ArticleScience advances2015
Local variations of HER2 dimerization in breast cancer cells discovered by correlative fluorescence and liquid electron microscopy.
Article in Science advances, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 110 citations in OpenAlex.
- Explainable Artificial Intelligence (XAI) and Molecular Modeling Techniques to Discover Putative HER2 Inhibitors.International journal of molecular sciences · 2026Article
- In situ imaging of proximal biomolecules via Proximity Anchored Modules Assembly.Journal of nanobiotechnology · 2026Article
- ErbB family receptor dimerization dynamics and dysregulation via long-term single-molecule imaging.Cell · 2026Article
- A Review on Anticancer Potential and Structure-Activity Relationships (SAR) of Novel EGFR/HER2 Inhibitors.Current topics in medicinal chemistry · 2026Review
- Building a dynamic model for EGFR-family dimerization using quantitative, live-cell fluorescence methods.Biophysical journal · 2025Review
- Imaging of Hydrated and Living Cells in Transmission Electron Microscope: Summary, Challenges, and Perspectives.ACS nano · 2025Review
- A facile yeast-display approach for antibody mask discovery.Protein engineering, design & selection : PEDS · 2025Article
- Investigating and evaluating potential antigen binding sites for monoclonal anti-HER2 antibodies: The LightDock approach.Computational and structural biotechnology journal · 2025Article
- Liquid Phase Electron Microscopy of Bacterial Ultrastructure.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Advanced multiparametric image spectroscopy and super-resolution microscopy reveal a minimal model of CD95 signal initiation.Science advances · 2024Article
- Dysregulation of cellular membrane homeostasis as a crucial modulator of cancer risk.The FEBS journal · 2024Review
- Detecting Disruption of HER2 Membrane Protein Organization in Cell Membranes with Nanoscale Precision.ACS sensors · 2024Article
- Ligand Separation on Nanoconstructs Affects Targeting Selectivity to Protein Dimers on Cell Membranes.Nano letters · 2024Article
- Structure and dynamics of the EGFR/HER2 heterodimer.Cell discovery · 2023Article
- Article
- Using quantitative single molecule localization microscopy to optimize multivalent HER2-targeting ligands.Frontiers in medicine · 2023Article
- Inactivating Amplified HER2: Challenges, Dilemmas, and Future Directions.Cancer research · 2022Article
- Critical roles for EGFR and EGFR-HER2 clusters in EGF binding of SW620 human carcinoma cells.Journal of the Royal Society, Interface · 2022Article
- Treatment of small (T1mic, T1a, and T1b) node-negative HER2+ breast cancer - a review of current evidence for and against the use of anti-HER2 treatment regimens.Expert review of anticancer therapy · 2022Review
- Extensive conformational and physical plasticity protects HER2-HER3 tumorigenic signaling.Cell reports · 2022Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of HER2 homodimers plays an important role in breast cancer aggressiveness and progression; however, little is known about its localization. We have studied the intra- and intercellular variation of HER2 at the single-molecule level in intact SKBR3 breast cancer cells. Whole cells were visualized in hydrated state with correlative fluorescence microscopy and environmental scanning electron microscopy (ESEM). The locations of individual HER2 receptors were detected using an anti-HER2 affibody in combination with a quantum dot (QD), a fluorescent nanoparticle. Fluorescence microscopy revealed considerable differences of HER2 membrane expression between individual cells and between different membrane regions of the same cell (that is, membrane ruffles and flat areas). Subsequent ESEM of the corresponding cellular regions provided images of individually labeled HER2 receptors. The high spatial resolution of 3 nm and the close proximity between the QD and the receptor allowed quantifying the stoichiometry of HER2 complexes, distinguishing between monomers, dimers, and higher-order clusters. Downstream data analysis based on calculating the pair correlation function from receptor positions showed that cellular regions exhibiting membrane ruffles contained a substantial fraction of HER2 in homodimeric state. Larger-order clusters were also present. Membrane areas with homogeneous membrane topography, on the contrary, displayed HER2 in random distribution. Second, HER2 homodimers appeared to be absent from a small subpopulation of cells exhibiting a flat membrane topography, possibly resting cells. Local differences in homodimer presence may point toward functional differences with possible relevance for studying metastasis and drug response.
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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.