Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors

Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors

Johnsson, B., Löfås, S., & Lindquist, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90424-r · Cited by 1,279

Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system

Karlsson, R., Michaelsson, A., & Mattsson, L. (1991) · Journal of Immunological Methods · doi:10.1016/0022-1759(91)90331-9 · Cited by 1,084

Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins

Stenberg, E., Persson, B. S., Roos, H., & Urbaniczky, C. (1991) · Journal of Colloid and Interface Science · doi:10.1016/0021-9797(91)90284-f · Cited by 1,059

Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology.

Jönsson, U., Fägerstam, L. G., Ivarsson, B., Johnsson, B., Karlsson, R., Lundh, K., Löfås, S., Persson, B. S., Roos, H., & Rönnberg, I. (1991) · PubMed · Cited by 902

A novel hydrogel matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands

Löfås, S., & Johnsson, B. (1990) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39900001526 · Cited by 767

Determination of Rate and Equilibrium Binding Constants for Macromolecular Interactions Using Surface Plasmon Resonance: Use of Nonlinear Least Squares Analysis Methods

O'Shannessy, D. J., Brigham-Burke, M. R., Soneson, K. K., Hensley, P., & Brooks, I. S. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1355 · Cited by 551

Antigen-Antibody Binding and Mass Transport by Convection and Diffusion to a Surface: A Two-Dimensional Computer Model of Binding and Dissociation Kinetics

Glaser, R. W. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1399 · Cited by 364

Interpreting Complex Binding Kinetics from Optical Biosensors: A Comparison of Analysis by Linearization, the Integrated Rate Equation, and Numerical Integration

Morton, T. A., Myszka, D. G., & CHAIKEN, I. M. (1995) · Analytical Biochemistry · doi:10.1006/abio.1995.1268 · Cited by 338

Cholera Toxin Binding Affinity and Specificity for Gangliosides Determined by Surface Plasmon Resonance

Kuziemko, G. M., Stroh, M., & Stevens, R. C. (1996) · Biochemistry · doi:10.1021/bi952314i · Cited by 338

Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants

Raghavan, M., Bonagura, V. R., Morrison, S. L., & Bjorkman, P. J. (1995) · Biochemistry · doi:10.1021/bi00045a005 · Cited by 317

Natural inhibitors: innate immunity to snake venoms.

Perales, J., Domont, G. B., Neves‐Ferreira, A. G. C., Valente, R. H., & Mackessy, S. P. (2009) · Cited by 20

[36] Studying initial phase of biofilm formation: Molecular interaction of host proteins and bacterial surface components

Amano, A., Nakagawa, I., & Hamada, S. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)10038-7 · Cited by 20

Non-glycosylphosphatidylinositol (GPI)-anchored recombinant prion protein with dominant-negative mutation inhibits PrPScreplicationin vitro

Kishida, H., Sakasegawa, Y., Watanabe, K., Yamakawa, Y., Nishijima, M., Kuroiwa, Y., Hachiya, N., & Kaneko, K. (2004) · Amyloid · doi:10.1080/13506120410001689634 · Cited by 20

Eukaryotic translation initiation is controlled by cooperativity effects within ternary complexes of 4E‐BP1, eIF4E, and the mRNA 5′ cap

Modrak‐Wójcik, A., Górka, M., Niedźwiecka, K., Zdanowski, K., Zuberek, J., Niedźwiecka-Kornaś, A., & Stolarski, R. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.10.043 · Cited by 21

Nanobiology of RNA Polymerase: Biological Consequence of Inhomogeneity in Reactant

Shimamoto, N. (2013) · Chemical Reviews · doi:10.1021/cr400006b · Cited by 20

[52] Identification and characterization of calmodulin binding sites in cGMP-gated channel using surface plasmon resonance spectroscopy

Koch, K. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)15882-3 · Cited by 20

pH-dependent kinetics of copper ions binding to amyloid-β peptide

Bin, Y., Chen, S., & Xiang, J. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.10.013 · Cited by 19

Nonlinear Analyte Concentration Gradients for One-Step Kinetic Analysis Employing Optical Microring Resonators

Marty, M. T., Sloan, C. D. K., Bailey, R. C., & Sligar, S. G. (2012) · Analytical Chemistry · doi:10.1021/ac300478f · Cited by 19

Quantifying the interaction of the C-terminal regions of polycystin-2 and polycystin-1 attached to a lipid bilayer by means of QCM

Behn, D., Bosk, S., Hoffmeister, H., Janshoff, A., Witzgall, R., & Steinem, C. (2010) · Biophysical Chemistry · doi:10.1016/j.bpc.2010.02.005 · Cited by 19

Quantitative Detection of Weak D Antigen Variants in Blood Typing using SPR

Then, W. L., Aguilar, M., & Garnier, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-01817-x · Cited by 19

Optimal Conditions for Protein Array Deposition Using Continuous Flow

Natarajan, S., Hatch, A. C., Myszka, D. G., & Gale, B. K. (2008) · Analytical Chemistry · doi:10.1021/ac8014609 · Cited by 19

Laser-induced thermal effect in surface plasmon resonance

Xiao, X., Gao, Y., Xiang, J., & Zhou, F. (2010) · Analytica Chimica Acta · doi:10.1016/j.aca.2010.07.038 · Cited by 19

NMR studies of BPTI aggregation by using paramagnetic relaxation reagents

Bernini, A., Spiga, O., Ciutti, A., Venditti, V., Prischi, F., Governatori, M., Bracci, L., Lelli, B., Pileri, S., Botta, M., et al. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.02.013 · Cited by 19

μ-Surrogate Light Chain Physicochemical Interactions of the Human PreB Cell Receptor: Implications for VH Repertoire Selection and Cell Signaling at the PreB Cell Stage

Gauthier, L., Lemmers, B., Guelpa‐Fonlupt, V., Fougereau, M., & Schiff, C. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.1.41 · Cited by 19

Analyzing surface plasmon resonance data: Choosing a correct biphasic model for interpretation

Tiwari, P. B., Wang, X., He, J. M., & Darici, Y. (2015) · Review of Scientific Instruments · doi:10.1063/1.4914027 · Cited by 19

Imaging and kinetics of the bimolecular complex formed by the tumor suppressor p53 with ubiquitin ligase COP1 as studied by atomic force microscopy and surface plasmon resonance

Moscetti, I., Bizzarri, A. R., & Cannistraro, S. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s152214 · Cited by 18

Application of Different Surface Plasmon Resonance Biosensor Chips to Monitor the Interaction of the CaM-Binding Site of Nitric Oxide Synthase I and Calmodulin

Fischer, T., Beyermann, M., & Koch, K. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5206 · Cited by 18

INTERFACIAL AND MATERIALS ASPECTS OF THE IMMOBILIZATION OF BIOMOLECULES ONTO SOLID SURFACES

Albers, W. M., Vikholm, I., Viitala, T., & Peltonen, J. P. K. (2001) · Elsevier eBooks · doi:10.1016/b978-012513910-6/50058-x · Cited by 18

Exploring the physicochemical interactions and loading strategies of mesoporous silicon dioxide nanoparticles for drug delivery

Kovtareva, S. Y., Копишев, Э. Е., Zhang, H., & Filippov, S. K. (2025) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2025.114654 · Cited by 17

Computational prediction and experimental validation of low-affinity target of triptolide and its analogues

Liu, X., Wang, K., Duan, N., Yan, L., Ma, P., Zheng, H., Zheng, W., Li, J., & Hua, Z. (2015) · RSC Advances · doi:10.1039/c4ra17009a · Cited by 17

Interaction of mutant p53 with p73: A Surface Plasmon Resonance and Atomic Force Spectroscopy study

Santini, S., Agostino, S. D., Coppari, E., Bizzarri, A. R., Blandino, G., & Cannistraro, S. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.02.014 · Cited by 17

Use of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid protein

Zhang, X., & Oglesbee, M. (2003) · Biological Procedures Online · doi:10.1251/bpo59 · Cited by 17

In vitro binding of purified NahR regulatory protein with promoter Psal

Park, H. H., Lim, W. K., & Shin, H. J. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.05.015 · Cited by 17

Studies of interaction of tumor suppressor p53 with apo-MT using surface plasmon resonance

Xia, N., Liu, L., Yi, X., & Wang, J. (2009) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-009-3174-1 · Cited by 17

Discovery of DC_H31 as potential mutant IDH1 inhibitor through NADPH-based high throughput screening

Duan, Z., Liu, J., Niu, L., Wang, J., Feng, M., Chen, H., & Luo, C. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.05.040 · Cited by 17

Subtle Differences in Dissociation Rates of Interactions between Destabilized Human Carbonic Anhydrase II Mutants and Immobilized Benzenesulfonamide Inhibitors Probed by a Surface Plasmon Resonance Biosensor

Svedhem, S., Enander, K., Karlsson, M., Sjöbom, H., Liedberg, B., Löfås, S., Mårtensson, L., Sjöstrand, S. E., Svensson, S., Carlsson, U., et al. (2001) · Analytical Biochemistry · doi:10.1006/abio.2001.5301 · Cited by 17

Role of the 88–97 loop in plasminogen activation by streptokinase probed through site-specific mutagenesis

Yadav, S., Datt, M., Singh, B., & Sahni, G. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.05.013 · Cited by 17

Use of azobenzene amino acids as photo‐responsive conformational switches to regulate antibody–antigen interaction

Parisot, J., Kurz, K., Hilbrig, F., & Freitag, R. (2009) · Journal of Separation Science · doi:10.1002/jssc.200800698 · Cited by 17

Baculovirus-Mediated Large-Scale Expression and Purification of a Polyhistidine-Tagged Rubella Virus Capsid Protein

Schmidt, M., Tuominen, N., Johansson, T., Weiss, S. A., KEINÄNEN, K. P., & Oker‐Blom, C. (1998) · Protein Expression and Purification · doi:10.1006/prep.1997.0851 · Cited by 17

DNA‐Binding Small‐Ligand‐Immobilized Surface Plasmon Resonance Biosensor for Detecting Thymine‐Related Single‐Nucleotide Polymorphisms

Miura, S., Nishizawa, S., Suzuki, A., Fujimoto, Y., Ono, K., Gao, Q., & Teramae, N. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201101290 · Cited by 16

Surface Plasmon Resonance for Therapeutic Antibody Characterization

Davidoff, S. N., Ditto, N. T., Brooks, A. E., Eckman, J. W., & Brooks, B. D. (2015) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-2617-6_3 · Cited by 16

Controllable Activation of Nanoscale Dynamics in a Disordered Protein Alters Binding Kinetics

Callaway, D. J. E., Matsui, T., Weiss, T. M., Stingaciu, L. R., Stanley, C. B., Heller, W. T., & Bu, Z. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.003 · Cited by 17

Ligand induced interaction of thyroid hormone receptor beta with its coregulators

Valadares, N. F., Polikarpov, I., & Garratt, R. C. (2008) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2008.10.006 · Cited by 16

Characterization of Polysaccharide Conformational Epitopes by Surface Plasmon Resonance

MacKenzie, C. R., & Jennings, H. J. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)01063-2 · Cited by 16

Surface plasmon resonance

Malmqvist, M., & Ivarsson, B. (2002) · CRC Press eBooks · doi:10.1201/9780203212196.ch9 · Cited by 16

Peeking into a secret world of pore-forming toxins: membrane binding processes studied by surface plasmon resonance

Anderluh, G., Maček, P., & Lakey, J. H. (2003) · Toxicon · doi:10.1016/s0041-0101(03)00197-1 · Cited by 16

Three-Dimensional Polyglycerol–PEG-Based Hydrogels as a Universal High-Sensitivity Platform for SPR Analysis

Krage, C., Adigüzel, S., Thongrom, B., Dimde, M., Block, S., Saeed, M., Schulze, M., Junge, F., Klimek, A., Achazi, K., et al. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c00499 · Cited by 15

High-throughput biomolecular interaction analysis probing by an array fluorescent biosensor platform

Liu, L., Zhou, X., Ma, R., He, M., Shi, H., & Qian, Y. T. (2017) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2017.12.119 · Cited by 15

Effect of repeat unit structure and molecular mass of lactic acid bacteria hetero-exopolysaccharides on binding to milk proteins

Birch, J., Harðarson, H. K., Khan, S., Calsteren, M. V., Ipsen, R., Garrigues, C., Almdal, K., Hachem, M. A., & Svensson, B. (2017) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2017.08.055 · Cited by 15

Kinetic analysis and fragment screening with Fujifilm AP-3000

Rich, R. L., & Myszka, D. G. (2010) · Analytical Biochemistry · doi:10.1016/j.ab.2010.03.043 · Cited by 15

HLA antibody affinity determination: From HLA ‐specific monoclonal antibodies to donor HLA specific antibodies ( DSA ) in patient serum

Hug, M. N., Keller, S., Marty, T., Gygax, D., Meinel, D. M., Spies, P., Handschin, J., Kleiser, M., Vazquez, N., Linnik, J., et al. (2023) · HLA · doi:10.1111/tan.15047 · Cited by 15

Molecular design of small organic molecules based on structural information for a conformationally constrained peptide that binds to G-CSF receptor

El-Haggar, R. S., Kamikawa, K., Machi, K., Ye, Z., Ishino, Y., Tsumuraya, T., & Fujii, I. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.12.010 · Cited by 14

Differences in affinity of monoclonal and naturally acquired polyclonal antibodies against Plasmodium falciparum merozoite antigens

Reddy, S. B., Anders, R. F., Cross, N., Müeller, I., Senn, N., Stanisic, D. I., Siba, P. M., Wahlgren, M., Kironde, F., Beeson, J. G., et al. (2015) · BMC Microbiology · doi:10.1186/s12866-015-0461-1 · Cited by 14

Evaluation of kinetics using label-free optical biosensors

Sun, Y.-S., Landry, J. P., & Zhu, X. D. (2017) · Instrumentation Science & Technology · doi:10.1080/10739149.2016.1277535 · Cited by 14

Oligomerization of L-asparaginase from Erwinia carotovora

Mezentsev, Y. V., Molnar, A. A., Gnedenko, O. V., Krasotkina, Y. V., Sokolov, N. N., & Ivanov, A. S. (2007) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s199075080701009x · Cited by 14

Non-specific and specific interactions on functionalized polymer surface studied by FT-SPR

Wei, J., Yan, L., Hu, X., Chen, X., Huang, Y., & Jing, X. (2010) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2010.11.020 · Cited by 14

Lipid transfer protein binding of unmodified natural lipids as assessed by surface plasmon resonance methodology

Kernstock, R. M., & Girotti, A. W. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.02.018 · Cited by 14

Online optimization of surface plasmon resonance‐based biosensor experiments for improved throughput and confidence

Crescenzo, G. D., Woodward, L., & Srinivasan, B. (2008) · Journal of Molecular Recognition · doi:10.1002/jmr.894 · Cited by 14

Use of SPR to Study the Interaction of G7-18NATE Peptide with the Grb7-SH2 Domain

Gunzburg, M. J., Ambaye, N. D., Hertzog, J. T., Borgo, M. P. D., Pero, S. C., Krag, D. N., Wilce, M. C. J., Aguilar, M., Perlmutter, P., & Wilce, J. A. (2010) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-010-9222-z · Cited by 14

The binding of guanine?guanine mismatched DNA to naphthyridine dimer immobilized sensor surfaces: kinetic aspects

Nakatani, K., Kobori, A., Kumasawa, H., Goto, Y., & Saito, I. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.04.005 · Cited by 14

Biochemical Reactions on Helical Structures

Edwards, D. A. (2000) · SIAM Journal on Applied Mathematics · doi:10.1137/s0036139998343769 · Cited by 14

Biochemical passivation of metal surfaces for sensor application: reactive annealing of polycrystalline gold films in hydrogen sulfide atmosphere

Снопок, Б. А. (2000) · Semiconductor Physics Quantum Electronics & Optoelectronics · doi:10.15407/spqeo3.01.059 · Cited by 14

Quantitative Characterization of Three Carbonic Anhydrase Inhibitors by LESA Mass Spectrometry

Illes‐Toth, E., Stubbs, C. J., Sisley, E. K., Bellamy‐Carter, J., Simmonds, A. L., Mize, T. H., Styles, I. B., Goodwin, R. J. A., & Cooper, H. J. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00024 · Cited by 13

Leveraging bimodal kinetics to improve detection specificity

Shi, C., Mehrabani, S., & Armani, A. M. (2012) · Optics Letters · doi:10.1364/ol.37.001643 · Cited by 13

Examining the Interactions of the Splicing Factor MBNL1 with Target RNA Sequences via a Label-Free, Multiplex Method

Yadav, A. R., Mace, C. R., & Miller, B. L. (2013) · Analytical Chemistry · doi:10.1021/ac402603j · Cited by 13

The Convergence of Cell-Based Surface Plasmon Resonance and Biomaterials: The Future of Quantifying Bio-molecular Interactions—A Review

Mamer, S. B., Page, P. C. B., Murphy, M., Wang, J., Gallerne, P., Ansari, A., & Imoukhuede, P. I. (2019) · Annals of Biomedical Engineering · doi:10.1007/s10439-019-02429-4 · Cited by 13

An updated dataset and a structure‐based prediction model for protein– RNA binding affinity

Hong, X., Tong, X., Xie, J., Liu, P., Liu, X., Song, Q., Liu, S., & Liu, S. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26503 · Cited by 13

Investigation of the Mechanism of Binding between Internalin B and Heparin Using Surface Plasmon Resonance

Hrstka, S., Kemp, M. M., Muñoz, E. M., Azizad, O., Banerjee, M., Raposo, C., Kumaran, J., Ghosh, P., & Linhardt, R. J. (2007) · Biochemistry · doi:10.1021/bi062021x · Cited by 13

MDM2–MDM4 molecular interaction investigated by atomic force spectroscopy and surface plasmon resonance

Cannistraro, S., Moscetti, I., Teveroni, E., Moretti, F., & Bizzarri, A. R. (2016) · International Journal of Nanomedicine · doi:10.2147/ijn.s114705 · Cited by 13

Interaction of ERp57 with calreticulin: Analysis of complex formation and effects of vancomycin

Frasconi, M., Chichiarelli, S., Gaucci, E., Mazzei, F., Grillo, C., Chinazzi, A., & Fabio Altieri, F. (2011) · Biophysical Chemistry · doi:10.1016/j.bpc.2011.09.003 · Cited by 13

Recent Progress in Abasic Site-binding Small Molecules for Detecting Single-base Mutations in DNA

Nishizawa, S., Sato, Y., & Teramae, N. (2014) · Analytical Sciences · doi:10.2116/analsci.30.137 · Cited by 12

Topological Defects in Hyperbranched Glycopolymers Enhance Binding to Lectins

Salvadó, M., Reina, J. J., Rojo, J., Castillón, S., & Boutureira, O. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201703432 · Cited by 12

Surface Plasmon Resonance (SPR) and cyclic voltammetry based immunosensor for determination of teliosporic antigen and diagnosis of Karnal Bunt of wheat using anti-teliosporic antibody

Singh, S., Gupta, A. K., Gupta, S. C., Gupta, S. M., & Kumar, A. (2013) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2013.10.049 · Cited by 12

Receptor-Ligand Rebinding Kinetics in Confinement

Erbaş, A., de la Cruz, M. O., & Marko, J. F. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.02.033 · Cited by 12

SPRD: a surface plasmon resonance database of common factors for better experimental planning

Tiwari, P. B., Bencheqroun, C., Lemus, M., Shaw, T., Kouassi‐Brou, M., Alaoui, A., & Üren, A. (2021) · BMC Molecular and Cell Biology · doi:10.1186/s12860-021-00354-w · Cited by 12

Determination of Affinity and Kinetic Rate Constants Using Surface Plasmon Resonance

Masson, L., Mazza, A., & Crescenzo, G. D. (2003) · Humana Press eBooks · doi:10.1385/1-59259-052-7:189 · Cited by 12

Quantification of Small Molecule-Receptor Affinities and Kinetics by Acoustic Profiling

Li, X., Thompson, K. S. J., GODBER, B. L. J., & Cooper, M. A. (2006) · Assay and Drug Development Technologies · doi:10.1089/adt.2006.4.565 · Cited by 12

Inferring the Interfacial Reactivity of Gold Nanoparticles by Surface Plasmon Resonance Measurements

Romain, M., Roman, P., Saviot, L., Millot, N., & Boireau, W. (2023) · Langmuir · doi:10.1021/acs.langmuir.3c01365 · Cited by 11

Moment analysis of near-equilibrium binding interactions during electrophoresis

Daneshbod, Y., Sterling, J. D., & Nadim, A. (2007) · Physical Review E · doi:10.1103/physreve.76.051922 · Cited by 11

The Impact of mRNA Structure on Guide RNA Targeting in Kinetoplastid RNA Editing

Reifur, L., Yu, L. E., Cruz‐Reyes, J., vanHartesvelt, M., & Koslowsky, D. J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012235 · Cited by 11

Evaluating energetics of erythropoietin ligand binding to homodimerized receptor extracellular domains

Hensley, P., Doyle, M. L., Myszka, D. G., Woody, R. W., Brigham-Burke, M. R., Erickson‐Miller, C. L., Griffin, C., Jones, C. S., McNulty, D. E., O'Brien, S. P., et al. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)23367-3 · Cited by 11

Diffusion Models at the Drug Discovery Frontier: A Review on Generating Small Molecules Versus Therapeutic Peptides

Wang, Y., Ma, Y., Chang, Y.-H., Yan, J., Zhang, J., Cai, M.-Y., & Wei, K. (2025) · Biology · doi:10.3390/biology14121665 · Cited by 11

Effect of Gravity on Bacterial Adhesion to Heterogeneous Surfaces

Hogan, K., Paul, S., Lin, G., Fuerte-Stone, J., Sokurenko, E. V., & Thomas, W. E. (2023) · Pathogens · doi:10.3390/pathogens12070941 · Cited by 10

Capture molecules preconditioned for kinetic analysis of high-affinity antigen–antibody complex in Biacore A100

Katayama, M., Sato, T., & Kuromitsu, J. (2012) · Analytical Biochemistry · doi:10.1016/j.ab.2012.02.006 · Cited by 10

Receptor Binding Kinetics of Human IL-3 Variants with Altered Proliferative Activity

Klein, B. K., Shieh, J.-J. J., Grabbe, E. S., Li, X., Welply, J. K., & McKearn, J. P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5907 · Cited by 10

Avidin−Biotin−PEG−CPA Complexes as Potential EPR-Directed Therapeutic Protein Carriers: Preparation and Characterization

Ke, S., Wright, J. C., & Kwon, G. S. (2007) · Bioconjugate Chemistry · doi:10.1021/bc700182t · Cited by 10

Single injection microarray-based biosensor kinetics

Krishnamoorthy, G., Carlen, E. T., Beusink, J. B., Schasfoort, R. B. M., & van den Berg, A. (2009) · Analytical Methods · doi:10.1039/b9ay00176j · Cited by 10

Design, Production, and Characterization of an Engineered Biotin Ligase (BirA) and Its Application for Affinity Purification of Staphylokinase Produced from Bacillus subtilis via Secretion

Wu, S., Yeung, J. C., Hwang, P. M., & Wong, S. (2002) · Protein Expression and Purification · doi:10.1006/prep.2001.1583 · Cited by 10

Evaluation of Protein Adsorption on Chitosan Surfaces with Reflectometry Interference Spectroscopy

Lü, X. Y., Huang, Y., & Ma, C. Q. (2001) · Sensors · doi:10.3390/s10500148 · Cited by 10

Detection of Nucleic Acid Interactions Using Surface Plasmon Resonance

Crouch, R. J., Wakasa, M., & Haruki, M. (2003) · Humana Press eBooks · doi:10.1385/1-59259-676-2:143 · Cited by 10

Theory of Faradaically Modulated Redox Active Electrodes for Electrochemically Mediated Selective Adsorption Processes

He, F., Bazant, M. Z., & Hatton, T. A. (2021) · Journal of The Electrochemical Society · doi:10.1149/1945-7111/abfefd · Cited by 9

Screening Oligosaccharide Libraries against Lectins Using the Proxy Protein Electrospray Ionization Mass Spectrometry Assay

Han, L., Shams‐Ud‐Doha, K., Kitova, E. N., & Klassen, J. S. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02044 · Cited by 9

Kinetics and Thermodynamics of DbpA Protein’s C-Terminal Domain Interaction with RNA

de Victoria, A. L., Moore, A. F. T., Gittis, A. G., & Koculi, E. (2017) · ACS Omega · doi:10.1021/acsomega.7b01205 · Cited by 9

Markierungsfreie “Microscale Thermophoresis” zur Bestimmung von Bindestellen und Affinitäten bei Protein‐Liganden‐Wechselwirkungen

Seidel, S. A. I., Wienken, C. J., Geissler, S., Jerabek‐Willemsen, M., Duhr, S., Reiter, A., Trauner, D. H., Braun, D., & Baaske, P. (2012) · Angewandte Chemie · doi:10.1002/ange.201204268 · Cited by 9

Immobilization of Escherichia coli for detection of phage T4 using surface plasmon resonance

Xiao, C.-Q., Jiang, F., Zhou, B., Li, R., & Liu, Y. (2012) · Science China Chemistry · doi:10.1007/s11426-012-4553-6 · Cited by 9

Calibration of a fan-shaped beam surface plasmon resonance instrument for quantitative adsorbed thin film studies—No metal film thickness or optical properties required

Badia, A., Chen, C.-I., & Norman, L. L. (2012) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2012.09.002 · Cited by 9

Development of Surface Plasmon Resonance (SPR) Based Immuno-Sensing System for Detection of Fungal Teliospores of Karnal Bunt (Tilletia indica), a Quarantined Disease of Wheat

Singh, S. (2012) · Journal of Biosensors & Bioelectronics · doi:10.4172/2155-6210.1000125 · Cited by 9

SPR and differential proteolysis/MS provide further insight into the interaction between PGIP2 and EPGs

Gutiérrez‐Sánchez, G., King, D. A., Kemp, G., & Bergmann, C. (2012) · Fungal Biology · doi:10.1016/j.funbio.2012.04.010 · Cited by 10

Heterogeneity of Platelet Alloantigens and Alloantibodies: New Insights into Structure and Function

Socher, I., Kroll, H., & Santoso, S. (2006) · Transfusion Medicine and Hemotherapy · doi:10.1159/000092578 · Cited by 9

Characterization of the interaction between human complement protein C4 and a single‐chain variable fragment antibody by capillary electrophoresis and surface plasmon resonance

Seifar, R. M., Cool, R. H., Quax, W. J., & Bischoff, R. (2004) · Electrophoresis · doi:10.1002/elps.200405887 · Cited by 9

Immunoassays in agricultural biotechnology.

Shan, G. (2011) · Cited by 9

Affinity Measurements Using Quartz Crystal Microbalance (QCM)

Johansson, T. (2010) · Springer eBooks · doi:10.1007/978-3-642-01144-3_43 · Cited by 8

In vitro affinity optimization of an anti-BDNF monoclonal antibody translates to improved potency in targeting chronic pain states in vivo

Stack, E., McMurray, S., McMurray, G., Wade, J. M., Clark, M., Young, G. T., Marquette, K., Jain, S., Kelleher, K. S., Chen, T., et al. (2020) · mAbs · doi:10.1080/19420862.2020.1755000 · Cited by 8

Universal Sensing Strategy for the Detection of Nucleic Acid Targets by Optical Biosensor Based on Surface Plasmon Resonance

Yuan, B., Hao, Y., & Tan, Z. (2004) · Clinical Chemistry · doi:10.1373/clinchem.2003.030783 · Cited by 8

Identification of Troponin C Antagonists from a Phage-displayed Random Peptide Library

Pierce, H., Schachat, F. H., Brandt, P. W., Lombardo, C. R., & Kay, B. K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.36.23448 · Cited by 8

Biosensor Analysis of Receptor-Ligand Interactions

Wu, S., & CHAIKEN, I. M. (2003) · Humana Press eBooks · doi:10.1385/1-59259-667-3:93 · Cited by 8

A Positive Cooperativity Binding Model between Ly49 Natural Killer Cell Receptors and the Viral Immunoevasin m157

Romasanta, P. N., Curto, L. M., Urtasun, N., Sarratea, M. B., Chiappini, S., Miranda, M. V., Delfino, J. M., Mariuzza, R. A., Fernández, M. M., & Malchiodi, E. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.532929 · Cited by 7

Multiple Surface-Based Biosensors for Enhanced Molecular Detection in Fluid Flow Systems

Abolfath-Beygi, M., Krishnamurthy, V., & Cornell, B. A. (2013) · IEEE Sensors Journal · doi:10.1109/jsen.2012.2229268 · Cited by 7

Side Effect of Tris on the Interaction of Amyloid β-peptide with Cu2+: Evidence for Tris–Aβ–Cu2+ Ternary Complex Formation

Bin, Y., Jiang, Z., & Xiang, J. (2015) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-015-1512-7 · Cited by 7

Modulation of Toxin Stability by 4-Phenylbutyric Acid and Negatively Charged Phospholipids

Ray, S., Taylor, M., Burlingame, M., Tatulian, S. A., & Teter, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023692 · Cited by 7

Surface Plasmon Resonance: Measuring Protein Interactions in Real Time

Panayotou, G. (2003) · Humana Press eBooks · doi:10.1385/0-89603-487-9:1 · Cited by 7

Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions

Fisher, R. J., & Fivash, M. J. (1994) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(94)90047-7 · Cited by 74

USE OF SURFACE PLASMON RESONANCE TO PROBE THE EQUILIBRIUM AND DYNAMIC ASPECTS OF INTERACTIONS BETWEEN BIOLOGICAL MACROMOLECULES

Schuck, P. (1997) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.26.1.541 · Cited by 659

Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature

O'Shannessy, D. J. (1994) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(05)80072-2 · Cited by 144

Kinetic Characterization by Surface Plasmon Resonance-Based Biosensors: Principle and Emerging Trends

Crescenzo, G. D., Boucher, C., Durocher, Y., & Jolicœur, M. (2008) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-008-0035-5 · Cited by 38