Expression of p95HER2, a truncated form of the HER2 receptor, and response to anti-HER2 therapies in breast cancer.
By M. Scaltriti, F. Rojo, A. Ocaña, J. Anido, M. Guzman, J. Cortés, S. Di Cosimo, X. Matías-Guiu, S. Ramón y. Cajal, J. Arribas and 1 more. Journal of the National Cancer Institute, 2007
892 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/8409edd66407c15bd72eb9e4b6404091e1191ae3
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Citations in the corpus
- Novel anticancer targets: revisiting ERBB2 and discovering ERBB3 (2009, result): “This is in contrast to lapatinib, which can inhibit the truncated form of ERBB2, as shown in studies in breast cancer cells and xenograft model”
- Target Binding Properties and Cellular Activity of Afatinib (BIBW 2992), an Irreversible ErbB Family Blocker (2012, background): “Likewise, resistance to trastuzumab in breast carcinoma cells may be mediated by increased expression of EGFR and ErbB-3 (Narayan et al., 2009) and cognate ErbB ligands (Ritter et al., 2007) or truncated HER2 isoforms such as p95HER2 (Scaltriti et al., 2007).”
- Human Epidermal Growth Factor Receptor 2 (HER2) in Cancers: Overexpression and Therapeutic Implications (2014, positive): “For the same reason, p95 is not detected by antibodies that target the extracellular domain [21, 22].”
- Targeting HER2-positive breast cancer: advances and future directions (2022, background): “Cell lines and xenografts expressing the p95 variant that lack the trastuzumab-binding ECD were susceptible to lapatinib, presumably because it targets the intracellular kinase domain of HER2 (ref.(46)).”