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Titolo:
Fluorescence resonance energy transfer microscopy: a mini review
Autore:
Periasamy, A;
Indirizzi:
Univ Virginia, WM Keck Ctr Cellular Imaging, Dept Biol, Charlottesville, VA 22904 USA Univ Virginia Charlottesville VA USA 22904 Charlottesville, VA 22904 USA
Titolo Testata:
JOURNAL OF BIOMEDICAL OPTICS
fascicolo: 3, volume: 6, anno: 2001,
pagine: 287 - 291
SICI:
1083-3668(200107)6:3<287:FRETMA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIFETIME DETERMINATION METHOD; IMAGING MICROSCOPY; PROTEIN INTERACTIONS; 2-PHOTON EXCITATION; FRET MICROSCOPY; LIVING CELL; VISUALIZATION; RESOLUTION; SURFACE; SYSTEM;
Keywords:
fluorescence resonance energy transfer; protein interactions; wide-field; confocal; two-photon; lifetime imaging; FRET microscopy; CAATT/enhancer binding protein alpha (C/EBP alpha);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Engineering, Computing & Technology
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Periasamy, A Univ Virginia, WM Keck Ctr Cellular Imaging, Dept Biol, Gilmer Hall, Charlottesville, VA 22904 USA Univ Virginia Gilmer Hall Charlottesville VA USA 22904 04 USA
Citazione:
A. Periasamy, "Fluorescence resonance energy transfer microscopy: a mini review", J BIOMED OP, 6(3), 2001, pp. 287-291

Abstract

Fluorescence resonance energy transfer (FRET) microscopy is a better method than the x-ray diffraction, nuclear magnetic resonance, or electron microscopy for studying the structure and localization of proteins under physiological conditions. In this paper, we describe four different light microscopy techniques to visualize the interactions of the transcription factor CAATT/enhancer binding protein alpha (C/EBP alpha) in living pituitary cells. In wide-field, confocal, and two-photon microscopy the FRET image provides two-dimensional spatial distribution of steady-state protein-protein interactions. The two-photon imaging technique provides a better FRET signal (less bleedthrough and photobleaching) compared to the other two techniques. This information, although valuable, falls short of revealing transient interactions of proteins in real time. The fluorescence lifetime methods allow us to monitor FRET signals at the moment of the protein interactions at a resolution on the order of subnanoseconds, providing high temporal, as well as spatial resolution. This paper will provide a brief review of the above-mentioned FRET techniques. (C) 2001 Society of Photo-Optical InstrumentationEngineers.

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Documento generato il 25/01/20 alle ore 18:51:31