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Volumn , Issue , 2013, Pages 95-139

Biophysical considerations for development of antibody-based therapeutics

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EID: 84930144683     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4419-5955-3_5     Document Type: Chapter
Times cited : (5)

References (80)
  • 1
    • 48249146140 scopus 로고    scopus 로고
    • Probing the binding mechanism and affinity of tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors
    • Abdiche YN, Malashock DS, Pons J (2008) Probing the binding mechanism and affinity of tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors. Protein Sci 17:1326-1335
    • (2008) Protein Sci , vol.17 , pp. 1326-1335
    • Abdiche, Y.N.1    Malashock, D.S.2    Pons, J.3
  • 2
    • 59749089793 scopus 로고    scopus 로고
    • Exploring blocking assays using Octet, ProteOn, and Biacore biosensors
    • Abdiche YN, Malashock DS, Pinkerton A et al (2009) Exploring blocking assays using Octet, ProteOn, and Biacore biosensors. Anal Biochem 386:172-180
    • (2009) Anal Biochem , vol.386 , pp. 172-180
    • Abdiche, Y.N.1    Malashock, D.S.2    Pinkerton, A.3
  • 3
    • 0033168627 scopus 로고    scopus 로고
    • Identification and optimization of regeneration conditions for affinity-based biosensor assays: A multivariate cocktail approach
    • Andersson K, Hamalainen M, Malmqvist M (1999) Identification and optimization of regeneration conditions for affinity-based biosensor assays: a multivariate cocktail approach. Anal Chem 71:2475-2481
    • (1999) Anal Chem , vol.71 , pp. 2475-2481
    • Andersson, K.1    Hamalainen, M.2    Malmqvist, M.3
  • 4
    • 0346665817 scopus 로고    scopus 로고
    • Allosteric binding properties of a monoclonal antibody and its Fab fragment
    • Blake RC, Delehanty JB, Khosraviani M et al (2003) Allosteric binding properties of a monoclonal antibody and its Fab fragment. Biochemistry 42:497-508
    • (2003) Biochemistry , vol.42 , pp. 497-508
    • Blake, R.C.1    Delehanty, J.B.2    Khosraviani, M.3
  • 5
    • 1642578938 scopus 로고    scopus 로고
    • Kinetic screening of antibodies from crude hybridoma samples using Biacore
    • Canziani GA, Klakamp S, Myszka DG (2004) Kinetic screening of antibodies from crude hybridoma samples using Biacore. Anal Biochem 325:301-307
    • (2004) Anal Biochem , vol.325 , pp. 301-307
    • Canziani, G.A.1    Klakamp, S.2    Myszka, D.G.3
  • 6
    • 0036179899 scopus 로고    scopus 로고
    • Binding to CD20 by anti-B1 antibody or F(ab')(2) is sufficient for induction of apoptosis in B-cell lines
    • Cardarelli PM, Quinn M, Buckman D et al (2002) Binding to CD20 by anti-B1 antibody or F(ab')(2) is sufficient for induction of apoptosis in B-cell lines. Cancer Immunol Immunother 51:15-24
    • (2002) Cancer Immunol Immunother , vol.51 , pp. 15-24
    • Cardarelli, P.M.1    Quinn, M.2    Buckman, D.3
  • 7
    • 0031194188 scopus 로고    scopus 로고
    • Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation
    • Christensen LLH (1997) Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation. Anal Biochem 249:153-164
    • (1997) Anal Biochem , vol.249 , pp. 153-164
    • Llh, C.1
  • 8
    • 14644433149 scopus 로고    scopus 로고
    • Kinetic exclusion assay technology: Characterization of molecular interactions
    • Darling RJ, Brault PA (2004) Kinetic exclusion assay technology: characterization of molecular interactions. Assay Drug Dev Techn 2:647-657
    • (2004) Assay Drug Dev Techn , vol.2 , pp. 647-657
    • Darling, R.J.1    Brault, P.A.2
  • 9
    • 0036228119 scopus 로고    scopus 로고
    • Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface-and solution-based biophysical methods
    • Day YS, Baird CL, Rich RL et al (2002) Direct comparison of binding equilibrium, thermodynamic, and 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.1    Baird, C.L.2    Rich, R.L.3
  • 10
    • 0002860629 scopus 로고
    • The binding of multivalent ligands to cell surface receptors
    • Perelson AS, DeLisi C, Wiegel FW (eds) Marcel Dekker, New York
    • Dower SK, Titus JA, Segal DM (1984) The binding of multivalent ligands to cell surface receptors. In: Perelson AS, DeLisi C, Wiegel FW (eds) Cell surface dynamics: concepts and models. Marcel Dekker, New York
    • (1984) Cell Surface Dynamics: Concepts and Models
    • Dower, S.K.1    Titus, J.A.2    Segal, D.M.3
  • 11
    • 0031027122 scopus 로고    scopus 로고
    • Characterization of binding interactions by isothermal titration calorimetry
    • Doyle ML (1997) Characterization of binding interactions by isothermal titration calorimetry. Curr Opin Biotechnol 8:31-35
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 31-35
    • Doyle, M.L.1
  • 12
    • 33845912400 scopus 로고    scopus 로고
    • A rigorous multiple independent binding site model for determining cell-based equilibrium dissociation constants
    • Drake AW, Klakamp SL (2007) A rigorous multiple independent binding site model for determining cell-based equilibrium dissociation constants. J Immunol Methods 318:147-152
    • (2007) J Immunol Methods , vol.318 , pp. 147-152
    • Drake, A.W.1    Klakamp, S.L.2
  • 13
    • 79960938283 scopus 로고    scopus 로고
    • A strategic and systematic approach for the determination of biosensor regeneration conditions
    • Drake AW, Klakamp SL (2011) A strategic and systematic approach for the determination of biosensor regeneration conditions. J Immunol Methods 371:165-169
    • (2011) J Immunol Methods , vol.371 , pp. 165-169
    • Drake, A.W.1    Klakamp, S.L.2
  • 14
    • 1842787056 scopus 로고    scopus 로고
    • Characterizing high-affinity antigen/antibody complexes by kinetic-and equilibrium-based methods
    • Drake AW, Myszka DG, Klakamp SL (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
  • 15
    • 23444440845 scopus 로고    scopus 로고
    • Affinity ranking of antibodies using flow cytometry: Application in antibody phage display-based target discovery
    • Geuijen CAW, Clijsters-van der Horst M, Cox F et al (2005) Affinity ranking of antibodies using flow cytometry: application in antibody phage display-based target discovery. J Immunol Methods 302:68-77
    • (2005) J Immunol Methods , vol.302 , pp. 68-77
    • Caw, G.1    Clijsters-Van Der Horst, M.2    Cox, F.3
  • 16
    • 0028836038 scopus 로고
    • Scatchard analysis of fluorescent concanavalin A binding to lymphocytes
    • Gordon IL (1995) Scatchard analysis of fluorescent concanavalin A binding to lymphocytes. Cytometry 20:238-244
    • (1995) Cytometry , vol.20 , pp. 238-244
    • Gordon, I.L.1
  • 17
    • 33646934762 scopus 로고    scopus 로고
    • Spectrophotometric determination of protein concentration
    • Taylor G (ed) Wiley, Hoboken
    • Grimsley GR, Pace CN (2003) Spectrophotometric determination of protein concentration. In: Taylor G (ed) Current protocols in protein science. Wiley, Hoboken, pp 3.1.1-3.1.9
    • (2003) Current Protocols in Protein Science , pp. 311-319
    • Grimsley, G.R.1    Pace, C.N.2
  • 18
    • 0033002586 scopus 로고    scopus 로고
    • Steric effects on multivalent ligand-receptor binding: Exclusion of ligand sites by bound cell surface receptors
    • Hlavacek WS, Posner RG, Perelson AS (1999) Steric effects on multivalent ligand-receptor binding: exclusion of ligand sites by bound cell surface receptors. Biophys J 76:3031-3043
    • (1999) Biophys J , vol.76 , pp. 3031-3043
    • Hlavacek, W.S.1    Posner, R.G.2    Perelson, A.S.3
  • 19
    • 0037309153 scopus 로고    scopus 로고
    • High-speed cell sorting: Fundamentals and recent advances
    • Ibrahim SF, van den Engh G (2003) High-speed cell sorting: fundamentals and recent advances. Curr Opin Biotechnol 14:5-12
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 5-12
    • Ibrahim, S.F.1    Van Den Engh, G.2
  • 20
    • 21344433863 scopus 로고    scopus 로고
    • Fluorescence polarization/anisotropy approaches to study protein-ligand interactions: Effects of errors and uncertainties
    • Nienhaus GU (ed) Methods in molecular biologyHumana Press Inc, Totowa
    • Jameson DM, Mocz G (2005) Fluorescence polarization/anisotropy approaches to study protein-ligand interactions: effects of errors and uncertainties. In: Nienhaus GU (ed) Protein-ligand interactions: methods and applications, vol 305., Methods in molecular biologyHumana Press Inc, Totowa, pp 301-322
    • (2005) Protein-ligand Interactions: Methods and Applications, Vol 305 , pp. 301-322
    • Jameson, D.M.1    Mocz, G.2
  • 21
    • 0032144280 scopus 로고    scopus 로고
    • Interpreting kinetic rate constants from optical biosensor data recorded on a decaying surface
    • Joss L, Morton TA, Doyle ML et al (1998) Interpreting kinetic rate constants from optical biosensor data recorded on a decaying surface. Anal Biochem 261:203-210
    • (1998) Anal Biochem , vol.261 , pp. 203-210
    • Joss, L.1    Morton, T.A.2    Doyle, M.L.3
  • 22
    • 84930150325 scopus 로고    scopus 로고
    • Multivalent ligand-receptor interactions on planar supported membranes: An on-chip approach
    • Huck WTS (ed) Springer, New York
    • Jung SY, Castellana ET, Holden MA et al (2005) Multivalent ligand-receptor interactions on planar supported membranes: an on-chip approach. In: Huck WTS (ed) Nanoscale assembly: chemical techniques. Springer, New York
    • (2005) Nanoscale Assembly: Chemical Techniques
    • Jung, S.Y.1    Castellana, E.T.2    Holden, M.A.3
  • 23
    • 43149123796 scopus 로고    scopus 로고
    • Impact of hapten presentation on antibody binding at lipid membrane interfaces
    • Jung H, Yang T, Lasagna MD et al (2008) Impact of hapten presentation on antibody binding at lipid membrane interfaces. Biophys J 94:3094-3103
    • (2008) Biophys J , vol.94 , pp. 3094-3103
    • Jung, H.1    Yang, T.2    Lasagna, M.D.3
  • 24
    • 69249202275 scopus 로고    scopus 로고
    • Multivalent ligand-receptor binding on supported lipid bilayers
    • Jung H, Robison AD, Cremer PS (2009) Multivalent ligand-receptor binding on supported lipid bilayers. J Struct Biol 168:90-94
    • (2009) J Struct Biol , vol.168 , pp. 90-94
    • Jung, H.1    Robison, A.D.2    Cremer, P.S.3
  • 25
    • 0032702275 scopus 로고    scopus 로고
    • Affinity analysis of non-steady-state data obtained under mass transport limited conditions using Biacore technology
    • Karlsson R (1999) Affinity analysis of non-steady-state data obtained under mass transport limited conditions using Biacore technology. J Mol Recognit 12:285-292
    • (1999) J Mol Recognit , vol.12 , pp. 285-292
    • Karlsson, R.1
  • 26
    • 0342813129 scopus 로고    scopus 로고
    • Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors
    • Karlsson R, Fält A (1997) Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J Immunol Methods 200:121-133
    • (1997) J Immunol Methods , vol.200 , pp. 121-133
    • Karlsson, R.1    Fält, A.2
  • 27
    • 0027517259 scopus 로고
    • Analysis of active antibody concentration. Separation of affinity and concentration parameters
    • Karlsson R, Fägerstam L, Nilshans H et al (1993) Analysis of active antibody concentration. Separation of affinity and concentration parameters. J Immunol Methods 166:75-84
    • (1993) J Immunol Methods , vol.166 , pp. 75-84
    • Karlsson, R.1    Fägerstam, L.2    Nilshans, H.3
  • 28
    • 0010345821 scopus 로고
    • Kinetic and concentration analysis using BIA technology
    • Karlsson R, Hakan R, Lars F et al (1994) Kinetic and concentration analysis using BIA technology. Methods 6:99-110
    • (1994) Methods , vol.6 , pp. 99-110
    • Karlsson, R.1    Hakan, R.2    Lars, F.3
  • 29
    • 0026705890 scopus 로고
    • Effect of bivalent interaction upon apparent antibody affinity: Experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays
    • Kaufman EN, Jain RK (1992) Effect of bivalent interaction upon apparent antibody affinity: experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays. Cancer Res 52:4157-4167
    • (1992) Cancer Res , vol.52 , pp. 4157-4167
    • Kaufman, E.N.1    Jain, R.K.2
  • 32
    • 0019921557 scopus 로고
    • Antibody affinity may influence antigenic modulation of the common acute lymphoblastic leukemia antigen in vitro
    • Lebien TW, Boué DR, Bradley JG et al (1982) Antibody affinity may influence antigenic modulation of the common acute lymphoblastic leukemia antigen in vitro. J Immunol 129:2287-2292
    • (1982) J Immunol , vol.129 , pp. 2287-2292
    • Lebien, T.W.1    Boué, D.R.2    Bradley, J.G.3
  • 33
    • 34250028151 scopus 로고    scopus 로고
    • High throughput ranking of recombinant avian scFv antibody fragments from crude lysates using the Biacore A100
    • Leonard P, Säfsten P, Hearty S et al (2007) High throughput ranking of recombinant avian scFv antibody fragments from crude lysates using the Biacore A100. J Immunol Methods 323: 172-179
    • (2007) J Immunol Methods , vol.323 , pp. 172-179
    • Leonard, P.1    Säfsten, P.2    Hearty, S.3
  • 34
    • 49049108184 scopus 로고    scopus 로고
    • Exact analysis of ligand-induced dimerization of monomeric receptors
    • Mack ET, Perez-Castillejos R, Suo Z et al (2008) Exact analysis of ligand-induced dimerization of monomeric receptors. Anal Chem 80:5550-5555
    • (2008) Anal Chem , vol.80 , pp. 5550-5555
    • Mack, E.T.1    Perez-Castillejos, R.2    Suo, Z.3
  • 35
    • 0343976592 scopus 로고    scopus 로고
    • Disadvantages of double reciprocal plots
    • Martin RB (1997) Disadvantages of double reciprocal plots. J Chem Educ 74:1238-1240
    • (1997) J Chem Educ , vol.74 , pp. 1238-1240
    • Martin, R.B.1
  • 37
    • 0032321401 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Abelson JN, Simon MI, Ackers GK (eds) Academic Press, New York
    • Morton TA, Myszka DG (1998) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. In: Abelson JN, Simon MI, Ackers GK (eds) Energetics of biological macromolecules. Methods Enzymol, part B, vol 295. Academic Press, New York, pp 268-294
    • (1998) Energetics of Biological Macromolecules. Methods Enzymol, Part B, Vol 295 , pp. 268-294
    • Morton, T.A.1    Myszka, D.G.2
  • 38
    • 51249103104 scopus 로고    scopus 로고
    • Using Biacore to measure the binding kinetics of an antibody-antigen interaction
    • Murphy M, Jason-Moller L, Bruno J (2006) Using Biacore to measure the binding kinetics of an antibody-antigen interaction. Curr Protoc Protein Sci 45:19.14.1-19.14.17
    • (2006) Curr Protoc Protein Sci , vol.45 , pp. 19141-191417
    • Murphy, M.1    Jason-Moller, L.2    Bruno, J.3
  • 39
    • 0031014046 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Myszka DG (1997) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Curr Opin Biotechnol 8:50-57
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 50-57
    • Myszka, D.G.1
  • 40
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka DG (1999a) Improving biosensor analysis. J Mol Recognit 12:279-284
    • (1999) J Mol Recognit , vol.12 , pp. 279-284
    • Myszka, D.G.1
  • 41
    • 0033226378 scopus 로고    scopus 로고
    • Survey of the 1998 optical biosensor literature
    • Myszka DG (1999b) Survey of the 1998 optical biosensor literature. J Mol Recognit 12:390-408
    • (1999) J Mol Recognit , vol.12 , pp. 390-408
    • Myszka, D.G.1
  • 42
    • 0030890210 scopus 로고    scopus 로고
    • Kinetic analysis of a protein antigen-antibody interaction limited by mass transport on an optical biosensor
    • Myszka DG, Morton TA, Doyle ML et al (1997) Kinetic analysis of a protein antigen-antibody interaction limited by mass transport on an optical biosensor. Biophys Chem 64:127-137
    • (1997) Biophys Chem , vol.64 , pp. 127-137
    • Myszka, D.G.1    Morton, T.A.2    Doyle, M.L.3
  • 43
    • 0031848098 scopus 로고    scopus 로고
    • Extending the range of rate constants available from Biacore: Interpreting mass transport influenced binding data
    • Myszka DG, He X, Dembo M, Morton TA et al (1998) Extending the range of rate constants available from Biacore: interpreting mass transport influenced binding data. Biophys J 75:583-594
    • (1998) Biophys J , vol.75 , pp. 583-594
    • Myszka, D.G.1    He, X.2    Dembo, M.3    Morton, T.A.4
  • 44
    • 0032861406 scopus 로고    scopus 로고
    • Fluorescence polarization: An analytical tool for immunoassay and drug discovery
    • Nasir MS, Jolley ME (1999) Fluorescence polarization: an analytical tool for immunoassay and drug discovery. Comb Chem High Throughput Screening 2:177-190
    • (1999) Comb Chem High Throughput Screening , vol.2 , pp. 177-190
    • Nasir, M.S.1    Jolley, M.E.2
  • 45
  • 46
    • 0035878160 scopus 로고    scopus 로고
    • An immunoassay for small analytes with theoretical detection limits
    • Ohmura N, Lackie SJ, Saiki H (2001) An immunoassay for small analytes with theoretical detection limits. Anal Chem 73:3392-3399
    • (2001) Anal Chem , vol.73 , pp. 3392-3399
    • Ohmura, N.1    Lackie, S.J.2    Saiki, H.3
  • 47
    • 0027366723 scopus 로고
    • Re-evaluation of the concept of functional affinity as applied to bivalent antibody binding to cell surface antigens
    • Ong GL, Mattes MJ (1993) Re-evaluation of the concept of functional affinity as applied to bivalent antibody binding to cell surface antigens. Mol Immunol 30:1455-1462
    • (1993) Mol Immunol , vol.30 , pp. 1455-1462
    • Ong, G.L.1    Mattes, M.J.2
  • 48
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L et al (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411-2423
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3
  • 49
    • 0032720338 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of protein-protein interactions
    • Pierce MM, Raman CS, Nall BT (1999) Isothermal titration calorimetry of protein-protein interactions. Methods 19:213-221
    • (1999) Methods , vol.19 , pp. 213-221
    • Pierce, M.M.1    Raman, C.S.2    Nall, B.T.3
  • 50
    • 37049021526 scopus 로고    scopus 로고
    • High-affinity binding measurements of antibodies to cell-surface-expressed antigens
    • Rathanaswami P, Babcook J, Gallo M (2008) High-affinity binding measurements of antibodies to cell-surface-expressed antigens. Anal Biochem 373:52-60
    • (2008) Anal Biochem , vol.373 , pp. 52-60
    • Rathanaswami, P.1    Babcook, J.2    Gallo, M.3
  • 51
    • 0028057250 scopus 로고
    • Depletion of B cells in vivo by a chimeric mouse human monoclonal antibody to CD20
    • Reff ME, Carner K, Chambers KS et al (1994) Depletion of B cells in vivo by a chimeric mouse human monoclonal antibody to CD20. Blood 83:435-445
    • (1994) Blood , vol.83 , pp. 435-445
    • Reff, M.E.1    Carner, K.2    Chambers, K.S.3
  • 52
    • 0018798884 scopus 로고
    • Interaction of divalent antibody with cell surface antigens
    • Reynolds JA (1979) Interaction of divalent antibody with cell surface antigens. Biochemistry 18:264-269
    • (1979) Biochemistry , vol.18 , pp. 264-269
    • Reynolds, J.A.1
  • 53
    • 0033667738 scopus 로고    scopus 로고
    • Survey of the 1999 surface plasmon resonance biosensor literature
    • Rich RL, Myszka DG (2000) Survey of the 1999 surface plasmon resonance biosensor literature. J Mol Recognit 13:388-407
    • (2000) J Mol Recognit , vol.13 , pp. 388-407
    • Rich, R.L.1    Myszka, D.G.2
  • 54
    • 0035152823 scopus 로고    scopus 로고
    • Survey of the year 2000 commercial optical biosensor literature
    • Rich RL, Myszka DG (2001) Survey of the year 2000 commercial optical biosensor literature. J Mol Recognit 14:273-294
    • (2001) J Mol Recognit , vol.14 , pp. 273-294
    • Rich, R.L.1    Myszka, D.G.2
  • 55
    • 0036873472 scopus 로고    scopus 로고
    • Survey of the year 2001 commercial optical biosensor literature
    • Rich RL, Myszka DG (2002) Survey of the year 2001 commercial optical biosensor literature. J Mol Recognit 15:352-376
    • (2002) J Mol Recognit , vol.15 , pp. 352-376
    • Rich, R.L.1    Myszka, D.G.2
  • 56
    • 0842331880 scopus 로고    scopus 로고
    • Survey of the year 2002 commercial optical biosensor literature
    • Rich RL, Myszka DG (2003) Survey of the year 2002 commercial optical biosensor literature. J Mol Recognit 16:351-382
    • (2003) J Mol Recognit , vol.16 , pp. 351-382
    • Rich, R.L.1    Myszka, D.G.2
  • 57
    • 11244313892 scopus 로고    scopus 로고
    • Survey of the year 2003 commercial optical biosensor literature
    • Rich RL, Myszka DG (2004) Survey of the year 2003 commercial optical biosensor literature. J Mol Recognit 18:1-39
    • (2004) J Mol Recognit , vol.18 , pp. 1-39
    • Rich, R.L.1    Myszka, D.G.2
  • 58
    • 27744519033 scopus 로고    scopus 로고
    • Survey of the year 2004 commercial optical biosensor literature
    • Rich RL, Myszka DG (2005) Survey of the year 2004 commercial optical biosensor literature. J Mol Recognit 18:431-478
    • (2005) J Mol Recognit , vol.18 , pp. 431-478
    • Rich, R.L.1    Myszka, D.G.2
  • 59
    • 33845931650 scopus 로고    scopus 로고
    • Survey of the year 2005 commercial optical biosensor literature
    • Rich RL, Myszka DG (2006) Survey of the year 2005 commercial optical biosensor literature. J Mol Recognit 19:478-534
    • (2006) J Mol Recognit , vol.19 , pp. 478-534
    • Rich, R.L.1    Myszka, D.G.2
  • 60
    • 37549010341 scopus 로고    scopus 로고
    • Survey of the year 2006 commercial optical biosensor literature
    • Rich RL, Myszka DG (2007) Survey of the year 2006 commercial optical biosensor literature. J Mol Recognit 20:300-366
    • (2007) J Mol Recognit , vol.20 , pp. 300-366
    • Rich, R.L.1    Myszka, D.G.2
  • 61
    • 56849122146 scopus 로고    scopus 로고
    • Survey of the year 2007 commercial optical biosensor literature
    • Rich RL, Myszka DG (2008) Survey of the year 2007 commercial optical biosensor literature. J Mol Recognit 21:355-400
    • (2008) J Mol Recognit , vol.21 , pp. 355-400
    • Rich, R.L.1    Myszka, D.G.2
  • 62
    • 73249137770 scopus 로고    scopus 로고
    • Grading the commercial optical biosensor literature-class of 2008: "the mighty binders"
    • Rich RL, Myszka DG (2010) Grading the commercial optical biosensor literature-class of 2008: "the mighty binders". J Mol Recognit 23:1-64
    • (2010) J Mol Recognit , vol.23 , pp. 1-64
    • Rich, R.L.1    Myszka, D.G.2
  • 63
    • 58349120186 scopus 로고    scopus 로고
    • Detergent screening of a G-protein coupled receptor using serial and array biosensor technologies
    • Rich RL, Miles AR, Gale BK et al (2009) Detergent screening of a G-protein coupled receptor using serial and array biosensor technologies. Anal Biochem 386:98-104
    • (2009) Anal Biochem , vol.386 , pp. 98-104
    • Rich, R.L.1    Miles, A.R.2    Gale, B.K.3
  • 64
    • 61649092140 scopus 로고    scopus 로고
    • Molecular engineering II: Antibody affinity
    • Dübel S (ed) Wiley-VCH, Weinheim
    • Roskos L, Klakamp S, Liang M et al (2007) Molecular engineering II: antibody affinity. In: Dübel S (ed) Handbook of therapeutic antibodies. Wiley-VCH, Weinheim
    • (2007) Handbook of Therapeutic Antibodies
    • Roskos, L.1    Klakamp, S.2    Liang, M.3
  • 65
    • 84858180137 scopus 로고    scopus 로고
    • Epitope mapping by surface plasmon resonance
    • Säfsten P (2009) Epitope mapping by surface plasmon resonance. Methods Mol Biol 524:67-76
    • (2009) Methods Mol Biol , vol.524 , pp. 67-76
    • Säfsten, P.1
  • 66
    • 33646850042 scopus 로고    scopus 로고
    • Screening antibody-antigen interactions in parallel using Biacore A100
    • Säfsten P, Klakamp SL, Drake AW et al (2006) Screening antibody-antigen interactions in parallel using Biacore A100. Anal Biochem 353:181-190
    • (2006) Anal Biochem , vol.353 , pp. 181-190
    • Säfsten, P.1    Klakamp, S.L.2    Drake, A.W.3
  • 67
    • 16244362060 scopus 로고    scopus 로고
    • Validation of accuracy of enzyme-linked immunosorbent assay in hybridoma screening and proposal of an improved screening method
    • Sasaki K, Glass TR, Ohmura N (2005) Validation of accuracy of enzyme-linked immunosorbent assay in hybridoma screening and proposal of an improved screening method. Anal Chem 77:1933-1939
    • (2005) Anal Chem , vol.77 , pp. 1933-1939
    • Sasaki, K.1    Glass, T.R.2    Ohmura, N.3
  • 68
    • 33746921655 scopus 로고    scopus 로고
    • Monoclonal antibody classification based on epitope-binding using differential antigen disruption
    • Shi E, Fury W, Li W et al (2006) Monoclonal antibody classification based on epitope-binding using differential antigen disruption. J Immunol Methods 314:9-20
    • (2006) J Immunol Methods , vol.314 , pp. 9-20
    • Shi, E.1    Fury, W.2    Li, W.3
  • 69
    • 44849121670 scopus 로고    scopus 로고
    • Affinity maturation of tacrolimus antibody for improved immunoassay performance
    • Siegel RW, Baugher W, Rahn T et al (2008) Affinity maturation of tacrolimus antibody for improved immunoassay performance. Clin Chem 54:1008-1017
    • (2008) Clin Chem , vol.54 , pp. 1008-1017
    • Siegel, R.W.1    Baugher, W.2    Rahn, T.3
  • 70
    • 33644867597 scopus 로고    scopus 로고
    • Rapid kinetic-based screening of human Fab fragments
    • Steukers M, Schaus JM, van Gool R et al (2006) Rapid kinetic-based screening of human Fab fragments. J Immunol Methods 310:126-135
    • (2006) J Immunol Methods , vol.310 , pp. 126-135
    • Steukers, M.1    Schaus, J.M.2    Van Gool, R.3
  • 71
    • 61649112477 scopus 로고    scopus 로고
    • Translational strategies for development of monoclonal antibodies from discovery to the clinic
    • Tabrizi MA, Bornstein GG, Klakamp SL et al (2009) Translational strategies for development of monoclonal antibodies from discovery to the clinic. Drug Discov Today 14:298-305
    • (2009) Drug Discov Today , vol.14 , pp. 298-305
    • Tabrizi, M.A.1    Bornstein, G.G.2    Klakamp, S.L.3
  • 72
    • 69149104578 scopus 로고    scopus 로고
    • High-affinity lamprey VLRA and VLRB monoclonal antibodies
    • Tasumi S, Velikovsky CA, Xu G et al (2009) High-affinity lamprey VLRA and VLRB monoclonal antibodies. PNAS 106:12891-12896
    • (2009) PNAS , vol.106 , pp. 12891-12896
    • Tasumi, S.1    Velikovsky, C.A.2    Xu, G.3
  • 73
    • 78649769725 scopus 로고    scopus 로고
    • Surface plasmon resonance
    • Harding SE, Chowdhry BZ (eds) Oxford University Press, New York
    • van der Merwe PA (2001) Surface plasmon resonance. In: Harding SE, Chowdhry BZ (eds) Protein-ligand interactions: hydrodynamics and calorimetry. Oxford University Press, New York, pp 137-170
    • (2001) Protein-ligand Interactions: Hydrodynamics and Calorimetry , pp. 137-170
    • Van Der Merwe, P.A.1
  • 74
    • 0032448965 scopus 로고    scopus 로고
    • Measurement of antigen-antibody interactions with biosensors
    • Van Regenmortel MHV, Altschuh D, Chatellier J et al (1998) Measurement of antigen-antibody interactions with biosensors. J Mol Recognit 11:163-167
    • (1998) J Mol Recognit , vol.11 , pp. 163-167
    • Van Regenmortel Mhv1    Altschuh, D.2    Chatellier, J.3
  • 75
    • 0011328355 scopus 로고    scopus 로고
    • When bivalent proteins might walk across cell surfaces
    • Vanden Broek W, Thompson NL (1996) When bivalent proteins might walk across cell surfaces. J Phys Chem 100:11471-11479
    • (1996) J Phys Chem , vol.100 , pp. 11471-11479
    • Vanden Broek, W.1    Thompson, N.L.2
  • 76
    • 33645305964 scopus 로고    scopus 로고
    • High-throughput affinity ranking of antibodies using surface plasmon resonance microarrays
    • Wassaf D, Kuang G, Kopacz K et al (2006) High-throughput affinity ranking of antibodies using surface plasmon resonance microarrays. Anal Biochem 351:241-253
    • (2006) Anal Biochem , vol.351 , pp. 241-253
    • Wassaf, D.1    Kuang, G.2    Kopacz, K.3
  • 77
    • 3242663695 scopus 로고    scopus 로고
    • Quantitative analysis of protein-protein interactions
    • Fu H (ed) Protein-protein interactions: methods and protocol-sHumana Press Inc, Totowa
    • Wilkinson KD (2004) Quantitative analysis of protein-protein interactions. In: Fu H (ed) Methods in molecular biology, vol 261., Protein-protein interactions: methods and protocol-sHumana Press Inc, Totowa, pp 15-31
    • (2004) Methods in Molecular Biology, Vol 261 , pp. 15-31
    • Wilkinson, K.D.1
  • 78
    • 24344439743 scopus 로고    scopus 로고
    • Measurements of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay
    • Xie L, Mark Jones R, Glass TR et al (2005) Measurements of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay. J Immunol Methods 304:1-14
    • (2005) J Immunol Methods , vol.304 , pp. 1-14
    • Xie, L.1    Mark Jones, R.2    Glass, T.R.3
  • 79
    • 0037462084 scopus 로고    scopus 로고
    • Investigations of bivalent antibody binding on fluid-supported phospholipid membranes: The effect of hapten density
    • Yang T, Baryshnikova OK, Mao H et al (2002) Investigations of bivalent antibody binding on fluid-supported phospholipid membranes: the effect of hapten density. J Am Chem Soc 125:4779-4784
    • (2002) J Am Chem Soc , vol.125 , pp. 4779-4784
    • Yang, T.1    Baryshnikova, O.K.2    Mao, H.3
  • 80
    • 0042170392 scopus 로고    scopus 로고
    • Differential binding properties of B7-H1 and B7-DC to programmed death-1
    • Youngnak P, Kozono Y, Kozono H et al (2003) Differential binding properties of B7-H1 and B7-DC to programmed death-1. Biochem Biophys Res Commun 307:672-677
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 672-677
    • Youngnak, P.1    Kozono, Y.2    Kozono, H.3


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