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

Detection of growth factor binding to gelatin and heparin using a photonic crystal optical biosensor

Whittington, A. R., Chan, L. L., Şendemir, A., Cunningham, B. T., & Jamison, R. D. (2010) · Materials Science and Engineering C · doi:10.1016/j.msec.2010.02.025 · Cited by 7

Application of the Gyrolab Microfluidic Platform to Measure Picomolar Affinity of a PD-L1-Binding Adnectin™ Radioligand for Positron Emission Tomography

Dai, Z., Juneja, J., Schneeweis, L. A., Cohen, D., Marsilio, F., Morin, P. E., & DasGupta, R. (2020) · BioTechniques · doi:10.2144/btn-2020-0080 · Cited by 7

Molecular coevolution of coagulation factor VIII and von Willebrand factor

Zakas, P. M., Coyle, C. W., Brehm, A., Bayer, M., Solecka-Witulska, B., Radford, C. E., Brown, C., Nesbitt, K., Dwyer, C. N., Kannicht, C., et al. (2021) · Blood Advances · doi:10.1182/bloodadvances.2020002971 · Cited by 7

Biophysical Considerations for Development of Antibody-Based Therapeutics

Drake, A. W., & Papalia, G. A. (2012) · Springer eBooks · doi:10.1007/978-1-4419-5955-3_5 · Cited by 7

Spectroscopic methods to analyze drug metabolites

Yi, J.-J., Park, K., Kim, W.-J., Rhee, J., & Son, W. S. (2018) · Archives of Pharmacal Research · doi:10.1007/s12272-018-1010-x · Cited by 7

Significance Testing and Multivariate Analysis of Datasets from Surface Plasmon Resonance and Surface Acoustic Wave Biosensors: Prediction and Assay Validation for Surface Binding of Large Analytes

Puiu, M., Zamfir, L.-G., Buiculescu, V., Baracu, A. M., Mitrea, C., & Bala, C. (2018) · Sensors · doi:10.3390/s18103541 · Cited by 7

Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups' binding with human aFGF and bFGF

Wu, X., Xu, Y., Guo-xin, S., Kamei, K., Takano, R., & Hara, S. (2003) · Journal of Zhejiang University. Science A · doi:10.1631/bf02841085 · Cited by 7

Surface Plasmon Resonance Sensogram Based Characterization of Antibodies Raised Against Intact Teliospores and Purified Diagnostic Antigen for Development of Nano-Immunosensor for Fungal Spore Antigen of Karnal Bunt (Tilletia indica) of Wheat

Singh, S., Gupta, S. M., Gupta, A. K., Singh, M. P., & Kumar, A. (2013) · Proceedings of the National Academy of Sciences India Section B Biological Sciences · doi:10.1007/s40011-013-0176-8 · Cited by 7

Exploring computational lead optimisation with affinity constants obtained by surface plasmon resonance for the interaction of PorA epitope peptides with antibody against Neisseria meningitidis

Fischer, M. J. E., Kuipers, C., Hofkes, R. P., Hofmeyer, L. J. F., Moret, E. E., & de Mol, N. J. (2001) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(01)00215-x · Cited by 7

Development of New Biological Nanopores and Their Application for Biosensing and Disease Detection

Wang, S. (2016) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2016.428 · Cited by 6

Integration of Principles of Systems Biology and Radiation Biology: Toward Development of in silico Models to Optimize IUdR-Mediated Radiosensitization of DNA Mismatch Repair Deficient (Damage Tolerant) Human Cancers

Kinsella, T. J., Gürkan-Çavusoglu, E., Du, W., & Loparo, K. A. (2011) · Frontiers in Oncology · doi:10.3389/fonc.2011.00020 · Cited by 6

Kinetic Characterisation of a Single Chain Antibody against the Hormone Abscisic Acid: Comparison with Its Parental Monoclonal

Badescu, G. O., Marsh, A., Smith, T. R., Thompson, A. J., & Napier, R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152148 · Cited by 6

SPR Assisted Diabetes Detection

Sunilbhai, C. A., Alam, M. S., Sadasivuni, K. K., & Ansari, J. R. (2022) · Springer series on bio- and neurosystems · doi:10.1007/978-3-030-99728-1_6 · Cited by 6

Convection Effects in the BIAcore Dextran Layer: Surface Reaction Model

Edwards, D. A. (2006) · Bulletin of Mathematical Biology · doi:10.1007/s11538-005-9023-2 · Cited by 6

The AdoCbl–Riboswitch Interaction Investigated by In-Line Probing and Surface Plasmon Resonance Spectroscopy (SPR)

Schaffer, M., Choudhary, P. K., & Sigel, R. K. O. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801122-5.00020-9 · Cited by 6

Steady-State and Kinetics-Based Affinity Determination in Effector-Effector Target Interactions

Reinhard, A., & Nürnberger, T. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6859-6_7 · Cited by 6

Bacillus subtilis α-amylase: interactions of a partially folded conformer with small unilamellar vesicles

Colomer-Pallas, A., Petit‐Glatron, M., & Chambert, R. (2003) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2003.10.006 · Cited by 6

Surface Plasmon Resonance Biosensorics in Urine Proteomics

Luppa, P. B., Metzger, J., & Schneider, H. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-711-2_12 · Cited by 6

Surface Reaction Near a Stagnation Point

Edwards, D. A. (2000) · Studies in Applied Mathematics · doi:10.1111/1467-9590.00139 · Cited by 6

Getting the Most Value from Your Screens: Advances in Hardware, Software, and Methodologies to Enhance Surface Plasmon Resonance Based Fragment Screening and Hit-to-Lead Support

Giannetti, A. M., Gilbert, H., Huddler, D. P., Reiter, M., Strande, C., Pitts, K. E., & Bravo, B. J. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782620938-00019 · Cited by 5

First-passage time analysis of diffusion-controlled reactions in single-molecule detection

Lyu, Y., An, L., Zeng, H., Zheng, F., Guo, J., Zhang, P., Yang, H., & Li, H. (2023) · Talanta · doi:10.1016/j.talanta.2023.124569 · Cited by 5

Molecular recognition of mRNA 5′ cap by 3′ poly(A)-specific ribonuclease (PARN) differs from interactions known for other cap-binding proteins

Niedźwiecka-Kornaś, A., Nilsson, P., Worch, R., Stȩpiński, J., Darżynkiewicz, E., & Virtanen, A. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.01.002 · Cited by 5

Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family

Faltinek, L., Fujdiarová, E., Melicher, F., Houser, J., Kašáková, M., Kondakov, N. N., Kononov, L. O., Parkan, K., Vidal, S., & Wimmerová, M. (2019) · Molecules · doi:10.3390/molecules24244540 · Cited by 5

Duffy blood group (Fya & Fyb) analysis using surface plasmon resonance

Then, W. L., McLiesh, H., Aguilar, M., & Garnier, G. (2016) · Biomedical Microdevices · doi:10.1007/s10544-016-0123-6 · Cited by 5

Magnetoresistive sensors for measurements of DNA hybridization kinetics – effect of TINA modifications

Rizzi, G., Dufva, M., & Hansen, M. F. (2017) · Scientific Reports · doi:10.1038/srep41940 · Cited by 5

Bivalency of plasminogen monoclonal antibodies is required for plasminogen bridging to fibrin and enhanced plasmin formation

Domínguez, M., Montes, R., Páramo, J. A., & Anglés‐Cano, E. (2002) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s0167-4838(02)00364-3 · Cited by 5

The Revolution of Real‐Time, Label‐Free Biosensor Applications

Rich, R. L., & Myszka, D. G. (2011) · Wiley eBooks · doi:10.1002/9780470979129.ch1 · Cited by 5

Structural characterisation of diphtheria toxoid

Metz, B. (2005) · Utrecht University Repository (Utrecht University) · Cited by 5

Real-time investigation of the interaction between primaquine phosphate and bovine serum albumin (BSA) by piezoelectric quartz crystal impedance analysis

Long, Y. (2003) · Journal of Biotechnology · doi:10.1016/s0168-1656(03)00185-8 · Cited by 4

Some mathematical models of intermolecular autophosphorylation

Doherty, K., Meere, M., & Piiroinen, P. T. (2015) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2015.01.015 · Cited by 4

Detection of enzyme-catalyzed polysaccharide synthesis on surfaces

Clé, C., Martin, C. R., Field, R. A., Kuzmič, P., & Bornemann, S. (2009) · Biocatalysis and Biotransformation · doi:10.3109/10242420903388744 · Cited by 4

Biophysical Considerations for Development of Antibody-Based Therapeutics

Drake, A. W., Abdiche, Y. N., & Papalia, G. A. (2018) · Springer eBooks · doi:10.1007/978-981-13-0496-5_5 · Cited by 4

Application of mass transfer theory to biomarker capture by surface functionalized magnetic beads in microcentrifuge tubes

Scherr, T., Markwalter, C. F., Bauer, W. S., Gasperino, D. J., Wright, D. W., & Haselton, F. R. (2017) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2017.02.006 · Cited by 4

Estimation of Kinetic Parameters Involved in Solid-Phase Immunoassays by Affinity Chromatography

Robin, M., Tayakout‐Fayolle, M., Pitault, I., Jallut, C., & Drazek, L. (2020) · Industrial & Engineering Chemistry Research · doi:10.1021/acs.iecr.0c00922 · Cited by 4

Overview of the Quantitation of Protein Interactions

Philo, J. S. (1999) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps2001s17 · Cited by 4

Surface Plasmon Resonance for Measurements of Biological Interest

Bamdad, C. C. (1997) · Current Protocols in Molecular Biology · doi:10.1002/0471142727.mb2004s40 · Cited by 4

Specificity of molecular recognition in oligomerization of bacterial L-asparaginases

Mezentsev, Y. V., Molnar, A. A., Sokolov, N. N., Lisitsina, V. B., Ivanov, A. S., Archakov, A. I., & Archakov, M. A. (2012) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20125801050 · Cited by 4

A surface plasmon resonance assay for characterisation and epitope mapping of anti‐GLP‐1 antibodies

Thomsen, L., & Gurevich, L. (2018) · Journal of Molecular Recognition · doi:10.1002/jmr.2711 · Cited by 4

Natural Inhibitors

Perales, J., Domont, G. B., Neves‐Ferreira, A. G. C., & Valente, R. H. (2009) · CRC Press eBooks · doi:10.1201/9781420008661.ch12 · Cited by 4

Chemical kinetics and mass transport in an ion channel based biosensor

Monfared, S. M., Krishnamurthy, V., & Cornell, B. A. (2010) · IEEE Conference on Decision and Control (CDC) · doi:10.1109/cdc.2010.5718085 · Cited by 4

Protein Aggregation and Precipitation, Measurement and Control

Schein, C. H. (2010) · Wiley eBooks · doi:10.1002/9780470054581.eib052 · Cited by 4

Nisin Immunity and Food-Grade Transformation in Lactic Acid Bacteria

Takala, T. M. (2005) · Työväentutkimus Vuosikirja · Cited by 4

Thermodynamic Characterization of the Interaction of Biofunctionalized Gold Nanoclusters with Serum Albumin Using Two- and Three-Dimensional Methods

Juhász, Á., Gombár, G., Várkonyi, E. F., Wojnicki, M., Ungor, D., & Csapó, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242316760 · Cited by 3

Unraveling the GM1 Specificity of Galectin-1 Binding to Lipid Membranes

Scollo, F., Kulig, W., Nicita, G., Ludwig, A., Ricardo, J. C., Zito, V., Kapusta, P., Vattulainen, I., Cebecauer, M., Gabius, H., et al. (2025) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.5c00040 · Cited by 3

Unusual binding of Grb2 protein to a bivalent polyproline-ligand immobilized on a SPR sensor: Intermolecular bivalent binding

de Mol, N. J., Kruijtzer, J. A. W., Moret, E. E., Broutin, I., & Liskamp, R. M. J. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.11.001 · Cited by 3

The interaction of protein-coated bionanoparticles and surface receptors reevaluated: how important is the number of bonds?

Wang, W., Voigt, A., & Sundmacher, K. (2016) · Soft Matter · doi:10.1039/c6sm00995f · Cited by 3

Amine coupling versus biotin capture for the assessment of sulfonamide as ligands of hCA isoforms

Rogez‐Florent, T., Goossens, L., Drucbert, A., Duban‐Deweer, S., Six, P., Depreux, P., Danzé, P. M., Goossens, J., & Foulon, C. F. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.07.029 · Cited by 3

Analytical Method for Experimental Validation of Computer-Designed Antibody

Tanabe, A., & Tsumoto, K. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2609-2_23 · Cited by 3

Direct Determination of High-Affinity Binding Constants by Continuous Injection Isothermal Titration Calorimetry

Chang, J. W., Mu, Y., Armaou, A., & Rioux, R. M. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c05650 · Cited by 3

Direct Demonstration of Association of the Blood-Brain Barrier Proteins ZO-1 and Occludin Using Surface Plasmon Resonance Spectroscopy; Effect of SIN-1

Schmidt, A., Utepbergenov, D., Krause, G., & Blasig, I. E. (2004) · Elsevier eBooks · doi:10.1016/b978-012639011-7/50006-1 · Cited by 3

An imaging surface plasmon resonance sensor using polarisation modulation

Graham, D. J. L., & Watkins, L. R. (2010) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2010.09.023 · Cited by 3

Note: Four-port microfluidic flow-cell with instant sample switching

MacGriff, C. A., Wang, S., & Tao, N. J. (2013) · Review of Scientific Instruments · doi:10.1063/1.4826359 · Cited by 3

Comprehensive Study of the Interaction Between a Potential Antiprion Cationic Porphyrin and Human Prion Protein at Different pH by Using Multiple Spectroscopic Methods

Xiao, C.-Q., Feng, B., Ge, Y.-S., Fan, X., Jiang, F., Xiao, G., & Liu, Y. (2012) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.23420 · Cited by 3

Considerations on Circuit Design and Data Acquisition of a Portable Surface Plasmon Resonance Biosensing System

Chang, K., Chen, R., Wang, S., Li, J., Hu, X., Liang, H., Cao, B., Sun, X., Ma, L., Zhu, J., et al. (2015) · Sensors · doi:10.3390/s150820511 · Cited by 3

Macromolecular binding and kinetic analysis with optically sectioned planar format assays

Ghafari, H., Parambath, M., & Hanley, Q. S. (2012) · The Analyst · doi:10.1039/c2an35134j · Cited by 3

An irregular-shaped homogeneous refractive index model for interpretation of the surface plasmon resonance response from living cell attachment

Deng, S., Yu, X., & Wang, P. (2016) · Analytical Methods · doi:10.1039/c6ay00524a · Cited by 3

Specificity of molecular recognition in oligomerization of bacterial L-asparaginases

Mezentsev, Y. V., Molnar, A. A., Sokolov, N. N., Lisitsina, V. B., Shatskaya, M. A., Ivanov, A. S., & Archakov, A. I. (2011) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750811020107 · Cited by 3

Principles of Immunoassays

Sheedy, C., & Yau, K. Y. F. (2010) · Wiley eBooks · doi:10.1002/9780470909935.ch2 · Cited by 3

Anti-Idiotypic Antibody as a Booster Vaccine Against Respiratory Syncytial Virus

Mukhopadhyay, S., Manolaridis, I., Warren, C., Tang, A., O’Donnell, G. T., Luo, B., Staupe, R. P., Vora, K. A., & Chen, Z. (2025) · Vaccines · doi:10.3390/vaccines13010035 · Cited by 2

Transcription factor Rel regulates the transcription of effector genes involved in immune response by cooperating with IκBs in lamprey (Lethenteron reissneri)

Cai, Y., Du, X., Liu, A., Lv, M., Sun, F., & Su, P. (2025) · The Journal of Immunology · doi:10.1093/jimmun/vkae060 · Cited by 2

The interaction of human cytokeratins with isatin analogues

Бунеева, О. А., Gnedenko, O. V., Fedchenko, V. I., Ivanov, A. S., & Medvedev, A. E. (2010) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750810010142 · Cited by 2

Determination of Noncovalent Binding Using a Continuous Stirred Tank Reactor as a Flow Injection Device Coupled to Electrospray Ionization Mass Spectrometry

Santos, I. C., Waybright, V. B., Fan, H., Ramirez, S., Mesquita, R. B. R., Rangel, A. O. S. S., Fryčák, P., & Schug, K. A. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1113-2 · Cited by 2

Kinetic analysis of graphene oxide sheet and protein interactions using surface plasmon resonance biosensors

Huang, T.-Y., Chiu, N., & Lai, H. (2013) · Conference on Lasers and Electro-Optics Pacific Rim (CLEO-PR) · doi:10.1109/cleopr.2013.6600344 · Cited by 2

Characterizing Plexin GTPase Interactions Using Gel Filtration, Surface Plasmon Resonance Spectrometry, and Isothermal Titration Calorimetry

Muller‐Greven, J., Kim, S., Hota, P. K., Tong, Y., Borthakur, S., & Buck, M. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6448-2_6 · Cited by 2

Plasmonic Interferometers as TREM2 Sensors for Alzheimer’s Disease

Li, D., Odessey, R., Li, D., & Pacifici, D. (2021) · Biosensors · doi:10.3390/bios11070217 · Cited by 2

Neuroproteomics

Álzate, Ó. (2009) · Frontiers in neuroscience · doi:10.1201/9781420076264.ch1 · Cited by 2

Characterization of biotinylated human ACE2 and SARS-CoV-2 Omicron BA.4/5 spike protein reference materials

Stocks, B. B., Thibeault, M.-P., L’Abbé, D., Umer, M., Liu, Y., Stuible, M., Durocher, Y., & Melanson, J. E. (2024) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-024-05413-7 · Cited by 2

'Real-time' biomolecular interaction analysis: novel applications and developments

Quinn, J. G. (1999) · Arrow@dit (Dublin Institute of Technology) · Cited by 2

Charakterisierung des Ecdysteroidrezeptors als ‚target' für arthropodenspezifische Insektizide

Grebe, M. (2001) · Univ. Duesseldorf: Duesseldorfer Dokumenten- und Publikationsserver · Cited by 2

Biosensor Characterization of Structure–Function Relationships in Viral Proteins

Choulier, L., Altschuh, D., Zeder‐Lutz, G., & Regenmortel, M. H. V. V. (2004) · Methods in microbiology · doi:10.1016/s0580-9517(04)34008-0 · Cited by 2

Direct Optical Detection in Bioanalytics

Gauglitz, G., & Goddard, N. J. (2014) · Wiley eBooks · doi:10.1002/9783527654703.ch29 · Cited by 2

Computational Pipeline for Accelerating the Design of Glycomimetics

Xiao, Y., Lee, A. H., Mahmoud, S., Sameem, B., Wentworth, D., Wang, X., Miller, G. D., Grant, O. C., Foley, B. L., & Woods, R. J. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02282 · Cited by 1

Plasmon Biophotonic Arrays for Multi-analyte Biosensing in Complex Media

Shaw, A. M., Olkhov, R. V., Jerdev, A., & Barnes, W. L. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3933-2_6 · Cited by 1

Probing the primary structural determinants of streptokinase inter-domain linkers by site-specific substitution and deletion mutagenesis

Yadav, S., & Sahni, G. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.04.003 · Cited by 1

Kinetic Analysis of Biomolecular Interactions Using Label-Free Biosensors

Sun, Y.-S., & Zhu, X. D. (2014) · Instrumentation Science & Technology · doi:10.1080/10739149.2014.976830 · Cited by 1

Fractal Analysis of Binding and Dissociation of DNA–Analyte Interactions on Biosensor Surfaces

Sadana, A., & Sadana, N. (2008) · Elsevier eBooks · doi:10.1016/b978-044453010-3.50010-4 · Cited by 1

Interaction of human cytokeratins with isatin analogues

Бунеева, О. А., Gnedenko, O. V., Fedchenko, V. I., Ivanov, A. S., & Medvedev, A. E. (2010) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20105601138 · Cited by 1

SARS-CoV-2 S-Protein–Ace2 Binding Analysis Using Surface Plasmon Resonance

Baardsnes, J., & Paul‐Roc, B. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3666-4_5 · Cited by 1

Dynamic studies of antibody-antigen interactions with an electrolyte-gated organic transistor

Urbina, P. A. M., Paradisi, A., Hasler, R., Sensi, M., Berto, M., Saygin, G. D., Dostálek, J., Pinti, M., Greco, P., Borsari, M., et al. (2024) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2024.101919 · Cited by 1

Overview of molecular interactions using Biacore

Marín, M. T. I., & Riu, J. F. C. (2012) · Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona) · Cited by 1

Methods for Analysis of Protein-protein and Protein-ligand Interactions

Ďurech, M., Trčka, F., Vojtěšek, B., & Müller, P. (2014) · Klinicka onkologie · doi:10.14735/amko20141s75 · Cited by 1

A Biotechnology Perspective on Silicon Nanowire FETs for Biosensor Applications

Jokilaakso, N. (2013) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1

Peptide immunoassays

Regenmortel, M. H. V. V. (1999) · Laboratory techniques in biochemistry and molecular biology · doi:10.1016/s0075-7535(08)70449-2 · Cited by 1

Surface Plasmon Resonance Spectroscopy in the Biosciences

Yuan, J., Wu, Y., & Aguilar, M. (2011) · Wiley eBooks · doi:10.1002/9783527631841.ch7 · Cited by 1

Characterisation of the benzimidazole-binding site on the cytoskeletal protein tubulin

MacDonald, L. M. (2003) · Murdoch University Research Portal · Cited by 1

Protein engineering to explore and improve affinity ligands

Linhult, M. (2003) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1

Plasmonic Methods for the Study of Carbohydrate Interactions

Szunerits, S., & Boukherroub, R. (2015) · Wiley eBooks · doi:10.1002/9781118860212.ch2 · Cited by 1

The practical value of an explicit response model in quantitative uses Biacore™ biosensorsPreprint

Whyte, J. M. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/294843 · Cited by 1

Characterizing High Affinity Antigen/Antibody Complexes by Kinetic and Equilibrium Based Methods

Drake, A. W., Myszka, D. G., & Klakamp, S. L. (2009) · Springer eBooks · doi:10.1007/978-0-387-76643-0_11 · Cited by 1

In vitro studies of protein interactions on substrate supported artificial membranes

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Development of a Biomembrane Sensor Based on Reflectometry

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