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How Förster Resonance Energy Transfer Imaging Improves the Understanding of Protein Interaction Networks in Cancer Biology
Author(s) -
Fruhwirth Gilbert O.,
Fernandes Luis P.,
Weitsman Gregory,
Patel Gargi,
Kelleher Muireann,
Lawler Katherine,
Brock Adrian,
Poland Simon P.,
Matthews Daniel R.,
Kéri György,
Barber Paul R.,
Vojnovic Borivoj,
AmeerBeg Simon M.,
Coolen Anthony C. C.,
Fraternali Franca,
Ng Tony
Publication year - 2011
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201000866
Subject(s) - förster resonance energy transfer , computational biology , proteome , function (biology) , protein–protein interaction , nanotechnology , systems biology , computer science , biology , physics , biophysics , bioinformatics , materials science , microbiology and biotechnology , fluorescence , quantum mechanics
Herein we discuss how FRET imaging can contribute at various stages to delineate the function of the proteome. Therefore, we briefly describe FRET imaging techniques, the selection of suitable FRET pairs and potential caveats. Furthermore, we discuss state‐of‐the‐art FRET‐based screening approaches (underpinned by protein interaction network analysis using computational biology) and preclinical intravital FRET‐imaging techniques that can be used for functional validation of candidate hits (nodes and edges) from the network screen, as well as measurement of the efficacy of perturbing these nodes/edges by short hairpin RNA (shRNA) and/or small molecule‐based approaches.