FRET imaging

By E. Jares-Erijman, T. Jovin. Nature Biotechnology, 2003

1,143 citations recorded by the source corpus.

Subfields: Biophysics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7b8e133ee7c44f5933654fcef0ba134e2054f7db

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Citations in the corpus

A quantitative protocol for dynamic measurements of protein interactions by Förster resonance energy transfer-sensitized fluorescence emission (2009, methodology): “…donor quantum yield, the refractive index of the medium through which the signals propagate and the orientation factor, k2, between the donor and acceptor dipole moments (Van Der Meer 2002), all of which may vary in time and in space within a living cell (Lakowicz 1999; Jares-Erijman & Jovin 2003).”
Learning rates and states from biophysical time series: a Bayesian approach to model selection and single-molecule FRET data. (2009, background): “FRET (10, 11, 12, 13) refers to the transfer of energy from a donor fluorophore (which has been excited by short-wavelength light) to an acceptor fluorophore (which then emits light of a longer wavelength) with an efficiency which decreases as the distance between the fluorophores increases.”
High mobility group box 1 protein interacts with multiple Toll-like receptors. (2006, methodology): “FRET-positive pixels and efficiencies were calculated by directly subtracting images obtained before acceptor photobleaching from images acquired immediately after acceptor photobleaching to reveal the increased fluorescence of the donor (4, 13, 20).”
Biosensing with Luminescent Semiconductor Quantum Dots (2006, background): “Fluorescence resonance energy transfer (FRET) between donor and acceptor molecules has been extensively used in biophysical and biochemical studies to probe ligand-receptor binding and molecular structural changes [2,105-107].”