Fluorescence Resonance Energy Transfer
"Fluorescence Resonance Energy Transfer" 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 type of FLUORESCENCE SPECTROSCOPY using two FLUORESCENT DYES with overlapping emission and absorption spectra, which is used to indicate proximity of labeled molecules. This technique is useful for studying interactions of molecules and PROTEIN FOLDING.
Descriptor ID |
D031541
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MeSH Number(s) |
E05.196.712.516.600.676.500 G01.154.240.280 G02.111.255.280
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Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Fluorescence Resonance Energy Transfer".
Below are MeSH descriptors whose meaning is more specific than "Fluorescence Resonance Energy Transfer".
This graph shows the total number of publications written about "Fluorescence Resonance Energy Transfer" by people in this website by year, and whether "Fluorescence Resonance Energy Transfer" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2005 | 1 | 1 | 2 |
2006 | 1 | 1 | 2 |
2009 | 0 | 1 | 1 |
2010 | 0 | 1 | 1 |
2011 | 0 | 1 | 1 |
2012 | 0 | 2 | 2 |
2014 | 0 | 1 | 1 |
2016 | 0 | 1 | 1 |
2017 | 0 | 1 | 1 |
2021 | 0 | 1 | 1 |
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Below are the most recent publications written about "Fluorescence Resonance Energy Transfer" by people in Profiles.
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Increased testosterone and proinflammatory cytokines in patients with polycystic ovary syndrome correlate with elevated GnRH receptor autoantibody activity assessed by a fluorescence resonance energy transfer-based bioassay. Endocrine. 2021 10; 74(1):163-171.
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An engineered transforming growth factor ß (TGF-ß) monomer that functions as a dominant negative to block TGF-ß signaling. J Biol Chem. 2017 04 28; 292(17):7173-7188.
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Real-time measurements to characterize dynamics of emulsion interface during simulated intestinal digestion. Colloids Surf B Biointerfaces. 2016 May 01; 141:233-241.
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Membrane-cytoskeleton interactions in cholesterol-dependent domain formation. Essays Biochem. 2015; 57:177-87.
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Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4. Biochim Biophys Acta. 2014 Dec; 1841(12):1716-24.
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Fluorescence analysis of the lipid binding-induced conformational change of apolipoprotein E4. Biochemistry. 2012 Jul 17; 51(28):5580-8.
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Monomer-monomer interactions propagate structural transitions necessary for pore formation by the cholesterol-dependent cytolysins. J Biol Chem. 2012 Jul 13; 287(29):24534-43.
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Zinc binding to human lactogenic hormones and the human prolactin receptor. FEBS Lett. 2011 Jun 23; 585(12):1783-8.
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Dimeric arrangement of the parathyroid hormone receptor and a structural mechanism for ligand-induced dissociation. J Biol Chem. 2010 Apr 16; 285(16):12435-44.
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Colloidal lenses allow high-temperature single-molecule imaging and improve fluorophore photostability. Nat Nanotechnol. 2010 Feb; 5(2):127-32.