Literature DB >> 16397825

Intensity range based quantitative FRET data analysis to localize protein molecules in live cell nuclei.

Ye Chen1, Ammasi Periasamy.   

Abstract

Förster (fluorescence) resonance energy transfer (FRET) is an ideal technique to estimate the distance between interacting protein molecules in live specimens using intensity-based microscopy. The spectral overlap of donor and acceptor- essential for FRET-also generates a contamination of the FRET signal. There are a number of algorithms available to remove this spectral bleedthrough (SBT) contamination and in this paper we compare two popular algorithms to estimate the SBT element and to calculate a more precise level of energy transfer efficiency, and with that a more accurate distance estimate.

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Year:  2006        PMID: 16397825     DOI: 10.1007/s10895-005-0024-1

Source DB:  PubMed          Journal:  J Fluoresc        ISSN: 1053-0509            Impact factor:   2.217


  23 in total

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Authors:  A Periasamy; R N Day
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Journal:  Biophys J       Date:  1984-05       Impact factor: 4.033

6.  High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes.

Authors:  A K Kenworthy; N Petranova; M Edidin
Journal:  Mol Biol Cell       Date:  2000-05       Impact factor: 4.138

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Authors:  Adam Hoppe; Kenneth Christensen; Joel A Swanson
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

9.  FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes.

Authors:  F S Wouters; P I Bastiaens; K W Wirtz; T M Jovin
Journal:  EMBO J       Date:  1998-12-15       Impact factor: 11.598

Review 10.  Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations.

Authors:  Rajesh Babu Sekar; Ammasi Periasamy
Journal:  J Cell Biol       Date:  2003-03-03       Impact factor: 10.539

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  21 in total

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Journal:  J Fluoresc       Date:  2009-07-09       Impact factor: 2.217

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7.  The subcellular localization of GABA transporters and its implication for seizure management.

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8.  Development of bimolecular fluorescence complementation using rsEGFP2 for detection and super-resolution imaging of protein-protein interactions in live cells.

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9.  Actin cytoskeleton-dependent Rab GTPase-regulated angiotensin type I receptor lysosomal degradation studied by fluorescence lifetime imaging microscopy.

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Review 10.  FRET microscopy in 2010: the legacy of Theodor Förster on the 100th anniversary of his birth.

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