.3 , pp. 197-209
    • McElroy, W.D.1    Deluca, M.A.2
  • 43
    • 0021062151 scopus 로고
    • Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis
    • Miller D.M., Olson J.S., Pflugrath J.W., and Quiocho F.A. Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis J. Biol. Chem. 258 1983 13665 13672
    • (1983) J. Biol. Chem. , vol.258 , pp. 13665-13672
    • Miller, D.M.1    Olson, J.S.2    Pflugrath, J.W.3    Quiocho, F.A.4
  • 44
    • 0027283560 scopus 로고
    • Detergent binding as a measure of hydrophobic surface area of integral membrane proteins
    • Moller J.V., and LeMaire M. Detergent binding as a measure of hydrophobic surface area of integral membrane proteins J. Biol. Chem. 268 1993 18659 18672
    • (1993) J. Biol. Chem. , vol.268 , pp. 18659-18672
    • Moller, J.V.1    Lemaire, M.2
  • 45
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu H.C., and Heppel L.A. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts J. Biol. Chem. 240 1965 3685 3692
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 46
    • 0019122765 scopus 로고
    • Solubilization and reconstitution of the lactose transport system from Escherichia coli
    • Newman N.J., and Wilson T.H. Solubilization and reconstitution of the lactose transport system from Escherichia coli J. Biol. Chem. 255 1980 10583 10586
    • (1980) J. Biol. Chem. , vol.255 , pp. 10583-10586
    • Newman, N.J.1    Wilson, T.H.2
  • 47
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • Patzlaff J.S., van der Heide T., and Poolman B. The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA J. Biol. Chem. 278 2003 29546 29551
    • (2003) J. Biol. Chem. , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    Van Der Heide, T.2    Poolman, B.3
  • 48
    • 7044274624 scopus 로고    scopus 로고
    • Bacterial osmosensing: Roles of membrane structure and electrostatics in lipid-protein and protein-protein interactions
    • Poolman B., Spitzer J., and Wood J.M. Bacterial osmosensing: Roles of membrane structure and electrostatics in lipid-protein and protein-protein interactions Biochim. Biophys. Acta 1666 2004 88 104
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 88-104
    • Poolman, B.1    Spitzer, J.2    Wood, J.M.3
  • 49
    • 0024604620 scopus 로고
    • Reconstitution of the histidine periplasmic transport system in membrane vesicles: Energy coupling and interaction between the binding protein and the membrane complex
    • Prossnitz E., Gee A., and Ames G.F. Reconstitution of the histidine periplasmic transport system in membrane vesicles: Energy coupling and interaction between the binding protein and the membrane complex J. Biol. Chem. 264 1989 5006 5014
    • (1989) J. Biol. Chem. , vol.264 , pp. 5006-5014
    • Prossnitz, E.1    Gee, A.2    Ames, G.F.3
  • 51
    • 0033579808 scopus 로고    scopus 로고
    • Restrictive use of detergents in the functional reconstitution of the secondary multidrug transporter LmrP
    • Putman M., van Veen H.W., Poolman B., and Konings W.N. Restrictive use of detergents in the functional reconstitution of the secondary multidrug transporter LmrP Biochemistry 38 1999 1002 1008
    • (1999) Biochemistry , vol.38 , pp. 1002-1008
    • Putman, M.1    Van Veen, H.W.2    Poolman, B.3    Konings, W.N.4
  • 52
    • 0037417765 scopus 로고    scopus 로고
    • Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle
    • Qu Q., Russell P.L., and Sharom F.J. Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle Biochemistry 42 2003 1170 1177
    • (2003) Biochemistry , vol.42 , pp. 1170-1177
    • Qu, Q.1    Russell, P.L.2    Sharom, F.J.3
  • 53
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho F.A., and Ledvina P.S. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes Mol. Microbiol. 20 1996 17 25
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 55
    • 0031788294 scopus 로고    scopus 로고
    • Purification and reconstitution of epithelial chloride channel cystic fibrosis transmembrane conductance regulator
    • Ramjeesingh M., Garami E., Galley K., Li C., Wang Y., and Bear C.E. Purification and reconstitution of epithelial chloride channel cystic fibrosis transmembrane conductance regulator Methods Enzymol. 294 1999 227 246
    • (1999) Methods Enzymol. , vol.294 , pp. 227-246
    • Ramjeesingh, M.1    Garami, E.2    Galley, K.3    Li, C.4    Wang, Y.5    Bear, C.E.6
  • 57
    • 0021101390 scopus 로고
    • Study of binding protein-ligand interaction by ammonium sulfate-assisted adsorption on cellulose esters filters
    • Richarme G., and Kepes A. Study of binding protein-ligand interaction by ammonium sulfate-assisted adsorption on cellulose esters filters Biochim. Biophys. Acta 742 1983 16 24
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 16-24
    • Richarme, G.1    Kepes, A.2
  • 59
    • 0242317916 scopus 로고    scopus 로고
    • Reconstitution of membrane proteins into liposomes
    • Rigaud J.L., and Levy D. Reconstitution of membrane proteins into liposomes Methods Enzymol. 372 2003 65 86
    • (2003) Methods Enzymol. , vol.372 , pp. 65-86
    • Rigaud, J.L.1    Levy, D.2
  • 60
    • 0024291663 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 2. Incorporation of the light-driven proton pump bacteriorhodopsin
    • Rigaud J.L., Paternostre M.T., and Bluzat A. Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 2. Incorporation of the light-driven proton pump bacteriorhodopsin Biochemistry 27 1988 2677 2688
    • (1988) Biochemistry , vol.27 , pp. 2677-2688
    • Rigaud, J.L.1    Paternostre, M.T.2    Bluzat, A.3
  • 62
    • 21244499439 scopus 로고    scopus 로고
    • GlnPQ from Lactococcus lactis: An ABC transporter with four extracytoplasmic substrate-binding domains
    • Schuurman-Wolters G.K., and Poolman B. GlnPQ from Lactococcus lactis: An ABC transporter with four extracytoplasmic substrate-binding domains J. Biol. Chem 280 2005 23785 23790
    • (2005) J. Biol. Chem , vol.280 , pp. 23785-23790
    • Schuurman-wolters, G.K.1    Poolman, B.2
  • 65
    • 0028987131 scopus 로고
    • Lipoproteins of gram-positive bacteria
    • Sutcliffe I.C., and Russell R.R. Lipoproteins of gram-positive bacteria J. Bacteriol. 177 1995 1123 1128
    • (1995) J. Bacteriol. , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.2
  • 66
    • 8344241152 scopus 로고    scopus 로고
    • How do ABC transporters drive transport?
    • van der Does C., and Tampé R. How do ABC transporters drive transport? Biol. Chem. 385 2004 927 933
    • (2004) Biol. Chem. , vol.385 , pp. 927-933
    • Van Der Does, C.1    Tampé, R.2
  • 67
    • 0034691129 scopus 로고    scopus 로고
    • Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane
    • van der Heide T., and Poolman B. Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane Proc. Natl. Acad. Sci. USA 97 2000 7102 7106
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7102-7106
    • Van Der Heide, T.1    Poolman, B.2
  • 68
    • 0036774002 scopus 로고    scopus 로고
    • ABC transporters: One, two or four extracytoplasmic substrate-binding sites?
    • van der Heide T., and Poolman B. ABC transporters: One, two or four extracytoplasmic substrate-binding sites? EMBO Rep. 3 2002 938 943
    • (2002) EMBO Rep. , vol.3 , pp. 938-943
    • Van Der Heide, T.1    Poolman, B.2
  • 69
    • 0037126588 scopus 로고    scopus 로고
    • On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine
    • van der Heide T., Stuart M.C., and Poolman B. On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine EMBO J. 20 2001 7022 7032
    • (2001) EMBO J. , vol.20 , pp. 7022-7032
    • Van Der Heide, T.1    Stuart, M.C.2    Poolman, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.