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FRET Detected Interactions of Cardiac Membrane Proteins in Living Cells

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 2010 English Publisher:Elsevier BVJournal:Biophysical Journal, volume 98, page 171a (issn: 0006-3495, Copyright policy )
Authors: Haydon, Suzanne M.; Winters, Deborah; Autry, J. Michael; Li, Ji; Robia, Seth L.; Thomas, David D.;

doi: 10.1016/j.bpj.2009.12.921

FRET Detected Interactions of Cardiac Membrane Proteins in Living Cells

Abstract

We have investigated the structure of phospholamban (PLB) and its regulation of the sarcoplasmic reticulum Ca-ATPase (SERCA) using fluorescence resonance energy transfer (FRET) on fluorescent fusion proteins expressed in living cells. Fusion proteins were created with either a donor fluorophore (cyan fluorescent protein, CFP), or an acceptor fluorophore (yellow fluorescent protein, YFP), attached to one terminus of the protein of interest. Both N-terminal and C-terminal fusions of CFP and YFP were made to SERCA and N-terminal fusions were made to PLB.

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Biophysics

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
0
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