ArticleOncotarget2015
Molecular architecture of the ErbB2 extracellular domain homodimer.
Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Characterization of mAb104, a mAb Targeting a Conformationally Exposed, Tumor-Specific Epitope of HER2.Molecular cancer therapeutics · 2025Article
- Facile phyto-mediated synthesis of ternary CuO/MnScientific reports · 2025Article
- SpyMask enables combinatorial assembly of bispecific binders.Nature communications · 2024Article
- Electrochemical Cellulase-Linked ELASA for Rapid Liquid Biopsy Testing of Serum HER-2/ACS measurement science au · 2023Article
- Potent anti-tumor immune response and tumor growth inhibition induced by HER2 subdomain fusion protein in a mouse tumor model.Journal of cancer research and clinical oncology · 2023Article
- Biased activation of the receptor tyrosine kinase HER2.Cellular and molecular life sciences : CMLS · 2023Article
- Rational Design, Synthesis and Biological Evaluation of Novel Pyrazoline-Based Antiproliferative Agents in MCF-7 Cancer Cells.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Whole-exome sequencing reveals a comprehensive germline mutation landscape and identifies twelve novel predisposition genes in Chinese prostate cancer patients.PLoS genetics · 2022Article
- Review
- Integrated approach to functional analysis of an ERBB2 variant of unknown significance detected by a cancer gene panel test.Cellular oncology (Dordrecht, Netherlands) · 2022Article
- Glycosylation promotes the cancer regulator EGFR-ErbB2 heterodimer formation - molecular dynamics study.Journal of molecular modeling · 2021Article
- Engineering an anti-HER2 biparatopic antibody with a multimodal mechanism of action.Nature communications · 2021Article
- Structural and dynamic characterization of the C-terminal tail of ErbB2: Disordered but not random.Biophysical journal · 2021Article
- Mechanisms and potential interventions associated with the cardiotoxicity of ErbB2-targeted drugs: Insights from in vitro, in vivo, and clinical studies in breast cancer patients.Cellular and molecular life sciences : CMLS · 2020Review
- Dynamical Rearrangement of Human Epidermal Growth Factor Receptor 2 upon Antibody Binding: Effects on the Dimerization.Biomolecules · 2019Article
- Mechanisms of Receptor Tyrosine-Protein Kinase ErbB-3 (ERBB3) Action in Human Neoplasia.The American journal of pathology · 2019Review
- A germline alteration ofOncology letters · 2019Article
- Visualisation of HER2 homodimers in single cells from HER2 overexpressing primary formalin fixed paraffin embedded tumour tissue.Molecular medicine (Cambridge, Mass.) · 2019Article
- The Effects of Pertuzumab and Its Combination with Trastuzumab on HER2 Homodimerization and Phosphorylation.Cancers · 2019Article
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human epidermal growth factor receptors (HERs or ErbBs) play crucial roles in numerous cellular processes. ErbB2 is a key member of ErbB family, and its overexpression is recognized as a frequent molecular abnormality. In cancer, this overexpression correlates with aggressive disease and poor patient outcomes. Dimer-dependent phosphorylation is a key event for the signal transduction of ErbBs. However, the molecular mechanism of the dimerization of ErbB2 remains elusive. In the present work, we report the homodimer architecture of the ErbB2 extracellular domain (ECD) which is unique compared with other dimer-models of ErbBs. The structure of the ErbB2 ECD homodimer represents a "back to head" interaction, in which a protruding β-hairpin arm in domain II of one ErbB2 protomer is inserted into a C-shaped pocket created by domains I-III of the adjacent ErbB2 protomer. This dimerized architecture and its impact on the phosphorylation of ErbB2 intracellular domain were further verified by a mutagenesis study. We also elucidated the different impacts of two clinically administered therapeutic antibodies, trastuzumab and pertuzumab, on ErbB2 dimerization. This information not only provides an understanding of the molecular mechanism of ErbBs dimerization but also elucidates ErbB2-targeted therapy at the molecular level.
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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.