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Bioluminescence resonance energy transfer

Part 3. Proteomics

3.3. Mapping of Biochemical Networks

Basic Techniques and Approaches

  1. Ralf Jockers,
  2. Stefano Marullo

Published Online: 15 NOV 2005

DOI: 10.1002/047001153X.g303417

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

How to Cite

Jockers, R. and Marullo, S. 2005. Bioluminescence resonance energy transfer. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.3:47.

Author Information

  1. Institut Cochin, Paris, France

Publication History

  1. Published Online: 15 NOV 2005

Abstract

Bioluminescence Resonance Energy Transfer (BRET) has become a method of choice to monitor and quantify both constitutive and regulated interactions among proteins in intact cells. Despite the fact that BRET cannot be used to visualize the subcellular compartment where the interaction between two proteins occurs, it offers a number of practical advantages over FRET, including higher sensitivity in microplate-based high-throughput assays. The advantages of BRET-based approaches are illustrated by some significant advances obtained in various fields, such as protein oligomerization, ligand-induced conformational changes, and regulated movement of proteins between subcellular compartments.

Keywords:

  • BRET;
  • FRET;
  • luciferase;
  • energy transfer;
  • receptor;
  • dimerization;
  • ß-arrestin;
  • ubiquitin;
  • protein–protein interaction