ArticleChemphyschem : a European journal of chemical physics and physical chemistry2026
Quantitative Mapping of Nanoscale EGFR-Grb2 Assemblies by DNA-PAINT.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Quantitative Mapping of Nanoscale EGFR-Grb2 Assemblies by DNA-PAINT.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Receptor tyrosine kinase signaling is initiated by extracellular ligand binding, which drives the formation of membrane-protein assemblies that activate intracellular signal transduction. Accurately resolving the molecular composition of these assemblies in situ remains challenging due to their nanoscale dimensions and intrinsic heterogeneity. Here, we introduce a single-molecule super-resolution imaging and analysis workflow designed to resolve and quantitatively characterize individual membrane-protein assembly sites in cells. We apply this approach to the nanoscale organization of the epidermal growth factor receptor (EGFR) and its adaptor protein Grb2 following stimulation with the native ligand epidermal growth factor. As activation progresses, we observe a reduction in EGFR density at the plasma membrane, a progressive accumulation of Grb2 at EGFR assembly sites, and an increase in both dimeric and higher-order oligomeric EGFR. The experimental and analytical framework presented here is broadly applicable to the study of diverse membrane-protein assemblies.
Indexed as
Identifiers
What Socratic 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 Socratic graph.