ArticleeLife2013
Her2 activation mechanism reflects evolutionary preservation of asymmetric ectodomain dimers in the human EGFR family.
Article in eLife, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.
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
46 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.
- Efficacy and safety of trastuzumab deruxtecan in the treatment of HER2-low/positive advanced breast cancer: a single-arm meta-analysis.Frontiers in pharmacology · 2023Pooled it
- ErbB family receptor dimerization dynamics and dysregulation via long-term single-molecule imaging.Cell · 2026Article
- Antibody-drug conjugates in recurrent or metastatic HNSCC: relevant targets, clinical development, and future prospects.Frontiers in immunology · 2026Review
- Structural analysis of HER2-trastuzumab complex reveals receptor conformational adaptation.Science advances · 2025Article
- Mechanism of action and future perspectives of ADCs in combination with immune checkpoint inhibitors for solid tumors.Clinical and experimental medicine · 2025Review
- Computational-aided rational mutation design of pertuzumab to overcome active HER2 mutation S310F through antibody-drug conjugates.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unlocking the potential of antibody-drug conjugates in cervical cancer: emerging targets and clinical trials.Frontiers in pharmacology · 2025Review
- Therapeutic strategies targeting the epidermal growth factor receptor signaling pathway in metastatic colorectal cancer.World journal of gastrointestinal oncology · 2024Review
- SpyMask enables combinatorial assembly of bispecific binders.Nature communications · 2024Article
- Upregulated Expression of ERBB2/HER2 in Multiple Myeloma as a Predictor of Poor Survival Outcomes.International journal of molecular sciences · 2023Article
- Review
- Chinese expert consensus on the diagnosis and treatment of HER2-altered non-small cell lung cancer.Thoracic cancer · 2023Article
- HB-EGF upregulates StAR expression and stimulates progesterone production through ERK1/2 signaling in human granulosa-lutein cells.Cell communication and signaling : CCS · 2022Article
- Article
- Integrated approach to functional analysis of an ERBB2 variant of unknown significance detected by a cancer gene panel test.Cellular oncology (Dordrecht, Netherlands) · 2022Article
- From Anti-HER-2 to Anti-HER-2-CAR-T Cells: An Evolutionary Immunotherapy Approach for Gastric Cancer.Journal of inflammation research · 2022Review
- Novel development strategies and challenges for anti-Her2 antibody-drug conjugates.Antibody therapeutics · 2022Review
- Quantum Dots: Synthesis, Antibody Conjugation, and HER2-Receptor Targeting for Breast Cancer Therapy.Journal of functional biomaterials · 2021Review
- Article
- Glycosylation promotes the cancer regulator EGFR-ErbB2 heterodimer formation - molecular dynamics study.Journal of molecular modeling · 2021Article
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 at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The receptor tyrosine kinase Her2, an intensely pursued drug target, differs from other members of the EGFR family in that it does not bind EGF-like ligands, relying instead on heterodimerization with other (ligand-bound) EGFR-family receptors for activation. The structural basis for Her2 heterodimerization, however, remains poorly understood. The unexpected recent finding of asymmetric ectodomain dimer structures of Drosophila EGFR (dEGFR) suggests a possible structural basis for Her2 heterodimerization, but all available structures for dimers of human EGFR family ectodomains are symmetric. Here, we report results from long-timescale molecular dynamics simulations indicating that a single ligand is necessary and sufficient to stabilize the ectodomain interface of Her2 heterodimers, which assume an asymmetric conformation similar to that of dEGFR dimers. This structural parallelism suggests a dimerization mechanism that has been conserved in the evolution of the EGFR family from Drosophila to human. DOI:http://dx.doi.org/10.7554/eLife.00708.001.
Indexed as
Identifiers
What OpenQuestion 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 OpenQuestion graph.