ArticleBiophysical journal2014
The FRET signatures of noninteracting proteins in membranes: simulations and experiments.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 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
63 citing papers in PubMed, 94 citations in OpenAlex.
- Local Iontophoretic Application for Pharmacological Induction of Long-Term Synaptic Depression.Bio-protocol · 2025Article
- Dual SLIPT-A Lipid Mimic to Enable Spatiotemporally Defined, Sequential Protein Dimerization.ACS chemical biology · 2025Article
- Transmembrane helix interactions regulate oligomerization of the receptor tyrosine kinase EphA2.The Journal of biological chemistry · 2024Article
- Utility of FRET in studies of membrane protein oligomerization: The concept of the effective dissociation constant.Biophysical journal · 2023Article
- One pattern analysis (OPA) for the quantitative determination of protein interactions in plant cells.Plant methods · 2023Article
- Micropeptide hetero-oligomerization adds complexity to the calcium pump regulatory network.Biophysical journal · 2023Article
- Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor-dependent signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Quantitative FRET Microscopy Reveals a Crucial Role of Cytoskeleton in Promoting PI(4,5)PInternational journal of molecular sciences · 2021Article
- Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane.The Biochemical journal · 2021Article
- Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors.International journal of molecular sciences · 2021Review
- P120 catenin potentiates constitutive E-cadherin dimerization at the plasma membrane and regulates trans binding.Current biology : CB · 2021Article
- Interactions between Ligand-Bound EGFR and VEGFR2.Journal of molecular biology · 2021Article
- Ceramide structure dictates glycosphingolipid nanodomain assembly and function.Nature communications · 2021Article
- Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules.Micromachines · 2021Review
- Quantifying single-cell ERK dynamics in colorectal cancer organoids reveals EGFR as an amplifier of oncogenic MAPK pathway signalling.Nature cell biology · 2021Article
- Probing Membrane Protein Association Using Concentration-Dependent Number and Brightness.Angewandte Chemie (International ed. in English) · 2021Article
- Differential Aggregation Properties of Mutant Human and Bovine Rhodopsin.Biochemistry · 2021Article
- The Biased Ligands NGF and NT-3 Differentially Stabilize Trk-A Dimers.Biophysical journal · 2021Article
- The biophysical basis of receptor tyrosine kinase ligand functional selectivity: Trk-B case study.The Biochemical journal · 2020Article
- Voltage modulates the effect of μ-receptor activation in a ligand-dependent manner.British journal of pharmacology · 2020Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Commented on byBackground FRET.2014
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Förster resonance energy transfer (FRET) experiments are often used to study interactions between integral membrane proteins in cellular membranes. However, in addition to the FRET of sequence-specific interactions, these experiments invariably record a contribution due to proximity FRET, which occurs when a donor and an acceptor approach each other by chance within distances of ∼100 Å. This effect does not reflect specific interactions in the membrane and is frequently unappreciated, despite the fact that its magnitude can be significant. Here we develop a computational description of proximity FRET, simulating the cases of proximity FRET when fluorescent proteins are used to tag monomeric, dimeric, trimeric, and tetrameric membrane proteins, as well as membrane proteins existing in monomer-dimer equilibria. We also perform rigorous experimental measurements of this effect, by identifying membrane receptors that do not associate in mammalian membranes. We measure the FRET efficiencies between yellow fluorescent protein and mCherry-tagged versions of these receptors in plasma-membrane-derived vesicles as a function of receptor concentration. Finally, we demonstrate that the experimental measurements are well described by our predictions. The work presented here brings additional rigor to FRET-based studies of membrane protein interactions, and should have broad utility in membrane biophysics research.
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.