Modeling ErbB2-p130Cas interaction to design new potential anticancer agents
Author:
Funder
University of Torino: Ex-60% Funding
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-39510-w.pdf
Reference39 articles.
1. Ferlay, J. et al. Cancer incidence and mortality worldwide: sources, methods and major patterns in GLOBOCAN 2012. Int J Cancer 136, E359–386 (2015).
2. Lemmon, M. A. & Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 141, 1117–1134 (2010).
3. Harari, D. & Yarden, Y. Molecular mechanisms underlying ErbB2/HER2 action in breast cancer. Oncogene 19, 6102–6114 (2000).
4. Appert-Collin, A., Hubert, P., Cremel, G. & Bennasroune, A. Role of ErbB Receptors in Cancer Cell Migration and Invasion. Front Pharmacol 6, 283 (2015).
5. Bisaro, B. et al. p130Cas scaffold protein regulates ErbB2 stability by altering breast cancer cell sensitivity to autophagy. Oncotarget 7, 4442–4453 (2016).
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1. Interrupting specific hydrogen bonds between ELF3 and MED23 as an alternative drug resistance-free strategy for HER2-overexpressing cancers;Journal of Advanced Research;2023-05
2. P130cas-FAK interaction is essential for YAP-mediated radioresistance of non-small cell lung cancer;Cell Death & Disease;2022-09-10
3. p130Cas/BCAR1 and p140Cap/SRCIN1 Adaptors: The Yin Yang in Breast Cancer?;Frontiers in Cell and Developmental Biology;2021-10-11
4. First-in-human, phase I single-ascending-dose study of the safety, pharmacokinetics, and relative bioavailability of selatinib, a dual EGFR-ErbB2 inhibitor in healthy subjects;Investigational New Drugs;2020-06-13
5. Author Correction: Modeling ErbB2-p130Cas interaction to design new potential anticancer agents;Scientific Reports;2019-11-22
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