ArticleNature communications2025
Spatial and stoichiometric in situ analysis of biomolecular oligomerization at single-protein resolution.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Spontaneous and indefinite blinking in upconverting nanoparticles for ångström-precision multicolour super-resolution imaging.Nature nanotechnology · 2026Article
- Stoichiometrically Defined Antibody-DNA Conjugates for Quantitative Super-Resolution Imaging.Nano letters · 2026Article
- Quantitative Mapping of Nanoscale EGFR-Grb2 Assemblies by DNA-PAINT.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Dynamic monomer-dimer transition in ligand-induced apelin receptor activation.Nature communications · 2026Article
- Dynamic Binder Exchange Improves Protein Labeling Efficiency in DNA-PAINT up to 15-Fold.Angewandte Chemie (International ed. in English) · 2026Article
- Molecular mapping in DNA-PAINT via modified Gaussian Mixture Modeling.Nature communications · 2026Article
- Quantitative Stimulated Emission Depletion (STED) Microscopy with DNA-Fluorophore Labels.ACS nano · 2026Article
- 4Pi-SIMFLUX: 4Pi single-molecule localization microscopy with structured illumination.Nature methods · 2026Article
- HDCluster: High-Degree Graph Clustering for Robust Analysis of Single Molecule Localization Microscopy.bioRxiv : the preprint server for biology · 2025Article
- Localization of single molecules with structured illumination and structured detection.Light, science & applications · 2025Article
- Resolving the structural basis of therapeutic antibody function in cancer immunotherapy with RESI.Nature communications · 2025Article
Corrections and comments
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Latest advances in super-resolution microscopy allow the study of subcellular features at the level of single proteins, which could lead to discoveries in fundamental biological processes, specifically in cell signaling mediated by membrane receptors. Despite these advances, accurately extracting quantitative information on molecular arrangements of proteins at the 1-20 nm scale through rigorous image analysis remains a significant challenge. Here, we present SPINNA (Single-Protein Investigation via Nearest-Neighbor Analysis): an analysis framework that compares nearest-neighbor distances from experimental single-protein position data with those obtained from realistic simulations based on a user-defined model of protein oligomerization states. We demonstrate SPINNA in silico, in vitro, and in cells. In particular, we quantitatively assess the oligomerization of the epidermal growth factor receptor (EGFR) upon EGF treatment and investigate the dimerization of CD80 and PD-L1, key surface ligands involved in immune cell signaling. Importantly, we offer an open-source Python implementation and a GUI to facilitate SPINNA's widespread use in the scientific community.
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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.