Literature DB >> 1578295

Fluorescence resonance energy transfer measurements on cell surfaces. A spectroscopic tool for determining protein interactions.

L Mátyus1.   

Abstract

The interaction of cell surface components may influence several events during the process of transmembrane signalling. Receptor clustering, conformational changes and altered molecular interactions often play essential roles in the final outcome of ligand receptor interactions. Fluorescence resonance energy transfer (FRET) is an excellent tool which can be used to determine distance relationships and supramolecular structure on cell surfaces. This paper reviews the theoretical basis of fluorescence resonance energy transfer, its spectrofluorometric and flow cytometric applications, and provides a critical evaluation of the methods. Finally, examples are given to illustrate the use of the method of fluorescence resonance energy transfer in solving biological problems.

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Year:  1992        PMID: 1578295     DOI: 10.1016/1011-1344(92)85039-w

Source DB:  PubMed          Journal:  J Photochem Photobiol B        ISSN: 1011-1344            Impact factor:   6.252


  22 in total

1.  Approaches to studying cellular signaling: a primer for morphologists.

Authors:  Kathy Kay Hartford Svoboda; Wende R Reenstra
Journal:  Anat Rec       Date:  2002-04-15

2.  FRET or no FRET: a quantitative comparison.

Authors:  Claude Berney; Gaudenz Danuser
Journal:  Biophys J       Date:  2003-06       Impact factor: 4.033

3.  Detection of channel proximity by nanoparticle-assisted delaying of toxin binding; a combined patch-clamp and flow cytometric energy transfer study.

Authors:  Bálint Rubovszky; Péter Hajdú; Zoltán Krasznai; Rezsõ Gáspár; Thomas A Waldmann; Sándor Damjanovich; László Bene
Journal:  Eur Biophys J       Date:  2005-03       Impact factor: 1.733

4.  Optimal bundling of transmembrane helices using sparse distance constraints.

Authors:  Ken Sale; Jean-Loup Faulon; Genetha A Gray; Joseph S Schoeniger; Malin M Young
Journal:  Protein Sci       Date:  2004-08-31       Impact factor: 6.725

5.  Additional correction for energy transfer efficiency calculation in filter-based Forster resonance energy transfer microscopy for more accurate results.

Authors:  Yuansheng Sun; Ammasi Periasamy
Journal:  J Biomed Opt       Date:  2010 Mar-Apr       Impact factor: 3.170

6.  The region of XRCC1 which harbours the three most common nonsynonymous polymorphic variants, is essential for the scaffolding function of XRCC1.

Authors:  Audun Hanssen-Bauer; Karin Solvang-Garten; Karin Margaretha Gilljam; Kathrin Torseth; David M Wilson; Mansour Akbari; Marit Otterlei
Journal:  DNA Repair (Amst)       Date:  2012-01-26

7.  Rational design and evaluation of FRET experiments to measure protein proximities in cells.

Authors:  Erik L Snapp; Ramanujan S Hegde
Journal:  Curr Protoc Cell Biol       Date:  2006-10

8.  Analysis of cell surface molecular distributions and cellular signaling by flow cytometry.

Authors:  J Matkó; L Mátyus; J Szöllösi; L Bene; A Jenei; P Nagy; A Bodnár; S Damjanovich
Journal:  J Fluoresc       Date:  1994-12       Impact factor: 2.217

9.  Reversible penetration of alpha-glutathione S-transferase into biological membranes revealed by photosensitized labelling in situ.

Authors:  N Merezhinskaya; G A Kuijpers; Y Raviv
Journal:  Biochem J       Date:  1998-11-01       Impact factor: 3.857

10.  WRN helicase and FEN-1 form a complex upon replication arrest and together process branchmigrating DNA structures associated with the replication fork.

Authors:  Sudha Sharma; Marit Otterlei; Joshua A Sommers; Henry C Driscoll; Grigory L Dianov; Hui-I Kao; Robert A Bambara; Robert M Brosh
Journal:  Mol Biol Cell       Date:  2003-12-02       Impact factor: 4.138

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