ArticleeLife2016
Monochromatic multicomponent fluorescence sedimentation velocity for the study of high-affinity protein interactions.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed.
- Analysis of Giant-Shell CdSe/CdS Quantum Dots via Analytical Ultracentrifugation Combined with Spectrally Resolved Photoluminescence.Small methods · 2026Article
- Nucleic acid-induced dimerization of HIV-1 Gag protein.The Journal of biological chemistry · 2019Article
- A multiwavelength emission detector for analytical ultracentrifugation.Nanoscale advances · 2019Article
- Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity.Nature communications · 2018Article
- Sedimentation velocity analytical ultracentrifugation for characterization of therapeutic antibodies.Biophysical reviews · 2018Review
- Article
- Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.Nature protocols · 2017Article
- Sedimentation of Reversibly Interacting Macromolecules with Changes in Fluorescence Quantum Yield.Biophysical journal · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
The dynamic assembly of multi-protein complexes underlies fundamental processes in cell biology. A mechanistic understanding of assemblies requires accurate measurement of their stoichiometry, affinity and cooperativity, and frequently consideration of multiple co-existing complexes. Sedimentation velocity analytical ultracentrifugation equipped with fluorescence detection (FDS-SV) allows the characterization of protein complexes free in solution with high size resolution, at concentrations in the nanomolar and picomolar range. Here, we extend the capabilities of FDS-SV with a single excitation wavelength from single-component to multi-component detection using photoswitchable fluorescent proteins (psFPs). We exploit their characteristic quantum yield of photo-switching to imprint spatio-temporal modulations onto the sedimentation signal that reveal different psFP-tagged protein components in the mixture. This novel approach facilitates studies of heterogeneous multi-protein complexes at orders of magnitude lower concentrations and for higher-affinity systems than previously possible. Using this technique we studied high-affinity interactions between the amino-terminal domains of GluA2 and GluA3 AMPA receptors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.