ArticleCommunications biology2021
Apoptosis-inducing anti-HER2 agents operate through oligomerization-induced receptor immobilization.
Article in Communications biology, 2021. 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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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Engineering bispecific HER2xVEGF designed ankyrin repeat proteins for targeted nanobiotechnology applications.Journal of nanobiotechnology · 2025Article
- Structural analysis of HER2-trastuzumab complex reveals receptor conformational adaptation.Science advances · 2025Article
- The Psu protein of phage satellite P4 inhibits transcription termination factor ρ by forced hyper-oligomerization.Nature communications · 2025Article
- An overview of mechanisms, biomarkers, and treatment strategies for acquired anti-EGFR resistance in RAS wild-type colorectal cancer.Frontiers in pharmacology · 2025Review
- Biparatopic HER2-targeted nanobody binder synergizes with trastuzumab in resistant tumor cells.Frontiers in immunology · 2025Article
- SpyMask enables combinatorial assembly of bispecific binders.Nature communications · 2024Article
- Computational design of newly engineered DARPins as HER2 receptor inhibitors for breast cancer treatment.Research in pharmaceutical sciences · 2023Article
- Engineering of a Bispecific Nanofitin with Immune Checkpoint Inhibitory Activity Conditioned by the Cross-Arm Binding to EGFR and PDL1.Biomolecules · 2023Article
- A novel nanobody-based HER2-targeting antibody exhibits potent synergistic antitumor efficacy in trastuzumab-resistant cancer cells.Frontiers in immunology · 2023Article
- Using quantitative single molecule localization microscopy to optimize multivalent HER2-targeting ligands.Frontiers in medicine · 2023Article
- Choosing the Probe for Single-Molecule Fluorescence Microscopy.International journal of molecular sciences · 2022Review
- Article
- Molecular Assessment of HER2 to Identify Signatures Associated with Therapy Response in HER2-Positive Breast Cancer.Cancers · 2022Article
- Engineering an anti-HER2 biparatopic antibody with a multimodal mechanism of action.Nature communications · 2021Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Overexpression of the receptor tyrosine kinase HER2 plays a critical role in the development of various tumors. Biparatopic designed ankyrin repeat proteins (bipDARPins) potently induce apoptosis in HER2-addicted breast cancer cell lines. Here, we have investigated how the spatiotemporal receptor organization at the cell surface is modulated by these agents and is distinguished from other molecules, which do not elicit apoptosis. Binding of conventional antibodies is accompanied by moderate reduction of receptor mobility, in agreement with HER2 being dimerized by the bivalent IgG. In contrast, the most potent apoptosis-inducing bipDARPins lead to a dramatic arrest of HER2. Dual-color single-molecule tracking revealed that the HER2 "lockdown" by these bipDARPins is caused by the formation of HER2-DARPin oligomer chains, which are trapped in nanoscopic membrane domains. Our findings establish that efficient neutralization of receptor tyrosine kinase signaling can be achieved through intermolecular bipDARPin crosslinking alone, resulting in inactivated, locked-down bipDARPin-HER2 complexes.
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