ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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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.
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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.
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Who cites it
14 citing papers in PubMed.
- Visualization of membrane-stabilized SorCS2Journal of structural biology: X · 2026Article
- Jammed interconnected bilayer emulsions as 3D-printable biological tissue mimics.Nature materials · 2026Article
- A Novel Technology Platform for Extracellular Vesicle-Targeted Expression of Drug-Metabolizing Enzymes: Driving CYP3A4 Expression and Secretion via the EABR Motif.Biomedicines · 2026Article
- Integrative structural and dynamics studies of epidermal growth factor receptor (EGFR).Experimental & molecular medicine · 2026Review
- The evolving role of structural biology in pharma: integration of X-ray crystallography, cryo-electron microscopy and beyond.Acta crystallographica. Section D, Structural biology · 2026Review
- mRNA delivery of mosaic-8 pan-sarbecovirus RBD vaccines elicits distinct antibody epitope signatures.Cell reports · 2026Article
- The role of kinase domain dimerization in EGFR activation.Structure (London, England : 1993) · 2026Article
- Resolving structural heterogeneity in situ through cryogenic electron tomography.Current opinion in structural biology · 2026Review
- Lipids regulate epidermal growth factor receptor activation by its ligands.Biochemical Society transactions · 2026Review
- The Dual Role of Extracellular Vesicles in Aging and Age-Related Diseases: Pathophysiology and Therapeutic Potential.International journal of nanomedicine · 2026Review
- mRNA delivery of genetically encoded mosaic-8 pan-sarbecovirus RBD vaccines.bioRxiv : the preprint server for biology · 2025Article
- Visualization of lysosomal membrane proteins by cryo electron tomography.Nature communications · 2025Article
- Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Influence of Phosphoinositide Lipids in the Molecular Biology of Membrane Proteins: Recent Insights from Simulations.Journal of molecular biology · 2025Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
We report here transport of full-length epidermal growth factor receptor (EGFR), Insulin Receptor, 7-pass transmembrane receptor Smoothened, and 13-pass Sodium-iodide symporter to extracellular vesicles (EVs) for structural and functional studies. Mass spectrometry confirmed the transported proteins are the most abundant in EV membranes, and the presence of many receptor-interacting proteins in EVs demonstrates their utility for characterizing membrane protein interactomes. Cryo-electron tomography of EGFR-containing EVs reveals that EGFR forms clusters in both the presence and absence of EGF with a ~3 nm gap between the inner membrane and cytoplasmic density. EGFR extracellular region (ECR) dimers do not form regular arrays in these clusters. Subtomogram averaging of the 150 kDa EGF-bound EGFR ECR dimer yielded a 15 Å map into which the crystal structure of the ligand-bound EGFR ECR dimer fits well. These findings refine our understanding of EGFR activation, clustering, and signaling and establish EVs as a versatile platform for structural and functional characterization of human membrane proteins in cell-derived membranes.
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