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Chapter 19: Measurement of Protein–Protein Interactions Using Surface Plasmon Resonance Spectroscopy—References

Altschuh D., Dubs M.C., Weiss E., Zeder-Lutz G., and Van Regenmortel M.H. 1992. Determination of kinetic constants for the interaction between a monoclonal antibody and peptides using surface plasmon resonance. Biochemistry 31: 6298–6304.

Andersson K., Areskoug D., and Hardenborg E. 1999. Exploring buffer space for molecular interactions. J. Mol. Recognit. 12: 310–315.

BIAtechnology Handbook. 1998. Biacore AB, Uppsala, Sweden.

Celia H., Wilson-Kubalek E., Milligan R.A., and Teyton L. 1999. Structure and function of a membrane-bound murine MHC class I molecule. Proc. Natl. Acad. Sci. 96: 5634–5639.

Christensen L.L. 1997. Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation. Anal. Biochem. 249: 153–164.

Day Y.S. and Myszka D.G. 2003. Characterizing a drug's primary binding site on albumin. J. Pharm. Sci. 92: 333–343.

Day Y.S., Baird C.L., Rich R.L., and Myszka D.G. 2002. Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods. Protein Sci. 11: 1017–1025.

Fisher R.J. and Fivash M. 1994. Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions. Curr. Opin. Biotechnol. 5: 389–395.

Fisher R.J., Fivash M., Casas-Finet J., Erickson J.W., Kondoh A., Bladen S.V., Fisher C., Watson D.K., and Papas T. 1994. Real-time DNA binding measurements of the ETS1 recombinant oncoproteins reveal significant kinetic differences between the p42 and p51 isoforms. Protein Sci. 3: 257–266.

Fivash M.J. 2001. Surface plasmon resonance. In Nature encyclopedia of life sciences. Nature Publishing Group, London. http://www.els.net/ [doi: 10.1038/npg.els.0002699].

Jonsson U., Fagerstam L., Ivarsson B., Johnsson B., Karlsson R., Lundh K., Lofas S., Persson B., Roos H., Ronnberg I., Roos H., Sjolander S., Stahlberg R., Stenberg E., and Urbaniczky C. 1991. Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology. Biotechniques 11: 620–627.

Karlsson R. and Falt A. 1997. Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 200: 121–133.

Karlsson R., Michaelsson A., and Mattsson L. 1991. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods 145: 229–240.

Karlsson R., Fagerstam L., Nilshans H., and Persson B. 1993. Analysis of active antibody concentration. Separation of affinity and concentration parameters. J. Immunol. Methods 166: 75–84.

Ladbury J.E., Lemmon M.A., Zhou M., Green J., Botfield M.C., and Schlessinger J. 1995. Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: A reappraisal. Proc. Natl. Acad. Sci. 92: 3199–3203.

Morgan H. and Taylor D.M. 1992. A surface plasmon resonance immunosensor based on the streptavidin-biotin complex. Biosens. Bioelectron. 7: 405–410.

Muller K.M., Arndt K.M., and Pluckthun A. 1998. Model and simulation of multivalent binding to fixed ligands. Anal. Biochem. 261: 149–158.

Myszka D.G. 1999a. Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Curr. Opin. Biotechnol. 8: 50–57.

Myszka D.G. 1999b. Improving Biosensor Analysis. J. Mol. Recognit. 12: 279–284.

Myszka D.G., Jonsen M.D., and Graves B.J. 1998a. Equilibrium analysis of high affinity interactions using BIACORE. Anal. Biochem. 265: 326–330.

Myszka D.G., He X., Dembo M., Morton T.A., and Goldstein B. 1998b. Extending the range of rate constants available from BIACORE: Interpreting mass transport-influenced binding data. Biophys. J. 75: 583–594.

Myszka D.G., Abdiche Y.N., Arisaka F., Byron O., Eisenstein E., Hensley P., Thomson J.A., Lombardo C.R., Schwarz F., Stafford W., and Doyle M.L. 2003. The ABRF-MIRG'02 study: Assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction. J. Biomol. Tech. 14: 247–269.

Nieba L., Krebber A., and Pluckthun A. 1996. Competition BIAcore for measuring true affinities: Large differences from values determined from binding kinetics. Anal. Biochem. 234: 155–165.

Nieba L., Nieba-Axmann S.E., Persson A., Hamalainen M., Edebratt F., Hansson A., Lidholm J., Magnusson K., Karlsson A.F., and Pluckthun A. 1997. BIACORE analysis of histidine-tagged proteins using a chelating NTA sensor chip. Anal. Biochem. 252: 217–228.

O'Shannessy D.J., Brigham-Burke M., and Peck K. 1992. Immobilization chemistries suitable for use in the BIAcore surface plasmon resonance detector. Anal. Biochem. 205: 132–136.

O'Shannessy D.J., Brigham-Burke M., Soneson K.K., Hensley P., and Brooks I. 1993. Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: Use of nonlinear least squares analysis methods. Anal. Biochem. 212: 457–468.

Pellequer J.L. and Van Regenmortel M.H. 1993. Measurement of kinetic binding constants of viral antibodies using a new biosensor technology. J. Immunol. Methods 166: 133–143.

Raut S., Weller L., and Barrowcliffe T.W. 1999. Phospholipid binding of factor VIII in different therapeutic concentrates. Br. J. Haematol. 107: 323–329.

Roden L.D. and Myszka D.G. 1996. Global analysis of a macromolecular interaction measured on BIAcore. Biochem. Biophys. Res. Commun. 225: 1073–1077.

Saenko E., Sarafanov A., Greco N., Shima M., Loster K., Schwinn H., and Josic D. 1999. Use of surface plasmon resonance for studies of protein-protein and protein-phospholipid membrane interactions. Application to the binding of factor VIII to von Willebrand factor and to phosphatidylserine-containing membranes. J. Chromatogr. A 852: 59–71.

Sambrook J. and Russell D.W. 2001. Molecular cloning: A laboratory manual, 3rd edition. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.

Schuck P., Millar D.B., and Kortt A.A. 1998. Determination of binding constants by equilibrium titration with circulating sample in a surface plasmon resonance biosensor. Anal. Biochem. 265: 79–91.

Shi Z.D., Lee K., Wei C.Q., Roberts L.R., Worthy K.M., Fisher R.J., and Burke T.R., Jr. 2004a. Synthesis of a 5-methylindolyl-containing macrocycle that displays ultrapotent Grb2 SH2 domain-binding affinity. J. Med. Chem. 47: 788–791.

Shi Z.D., Wei C.Q., Lee K., Liu H., Zhang M., Araki T., Roberts L.R., Worthy K.M., Fisher R.J., Neel B.G., Kelley J.A., Yang D., and Burke T.R., Jr. 2004b. Macrocyclization in the design of non-phosphorus-containing Grb2 SH2 domain-binding ligands. J. Med. Chem. 47: 2166–2169.

Sjolander S. and Urbaniczky C. 1991. Integrated fluid handling system for biomolecular interaction analysis. Anal. Chem. 63: 2338–2345.

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