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Volumn 21, Issue 7, 2010, Pages 1321-1330

Kinetic analysis of his-tagged protein binding to nickel-chelating nanolipoprotein particles

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; CHELATING AGENT; LIPOPROTEIN; MEMBRANE PROTEIN; NANOPARTICLE; NICKEL;

EID: 77954879671     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc100129s     Document Type: Article
Times cited : (26)

References (53)
  • 1
    • 0037205467 scopus 로고    scopus 로고
    • Structure of apolipophorin-III in discoidal lipoproteins - Interhelical distances in the lipid-bound state and conformational change upon binding to lipid
    • Garda, H. A., Arrese, E. L., and Soulages, J. L. (2002) Structure of apolipophorin-III in discoidal lipoproteins-Interhelical distances in the lipid-bound state and conformational change upon binding to lipid J. Biol. Chem. 277, 19773-19782
    • (2002) J. Biol. Chem. , vol.277 , pp. 19773-19782
    • Garda, H.A.1    Arrese, E.L.2    Soulages, J.L.3
  • 2
    • 0022556101 scopus 로고
    • Reconstitution of high-density-lipoproteins
    • Jonas, A. (1986) Reconstitution of high-density-lipoproteins Methods Enzymol. 128, 553-582
    • (1986) Methods Enzymol. , vol.128 , pp. 553-582
    • Jonas, A.1
  • 3
    • 0021154044 scopus 로고
    • Discoidal complexes of a and C apolipoproteins with lipids and their reactions with lecithin-cholesterol acyltransferase
    • Jonas, A., Sweeny, S. A., and Herbert, P. N. (1984) Discoidal complexes of a and C apolipoproteins with lipids and their reactions with lecithin-cholesterol acyltransferase J. Biol. Chem. 259, 6369-6375
    • (1984) J. Biol. Chem. , vol.259 , pp. 6369-6375
    • Jonas, A.1    Sweeny, S.A.2    Herbert, P.N.3
  • 4
    • 0034617305 scopus 로고    scopus 로고
    • Reorganization of the four-helix bundle of human apolipoprotein e in binding to phospholipid
    • Lu, B., Morrow, J. A., and Weisgraber, K. H. (2000) Reorganization of the four-helix bundle of human apolipoprotein E in binding to phospholipid J. Biol. Chem. 275, 20775-20781
    • (2000) J. Biol. Chem. , vol.275 , pp. 20775-20781
    • Lu, B.1    Morrow, J.A.2    Weisgraber, K.H.3
  • 5
    • 0025202156 scopus 로고
    • Structure of apolipoprotein-a-I in 3 homogeneous, reconstituted high-density-lipoprotein particles
    • Wald, J. H., Krul, E. S., and Jonas, A. (1990) Structure of apolipoprotein-a-I in 3 homogeneous, reconstituted high-density-lipoprotein particles J. Biol. Chem. 265, 20037-20043
    • (1990) J. Biol. Chem. , vol.265 , pp. 20037-20043
    • Wald, J.H.1    Krul, E.S.2    Jonas, A.3
  • 11
    • 33744928866 scopus 로고    scopus 로고
    • Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs
    • Bayburt, T. H., Grinkova, Y. V., and Sligar, S. G. (2006) Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs Arch. Biochem. Biophys. 450, 215-222
    • (2006) Arch. Biochem. Biophys. , vol.450 , pp. 215-222
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 13
    • 0142179052 scopus 로고    scopus 로고
    • Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers
    • Bayburt, T. H. and Sligar, S. G. (2003) Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers Protein Sci. 12, 2476-2481
    • (2003) Protein Sci. , vol.12 , pp. 2476-2481
    • Bayburt, T.H.1    Sligar, S.G.2
  • 14
    • 0037076392 scopus 로고    scopus 로고
    • Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks
    • Bayburt, T. H. and Sligar, S. G. (2002) Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks Proc. Natl. Acad. Sci. U.S.A. 99, 6725-30
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6725-6730
    • Bayburt, T.H.1    Sligar, S.G.2
  • 15
    • 0032170742 scopus 로고    scopus 로고
    • Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer
    • Bayburt, T. H., Carlson, J. W., and Sligar, S. G. (1998) Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer J. Struct. Biol. 123, 37-44
    • (1998) J. Struct. Biol. , vol.123 , pp. 37-44
    • Bayburt, T.H.1    Carlson, J.W.2    Sligar, S.G.3
  • 16
    • 33745511381 scopus 로고    scopus 로고
    • Functional reconstitution of beta2-adrenergic receptors utilizing self-assembling Nanodisc technology
    • Leitz, A. J., Bayburt, T. H., Barnakov, A. N., Springer, B. A., and Sligar, S. G. (2006) Functional reconstitution of beta2-adrenergic receptors utilizing self-assembling Nanodisc technology Biotechniques 40, 601-602
    • (2006) Biotechniques , vol.40 , pp. 601-602
    • Leitz, A.J.1    Bayburt, T.H.2    Barnakov, A.N.3    Springer, B.A.4    Sligar, S.G.5
  • 17
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • Whorton, M. R., Bokoch, M. P., Rasmussen, S. G., Huang, B., Zare, R. N., Kobilka, B., and Sunahara, R. K. (2007) A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein Proc. Natl. Acad. Sci. U.S.A. 104, 7682-7
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5    Kobilka, B.6    Sunahara, R.K.7
  • 19
    • 71749095971 scopus 로고    scopus 로고
    • Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs
    • Raschle, T., Hiller, S., Yu, T. Y., Rice, A. J., Walz, T., and Wagner, G. (2009) Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs J. Am. Chem. Soc. 131, 17777-17779
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17777-17779
    • Raschle, T.1    Hiller, S.2    Yu, T.Y.3    Rice, A.J.4    Walz, T.5    Wagner, G.6
  • 20
    • 34250816490 scopus 로고    scopus 로고
    • Kinetic properties of recombinant MAO-A on incorporation into phospholipid nanodisks
    • Cruz, F. and Edmondson, D. E. (2007) Kinetic properties of recombinant MAO-A on incorporation into phospholipid nanodisks J. Neural. Transm. 114, 699-702
    • (2007) J. Neural. Transm. , vol.114 , pp. 699-702
    • Cruz, F.1    Edmondson, D.E.2
  • 22
    • 55749092466 scopus 로고    scopus 로고
    • Nanodisks derived from amphotericin B lipid complex
    • Tufteland, M., Ren, G., and Ryan, R. O. (2008) Nanodisks derived from amphotericin B lipid complex J. Pharm. Sci. 97, 4425-4432
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4425-4432
    • Tufteland, M.1    Ren, G.2    Ryan, R.O.3
  • 25
    • 36049049858 scopus 로고    scopus 로고
    • Synthetic nano-LDL with paclitaxel oleate as a targeted drug delivery vehicle for glioblastoma multiforme
    • DOI 10.1016/j.jconrel.2007.09.007, PII S016836590700497X
    • Nikanjam, M., Gibbs, A. R., Hunt, C. A., Budinger, T. F., and Forte, T. M. (2007) Synthetic nano-LDL with paclitaxel oleate as a targeted drug delivery vehicle for glioblastoma multiforme J. Controlled Release 124, 163-171 (Pubitemid 350101886)
    • (2007) Journal of Controlled Release , vol.124 , Issue.3 , pp. 163-171
    • Nikanjam, M.1    Gibbs, A.R.2    Hunt, C.A.3    Budinger, T.F.4    Forte, T.M.5
  • 27
    • 33750524021 scopus 로고    scopus 로고
    • Properties of a versatile nanoparticle platform contrast agent to image and characterize atherosclerotic plaques by magnetic resonance imaging
    • Frias, J. C., Ma, Y., Williams, K. J., Fayad, Z. A., and Fisher, E. A. (2006) Properties of a versatile nanoparticle platform contrast agent to image and characterize atherosclerotic plaques by magnetic resonance imaging Nano Lett. 6, 2220-2224
    • (2006) Nano Lett. , vol.6 , pp. 2220-2224
    • Frias, J.C.1    Ma, Y.2    Williams, K.J.3    Fayad, Z.A.4    Fisher, E.A.5
  • 28
    • 0022262772 scopus 로고
    • Activation of lecithin-cholesterol acyltransferase by human apolipoprotein-E in discoidal complexes with lipids
    • Zorich, N., Jonas, A., and Pownall, H. J. (1985) Activation of lecithin-cholesterol acyltransferase by human apolipoprotein-E in discoidal complexes with lipids J. Biol. Chem. 260, 8831-8837
    • (1985) J. Biol. Chem. , vol.260 , pp. 8831-8837
    • Zorich, N.1    Jonas, A.2    Pownall, H.J.3
  • 29
    • 0037062581 scopus 로고    scopus 로고
    • Complex of human apolipoprotein C-1 with phospholipid: Thermodynamic or kinetic stability
    • Gursky, O., Ranjana, and Gantz, D. L. (2002) Complex of human apolipoprotein C-1 with phospholipid: thermodynamic or kinetic stability Biochemistry 41, 7373-7384
    • (2002) Biochemistry , vol.41 , pp. 7373-7384
    • Gursky, O.1    Ranjana2    Gantz, D.L.3
  • 30
    • 0028108646 scopus 로고
    • Binding of insect apolipophorin-III to dimyristoylphosphatidylcholine vesicles: Evidence for a conformational change
    • Wientzek, M., Kay, C. M., Oikawa, K., and Ryan, R. O. (1994) Binding of insect apolipophorin-III to dimyristoylphosphatidylcholine vesicles: evidence for a conformational change J. Biol. Chem. 269, 4605-4612
    • (1994) J. Biol. Chem. , vol.269 , pp. 4605-4612
    • Wientzek, M.1    Kay, C.M.2    Oikawa, K.3    Ryan, R.O.4
  • 33
    • 0026071781 scopus 로고
    • Metal-affinity separations: A new dimension in protein processing
    • Arnold, F. H. (1991) Metal-affinity separations: a new dimension in protein processing Biotechnology (N.Y.) 9, 151-156
    • (1991) Biotechnology (N.Y.) , vol.9 , pp. 151-156
    • Arnold, F.H.1
  • 34
    • 33646540098 scopus 로고    scopus 로고
    • Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on ni-nitrilotriacetic acid surfaces
    • Khan, F., He, M., and Taussig, M. J. (2006) Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on ni-nitrilotriacetic acid surfaces Anal. Chem. 78, 3072-3079
    • (2006) Anal. Chem. , vol.78 , pp. 3072-3079
    • Khan, F.1    He, M.2    Taussig, M.J.3
  • 35
    • 0030077272 scopus 로고    scopus 로고
    • A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance
    • Sigal, G. B., Bamdad, C., Barberis, A., Strominger, J., and Whitesides, G. M. (1996) A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance Anal. Chem. 68, 490-497
    • (1996) Anal. Chem. , vol.68 , pp. 490-497
    • Sigal, G.B.1    Bamdad, C.2    Barberis, A.3    Strominger, J.4    Whitesides, G.M.5
  • 37
    • 0031696253 scopus 로고    scopus 로고
    • Orientation and two-dimensional organization of proteins at chelator lipid interfaces
    • Dorn, I. T., Pawlitschko, K., Pettinger, S. C., and Tampe, R. (1998) Orientation and two-dimensional organization of proteins at chelator lipid interfaces Biol. Chem. 379, 1151-1159
    • (1998) Biol. Chem. , vol.379 , pp. 1151-1159
    • Dorn, I.T.1    Pawlitschko, K.2    Pettinger, S.C.3    Tampe, R.4
  • 40
    • 50049101521 scopus 로고    scopus 로고
    • Nanodiscs for immobilization of lipid bilayers and membrane receptors: Kinetic analysis of cholera toxin binding to a glycolipid receptor
    • Borch, J., Torta, F., Sligar, S. G., and Roepstorff, P. (2008) Nanodiscs for immobilization of lipid bilayers and membrane receptors: kinetic analysis of cholera toxin binding to a glycolipid receptor Anal. Chem. 80, 6245-6252
    • (2008) Anal. Chem. , vol.80 , pp. 6245-6252
    • Borch, J.1    Torta, F.2    Sligar, S.G.3    Roepstorff, P.4
  • 41
    • 0034650303 scopus 로고    scopus 로고
    • A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors
    • Cooper, M. A., Hansson, A., Lofas, S., and Williams, D. H. (2000) A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors Anal. Biochem. 277, 196-205
    • (2000) Anal. Biochem. , vol.277 , pp. 196-205
    • Cooper, M.A.1    Hansson, A.2    Lofas, S.3    Williams, D.H.4
  • 42
    • 3242688104 scopus 로고    scopus 로고
    • Surface plasmon resonance studies of the direct interaction between a drug/intestinal brush border membrane
    • Kim, K., Cho, S. P., Park, J. H., Byun, Y. R., Chung, H., Kwon, I. C., and Jeong, S. Y. (2004) Surface plasmon resonance studies of the direct interaction between a drug/intestinal brush border membrane Pharm. Res. 21, 1233-1239
    • (2004) Pharm. Res. , vol.21 , pp. 1233-1239
    • Kim, K.1    Cho, S.P.2    Park, J.H.3    Byun, Y.R.4    Chung, H.5    Kwon, I.C.6    Jeong, S.Y.7
  • 43
    • 27644593434 scopus 로고    scopus 로고
    • Properties of nonfused liposomes immobilized on an L1 Biacore chip and their permeabilization by a eukaryotic pore-forming toxin
    • Anderluh, G., Besenicar, M., Kladnik, A., Lakey, J. H., and Macek, P. (2005) Properties of nonfused liposomes immobilized on an L1 Biacore chip and their permeabilization by a eukaryotic pore-forming toxin Anal. Biochem. 344, 43-52
    • (2005) Anal. Biochem. , vol.344 , pp. 43-52
    • Anderluh, G.1    Besenicar, M.2    Kladnik, A.3    Lakey, J.H.4    MacEk, P.5
  • 44
    • 0034630369 scopus 로고    scopus 로고
    • Characterization of the surfaces generated by liposome binding to the modified dextran matrix of a surface plasmon resonance sensor chip
    • Erb, E. M., Chen, X. Y., Allen, S., Roberts, C. J., Tendler, S. J. B., Davies, M. C., and Forsen, S. (2000) Characterization of the surfaces generated by liposome binding to the modified dextran matrix of a surface plasmon resonance sensor chip Anal. Biochem. 280, 29-35
    • (2000) Anal. Biochem. , vol.280 , pp. 29-35
    • Erb, E.M.1    Chen, X.Y.2    Allen, S.3    Roberts, C.J.4    Tendler, S.J.B.5    Davies, M.C.6    Forsen, S.7
  • 45
    • 70349140553 scopus 로고    scopus 로고
    • Tris-nitrilotriacetic acids of subnanomolar affinity toward hexahistidine tagged molecules
    • Huang, Z. H., Hwang, P., Watson, D. S., Cao, L. M., and Szoka, F. C. (2009) Tris-nitrilotriacetic acids of subnanomolar affinity toward hexahistidine tagged molecules Bioconjugate Chem. 20, 1667-1672
    • (2009) Bioconjugate Chem. , vol.20 , pp. 1667-1672
    • Huang, Z.H.1    Hwang, P.2    Watson, D.S.3    Cao, L.M.4    Szoka, F.C.5
  • 46
    • 34250816490 scopus 로고    scopus 로고
    • Kinetic properties of recombinant MAO-A on incorporation into phospholipid nanodisks
    • Cruz, F. and Edmondson, D. E. (2007) Kinetic properties of recombinant MAO-A on incorporation into phospholipid nanodisks J. Neural Transm. 114, 699-702
    • (2007) J. Neural Transm. , vol.114 , pp. 699-702
    • Cruz, F.1    Edmondson, D.E.2
  • 48
    • 0032053630 scopus 로고    scopus 로고
    • Molecular recognition of histidine-tagged molecules by metal-chelating lipids monitored by fluorescence energy transfer and correlation spectroscopy
    • Dorn, I. T., Neumaier, K. R., and Tampe, R. (1998) Molecular recognition of histidine-tagged molecules by metal-chelating lipids monitored by fluorescence energy transfer and correlation spectroscopy J. Am. Chem. Soc. 120, 2753-2763
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 2753-2763
    • Dorn, I.T.1    Neumaier, K.R.2    Tampe, R.3
  • 49
    • 0035814333 scopus 로고    scopus 로고
    • Site-specific incorporation of fluorescent probes into protein: Hexahistidine-tag-mediated fluorescent labeling with (Ni2+: Nitrilotriacetic acid)(n)-fluorochrome conjugates
    • Kapanidis, A. N., Ebright, Y. W., and Ebright, R. H. (2001) Site-specific incorporation of fluorescent probes into protein: Hexahistidine-tag-mediated fluorescent labeling with (Ni2+: Nitrilotriacetic acid)(n)-fluorochrome conjugates J. Am. Chem. Soc. 123, 12123-12125
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 12123-12125
    • Kapanidis, A.N.1    Ebright, Y.W.2    Ebright, R.H.3
  • 50
    • 1842582037 scopus 로고    scopus 로고
    • Reversible site-selective labeling of membrane proteins in live cells
    • DOI 10.1038/nbt954
    • Guignet, E. G., Hovius, R., and Vogel, H. (2004) Reversible site-selective labeling of membrane proteins in live cells Nat. Biotechnol. 22, 440-444 (Pubitemid 38451375)
    • (2004) Nature Biotechnology , vol.22 , Issue.4 , pp. 440-444
    • Guignet, E.G.1    Hovius, R.2    Vogel, H.3
  • 51
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size
    • Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., and Sligar, S. G. (2004) Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size J. Am. Chem. Soc. 126, 3477-3487
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 52
    • 33646540098 scopus 로고    scopus 로고
    • Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on Ni-nitrilotriacetic acid surfaces
    • Khan, F., He, M. Y., and Taussig, M. J. (2006) Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on Ni-nitrilotriacetic acid surfaces Anal. Chem. 78, 3072-3079
    • (2006) Anal. Chem. , vol.78 , pp. 3072-3079
    • Khan, F.1    He, M.Y.2    Taussig, M.J.3
  • 53
    • 22944441978 scopus 로고    scopus 로고
    • High-affinity adaptors for switchable recognition of histidine-tagged proteins
    • Lata, S., Reichel, A., Brock, R., Tampe, R., and Piehler, J. (2005) High-affinity adaptors for switchable recognition of histidine-tagged proteins J. Am. Chem. Soc. 127, 10205-10215
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10205-10215
    • Lata, S.1    Reichel, A.2    Brock, R.3    Tampe, R.4    Piehler, J.5


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