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

A novel nanolayer biosensor principle

Jennissen, H. P., & Zumbrink, T. (2003) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2003.09.008 · Cited by 40

Slow molecular recognition by RNA

Gleitsman, K. R., Sengupta, R. N., & Herschlag, D. (2017) · RNA · doi:10.1261/rna.062026.117 · Cited by 40

Surface plasmon resonance biosensors as a tool in antibody engineering

Alfthan, K. (1998) · Biosensors and Bioelectronics · doi:10.1016/s0956-5663(98)00020-7 · Cited by 40

Study of substrate–enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor

Fong, C., Lai, W., Leung, Y., Lo, S. C., Wong, M., & Yang, M. (2002) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(02)00208-x · Cited by 39

Efficient and selective enzymatic synthesis of N-acetyl-lactosamine in ionic liquid: a rational explanation

Sandoval, M., Cortés-Cabrera, Á., Civera, C., Treviño, J., Ferreras, E., Vaultier, M., Berenguer, J., Lozano, P., & Hernáiz, M. J. (2012) · RSC Advances · doi:10.1039/c2ra20618h · Cited by 39

Electrospray ionization and matrix-assisted laser desorption ionization mass spectrometry

Bakhtiar, R., & Nelson, R. W. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00317-2 · Cited by 38

Multispot, label-free biodetection at a phantom plastic–water interface

Giavazzi, F., Salina, M., Cerbino, R., Bassi, M., Prosperi, D., Ceccarello, E., Damin, F., Solá, L., Rusnati, M., Chiari, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214589110 · Cited by 37

FimH adhesin from host unrestricted Salmonella Enteritidis binds to different glycoprotein ligands expressed by enterocytes from sheep, pig and cattle than FimH adhesins from host restricted Salmonella Abortus-ovis, Salmonella Choleraesuis and Salmonella Dublin

Grzymajło, K., Ugorski, M., Kolenda, R., Kedzierska, A. E., Kuźmińska-Bajor, M., & Wieliczko, A. (2013) · Veterinary Microbiology · doi:10.1016/j.vetmic.2013.07.004 · Cited by 37

Label Free Fiber Optic Apta-Biosensor for In-Vitro Detection of Dopamine

Zibaii, M. I., Latifi, H., Asadollahi, A., Bayat, A., Dargahi, L., & Haghparast, A. (2016) · Journal of Lightwave Technology · doi:10.1109/jlt.2016.2550533 · Cited by 37

Kinetic analysis of DNA binding by the c‐Myb DNA‐binding domainusing surface plasmon resonance

Oda, M., Furukawa, K., Sarai, A., & Nakamura, H. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00833-9 · Cited by 37

Surface plasmon resonance study of the molecular recognition between polymerase and DNA containing various mismatches and conformational changes of DNA–protein complexes

Tsoi, P. Y., & Yang, M. (2003) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2003.11.004 · Cited by 37

Lipid-free NisI: interaction with nisin and contribution to nisin immunity via secretion

Takala, T. M., Koponen, O., Qiao, M., & Saris, P. E. J. (2004) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2004.06.032 · Cited by 37

Multiplexed Analysis of Protein–Ligand Interactions by Fluorescence Anisotropy in a Microfluidic Platform

Cheow, L. F., Viswanathan, R., Chin, C.-S., Jennifer, N., Jones, R. C., Guccione, E., Quake, S. R., & Burkholder, W. F. (2014) · Analytical Chemistry · doi:10.1021/ac502605f · Cited by 37

Predicting the kinetics of peptide-antibody interactions using a multivariate experimental design of sequence and chemical space

Andersson, K., Choulier, L., H�m�l�inen, M. D., Regenmortel, M. H. V. V., Altschuh, D., & Malmqvist, M. (2001) · Journal of Molecular Recognition · doi:10.1002/1099-1352(200101/02)14:1 · Cited by 37

A biosensor approach to probe the structure and function of the adsorbed proteins: fibrinogen at the gold surface

Снопок, Б. А., Kostyukevych, K. V., Rengevych, O. V., Shirshov, Y. M., Venger, E. F., Колесникова, И. Н., & Lugovskoi, E. V. (1998) · Semiconductor Physics Quantum Electronics & Optoelectronics · doi:10.15407/spqeo1.01.121 · Cited by 37

A Region in Domain II of the Urokinase Receptor Required for Urokinase Binding

Bdeir, K. H., Kuo, A., Mazar, A. P., Sachais, B. S., Xiao, W., Gawlak, S. L., Harris, S., Higazi, A. A., & Cines, D. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001595200 · Cited by 36

Analysis of the Binding of the Fab Fragment of Monoclonal Antibody NC10 to Influenza Virus N9 Neuraminidase from Tern and Whale Using the BIAcore Biosensor: Effect of Immobilization Level and Flow Rate on Kinetic Analysis

Kortt, A. A., Nice, E. C., & GRUEN, L. C. (1999) · Analytical Biochemistry · doi:10.1006/abio.1999.4183 · Cited by 36

Purification and In Vitro Functional Analysis of the Arabidopsis thaliana Regulator of G-Protein Signaling-1

Willard, F. S., & Siderovski, D. P. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)89019-0 · Cited by 36

A single‐molecule force spectroscopy nanosensor for the identification of new antibiotics and antimalarials

Sisquella, X., Pourcq, K. D., Alguacil, J., Robles, J., Sanz, F., Anselmetti, D., Imperial, S., & Fernàndez‐Busquets, X. (2010) · The FASEB Journal · doi:10.1096/fj.10-155507 · Cited by 35

Use of an albumin-binding domain for the selective immobilisation of recombinant capture antibody fragments on ELISA plates

König, T., & Skerra, A. (1998) · Journal of Immunological Methods · doi:10.1016/s0022-1759(98)00112-4 · Cited by 35

Detection of sulphamethazine with an optical biosensor and anti-idiotypic antibodies

Akkoyun, A., Kohen, V. F., & Bilitewski, U. (2000) · Sensors and Actuators B Chemical · doi:10.1016/s0925-4005(00)00547-5 · Cited by 35

Two-Dimensional Label-Free Affinity Analysis of Tumor-Specific CD8 T Cells with a Biomimetic Plasmonic Sensor

Soler, M., Li, X., John‐Herpin, A., Schmidt, J., Coukos, G., & Altug, H. (2018) · ACS Sensors · doi:10.1021/acssensors.8b00523 · Cited by 34

Identification of small molecule inhibitors targeting the SMARCA2 bromodomain from a high-throughput screening assay

Lu, T., Hu, J., Lu, W., Han, J., Ding, H., Jiang, H., Zhang, Y., Yue, L., Chen, S., Jiang, H., et al. (2018) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.188 · Cited by 33

Graphene Oxide Based Surface Plasmon Resonance Biosensors

Chiu, N., Huang, T.-Y., & Lai, H. (2013) · InTech eBooks · doi:10.5772/56221 · Cited by 33

Intermolecular Interaction of Avidin and PEGylated Biotin

Ke, S., Wright, J. C., & Kwon, G. S. (2007) · Bioconjugate Chemistry · doi:10.1021/bc700204k · Cited by 33

Oxidation of C-reactive protein by hypochlorous acid leads to the formation of potent platelet activator

Boncler, M. A., Kehrel, B. E., Szewczyk, R., Stec‐Martyna, E., Bednarek, R., Brodde, M. F., & Watała, C. W. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.10.159 · Cited by 33

A Quantitative Approach to Membrane Binding of Human Ubiquitous Mitochondrial Creatine Kinase Using Surface Plasmon Resonance

Schlattner, U., & Wallimann, T. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005576831968 · Cited by 33

A strategic and systematic approach for the determination of biosensor regeneration conditions

Drake, A. W., & Klakamp, S. L. (2011) · Journal of Immunological Methods · doi:10.1016/j.jim.2011.06.003 · Cited by 32

Kinetic Analyses Reveal Multiple Steps in Forming TonB−FhuA Complexes from Escherichia coli

Khursigara, C. M., Crescenzo, G. D., Pawelek, P. D., & Coulton, J. W. (2005) · Biochemistry · doi:10.1021/bi047882p · Cited by 32

Novel Interactions between Urokinase and Its Receptor

Shliom, O., Huang, M., Sachais, B. S., Kuo, A., Weisel, J. W., Nagaswami, C., Nassar, T., Bdeir, K. H., Hiss, E., Gawlak, S. L., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002024200 · Cited by 32

Uterine Milk Protein, a Novel Activin-Binding Protein, Is Present in Ovine Allantoic Fluid

McFarlane, J. R., Foulds, L. M., O’Connor, A. E., Phillips, D. J., Jenkin, G., Hearn, M. T. W., & de Kretser, D. M. (1999) · Endocrinology · doi:10.1210/en.140.10.4745 · Cited by 32

Coiled-Coil Formation on Lipid Bilayers—Implications for Docking and Fusion Efficiency

Pähler, G., Panse, C. H., Diederichsen, U., & Janshoff, A. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.08.053 · Cited by 31

Kinetic study of various binding modes between human DNA polymerase β and different DNA substrates by surface-plasmon-resonance biosensor

Tsoi, P. Y., & Yang, M. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3610317 · Cited by 31

Applications of SPR for the characterization of molecules important in the pathogenesis and treatment of neurodegenerative diseases

Wittenberg, N. J., Wootla, B., Jordan, L. R., Đenić, A., Warrington, A. E., Oh, S., & Rodriguez, M. (2014) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2014.896199 · Cited by 31

Interaction of human hemoglobin and semi-hemoglobins with the Staphylococcus aureus hemophore IsdB: a kinetic and mechanistic insight

Gianquinto, E., Moscetti, I., Bei, O. D., Campanini, B., Marchetti, M., Luque, F. J., Cannistraro, S., Ronda, L., Bizzarri, A. R., Spyrakis, F., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-54970-w · Cited by 31

Plasma-polymerized films for biosensors II

Muguruma, H. (2007) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2007.03.003 · Cited by 31

Molecular interference of fibrin's divalent polymerization mechanism enables modulation of multiscale material properties

Brown, A. C., Baker, S. R., Douglas, A. M., Keating, M., Alvarez‐Elizondo, M. B., Botvinick, E. L., Guthold, M., & Barker, T. H. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.01.010 · Cited by 30

Threshold-Based Quantification in a Multiline Lateral Flow Assay via Computationally Designed Capture Efficiency

Gasperino, D. J., Leon, D., Lutz, B. R., Cate, D. M., Nichols, K. P., Bell, D., & Weigl, B. H. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b00440 · Cited by 30

Complete Thermodynamic and Kinetic Characterization of the Isomer-Specific Interaction between Pin1-WW Domain and the Amyloid Precursor Protein Cytoplasmic Tail Phosphorylated at Thr668

De, S., Greenwood, A. I., Rogals, M. J., Kovrigin, E. L., Lu, K. P., & Nicholson, L. K. (2012) · Biochemistry · doi:10.1021/bi3008214 · Cited by 30

Heparin molecularly imprinted polymer thin flm on gold electrode by plasma-induced graft polymerization for label-free biosensor

Orihara, K., Hikichi, A., Arita, T., Muguruma, H., & Yoshimi, Y. (2018) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2018.01.012 · Cited by 30

Interaction between Pyridoxal Kinase and Pyridoxal-5-phosphate-Dependent Enzymes

Cheung, P. Y. (2003) · The Journal of Biochemistry · doi:10.1093/jb/mvg201 · Cited by 30

Kinetic characterization of TAR RNA–Tat peptide and neomycin interactions by acoustic wave biosensor

Tassew, N. G., & Thompson, M. E. (2003) · Biophysical Chemistry · doi:10.1016/s0301-4622(03)00155-8 · Cited by 30

Involvement of a Nine-residue Loop of Streptokinase in the Generation of Macromolecular Substrate Specificity by the Activator Complex through Interaction with Substrate Kringle Domains

Dhar, J., Pande, A. H., Sundram, V., Nanda, J. S., Mande, S. C., & Sahni, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108422200 · Cited by 30

Plasmonic Based Kinetic Analysis of Hydrogen Reactions within Au−YSZ Nanocomposites

Joy, N. A., Settens, C. M., Matyi, R. J., & Carpenter, M. A. (2011) · The Journal of Physical Chemistry C · doi:10.1021/jp112228h · Cited by 29

Liganded Hemoglobin Structural Perturbations by the Allosteric Effector L35

Chen, Q., Lalezari, I., Nagel, R. L., & Hirsch, R. E. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.046136 · Cited by 29

Domain Truncation Studies Reveal That the Streptokinase-Plasmin Activator Complex Utilizes Long Range Protein-Protein Interactions with Macromolecular Substrate to Maximize Catalytic Turnover

Sundram, V., Nanda, J. S., Rajagopal, K., Dhar, J., Chaudhary, A., & Sahni, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303799200 · Cited by 29

Binding properties of the natural red dye carthamin with human serum albumin: Surface plasmon resonance, isothermal titration microcalorimetry, and molecular docking analysis

He, J., Li, S., Xu, K., Tang, B., Yang, H., Wang, Q., & Li, H. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.11.124 · Cited by 28

Kinetic Analysis of the Interactions between Troponin C and the C-terminal Troponin I Regulatory Region and Validation of a New Peptide Delivery/Capture System used for Surface Plasmon Resonance

Tripet, B., Crescenzo, G. D., Grothé, S., O'Connor‐McCourt, M. D., & Hodges, R. S. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00883-5 · Cited by 28

Unbiased binding assays for discovering small-molecule probes and drugs

Kemp, M. M., Weïwer, M., & Koehler, A. N. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.11.071 · Cited by 27

Kinetic and thermodynamic study of beta-Boswellic acid interaction with Tau protein investigated by surface plasmon resonance and molecular modeling methods

Haghaei, H., Hosseini, S. R. A., Soltani, S., Fathi, F., Mokhtari, F., Karima, S., & Rashidi, M. (2019) · Bioimpacts · doi:10.15171/bi.2020.03 · Cited by 27

A Novel Strategy for Analyzing RNA-Protein Interactions by Surface Plasmon Resonance Biosensor

Yang, Y., Wang, Q., & Guo, D. (2008) · Molecular Biotechnology · doi:10.1007/s12033-008-9066-3 · Cited by 27

Hunting Interactomes of a Membrane Protein

Roman, I., Figys, J., Steurs, G., & Zizi, M. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t600009-mcp200 · Cited by 27

Surface plasmon resonance biosensors: Advancements, applications, and future directions in molecular detection

biyari, N. E. (2026) · Biotechnology Notes · doi:10.1016/j.biotno.2026.01.002 · Cited by 26

On-chip bioorthogonal chemistry enables immobilization of in situ modified nanoparticles and small molecules for label-free monitoring of protein binding and reaction kinetics

Tassa, C., Liong, M., Hilderbrand, S. A., Sandler, J. E., Reiner, T., Keliher, E. J., Weissleder, R., & Shaw, S. Y. (2012) · Lab on a Chip · doi:10.1039/c2lc40337d · Cited by 26

Kinetic analyses and performance of a colloidal magnetic nanoparticle based immunoassay dedicated to allergy diagnosis

Teste, B., Kanoufi, F., Descroix, S., Poncet, P., Georgelin, T., Siaugue, J., Petr, J., Varenne, A., & Hennion, M. (2011) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-011-5021-4 · Cited by 26

Novel peptide surface for reversible immobilization of concanavalin A

Masárová, J., Dey, E. S., Carlsson, J., & Danielsson, B. R. G. (2004) · Journal of Biochemical and Biophysical Methods · doi:10.1016/j.jbbm.2004.05.005 · Cited by 26

Surface Plasmon Resonance for Measuring Interactions of Proteins with Lipid Membranes

Hodnik, V., & Anderluh, G. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-275-9_2 · Cited by 26

Intercalation of anticancer drug mitoxantrone into DNA: Studied by spectral and surface plasmon resonance methods

Ahar, M. J., Abdian, M., Maleki, S., Abbasgolizadeh, P., & Fathi, F. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.134509 · Cited by 26

Characterization and Analysis of Biopharmaceutical Proteins

Luo, Y., Matejic, T., Ng, C.-K., Nunnally, B. K., Porter, T. J., Raso, S. W., Rouse, J. C., Shang, T. Q., & Steckert, J. (2010) · Separation science and technology · doi:10.1016/b978-0-12-375680-0.00008-5 · Cited by 26

A novel peptide inhibitor of classical and lectin complement activation including ABO incompatibility

Mauriello, C. T., Pallera, H. K., Sharp, J. A., Woltmann, J. L., Qian, S., Hair, P. S., van der Pol, P., van Kooten, C., Thielens, N. M., Lattanzio, F. A., et al. (2012) · Molecular Immunology · doi:10.1016/j.molimm.2012.07.012 · Cited by 26

Analysis of Cre–loxP interaction by surface plasmon resonance: Influence of spermidine on cooperativity

Rüfer, A., Neuenschwander, P. F., & Sauer, B. (2002) · Analytical Biochemistry · doi:10.1016/s0003-2697(02)00247-6 · Cited by 26

Calibration free concentration analysis by surface plasmon resonance in a capture mode

Visentin, J., Minder, L., Lee, J.-H., Taupin, J., & Primo, C. D. (2015) · Talanta · doi:10.1016/j.talanta.2015.11.025 · Cited by 26

Discovery of Novel Disruptor of Silencing Telomeric 1-Like (DOT1L) Inhibitors using a Target-Specific Scoring Function for the (S)-Adenosyl- l -methionine (SAM)-Dependent Methyltransferase Family

Wang, Y., Li, L., Zhang, B., Xing, J., Chen, S., Wan, W., Song, Y., Jiang, H., Jiang, H., Luo, C., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01785 · Cited by 26

Impact of N-glycosylation on Fcγ receptor / IgG interactions: unravelling differences with an enhanced surface plasmon resonance biosensor assay based on coiled-coil interactions

Cambay, F., Henry, O., Durocher, Y., & Crescenzo, G. D. (2019) · mAbs · doi:10.1080/19420862.2019.1581017 · Cited by 29

Binding of Amphipathic Cell Penetrating Peptide p28 to Wild Type and Mutated p53 as studied by Raman, Atomic Force and Surface Plasmon Resonance spectroscopies

Signorelli, S., Santini, S., Yamada, T., Bizzarri, A. R., Beattie, C. W., & Cannistraro, S. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.01.022 · Cited by 25

Application of atomic force microscopy and grating coupler for the characterization of biosensor surfaces

Kuhlmeier, D., Rodda, E., Kolarik, L. O., Furlong, D. N., & Bilitewski, U. (2003) · Biosensors and Bioelectronics · doi:10.1016/s0956-5663(02)00213-0 · Cited by 25

Surface plasmon resonance: a study of the effect of biotinylation on the selection of antibodies for use in immunoassays

Pearson, J. E., Kane, J. W., Petraki-Kallioti, I., Gill, A., & Vadgama, P. M. (1998) · Journal of Immunological Methods · doi:10.1016/s0022-1759(98)00167-7 · Cited by 25

Binding Analysis of 1α- and 17α-Dihydrotestosterone Derivatives to Homodimeric Sex Hormone-Binding Globulin

Metzger, J., Schnitzbauer, A. A., Meyer, M., Söder, M., Cuilleron, C. Y., Hauptmann, H., Huber, E., & Luppa, P. B. (2003) · Biochemistry · doi:10.1021/bi035269k · Cited by 25

Analytes kinetics in lateral flow membrane analyzed by cTnI monitoring using magnetic method

Oh, S., Anandakumar, S., Lee, C., Kim, K. W., Lim, B., & Kim, C. (2011) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2011.08.058 · Cited by 24

Kinetics and binding geometries of the complex between β2-microglobulin and its antibody: An AFM and SPR study

Coppari, E., Santini, S., Bizzarri, A. R., & Cannistraro, S. (2016) · Biophysical Chemistry · doi:10.1016/j.bpc.2016.01.002 · Cited by 24

Staphylococcus aureus iron-regulated surface determinant B (IsdB) protein interacts with von Willebrand factor and promotes adherence to endothelial cells

Alfeo, M. J., Pagotto, A., Barbieri, G., Foster, T. J., Vanhoorelbeke, K., Filippis, V. D., Speziale, P., & Pietrocola, G. (2021) · Scientific Reports · doi:10.1038/s41598-021-02065-w · Cited by 24

Carbohydrate Binding Mechanism of the Macrophage Galactose-type C-type Lectin 1 Revealed by Saturation Transfer Experiments

Sakakura, M., Oo-puthinan, S., Moriyama, C., Kimura, T., Moriya, J., Irimura, T., & Shimada, I. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804067200 · Cited by 24

Enhanced surface plasmon resonance immunoassay for human complement factor 4

Pei, R., Yang, X., & Wang, E. (2002) · Analytica Chimica Acta · doi:10.1016/s0003-2670(01)01417-9 · Cited by 24

Sensor Chip Using a Plasma-polymerized Film for Surface Plasmon Resonance Biosensors: Reliable Analysis of Binding Kinetics

Muguruma, H., Nagata, R., Nakamura, R., Sato, K., Uchiyama, S., & Karube, I. (2000) · Analytical Sciences · doi:10.2116/analsci.16.347 · Cited by 24

Properties of polyglutamine expansion in vitro and in a cellular model for Huntington's disease

Lunkes, A., Trottier, Y., Fagart, J., Schultz, P., Zeder‐Lutz, G., Moras, D., & Mandel, J. (1999) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1999.0453 · Cited by 24

Label-free optical biosensors based on a planar optical waveguide

Li, B., & Ju, H. (2013) · BioChip Journal · doi:10.1007/s13206-013-7401-7 · Cited by 23

Thermodynamic and kinetic insights into the interaction of kynurenic acid with human serum albumin: Spectroscopic and calorimetric approaches

Hornok, V., Juhász, Á., Paragi, G., Kovács, A. N., & Csapó, E. (2020) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2020.112869 · Cited by 23

Characterization of von Willebrand Factor Interaction with Collagens in Real Time Using Surface Plasmon Resonance

Li, F., Moake, J. L., & McIntire, L. V. (2002) · Annals of Biomedical Engineering · doi:10.1114/1.1521931 · Cited by 23

Changes in structural dynamics of the Grb2 adaptor protein upon binding of phosphotyrosine ligand to its SH2 domain

de Mol, N. J., Catalina, M., Fischer, M. J. E., Broutin, I., Maier, C. S., & Heck, A. J. R. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.03.016 · Cited by 23

Interaction of the Family-B DNA Polymerase from the Archaeon Pyrococcus furiosus with Deaminated Bases

Gill, S., O'Neill, R. J., Lewis, R. J., & Connolly, B. A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.07.015 · Cited by 24

Potential of biosensor technology for the characterization of interactions by quantitative affinity chromatography

Hall, D. R., & Winzor, D. J. (1998) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(97)00649-x · Cited by 23

ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1 1Edited by M. Yaniv

Dekker, J., Kanellopoulos, P. N., van Oosterhout, J. A. W. M., Stier, G., Tucker, P. A., & van der Vliet, P. C. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1652 · Cited by 23

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Day, E. S., Capili, A. D., Borysenko, C. W., Zafari, M. R., & Whitty, A. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.05.012 · Cited by 22

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Burkovitz, A., Leiderman, O., Sela‐Culang, I., Byk, G., & Ofran, Y. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1200757 · Cited by 21

Development of Antibody-Based Therapeutics

Tabrizi, M. A., Klakamp, S. L., & Bornstein, G. G. (2012) · Springer eBooks · doi:10.1007/978-1-4419-5955-3 · Cited by 23

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Dai, Y., Chiu, L., Sui, Y., Dai, Q., Penumutchu, S. R., Jain, N., Dai, L., Zorman, C. A., Tolbert, B. S., Sankaran, R. M., et al. (2018) · Talanta · doi:10.1016/j.talanta.2018.11.021 · Cited by 22

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Šakanović, A., Hodnik, V., Zavec, A. B., Eleršič, K., & Anderluh, G. (2019) · Methods in molecular biology · doi:10.1007/978-1-0716-5054-7_3 · Cited by 22

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Oh, M. H., Lee, J., Bae, S. Y., Seok, J. H., Kim, S., Chung, Y. B., Han, K. R., Kim, K. H., & Chung, M. S. (2014) · Food Control · doi:10.1016/j.foodcont.2014.07.056 · Cited by 22

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DiGiacomo, R., Xie, L., Cullen, C., & Indelicato, S. R. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.01.006 · Cited by 22

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Mohan, M. L., Jha, B. K., Gupta, M. K., Vasudevan, N. T., Martelli, E. E., Mosinski, J. D., & Prasad, S. V. N. (2013) · Science Signaling · doi:10.1126/scisignal.2003308 · Cited by 22

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Quinn, J. G., & O’Kennedy, R. J. (1999) · Analytical Letters · doi:10.1080/00032719908542911 · Cited by 22

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MacKenzie, C. R., & Hirama, T. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)12911-8 · Cited by 22

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Csapó, E., Juhász, Á., Varga, N., Sebők, D., Hornok, V., Janovák, L., & Dékány, I. (2016) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2016.05.090 · Cited by 21

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Saß, S., Stöcklein, W., Klevesath, A., Hurpin, J., Menger, M., & Hille, C. (2019) · The Analyst · doi:10.1039/c9an01247h · Cited by 21

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Khursigara, C. M., Crescenzo, G. D., Pawelek, P. D., & Coulton, J. W. (2005) · Protein Science · doi:10.1110/ps.051342505 · Cited by 21

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Witz, J. (1999) · Analytical Biochemistry · doi:10.1006/abio.1999.4087 · Cited by 21

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Slepak, V. Z. (2000) · Journal of Molecular Recognition · doi:10.1002/(sici)1099-1352(200001/02)13:1 · Cited by 21

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Wang, N., Xin, C., Li, Z., Zhang, G., Bai, L., Gong, Q., Xu, C., Xu, H., Yu, C., Li, L., et al. (2018) · Dyes and Pigments · doi:10.1016/j.dyepig.2018.12.027 · Cited by 20

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Sriram, R., Yadav, A. R., Mace, C. R., & Miller, B. L. (2011) · Analytical Chemistry · doi:10.1021/ac2001302 · Cited by 20

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Arauz, E. J., Aggarwal, V., Jain, A., Ha, T., & Chen, J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04127 · Cited by 20

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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

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

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

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