Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex.

By M. Franklin, Kendall D. Carey, F. Vajdos, D. Leahy, A. D. de Vos, M. Sliwkowski. Cancer Cell, 2004

1,125 citations recorded by the source corpus.

Subfields: Oncology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/3ab03f309a1a89b64b5b1ff222f8fd4bb3191012

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Oncology

1. J. Baselga
2. M. Moasser
3. N. Hynes
4. S. Swain
5. Carlos L. Arteaga
6. R. Nahta
7. J. Engelman
8. M. Wieduwilt

In Radiology, Nuclear Medicine and Imaging

1. J. Baselga
2. N. Hynes
3. M. Moasser
4. Carlos L. Arteaga
5. S. Swain
6. R. Nahta
7. J. Engelman
8. M. Sliwkowski

Citations in the corpus

• A molecularly annotated platform of patient-derived xenografts ("xenopatients") identifies HER2 as an effective therapeutic target in cetuximab-resistant colorectal cancer. (2011, background): “We selected pertuzumab, a recombinant humanized monoclonal antibody that disrupts HER2 heterodimerization with EGFR and with other HER partners (42), and lapatinib, a small molecule inhibitor with high selectivity for both HER2 and EGFR (43).”
• Antibodies and cancer therapy: versatile platforms for cancer immunotherapy (2010, background): “Another HER2-directed antibody, pertuzumab (Omnitarg; Genentech/Roche), binds at a distinct site from trastuzumab and sterically inhibits receptor dimerizatio”
• Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941. (2009, background): “Previously, we reported that pertuzumab, a therapeutic antibody that binds extracellular domain II of HER2 (Franklin et al., 2004), functions by blocking the association of HER2 with ligand-occupied HER3 (Agus et al.”
• Risk Factors and Preventions of Breast Cancer (2017, neutral): “However, the binding domain is different [124].”
• The epidermal growth factor receptor family: Biology driving targeted therapeutics (2008, background): “Since the structural basis for ErbB dimerization has been elucidated, a second ErbB2-targeting mAb, pertuzumab, has been developed that binds to the dimerization interface of the ErbB2 ECD [169].”
• A glimpse of structural biology through X-ray crystallography. (2014, background): “Pertuzumab, on the other hand, prevents receptor dimerization by binding to the extracellular domain of ErbB2/HER2 (Franklin et al., 2004).”
• Treatment of HER2-positive breast cancer: current status and future perspectives (2012, background): “The monoclonal antibody, pertuzumab, binds to the HER2 ECD but at a different site to trastuzumab, and is able to inhibit ligand-induced dimerization of HER2 with its receptor partners”
• Strongly enhanced antitumor activity of trastuzumab and pertuzumab combination treatment on HER2-positive human xenograft tumor models. (2009, background): “Pertuzumab prevents the HER2 protein from dimerizing with HER3 and/or HER1 (26, 27, 29, 43), thus blocking these potential escape pathways.”
• Pertuzumab plus Trastuzumab plus Docetaxel for Metastatic Breast Cancer (2011, positive): “New therapies directed at HER2 are being developed,(9-13) among them pertuzumab, a humanized monoclonal antibody that binds HER2 at a different epitope of the HER2 extracellular domain (subdomain II) than that at which trastuzumab binds.(14) Pertuzumab prevents HER2 from dimerizing with other ligand”
• Phase II trial of pertuzumab and trastuzumab in patients with human epidermal growth factor receptor 2-positive metastatic breast cancer that progressed during prior trastuzumab therapy. (2010, background): “Pertuzumab, a recombinant humanized monoclonal antibody binding to the HER2 dimerization domain, prevents dimerization of HER2 with other HER receptors (HER3, HER1, and HER4).(10-12) Thus, pertuzumab is a potent inhibitor of HER-mediated signaling(12,13) and has demonstrated excellent activity again”
• ERBB receptors: From oncogene discovery to basic science to mechanism-based cancer therapeutics (2014, background): “Because pertuzumab and trastuzumab bind to different epitopes in the HER2 ectodomain (Franklin et al., 2004), hence their complementary abilities to disrupt HER2-containing dimers, the combination of pertuzumab and trastuzumab has shown synergy in preclinical studies (Scheuer et al., 2009) and…”
• Novel anticancer targets: revisiting ERBB2 and discovering ERBB3 (2009, background): “Pertuzumab (Genentech/Hoffmann-La Roche) is a humanized monoclonal antibody that binds to an epitope in domain II, the dimerization domain of the ERBB2 extracellular domain, which is distinct from the binding site of trastuzumab in domain I”
• A central role for HER3 in HER2-amplified breast cancer: implications for targeted therapy. (2008, background): “By contrast, another HER2 antagonistic antibody, pertuzumab (2C4), binds to the subdomain II dimerization arm of HER2 and inhibits formation of ligand-induced HER2 heterodimers (15, 17).”