ArticleBiophysical journal2013
FRET spectrometry: a new tool for the determination of protein quaternary structure in living cells.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- VEGFR2 dimerization kinetics on the cell surface determined by microscopy and mathematical modeling.Biophysical journal · 2026Article
- Precise Alternation Between Image-Forming Sample Planes Enables Quantitative Monitoring of Receptor-Arrestin Interaction Dynamics at the Plasma Membrane of Live Cells.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic insights from the atomic-level quaternary structure of short-lived GPCR oligomers of the human secretin receptor in live cells.Communications biology · 2025Article
- Protein lipidation in the tumor microenvironment: enzymology, signaling pathways, and therapeutics.Molecular cancer · 2025Review
- Mechanistic insights from the atomic-level quaternary structure of short-lived GPCR oligomers in live cells.Research square · 2024Article
- Implementation of FRET Spectrometry Using Temporally Resolved Fluorescence: A Feasibility Study.International journal of molecular sciences · 2024Article
- Atomistic View of the Energy Transfer in a Fluorophore-Functionalized Gold Nanocluster.Journal of the American Chemical Society · 2023Article
- Monoclonal Antibodies as Probes to Study Ligand-Induced Conformations of Troponin Subunits.Frontiers in physiology · 2022Article
- Ab Initio Derivation of the FRET Equations Resolves Old Puzzles and Suggests Measurement Strategies.Biophysical journal · 2019Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- New Techniques to Study Intracellular Receptors in Living Cells: Insights Into RIG-I-Like Receptor Signaling.Advances in experimental medicine and biology · 2019Review
- Fluorescence-based approaches for monitoring membrane receptor oligomerization.Journal of biosciences · 2018Review
- Biophysical aspects of biomineralization.Biophysical reviews · 2017Review
- Quantifying the Interaction between EGFR Dimers and Grb2 in Live Cells.Biophysical journal · 2017Article
- Quantitative microspectroscopic imaging reveals viral and cellular RNA helicase interactions in live cells.The Journal of biological chemistry · 2017Article
- Carbonic Anhydrases Function in Anther Cell Differentiation Downstream of the Receptor-Like Kinase EMS1.The Plant cell · 2017Article
- Methods used to study the oligomeric structure of G-protein-coupled receptors.Bioscience reports · 2017Review
- An intermolecular FRET sensor detects the dynamics of T cell receptor clustering.Nature communications · 2017Article
- Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination.Plant physiology · 2017Article
- Detecting stoichiometry of macromolecular complexes in live cells using FRET.Nature communications · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Förster resonance energy transfer (FRET) is an exquisitely sensitive method for detection of molecular interactions and conformational changes in living cells. The recent advent of fluorescence imaging technology with single-molecule (or molecular-complex) sensitivity, together with refinements in the kinetic theory of FRET, provide the necessary tool kits for determining the stoichiometry and relative disposition of the protomers within protein complexes (i.e., quaternary structure) of membrane receptors and transporters in living cells. In contrast to standard average-based methods, this method relies on the analysis of distributions of apparent FRET efficiencies, E(app), across the image pixels of individual cells expressing proteins of interest. The most probable quaternary structure of the complex is identified from the number of peaks in the E(app) distribution and their dependence on a single parameter, termed pairwise FRET efficiency. Such peaks collectively create a unique FRET spectrum corresponding to each oligomeric configuration of the protein. Therefore, FRET could quite literally become a spectrometric method--akin to that of mass spectrometry--for sorting protein complexes according to their size and shape.
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