Abstract
Activation of receptor tyrosine kinases (RTK), such as those belonging to the human epidermal growth factor receptor (HER) family, occurs only after receptor dimerization, which is a crucial step for cellular signal transduction and diversification. The HER family includes four members (EGFR/HER1, HER2, HER3, and HER4) that can homodimerize or heterodimerize. Here, we describe immunoassays based on time-resolved Förster resonance energy transfer (TR-FRET) to profile EGFR-EGFR, HER2-HER2, and EGFR-HER2 dimers directly in tumor samples.
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Acknowledgments
This work was supported by ANR grant 07-RIB-003/Dim-HER.
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Lopez-Crapez, E., Ho-Pun-Cheung, A., Garnero, P., Bazin, H. (2015). Evaluation of the Dimerization Profiles of HER Tyrosine Kinases by Time-Resolved Förster Resonance Energy Transfer (TR-FRET). In: Germano, S. (eds) Receptor Tyrosine Kinases. Methods in Molecular Biology, vol 1233. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-1789-1_5
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DOI: https://doi.org/10.1007/978-1-4939-1789-1_5
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Publisher Name: Humana Press, New York, NY
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Online ISBN: 978-1-4939-1789-1
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