 Surface Plasmon Resonance
"Surface Plasmon Resonance" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A biosensing technique in which biomolecules capable of binding to specific analytes or ligands are first immobilized on one side of a metallic film. Light is then focused on the opposite side of the film to excite the surface plasmons, that is, the oscillations of free electrons propagating along the film's surface. The refractive index of light reflecting off this surface is measured. When the immobilized biomolecules are bound by their ligands, an alteration in surface plasmons on the opposite side of the film is created which is directly proportional to the change in bound, or adsorbed, mass. Binding is measured by changes in the refractive index. The technique is used to study biomolecular interactions, such as antigen-antibody binding.
| Descriptor ID |
D020349
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| MeSH Number(s) |
E05.196.890 E05.601.043.700
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| Concept/Terms |
Surface Plasmon Resonance- Surface Plasmon Resonance
- Plasmon Resonance, Surface
- Plasmon Resonances, Surface
- Resonance, Surface Plasmon
- Resonances, Surface Plasmon
- Surface Plasmon Resonances
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Below are MeSH descriptors whose meaning is more general than "Surface Plasmon Resonance".
Below are MeSH descriptors whose meaning is more specific than "Surface Plasmon Resonance".
This graph shows the total number of publications written about "Surface Plasmon Resonance" by people in this website by year, and whether "Surface Plasmon Resonance" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
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| 2007 | 1 | 0 | 1 | | 2008 | 1 | 0 | 1 | | 2010 | 0 | 1 | 1 | | 2013 | 0 | 1 | 1 | | 2015 | 0 | 1 | 1 | | 2017 | 0 | 1 | 1 |
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Below are the most recent publications written about "Surface Plasmon Resonance" by people in Profiles.
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Lee CH, Romain G, Yan W, Watanabe M, Charab W, Todorova B, Lee J, Triplett K, Donkor M, Lungu OI, Lux A, Marshall N, Lindorfer MA, Goff OR, Balbino B, Kang TH, Tanno H, Delidakis G, Alford C, Taylor RP, Nimmerjahn F, Varadarajan N, Bruhns P, Zhang YJ, Georgiou G. IgG Fc domains that bind C1q but not effector Fc? receptors delineate the importance of complement-mediated effector functions. Nat Immunol. 2017 Aug; 18(8):889-898.
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Hoffmann C, Castro M, Rinken A, Leurs R, Hill SJ, Vischer HF. Ligand Residence Time at G-protein-Coupled Receptors-Why We Should Take Our Time To Study It. Mol Pharmacol. 2015 Sep; 88(3):552-60.
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Craft JW, Zhang H, Charendoff MN, Mindrebo JT, Schwartz RJ, Briggs JM. Associations between the Rho kinase-1 catalytic and PH domain regulatory unit. J Mol Graph Model. 2013 Nov; 46:74-82.
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Carreño R, Brown WS, Li D, Hernandez JA, Wang Y, Kim TK, Craft JW, Komanduri KV, Radvanyi LG, Hwu P, Molldrem JJ, Legge GB, McIntyre BW, Ma Q. 2E8 binds to the high affinity I-domain in a metal ion-dependent manner: a second generation monoclonal antibody selectively targeting activated LFA-1. J Biol Chem. 2010 Oct 22; 285(43):32860-8.
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Yao M, Tan OK, Tjin SC, Wolfe JC. Effects of intermediate dielectric films on multilayer surface plasmon resonance behavior. Acta Biomater. 2008 Nov; 4(6):2016-27.
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Lapotko DO, Lukianova-Hleb EY, Oraevsky AA. Clusterization of nanoparticles during their interaction with living cells. Nanomedicine (Lond). 2007 Apr; 2(2):241-53.
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