The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Analyzing a kinetic titration series using affinity biosensors
Abstract
The classical method of measuring binding constants with affinity-based biosensors involves testing several analyte concentrations over the same ligand surface and regenerating the surface between binding cycles. Here we describe an alternative approach to collecting kinetic binding data, which we call "kinetic titration." This method involves sequentially injecting an analyte concentration series without any regeneration steps. Through a combination of simulation and experimentation, we show that this method can be as robust as the classical method of analysis. In addition, kinetic titrations can be more efficient than the conventional data collection method and allow us to fully characterize analyte binding to ligand surfaces that are difficult to regenerate.
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“Phospho-mimetic mutations (T231E, S235E or T231E/S235E) located near the B1-1 epitope abolished light-induced phase separation.31”
From A Proline-Rich-Domain-Binding Single Domain Antibody Selectively Inhibits RNA-Induced Phase Separation of Tau (2026) · cites this paper as [31]
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“Interestingly, the PRD of tau can form clusters in cells when fused to a photosensitive oligomerization domain, unlike the MTBD region.”
From A Proline-Rich-Domain-Binding Single Domain Antibody Selectively Inhibits RNA-Induced Phase Separation of Tau (2026) · cites this paper as [31]
Citations
Cites
Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
Myszka, D. G. (1997) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(97)80157-7 · Cited by 552
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Research works printed but not linked: 13
- Myszka, 1999, Survey of the 1998 optical biosensor literature, J. Mol. Recognit., 12, 390, 10.1002/(SICI)1099-1352(199911/12)12:6<390::AID-JMR482>3.0.CO;2-8 · DOI
- Rich, 2002, Survey of the year 2001 commercial optical biosensor literature, J. Mol. Recognit., 15, 352, 10.1002/jmr.598 · DOI
- Myszka, 1998, Equilibrium analysis of high affinity interactions using BIACORE, Anal. Biochem., 265, 326, 10.1006/abio.1998.2937 · DOI
- Myszka, 1998, CLAMP: a biosensor kinetic data analysis program, Trends Biochem. Sci., 23, 149, 10.1016/S0968-0004(98)01183-9 · DOI
- Myszka, 1999, Improving biosensor analysis, J. Mol. Recognit., 12, 279, 10.1002/(SICI)1099-1352(199909/10)12:5<279::AID-JMR473>3.0.CO;2-3 · DOI · Paper page
- Karlsson, 2000, Biosensor analysis of drug-target interactions: direct and competitive binding assays for investigation of interactions between thrombin and thrombin inhibitors, Anal. Biochem., 278, 1, 10.1006/abio.1999.4406 · DOI
- Karlsson, 1991, Kinetic analysis of monoclonal antibody–antigen interactions with a new biosensor based analytical system, J. Immunol. Methods, 145, 229, 10.1016/0022-1759(91)90331-9 · DOI
- Karlsson, 1995, Surface plasmon resonance detection and multispot sensing for direct monitoring of interactions involving low-molecular-weight analytes and for determination of low affinities, Anal. Biochem., 228, 274, 10.1006/abio.1995.1350 · DOI
- Cannon, 2004, Comparative analyses of a small molecule/enzyme interaction by multiple users of Biacore technology, Anal. Biochem., 330, 98, 10.1016/j.ab.2004.02.027 · DOI
- Karlsson, 1997, Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors, J. Immunol. Methods, 200, 121, 10.1016/S0022-1759(96)00195-0 · DOI
- Navratilova, 2005, Measuring long association phases using Biacore, Anal. Biochem., 344, 295, 10.1016/j.ab.2005.05.025 · DOI
- Drake, 2004, Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods, Anal. Biochem., 328, 35, 10.1016/j.ab.2003.12.025 · DOI
- Karlsson, 1999, Affinity analysis of non-steady-state data obtained under mass transport limited conditions using BIAcore technology, J. Mol. Recognit., 12, 285, 10.1002/(SICI)1099-1352(199909/10)12:5<285::AID-JMR469>3.0.CO;2-Y · DOI · Paper page
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Thiou, S., Martin, L., Manousaki, E., Nguyen, M., Mortelecque, J., Heidsieck, L., Cantrelle, F.-X., Blum, D., Buée-Scherrer, V., Buée, L., et al. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6c00110 · Cited by 1
Metadata
- Authors
- Karlsson, R., Katsamba, P. S., Nordin, H., Pol, E., & Myszka, D. G.
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 2006-02
- Volume
- 349
- Issue
- 1
- Pages
- 136-147
- ISSN
- 0003-2697
- Cited by
- 382
- References
- 1
- Language
- en
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