Imaging protein molecules using FRET and FLIM microscopy.

By Horst Wallrabe, A. Periasamy. Current Opinion in Biotechnology, 2005

736 citations recorded by the source corpus.

Subfields: Biophysics, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/8082332a1dd78306af09847c4ae927b72457a952

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In Molecular Biology

1. D. Auld

Citations in the corpus

• High-throughput screening assays for the identification of chemical probes. (2007, methodology): “Intracellular indicators of specific kinase activity have been described using phosphorylation-activated FRET sensors engineered from fluorescent protein pair”
• Fluorescence lifetime imaging microscopy in life sciences (2010, neutral): “back [37–42].”
• A quantitative protocol for dynamic measurements of protein interactions by Förster resonance energy transfer-sensitized fluorescence emission (2009, methodology): “For in-depth reviews on FRET imaging, see Pollok & Heim (1999), Jares-Erijman & Jovin (2003, 2006), Miyawaki (2003),Periasamy&Day (2005),VanMunster et al. (2005) and Wallrabe & Periasamy (2005).”
• Multiphoton time-domain fluorescence lifetime imaging microscopy: practical application to protein–protein interactions using global analysis (2009, background): “The detection of Förster (or fluorescence) resonance energy transfer (FRET) is one such technique, which is sensitive at these small distance scales (Voss et al. 2005; Wallrabe & Periasamy 2005).”