ArticleThe journal of physiological sciences : JPS2011
Comparison of protein behavior between wild-type and G601S hERG in living cells by fluorescence correlation spectroscopy.
Article in The journal of physiological sciences : JPS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Intracellular Macromolecular Crowding within Individual Stress Fibers Analyzed by Fluorescence Correlation Spectroscopy.Cellular and molecular bioengineering · 2024Article
- Intracellular Binding of Terfenadine Competes with Its Access to Pancreatic ß-cell ATP-Sensitive KThe Journal of membrane biology · 2023Article
- Micro-pharmacokinetics: Quantifying local drug concentration at live cell membranes.Scientific reports · 2018Article
- Role of slow delayed rectifying potassium current in dynamics of repolarization and electrical memory in swine ventricles.The journal of physiological sciences : JPS · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human ether-a-go-go-related gene (hERG) protein is a cardiac potassium channel. Mutations in hERG can result in reductions in membrane channel current, cardiac repolarization, prolongation of QT intervals, and lethal arrhythmia. In the last decade, it has been found that some mutants of hERG involved in long QT syndrome exhibit intracellular protein trafficking defects, while other mutants sort to the membrane but cannot form functional channels. Due to the close relationship between intracellular trafficking and functional protein expression, we aimed to measure differences in protein behavior/motion between wild-type and mutant hERG by directly analyzing the fluorescence fluctuations of green fluorescent protein-labeled proteins using fluorescence correlation spectroscopy (FCS). Our data imply that FCS can be applied as a new diagnostic tool to assess whether the defect in a particular mutant channel protein involves aberrant intracellular trafficking.
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Registered trials
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