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Volumn , Issue , 2008, Pages 121-140

Probing Membrane Protein Interactions with Real-Time Biosensor Technology

Author keywords

Biophysical analysis; Extracellular domains; Interactions; Large assemblies; Membrane protein interactions; Membrane proteins; Molecular interaction; Proteins embedded in lipid layers; Real time biosensor technology; Soluble proteins with lipid layers

Indexed keywords


EID: 58349094263     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527621224.ch5     Document Type: Chapter
Times cited : (5)

References (43)
  • 1
    • 27744519033 scopus 로고    scopus 로고
    • Survey of the year 2004 commercial optical biosensor literature
    • Rich R. L., Myszka D. G. (2005) Survey of the year 2004 commercial optical biosensor literature, J. Mol. Recog. 18: 431-478.
    • (2005) J. Mol. Recog. , vol.18 , pp. 431-478
    • Rich, R.L.1    Myszka, D.G.2
  • 2
    • 33845931650 scopus 로고    scopus 로고
    • Survey of the year 2005 commercial optical biosensor literature
    • Rich R. L., Myszka D. G. (2006) Survey of the year 2005 commercial optical biosensor literature, J. Mol. Recog. 19: 478-534.
    • (2006) J. Mol. Recog. , vol.19 , pp. 478-534
    • Rich, R.L.1    Myszka, D.G.2
  • 3
    • 0036228119 scopus 로고    scopus 로고
    • Direct comparison of equilibrium, thermodynamic, and kinetic rate constants determined by surface-and solution-based biophysical methods
    • Day Y. S. N., Baird C. L., Rich R. L., Myszka D. G. (2002) Direct comparison of equilibrium, thermodynamic, and kinetic rate constants determined by surface-and solution-based biophysical methods, Protein Sci. 11: 1017-1025.
    • (2002) Protein Sci. , vol.11 , pp. 1017-1025
    • Day, Y.S.N.1    Baird, C.L.2    Rich, R.L.3    Myszka, D.G.4
  • 5
    • 1842787056 scopus 로고    scopus 로고
    • Characterizing high-affinity antigen/antibody complexes by kinetic-and equilibrium-based methods
    • Drake A. W., Myszka D. G., Klakamp S. L. (2004) Characterizing high-affinity antigen/antibody complexes by kinetic-and equilibrium-based methods, Anal. Biochem. 328: 35-43.
    • (2004) Anal. Biochem. , vol.328 , pp. 35-43
    • Drake, A.W.1    Myszka, D.G.2    Klakamp, S.L.3
  • 8
    • 33845902552 scopus 로고    scopus 로고
    • Higher-throughput, label-free, real-time molecular interaction analysis
    • Rich R. L., Myszka D. G. (2007) Higher-throughput, label-free, real-time molecular interaction analysis, Anal. Biochem. 361: 1-6.
    • (2007) Anal. Biochem. , vol.361 , pp. 1-6
    • Rich, R.L.1    Myszka, D.G.2
  • 9
    • 28244489661 scopus 로고    scopus 로고
    • Surface plasmon resonance
    • in: Methods for Structural Analysis of Protein Pharmaceuticals, Jiskoot W., Crommelin D. (Eds.), AAPS Press: Arlington, VA
    • Cannon M. J., Myszka D. G. (2005) Surface plasmon resonance, in: Methods for Structural Analysis of Protein Pharmaceuticals, Jiskoot W., Crommelin D. (Eds.), AAPS Press: Arlington, VA, pp. 527-544.
    • (2005) , pp. 527-544
    • Cannon, M.J.1    Myszka, D.G.2
  • 10
    • 33751231711 scopus 로고    scopus 로고
    • Optical biosensors: where next and how soon?
    • Cooper M. A. (2006) Optical biosensors: where next and how soon? Drug Discov. Today 11: 1061-1070.
    • (2006) Drug Discov. Today , vol.11 , pp. 1061-1070
    • Cooper, M.A.1
  • 11
    • 33749499143 scopus 로고    scopus 로고
    • Surface plasmon resonance instruments diversify
    • Mukhopadhyay R. (2005) Surface plasmon resonance instruments diversify, Anal. Chem. 77: 313A-317A.
    • (2005) Anal. Chem. , vol.77
    • Mukhopadhyay, R.1
  • 12
    • 3142567042 scopus 로고    scopus 로고
    • Advances in membrane receptor screening and analysis
    • Cooper M. A. (2004) Advances in membrane receptor screening and analysis, J. Mol. Recog. 17: 286-315.
    • (2004) J. Mol. Recog. , vol.17 , pp. 286-315
    • Cooper, M.A.1
  • 13
    • 33746728985 scopus 로고    scopus 로고
    • Surface plasmon resonance in protein-membrane interactions
    • Besenidar M., Madek P., Lakey J. H., Anderluh G. (2006) Surface plasmon resonance in protein-membrane interactions, Chem. Phys. Lipids 141: 169-178.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 169-178
    • Besenidar, M.1    Madek, P.2    Lakey, J.H.3    Anderluh, G.4
  • 14
    • 0036391231 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy: an emerging tool for the study of peptide-membrane interactions
    • Mozsolits H., Aguilar M.-I. (2002) Surface plasmon resonance spectroscopy: an emerging tool for the study of peptide-membrane interactions, Biopolymers (Peptide Science) 66: 3-18.
    • (2002) Biopolymers (Peptide Science) , vol.66 , pp. 3-18
    • Mozsolits, H.1    Aguilar, M.-I.2
  • 15
    • 23944492861 scopus 로고    scopus 로고
    • Surface plasmon resonance: applications in understanding receptor-ligand interaction
    • Pattnaik P. (2005) Surface plasmon resonance: applications in understanding receptor-ligand interaction, Appl. Biochem. Biotechnol. 126: 79-92.
    • (2005) Appl. Biochem. Biotechnol. , vol.126 , pp. 79-92
    • Pattnaik, P.1
  • 16
    • 0027132013 scopus 로고
    • Comparison of a structural and functional epitope
    • Cunningham B. C., Wells J. A. (1993) Comparison of a structural and functional epitope, J. Mol. Biol. 234: 554-563.
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 17
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., Wells J. A. (1995) A hot spot of binding energy in a hormone-receptor interface, Science 267: 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 19
    • 0030448925 scopus 로고    scopus 로고
    • Kinetic analysis of ligand binding to interleukin-2 receptor complexes created on an optical biosensor surface
    • Myszka D. G., Arulanantham P. R., Sana T., Wu Z., Morton T. A., Ciardelli T. L. (1996) Kinetic analysis of ligand binding to interleukin-2 receptor complexes created on an optical biosensor surface, Protein Sci. 5: 2468-2478.
    • (1996) Protein Sci. , vol.5 , pp. 2468-2478
    • Myszka, D.G.1    Arulanantham, P.R.2    Sana, T.3    Wu, Z.4    Morton, T.A.5    Ciardelli, T.L.6
  • 21
    • 30144433991 scopus 로고    scopus 로고
    • Oligomerization of Clostridium perfringens ε-toxin is dependent upon membrane fluidity in liposomes
    • Nagahama M., Hara H., Fernandez-Miyakawa M., Itohayashi Y., Sakurai J. (2006) Oligomerization of Clostridium perfringens ε-toxin is dependent upon membrane fluidity in liposomes, Biochemistry 45: 296-302.
    • (2006) Biochemistry , vol.45 , pp. 296-302
    • Nagahama, M.1    Hara, H.2    Fernandez-Miyakawa, M.3    Itohayashi, Y.4    Sakurai, J.5
  • 22
    • 33749060200 scopus 로고    scopus 로고
    • Steroid structural requirements for interaction of ostreolysin, a lipid-raft binding cytolysin, with lipid monolayers and bilayers
    • Rebolj K., Ulrih N. P., Macek P., Sepdic K. (2006) Steroid structural requirements for interaction of ostreolysin, a lipid-raft binding cytolysin, with lipid monolayers and bilayers, Biochim. Biophys. Acta 1758: 1662-1670.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1662-1670
    • Rebolj, K.1    Ulrih, N.P.2    Macek, P.3    Sepdic, K.4
  • 23
    • 1942540796 scopus 로고    scopus 로고
    • Supine orientation of a murine MHC class I molecule on the membrane bilayer
    • Mitra A. K., Célia H., Ren G., Luz J. G., Wilson I. A., Teyton L. (2004) Supine orientation of a murine MHC class I molecule on the membrane bilayer, Curr. Biol. 14: 718-724.
    • (2004) Curr. Biol. , vol.14 , pp. 718-724
    • Mitra, A.K.1    Célia, H.2    Ren, G.3    Luz, J.G.4    Wilson, I.A.5    Teyton, L.6
  • 25
    • 0034650303 scopus 로고    scopus 로고
    • A vesicle capture sensor chip for kinetic analysis of binding to membrane-bound receptors
    • Cooper M. A., Hansson A., Löfås S., Williams D. H. (2000) A vesicle capture sensor chip for kinetic analysis of binding to membrane-bound receptors, A nal. Biochem. 277: 196-205.
    • (2000) A nal. Biochem. , vol.277 , pp. 196-205
    • Cooper, M.A.1    Hansson, A.2    Löfås, S.3    Williams, D.H.4
  • 26
    • 27644593434 scopus 로고    scopus 로고
    • Properties of nonfused liposomes immobilized on an L1 Biacore chip and their permabilization by a eukaryotic pore-forming toxin
    • Anderluh G., Besenidar M., Kladnik A., Lakey J. H., Madek P. (2005) Properties of nonfused liposomes immobilized on an L1 Biacore chip and their permabilization by a eukaryotic pore-forming toxin, Anal. Biochem. 344: 43-52.
    • (2005) Anal. Biochem. , vol.344 , pp. 43-52
    • Anderluh, G.1    Besenidar, M.2    Kladnik, A.3    Lakey, J.H.4    Madek, P.5
  • 27
    • 0036853993 scopus 로고    scopus 로고
    • Surface plasmon resonance characterization of drug-liposome interactions
    • Baird C. L., Courtenay E. S., Myszka D. G. (2002) Surface plasmon resonance characterization of drug-liposome interactions, Anal. Biochem. 310: 93-99.
    • (2002) Anal. Biochem. , vol.310 , pp. 93-99
    • Baird, C.L.1    Courtenay, E.S.2    Myszka, D.G.3
  • 28
    • 2142767300 scopus 로고    scopus 로고
    • Probing the mechanism of drug/lipid membrane interactions using Biacore
    • Abdiche Y. N., Myszka D. G. (2004) Probing the mechanism of drug/lipid membrane interactions using Biacore, Anal. Biochem. 328: 233-243.
    • (2004) Anal. Biochem. , vol.328 , pp. 233-243
    • Abdiche, Y.N.1    Myszka, D.G.2
  • 30
    • 33747036119 scopus 로고    scopus 로고
    • Lipidation and glycosylation of a T cell antigen receptor (TCR) transmembrane hydrophobic peptide dramatically enhances in vitro and in vivo function
    • Amon M. A., Ali M., Bender V., Chan Y.-N., Toth I., Manolios N. (2006) Lipidation and glycosylation of a T cell antigen receptor (TCR) transmembrane hydrophobic peptide dramatically enhances in vitro and in vivo function, Biochim. Biophys. Acta 1763: 879-888.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 879-888
    • Amon, M.A.1    Ali, M.2    Bender, V.3    Chan, Y.-N.4    Toth, I.5    Manolios, N.6
  • 33
    • 33644834349 scopus 로고    scopus 로고
    • Cleavage of epidermal growth factor by caspase during apoptosis is independent of its internalization
    • He Y.-Y., Huang J.-L., Chignell C. F. (2006) Cleavage of epidermal growth factor by caspase during apoptosis is independent of its internalization, Oncogene 25: 1521-1531.
    • (2006) Oncogene , vol.25 , pp. 1521-1531
    • He, Y.-Y.1    Huang, J.-L.2    Chignell, C.F.3
  • 34
    • 0034633660 scopus 로고    scopus 로고
    • A biosensor assay for studying ligand-membrane receptor interactions: Binding of antibodies and HIV-1 Env to chemokine receptors
    • Hoffman T. L., Canziani G., Jia L., Rucker J., Doms R. W. (2000) A biosensor assay for studying ligand-membrane receptor interactions: Binding of antibodies and HIV-1 Env to chemokine receptors, Proc. Natl. Acad. Sci. USA 97: 11215-11220.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11215-11220
    • Hoffman, T.L.1    Canziani, G.2    Jia, L.3    Rucker, J.4    Doms, R.W.5
  • 35
    • 0037080991 scopus 로고    scopus 로고
    • Flow-mediated on-surface reconstitution of G-protein coupled receptors for applications in surface plasmon resonance biosensors
    • Karlsson O. P., Löfås S. (2002) Flow-mediated on-surface reconstitution of G-protein coupled receptors for applications in surface plasmon resonance biosensors, Anal. Biochem. 300: 132-138.
    • (2002) Anal. Biochem. , vol.300 , pp. 132-138
    • Karlsson, O.P.1    Löfås, S.2
  • 36
    • 0345236608 scopus 로고    scopus 로고
    • Capture and reconstitution of G protein-coupled receptors on biosensor surfaces
    • Stenlund P., Babcock G. J., Sodroski J., Myszka D. G. (2003) Capture and reconstitution of G protein-coupled receptors on biosensor surfaces, Anal. Biochem. 316: 243-250.
    • (2003) Anal. Biochem. , vol.316 , pp. 243-250
    • Stenlund, P.1    Babcock, G.J.2    Sodroski, J.3    Myszka, D.G.4
  • 37
    • 33144482517 scopus 로고    scopus 로고
    • Surface plasmon resonance study of G protein/receptor coupling in a lipid bilayer-free system
    • Komolov K. E., Senin I. I., Philippov P. P., Koch K.-W. (2006) Surface plasmon resonance study of G protein/receptor coupling in a lipid bilayer-free system, Anal. Chem. 78: 1228-1234.
    • (2006) Anal. Chem. , vol.78 , pp. 1228-1234
    • Komolov, K.E.1    Senin, I.I.2    Philippov, P.P.3    Koch, K.-W.4
  • 38
    • 3242726205 scopus 로고    scopus 로고
    • Measuring rhodopsin-G-protein interactions by surface plasmon resonance
    • Northup J. (2004) Measuring rhodopsin-G-protein interactions by surface plasmon resonance, Methods Mol. Biol. 261: 93-111.
    • (2004) Methods Mol. Biol. , vol.261 , pp. 93-111
    • Northup, J.1
  • 39
    • 0035720605 scopus 로고    scopus 로고
    • Elucidating kinetic and thermodynamic constants for interaction of G protein subunits and receptors by surface plasmon resonance spectroscopy
    • Rebois V., Schuck P., Northup J. K. (2002) Elucidating kinetic and thermodynamic constants for interaction of G protein subunits and receptors by surface plasmon resonance spectroscopy, Methods Enzymol. 344: 15-42.
    • (2002) Methods Enzymol. , vol.344 , pp. 15-42
    • Rebois, V.1    Schuck, P.2    Northup, J.K.3
  • 40
    • 33750492961 scopus 로고    scopus 로고
    • Dot-blot immunodetection as a versatile and high-throughput assay to evaluate recombinant GPCRs produced in the yeast Pichia pastoris
    • Zeder-Lutz G., Cherouati N., Reinhart C., Pattus F., Wagner R. (2006) Dot-blot immunodetection as a versatile and high-throughput assay to evaluate recombinant GPCRs produced in the yeast Pichia pastoris, Prot. Exp. Purif. 50: 118-127.
    • (2006) Prot. Exp. Purif. , vol.50 , pp. 118-127
    • Zeder-Lutz, G.1    Cherouati, N.2    Reinhart, C.3    Pattus, F.4    Wagner, R.5
  • 41
    • 15444376596 scopus 로고    scopus 로고
    • Solubilization, stabilization, and purification of chemokine receptors using Biacore technology
    • Navratilova I., Sodroski J., Myszka D. G. (2005) Solubilization, stabilization, and purification of chemokine receptors using Biacore technology, Anal. Biochem. 339: 271-281.
    • (2005) Anal. Biochem. , vol.339 , pp. 271-281
    • Navratilova, I.1    Sodroski, J.2    Myszka, D.G.3
  • 42
    • 33646854560 scopus 로고    scopus 로고
    • A biosensor-based approach toward purification and crystallization of G protein-coupled receptors
    • Navratilova I., Pancera M., Wyatt R. T., Myszka D. G. (2006) A biosensor-based approach toward purification and crystallization of G protein-coupled receptors, Anal. Biochem. 353: 278-273.
    • (2006) Anal. Biochem. , vol.353 , pp. 278-273
    • Navratilova, I.1    Pancera, M.2    Wyatt, R.T.3    Myszka, D.G.4
  • 43
    • 33745902222 scopus 로고    scopus 로고
    • Analyzing ligand and small molecule binding activity of solubilized GPCRs using biosensor technology
    • Navratilova I., Dioszegi M., Myszka D. G. (2006) Analyzing ligand and small molecule binding activity of solubilized GPCRs using biosensor technology, Anal. Biochem. 355: 132-139.
    • (2006) Anal. Biochem. , vol.355 , pp. 132-139
    • Navratilova, I.1    Dioszegi, M.2    Myszka, D.G.3


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