ArticleScientific reports2018
Optimal fluorescent protein tags for quantifying protein oligomerization in living cells.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed.
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- Resolving oligomeric states of photoactivatable proteins in living cells via photon counting histogram analysis.iScience · 2025Article
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- ProDOL: a general method to determine the degree of labeling for staining optimization and molecular counting.Nature methods · 2024Article
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- A cGAL-UAS bipartite expression toolkit forProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Assembly mechanism of the inflammasome sensor AIM2 revealed by single molecule analysis.Nature communications · 2023Article
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- Serotonin signaling regulates actomyosin contractility during morphogenesis in evolutionarily divergent lineages.Nature communications · 2023Article
- Influenza A Virus Infection Alters Lipid Packing and Surface Electrostatic Potential of the Host Plasma Membrane.Viruses · 2023Article
- Determining the Functional Oligomeric State of Membrane-Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles.Analytical chemistry · 2023Article
- Thermoplasmonic Vesicle Fusion Reveals Membrane Phase Segregation of Influenza Spike Proteins.Nano letters · 2023Article
- Enhancement of Vivid-based photo-activatable Gal4 transcription factor in mammalian cells.Cell structure and function · 2023Article
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6 authors.
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Abstract
Fluorescence fluctuation spectroscopy has become a popular toolbox for non-disruptive analysis of molecular interactions in living cells. The quantification of protein oligomerization in the native cellular environment is highly relevant for a detailed understanding of complex biological processes. An important parameter in this context is the molecular brightness, which serves as a direct measure of oligomerization and can be easily extracted from temporal or spatial fluorescence fluctuations. However, fluorescent proteins (FPs) typically used in such studies suffer from complex photophysical transitions and limited maturation, inducing non-fluorescent states. Here, we show how these processes strongly affect molecular brightness measurements. We perform a systematic characterization of non-fluorescent states for commonly used FPs and provide a simple guideline for accurate, unbiased oligomerization measurements in living cells. Further, we focus on novel red FPs and demonstrate that mCherry2, an mCherry variant, possesses superior properties with regards to precise quantification of oligomerization.
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