ArticleBiophysical journal2020
Determining the Stoichiometry of Small Protein Oligomers Using Steady-State Fluorescence Anisotropy.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
14 citing papers in PubMed.
- mSumireF a Monomeric Violet Fluorescent Protein.ACS bio & med chem Au · 2026Article
- Resolving oligomeric states of photoactivatable proteins in living cells via photon counting histogram analysis.iScience · 2025Article
- Effects of Charged Surface on Electrochemical Sensitivity to Protein Dimerization.Analytical chemistry · 2025Article
- Bayesian analysis and efficient algorithms for single-molecule fluorescence data and step counting.Biophysical journal · 2025Article
- Bayesian analysis and efficient algorithms for single-molecule fluorescence data and step counting.bioRxiv : the preprint server for biology · 2025Article
- HP1 loses its chromatin clustering and phase separation function across evolution.Nature communications · 2025Article
- Characterization and structural basis for the brightness of mCLIFY: A novel monomeric and circularly permuted bright yellow fluorescent protein.Biophysical journal · 2025Article
- Illuminating cellular architecture and dynamics with fluorescence polarization microscopy.Journal of cell science · 2024Review
- Characterization and structural basis for the brightness of mCLIFY: a novel monomeric and circularly permuted bright yellow fluorescent protein.Research square · 2024Article
- Quantitative fluorescence emission anisotropy microscopy for implementing homo-fluorescence resonance energy transfer measurements in living cells.Molecular biology of the cell · 2023Article
- Probing Oxidant Effects on Superoxide Dismutase 1 Oligomeric States in Live Cells Using Single-Molecule Fluorescence Anisotropy.Chemical & biomedical imaging · 2023Article
- Unraveling the hidden temporal range of fast βCommunications biology · 2022Article
- Bacterial Transcriptional Regulators: A Road Map for Functional, Structural, and Biophysical Characterization.International journal of molecular sciences · 2022Review
- Unraveling protein's structural dynamics: from configurational dynamics to ensemble switching guides functional mesoscale assemblies.Current opinion in structural biology · 2021Review
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
No grant is acknowledged in the PubMed record.
Abstract
A large fraction of soluble and membrane-bound proteins exists as non-covalent dimers, trimers, and higher-order oligomers. The experimental determination of the oligomeric state or stoichiometry of proteins remains a nontrivial challenge. In one approach, the protein of interest is genetically fused to green fluorescent protein (GFP). If a fusion protein assembles into a non-covalent oligomeric complex, exciting their GFP moiety with polarized fluorescent light elicits homotypic Förster resonance energy transfer (homo-FRET), in which the emitted radiation is partially depolarized. Fluorescence depolarization is associated with a decrease in fluorescence anisotropy that can be exploited to calculate the oligomeric state. In a classical approach, several parameters obtained through time-resolved and steady-state anisotropy measurements are required for determining the stoichiometry of the oligomers. Here, we examined novel approaches in which time-resolved measurements of reference proteins provide the parameters that can be used to interpret the less expensive steady-state anisotropy data of candidates. In one approach, we find that using average homo-FRET rates (k
Indexed as
Identifiers
What OpenQuestion holds
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.