The DOI matches its Crossref record; 78 of the 78 references it cites were found in a registry or an index.
USE OF SURFACE PLASMON RESONANCE TO PROBE THE EQUILIBRIUM AND DYNAMIC ASPECTS OF INTERACTIONS BETWEEN BIOLOGICAL MACROMOLECULES
Abstract
▪ Abstract Surface plasmon resonance biosensors have become increasingly popular for the qualitative and quantitative characterization of the specific binding of a mobile reactant to a binding partner immobilized on the sensor surface. This article reviews the use of this new technique to measure the binding affinities and the kinetic constants of reversible interactions between biological macromolecules. Immobilization techniques, the most commonly employed experimental strategies, and various analytical approaches are summarized. In recent years, several sources of potential artifacts have been identified: immobilization of the binding partner, steric hindrance of binding to adjacent binding sites at the sensor surface, and finite rate of mass transport of the mobile reactant to the sensor surface. Described here is the influence of these artifacts on the measured binding kinetics and equilibria, together with suggested control experiments.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The adsorption of gases on plane surfaces of glass, mica and platinum
Langmuir, I. (1918) · Journal of the American Chemical Society · doi:10.1021/ja02242a004 · Cited by 23,242
Notizen: Radiative Decay of Non Radiative Surface Plasmons Excited by Light
Kretschmann, E., & Raether, H. (1968) · Zeitschrift für Naturforschung A · doi:10.1515/zna-1968-1247 · Cited by 3,377
Supported Membranes: Scientific and Practical Applications
Sackmann, E. (1996) · Science · doi:10.1126/science.271.5245.43 · Cited by 2,151
Macromolecular Crowding: Biochemical, Biophysical, and Physiological Consequences
Zimmerman, S. B., & Minton, A. P. (1993) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.22.060193.000331 · Cited by 1,513
Johnsson, B., Löfås, S., & Lindquist, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90424-r · Cited by 1,262
Karlsson, R., Michaelsson, A., & Mattsson, L. (1991) · Journal of Immunological Methods · doi:10.1016/0022-1759(91)90331-9 · Cited by 1,077
Stenberg, E., Persson, B., Roos, H., & Urbaniczky, C. (1991) · Journal of Colloid and Interface Science · doi:10.1016/0021-9797(91)90284-f · Cited by 1,059
"Diabodies": small bivalent and bispecific antibody fragments.
Holliger, P., Prospero, T., & Winter, G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6444 · Cited by 874
Mrksich, M., & Whitesides, G. M. (1996) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.25.060196.000415 · Cited by 850
Löfås, S., & Johnsson, B. (1990) · J. Chem. Soc., Chem. Commun. · doi:10.1039/c39900001526 · Cited by 766
Cited by
Haes, A. J., & Van Duyne, R. P. (2002) · Journal of the American Chemical Society · doi:10.1021/ja020393x · Cited by 2,057
Theory of surface plasmons and surface-plasmon polaritons
Pitarke, J. M., Silkin, V. M., Chulkov, E. V., & Echenique, P. M. (2007) · Reports on Progress in Physics · doi:10.1088/0034-4885/70/1/r01 · Cited by 1,524
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
Microfluidic systems in proteomics
Lion, N., Rohner, T. C., Dayon, L., Arnaud, I. L., Damoc, E., Youhnovski, N., Wu, Z., Roussel, C., Josserand, J., Jensen, H., et al. (2003) · ELECTROPHORESIS · doi:10.1002/elps.200305629 · Cited by 262
Mutants of ETS domain PU.1 and GGAA/T recognition: Free energies and kinetics
Pio, F., Assa‐Munt, N., Yguerabide, J., & Maki, R. A. (1999) · Protein Science · doi:10.1110/ps.8.10.2098 · Cited by 22
Metadata
- Authors
- Schuck, P.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 1997-06
- Volume
- 26
- Issue
- 1
- Pages
- 541-566
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2145572269
- Cited by
- 657
- References
- 78
- FWCI
- 11.92
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: USE OF SURFACE PLASMON RESONANCE TO PROBE THE EQUILIBRIUM AND DYNAMIC ASPECTS OF INTERACTIONS BETWEEN BIOLOGICAL MACROMOLECULES. https://app.cochat.ai/papers/10.1146/annurev.biophys.26.1.541
- The paper
- Schuck, P. (1997). USE OF SURFACE PLASMON RESONANCE TO PROBE THE EQUILIBRIUM AND DYNAMIC ASPECTS OF INTERACTIONS BETWEEN BIOLOGICAL MACROMOLECULES. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.26.1.541
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.