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

Nanostructured Plasmonic Sensors

Stewart, M. E., Anderton, C., Thompson, L. B., Maria, J., Gray, S. K., Rogers, J. A., & Nuzzo, R. G. (2008) · Chemical Reviews · doi:10.1021/cr068126n · Cited by 2,440

Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding

Krishnamurthy, V. M., Kaufman, G. K., Urbach, A. R., Gitlin, I., Gudiksen, K. L., Weibel, D. B., & Whitesides, G. M. (2008) · Chemical Reviews · doi:10.1021/cr050262p · Cited by 775

Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL

Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751

Advances in surface plasmon resonance biosensor analysis

Rich, R. L. (2000) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(99)00054-3 · Cited by 683

Membrane-Protein Interactions in Cell Signaling and Membrane Trafficking

Cho, W., & Stahelin, R. V. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.33.110502.133337 · Cited by 628

A Strategy for the Generation of Surfaces Presenting Ligands for Studies of Binding Based on an Active Ester as a Common Reactive Intermediate: A Surface Plasmon Resonance Study

Lahiri, J., Isaacs, L., Tien, J., & Whitesides, G. M. (1999) · Analytical Chemistry · doi:10.1021/ac980959t · Cited by 599

An Apical PDZ Protein Anchors the Cystic Fibrosis Transmembrane Conductance Regulator to the Cytoskeleton

Short, D. B., Trotter, K. W., Reczek, D., Kreda, S. M., Bretscher, A. P., Boucher, R. C., Stutts, M. J., & Milgram, S. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19797 · Cited by 465

The intracellular trafficking pathway of transferrin

Mayle, K. M., Le, A. M., & Kamei, D. T. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.09.009 · Cited by 466

Extending the Range of Rate Constants Available from BIACORE: Interpreting Mass Transport-Influenced Binding Data

Myszka, D. G., He, X., Dembo, M., Morton, T. A., & Goldstein, B. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77549-6 · Cited by 421

Analyzing a kinetic titration series using affinity biosensors

Karlsson, R., Katsamba, P. S., Nordin, H., Pol, E., & Myszka, D. G. (2005) · Analytical Biochemistry · doi:10.1016/j.ab.2005.09.034 · Cited by 390

Surface Plasmon Resonance: Applications in Understanding Receptor–Ligand Interaction

Pattnaik, P. (2005) · Applied Biochemistry and Biotechnology · doi:10.1385/abab:126:2:079 · Cited by 358

BIACORE Analysis of Histidine-Tagged Proteins Using a Chelating NTA Sensor Chip

Nieba, L., Axmann, S. E., Persson, A., Hämäläinen, M., Edebratt, F., Hansson, A., Lidholm, J., Magnusson, K., Karlsson, Å. F., & Plückthun, A. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2326 · Cited by 349

A review on novel developments and applications of immunosensors in food analysis

Ricci, F., Volpe, G., Micheli, L., & Palleschi, G. (2007) · Analytica Chimica Acta · doi:10.1016/j.aca.2007.10.046 · Cited by 338

Effects of common mutations in the SARS-CoV-2 Spike RBD and its ligand, the human ACE2 receptor on binding affinity and kinetics

Barton, M. I., MacGowan, S. A., Kutuzov, M. A., Dushek, O., Barton, G. J., & van der Merwe, P. A. (2021) · eLife · doi:10.7554/elife.70658 · Cited by 346

Interaction of Muscle and Brain Sodium Channels with Multiple Members of the Syntrophin Family of Dystrophin-Associated Proteins

Gee, S., Madhavan, R., Levinson, S. R., Caldwell, J. H., Sealock, R. W., & Froehner, S. C. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-01-00128.1998 · Cited by 334

Protein Detection by Nanopores Equipped with Aptamers

Rotem, D., Jayasinghe, L., Salichou, M., & Bayley, H. (2012) · Journal of the American Chemical Society · doi:10.1021/ja2105653 · Cited by 311

[13] Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors

Morton, T. A., & Myszka, D. G. (1998) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(98)95044-3 · Cited by 311

Nonspecific Binding—Fundamental Concepts and Consequences for Biosensing Applications

Frutiger, A., Tanno, A., Hwu, S., Tiefenauer, R. F., Vörös, J., & Nakatsuka, N. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00044 · Cited by 287

Probing Low Affinity and Multivalent Interactions with Surface Plasmon Resonance: Ligands for Concanavalin A

Mann, D. A., Kanai, M., Maly, D. J., & Kiessling, L. L. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9818506 · Cited by 277

Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface‐ and solution‐based biophysical methods

Day, Y. S. N., Baird, C. L., Rich, R. L., & Myszka, D. G. (2002) · Protein Science · doi:10.1110/ps.4330102 · Cited by 273

Nix directly binds to GABARAP: A possible crosstalk between apoptosis and autophagy

Schwarten, M., Mohrlüder, J., Ma, P., Stoldt, M., Thielmann, Y., Stangler, T., Hersch, N., Hoffmann, B., Merkel, R., & Willbold, D. (2009) · Autophagy · doi:10.4161/auto.5.5.8494 · Cited by 224

Implementing surface plasmon resonance biosensors in drug discovery

Myszka, D. G., & Rich, R. L. (2000) · Pharmaceutical Science & Technology Today · doi:10.1016/s1461-5347(00)00288-1 · Cited by 236

Surface plasmon resonance in protein–membrane interactions

Beseničar, M. P., Maček, P., Lakey, J. H., & Anderluh, G. (2006) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2006.02.010 · Cited by 236

CLAMP©: a biosensor kinetic data analysis program

Myszka, D. G., & Morton, T. A. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01183-9 · Cited by 217

Frequency Domain Detection of Biomolecules Using Silicon Nanowire Biosensors

Zheng, G., Gao, X., & Lieber, C. M. (2010) · Nano Letters · doi:10.1021/nl1020975 · Cited by 214

BIAcore for macromolecular interaction

Fivash, M. J., Towler, E. M., & Fisher, R. J. (1998) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(98)80091-8 · Cited by 205

Biosensor-surface plasmon resonance: Quantitative analysis of small molecule–nucleic acid interactions

Nguyen, B., Tanious, F. A., & Wilson, W. D. (2007) · Methods · doi:10.1016/j.ymeth.2006.09.009 · Cited by 203

Binding Affinity and Kinetic Analysis of Targeted Small Molecule-Modified Nanoparticles

Tassa, C., Duffner, J. L., Lewis, T. A., Weissleder, R., Schreiber, S. L., Koehler, A. N., & Shaw, S. Y. (2009) · Bioconjugate Chemistry · doi:10.1021/bc900438a · Cited by 202

A Novel Mechanism of TRAF Signaling Revealed by Structural and Functional Analyses of the TRADD–TRAF2 Interaction

Park, Y. C., Ye, H., Hsia, C. Y., Segal, D., Rich, R. L., Liou, H.-C., Myszka, D. G., & Wu, H. (2000) · Cell · doi:10.1016/s0092-8674(00)80889-2 · Cited by 188

Obscurin Is a Ligand for Small Ankyrin 1 in Skeletal Muscle

Kontrogianni‐Konstantopoulos, A., Jones, E. M., van Rossum, D. B., & Bloch, R. J. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-07-0411 · Cited by 183

Molecular Interaction of Porphyromonas gingivalis with Host Cells: Implication for the Microbial Pathogenesis of Periodontal Disease

Amano, A. (2003) · Journal of Periodontology · doi:10.1902/jop.2003.74.1.90 · Cited by 183

Kinetic analysis of a high-affinity antibody/antigen interaction performed by multiple Biacore users

Katsamba, P. S., Navratilova, I. H., Calderon-Cacia, M., Fan, L., Thornton, K. H., Zhu, M., Bos, T. V., Forte, C. P., Friend, D. J., Laird‐Offringa, I. A., et al. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.01.034 · Cited by 182

Label‐Free Microscale Thermophoresis Discriminates Sites and Affinity of Protein–Ligand Binding

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 International Edition · doi:10.1002/anie.201204268 · Cited by 182

Enhanced Performance of an Affinity Biosensor Interface Based on Mixed Self-Assembled Monolayers of Thiols on Gold

Frederix, F., Bonroy, K., Laureyn, W., Reekmans, G., Campitelli, A., Dehaen, W., & Maes, G. (2003) · Langmuir · doi:10.1021/la026908f · Cited by 181

Phosphatidylinositol 3-Phosphate Induces the Membrane Penetration of the FYVE Domains of Vps27p and Hrs

Stahelin, R. V., Long, F., Diraviyam, K., Bruzik, K. S., Murray, D., & Cho, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201106200 · Cited by 175

Contrasting Membrane Interaction Mechanisms of AP180 N-terminal Homology (ANTH) and Epsin N-terminal Homology (ENTH) Domains

Stahelin, R. V., Long, F., Peter, B. J., Murray, D., Camilli, P. V. D., McMahon, H. T., & Cho, W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302865200 · Cited by 170

Exploring “one-shot” kinetics and small molecule analysis using the ProteOn XPR36 array biosensor

Bravman, T., Bronner, V., Lavie, K., Notcovich, A., Papalia, G. A., & Myszka, D. G. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.08.005 · Cited by 166

Genetics of epithelial polarity and pattern in the Drosophila retina

Reifegerste, R., & Moses, K. (1999) · BioEssays · doi:10.1002/(sici)1521-1878(199904)21:4 · Cited by 62

Simultaneous Multiple Immunoassays in a Compact Disc–Shaped Microfluidic Device Based on Centrifugal Force

Honda, N., Lindberg, U., Andersson, P., Hoffmann, S., & Takei, H. (2005) · Clinical Chemistry · doi:10.1373/clinchem.2005.053348 · Cited by 156

Binding Kinetics of Darunavir to Human Immunodeficiency Virus Type 1 Protease Explain the Potent Antiviral Activity and High Genetic Barrier

Dierynck, I., Wit, M. D., Gustin, E. M., Keuleers, I., Vandersmissen, J., Hallenberger, S., & Hertogs, K. (2007) · Journal of Virology · doi:10.1128/jvi.01184-07 · Cited by 157

High-Sensitivity Detection of Carbohydrate Antigen 15-3 Using a Gold/Zinc Oxide Thin Film Surface Plasmon Resonance-Based Biosensor

Chang, C., Chiu, N., Lin, D. S., Chu-Su, Y., Liang, Y.-H., & Lin, C. (2010) · Analytical Chemistry · doi:10.1021/ac901797j · Cited by 155

Binding of Polyubiquitin Chains to Ubiquitin-associated (UBA) Domains of HHR23A

Raasi, S., Orlov, I., Fleming, K. G., & Pickart, C. M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.06.057 · Cited by 159

Differential Roles of Ionic, Aliphatic, and Aromatic Residues in Membrane−Protein Interactions: A Surface Plasmon Resonance Study on Phospholipases A2

Stahelin, R. V., & Cho, W. (2001) · Biochemistry · doi:10.1021/bi0020325 · Cited by 154

Mechanism of Diacylglycerol-induced Membrane Targeting and Activation of Protein Kinase Cθ

Melowic, H. R., Stahelin, R. V., Blatner, N. R., Tian, W., Hayashi, K., Altman, A., & Cho, W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700119200 · Cited by 152

Nonenzymatic Glycation Impairs the Antiinflammatory Properties of Apolipoprotein A-I

Nobécourt, E., Tabet, F., Lambert, G. C., Puranik, R., Bao, S., Yan, L., Davies, M. J., Brown, B. E., Jenkins, A. J., Dusting, G. J., et al. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.201715 · Cited by 154

Membrane Binding Mechanisms of the PX Domains of NADPH Oxidase p40 and p47

Stahelin, R. V., Burian, A., Bruzik, K. S., Murray, D., & Cho, W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212579200 · Cited by 143

The Mechanism of Membrane Targeting of Human Sphingosine Kinase 1

Stahelin, R. V., Hwang, J.-H., Kim, J.-H., Park, Z., Johnson, K. R., Obeid, L. M., & Cho, W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507574200 · Cited by 143

Label‐free determination of protein–ligand binding constants using mass spectrometry and validation using surface plasmon resonance and isothermal titration calorimetry

Jecklin, M. C., Schauer, S., Dumelin, C. E., & Zenobi, R. (2009) · Journal of Molecular Recognition · doi:10.1002/jmr.951 · Cited by 145

Analytical aspects of biosensors

Pearson, J. E., Gill, A., & Vadgama, P. M. (2000) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/0004563001899131 · Cited by 141

Carbohydrate-lectin interactions assessed by surface plasmon resonance

Duverger, E. (2003) · Biochimie · doi:10.1016/s0300-9084(03)00060-9 · Cited by 137

Investigating the Interaction between Osteoprotegerin and Receptor Activator of NF-κB or Tumor Necrosis Factor-related Apoptosis-inducing Ligand

Vitovski, S., Phillips, J. S., Sayers, J. R., & Croucher, P. I. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706078200 · Cited by 133

Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods

Drake, A. W., Myszka, D. G., & Klakamp, S. L. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2003.12.025 · Cited by 131

Biomolecular interaction analysis: affinity biosensor technologies for functional analysis of proteins

Malmqvist, M., & Karlsson, R. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80077-4 · Cited by 131

A peptide derived from the nonreceptor binding region of urokinase plasminogen activator (uPA) inhibits tumor progression and angiogenesis and induces tumor cell death in vivo

Guo, Y., Higazi, A. A., Arakelian, A., Sachais, B. S., Cines, D., Goldfarb, R. H., Jones, T. R., Kwaan, H., Mazar, A. P., & Rabbani, S. A. (2000) · The FASEB Journal · doi:10.1096/fj.14.10.1400 · Cited by 130

Engineered Nanopore of Phi29 DNA-Packaging Motor for Real-Time Detection of Single Colon Cancer Specific Antibody in Serum

Wang, S., Haque, F., Rychahou, P. G., Evers, B. M., & Guo, P. (2013) · ACS Nano · doi:10.1021/nn404435v · Cited by 129

Ceramide 1-Phosphate Acts as a Positive Allosteric Activator of Group IVA Cytosolic Phospholipase A2α and Enhances the Interaction of the Enzyme with Phosphatidylcholine

Subramanian, P., Stahelin, R. V., Szulc, Z. M., Bielawska, A. E., Cho, W., & Chalfant, C. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414173200 · Cited by 128

Biochemical Characterization of the Interaction between the Saccharomyces cerevisiae MSH2-MSH6 Complex and Mispaired Bases in DNA

Marsischky, G., & Kolodner, R. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.26668 · Cited by 126

Biosensor Analysis of Drug–Target Interactions: Direct and Competitive Binding Assays for Investigation of Interactions between Thrombin and Thrombin Inhibitors

Karlsson, R., Kullman-Magnusson, M., Hämäläinen, M., Remaeus, A., Andersson, K., Borg, P., Gyzander, E., & Deinum, J. (2000) · Analytical Biochemistry · doi:10.1006/abio.1999.4406 · Cited by 126

The Molecular Basis of Differential Subcellular Localization of C2 Domains of Protein Kinase C-α and Group IVa Cytosolic Phospholipase A2

Stahelin, R. V., Rafter, J. D., Das, S., & Cho, W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212864200 · Cited by 124

Real-Time Monitoring of the Interactions of Two-Stranded de Novo Designed Coiled-Coils: Effect of Chain Length on the Kinetic and Thermodynamic Constants of Binding

Crescenzo, G. D., Litowski, J. R., Hodges, R. S., & O'Connor‐McCourt, M. D. (2003) · Biochemistry · doi:10.1021/bi0268450 · Cited by 123

Mechanism of Diacylglycerol-induced Membrane Targeting and Activation of Protein Kinase Cδ

Stahelin, R. V., Digman, M. A., Medkova, M., Ananthanarayanan, B., Rafter, J. D., Melowic, H. R., & Cho, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403191200 · Cited by 123

Roles of Ionic Residues of the C1 Domain in Protein Kinase C-α Activation and the Origin of Phosphatidylserine Specificity

Bittova, L., Stahelin, R. V., & Cho, W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008491200 · Cited by 121

Identification and Optimization of Regeneration Conditions for Affinity-Based Biosensor Assays. A Multivariate Cocktail Approach

Andersson, K., Hämäläinen, M., & Malmqvist, M. (1999) · Analytical Chemistry · doi:10.1021/ac981271j · Cited by 121

Membrane Binding Assays for Peripheral Proteins

Cho, W., Bittova, L., & Stahelin, R. V. (2001) · Analytical Biochemistry · doi:10.1006/abio.2001.5225 · Cited by 121

Comparison of biosensor platforms in the evaluation of high affinity antibody-antigen binding kinetics

Yang, D., Singh, A., Wu, H., & Kroe-Barrett, R. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.06.024 · Cited by 120

Technological Advances in High-Throughput Screening

Liu, B., Li, S., & Hu, J. (2004) · American Journal of PharmacoGenomics · doi:10.2165/00129785-200404040-00006 · Cited by 120

A structural basis for the inhibition of collagen‐stimulated platelet function by quercetin and structurally related flavonoids

Wright, B., Moraes, L. A., Kemp, C. F., Mullen, W., Crozier, A., Lovegrove, J. A., & Gibbins, J. M. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00632.x · Cited by 118

Plasma-polymerized films for biosensors

Muguruma, H. (1999) · TrAC Trends in Analytical Chemistry · doi:10.1016/s0165-9936(98)00098-3 · Cited by 116

Molecular Competition for NKG2D

O’Callaghan, C. A., Cerwenka, A., Willcox, B. E., Lanier, L. L., & Björkman, P. J. (2001) · Immunity · doi:10.1016/s1074-7613(01)00187-x · Cited by 115

Surface Plasmon Resonance Biomolecular Interaction Analysis Mass Spectrometry. 1. Chip-Based Analysis

Nelson, R. W., Krone, J. R., & Jansson, Ö. (1997) · Analytical Chemistry · doi:10.1021/ac970538w · Cited by 115

Peptide-Lipid Interactions: Experiments and Applications

Galdiero, S., Falanga, A., Cantisani, M., Vitiello, M., Morelli, G., & Galdiero, M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140918758 · Cited by 113

Equilibrium Analysis of High Affinity Interactions Using BIACORE

Myszka, D. G., Jonsen, M. D., & Graves, B. J. (1998) · Analytical Biochemistry · doi:10.1006/abio.1998.2937 · Cited by 111

The Conformation of Apolipoprotein A-I in High-Density Lipoproteins Is Influenced by Core Lipid Composition and Particle Size: A Surface Plasmon Resonance Study

Curtiss, L. K., Bonnet, D. J., & Rye, K. (2000) · Biochemistry · doi:10.1021/bi992902m · Cited by 110

Biodistribution of a Bispecific Single-chain Diabody and Its Half-life Extended Derivatives

Stork, R., Campigna, E., Robert, B., Müller, D., & Kontermann, R. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.027078 · Cited by 114

The Pleckstrin Homology Domain of Phospholipase C-β2 as an Effector Site for Rac

Snyder, J. T., Singer, A. U., Wing, M. R., Harden, T. K., & Sondek, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301418200 · Cited by 103

The Leukocyte Integrin αDβ2 Binds VCAM-1: Evidence for a Binding Interface Between I Domain and VCAM-1

van der Vieren, M., Crowe, D. T., Hoekstra, D., Vazeux, R., Hoffman, P. A., Grayson, M. H., Bochner, B. S., Gallatin, W. M., & Staunton, D. E. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.4.1984 · Cited by 103

Mechanism of Membrane Binding of the Phospholipase D1 PX Domain

Stahelin, R. V., Ananthanarayanan, B., Blatner, N. R., Singh, S. M., Bruzik, K. S., Murray, D., & Cho, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407798200 · Cited by 102

Examination of the Kinetics of Herpes Simplex Virus Glycoprotein D Binding to the Herpesvirus Entry Mediator, Using Surface Plasmon Resonance

Willis, S. H., Rux, A. H., Peng, C., Whitbeck, J. C., Nicola, A. V., Lou, H., Hou, W., Salvador, L., Eisenberg, R. J., & Cohen, G. H. (1998) · Journal of Virology · doi:10.1128/jvi.72.7.5937-5947.1998 · Cited by 102

Characterization of Interactions between the Anti-apoptotic Protein BAG-1 and Hsc70 Molecular Chaperones

Stuart, J. K., Myszka, D. G., Joss, L., Mitchell, R. S., McDonald, S. M., Xie, Z., Takayama, S.-I. J., Reed, J. C., & Ely, K. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22506 · Cited by 102

Kinetic studies on the interactions of heparin and complement proteins using surface plasmon resonance

YU, H., MUNOZ, E., Edens, R. E., & Linhardt, R. J. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.08.003 · Cited by 101

Surface Plasmon Resonance Enhanced Real-Time Photoelectrochemical Protein Sensing by Gold Nanoparticle-Decorated TiO2 Nanowires

Da, P., Li, W., Lin, X. H., Wang, Y., Tang, J., & Zheng, G. (2014) · Analytical Chemistry · doi:10.1021/ac501406x · Cited by 100

Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions

Stahelin, R. V. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0713 · Cited by 96

Biotechnological applications of surface plasmon resonance

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Detection of blood group antigens utilising immobilised antibodies and surface plasmon resonance

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