Trastuzumab (herceptin), a humanized anti-Her2 receptor monoclonal antibody, inhibits basal and activated Her2 ectodomain cleavage in breast cancer cells.

By M. Molina, J. Codony-Servat, J. Albanell, F. Rojo, J. Arribas, J. Baselga. Cancer Research, 2001

854 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/63c696446f97f6e35762f9226ef446de7bc22352

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Citations in the corpus

An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. (2003, unknown): “Struckinase activation (Molina et al., 2001).”
Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth. (2002, unknown): “HRG binding may (Molina et al., 2001).”
Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. (2004, unknown): “3 shedding as trastuzumab does (Molina et al., 2001).”
Trastuzumab: mechanism of action, resistance and future perspectives in HER2-overexpressing breast cancer. (2007, background): “[26] demonstrated that trastuzumab can block the shedding of the extracellular domain of HER2 by inhibiting metalloproteinase activity.”
Improved classification of breast cancer by analysis of genetic alterations and gene expression profiling (2011, background): “, 2000), inhibit HER2 extracellular domain cleavage (Molina et al., 2001), or inhibit PI3K/ AKT survival signaling, either by downregulating HER2 signaling (Yakes et al.”
Strongly enhanced antitumor activity of trastuzumab and pertuzumab combination treatment on HER2-positive human xenograft tumor models. (2009, background): “Previous studies have reported that trastuzumab can sterically inhibit access for the proteases that cleave the extracellular domain and, therefore, prevent the formation of p95HER2, the truncated and very active form of HER2 (15, 42).”
Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941. (2009, background): “However, some of the previously described mechanisms of action, including the ability to inhibit HER2 shedding (Molina et al., 2001), may still be valid in some context.”
ERBB receptors: From oncogene discovery to basic science to mechanism-based cancer therapeutics (2014, background): “Through glycoengineering of its Fc moiety, RG7116 mediates enhanced ADCC that correlates with HER3 receptor density (Mirschberger et al., 2013).”
PTEN activation contributes to tumor inhibition by trastuzumab, and loss of PTEN predicts trastuzumab resistance in patients. (2004, background): “, 1999), and the inhibition Overexpression of ErbB2, a 185 kDa membrane receptor tyro- of ErbB2 ectodomain cleavage (Molina et al., 2001).”