Results 11 to 20 of about 8,058,982 (114)

Fluorescence resonance energy transfer studies of protein interactions [PDF]

open access: yes, 2008
This thesis presents an investigation of fluorescence resonance energy transfer (FRET) as a reporting signal for protein-protein interactions. Quantitative optical assays to measure protein binding, conjugation and deconjugation are developed and results
Martin, Sarah Friede
core   +2 more sources

Advanced Fluorescence Microscopy Techniques-FRAP, FLIP, FLAP, FRET and FLIM [PDF]

open access: yes, 2012
Fluorescence microscopy provides an efficient and unique approach to study fixed and living cells because of its versatility, specificity, and high sensitivity.
Ankerhold, Richard   +5 more
core   +1 more source

No better time to FRET: shedding light on host pathogen interactions [PDF]

open access: yes, 2010
Understanding the spatio-temporal subversion of host cell signaling by bacterial virulence factors is key to combating infectious diseases. Following a recent study by Buntru and co-workers published in BMC Biology, we review how fluorescence (Forster ...
Leong, J.M.   +5 more
core   +1 more source

Linear approaches to intramolecular Förster Resonance Energy Transfer probe measurements for quantitative modeling [PDF]

open access: yes, 2011
Numerous unimolecular, genetically-encoded Forster Resonance Energy Transfer (FRET) probes for monitoring biochemical activities in live cells have been developed over the past decade.
Kurt I. Anderson   +24 more
core   +1 more source

Structural Changes of Yellow Cameleon Domains Observed by Quantitative FRET Analysis and Polarized Fluorescence Correlation Spectroscopy [PDF]

open access: yes, 2008
Förster resonance energy transfer (FRET) is a widely used method for monitoring interactions between or within biological macromolecules conjugated with suitable donor-acceptor pairs.
Laptenok, S.   +14 more
core   +1 more source

Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs [PDF]

open access: yes, 2010
Förster resonance energy transfer (FRET) is a powerful method for obtaining information about small-scale lengths between biomacromolecules. Visible fluorescent proteins (VFPs) are widely used as spectrally different FRET pairs, where one VFP acts as a ...
Birch, D.J.S.   +8 more
core   +1 more source

Energy transfer in complexes of water-soluble quantum dots and chlorin e6 molecules in different environments

open access: yesBeilstein Journal of Nanotechnology, 2013
The photoexcitation energy transfer is found and investigated in complexes of CdSe/ZnS cationic quantum dots and chlorin e6 molecules formed by covalent bonding and electrostatic interaction in aqueous solution and in porous track membranes.
Irina V. Martynenko   +5 more
doaj   +1 more source

FRET Ratiometric Nanoprobes for Nanoparticle Monitoring

open access: yesBiosensors, 2021
Fluorescence labelling is often used for tracking nanoparticles, providing a convenient assay for monitoring nanoparticle drug delivery. However, it is difficult to be quantitative, as many factors affect the fluorescence intensity.
Guangze Yang   +3 more
doaj   +1 more source

A Guide to Fluorescent Protein FRET Pairs

open access: yesSensors, 2016
Förster or fluorescence resonance energy transfer (FRET) technology and genetically encoded FRET biosensors provide a powerful tool for visualizing signaling molecules in live cells with high spatiotemporal resolution. Fluorescent proteins (FPs) are most
Bryce T. Bajar   +4 more
doaj   +1 more source

QTR-FRET: Efficient background reduction technology in time-resolved förster resonance energy transfer assays [PDF]

open access: yes, 2022
A novel homogeneous assay system QTR-FRET (Quencher modulated Time-Resolved Forster Resonance Energy Transfer) combining quenching resonance energy transfer (QRET) and time-resolved Forster resonance energy transfer (TR-FRET) was developed to reduce ...
Emmiliisa Vuorinen   +5 more
core   +1 more source

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