Added by |
mollevi |
Group name |
EquipeMY |
Item Type |
Journal Article |
Title |
Evaluation of the dimerization profiles of HER tyrosine kinases by time-resolved Förster resonance energy transfer (TR-FRET) |
Creator |
Lopez-Crapez et al. |
Author |
Evelyne Lopez-Crapez |
Author |
Alexandre Ho-Pun-Cheung |
Author |
Patrick Garnero |
Author |
Hervé Bazin |
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. |
Publication |
Methods in Molecular Biology (Clifton, N.J.) |
Volume |
1233 |
Pages |
45-55 |
Date |
2015 |
Journal Abbr |
Methods Mol. Biol. |
Language |
eng |
DOI |
10.1007/978-1-4939-1789-1_5 |
ISSN |
1940-6029 |
Library Catalog |
PubMed |
Extra |
PMID: 25319888 |
Tags |
Animals, Antibodies, Monoclonal, Humanized, Cell Line, Tumor, Cetuximab, Female, Fluorescence Resonance Energy Transfer, Fluorescent Dyes, Gene Expression Regulation, Neoplastic, Humans, Immunoassay, Mice, original, Ovarian Neoplasms, Protein Kinase Inhibitors, Protein Multimerization, Receptor, Epidermal Growth Factor, Receptor, ErbB-2, Signal Transduction, Trastuzumab, Xenograft Model Antitumor Assays |
Date Added |
2018/11/13 - 17:25:15 |
Date Modified |
2019/05/21 - 15:01:12 |