FRET or no FRET: a quantitative comparison.

By C. Berney, G. Danuser. Biophysical Journal, 2003

600 citations recorded by the source corpus.

Subfields: Biophysics, Molecular Biology, Physical and Theoretical Chemistry

View Paper: https://www.semanticscholar.org/paper/d01bb8b4e10c12a7f9911643545b478874b09507

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In Biophysics

1. Horst Wallrabe
2. G. Kremers
3. David W. Piston
4. A. Periasamy
5. Wolfgang Becker

In Molecular Biology

1. G. Kremers
2. David W. Piston
3. Horst Wallrabe
4. A. Periasamy

In Physical and Theoretical Chemistry

1. Horst Wallrabe
2. A. Periasamy

Citations in the corpus

• Imaging protein molecules using FRET and FLIM microscopy. (2005, methodology): “It is beyond the scope of this review to discuss SBT correction further, and instead readers are referred to the available literature [6 ,8 ,26 ,27 ].”
• A quantitative protocol for dynamic measurements of protein interactions by Förster resonance energy transfer-sensitized fluorescence emission (2009, background): “…to quantify, relates to the fact that not all donors and acceptors participate in FRET interactions and the signals need to be normalized to take into account the varying concentrations of participating interaction partners (Clegg 1995; Hoppe et al. 2002; Berney & Danuser 2003; Gu et al. J. R. Soc.”
• Fluorescent protein FRET: the good, the bad and the ugly. (2007, background): “A quantitative comparison has detailed the strengthsandweaknessesofmanyoftheseapproaches[ 63 ].”
• An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes (2015, unknown): “[151] Scanning electrochemical microscopy (SECM) Scanning electrochemical microscopy (SECM) was invented by Bard and co-workers in 1989 and it is an instrument which basically consists of a combination of electrochemical components, positioners and computer control.”