1997
DOI: 10.1023/a:1008209720526
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Epidermal growth factor receptor (EGFR) and EGFR mutations, function and possible role in clinical trials

Abstract: The epidermal growth factor receptor (EGFR) is a growth factor receptor that induces cell differentiation and proliferation upon activation through the binding of one of its ligands. The receptor is located at the cell surface, where the binding of a ligand activates a tyrosine kinase in the intracellular region of the receptor. This tyrosine kinase phosphorylates a number of intracellular substrates that activates pathways leading to cell growth, DNA synthesis and the expression of oncogenes such as fos and j… Show more

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Cited by 406 publications
(280 citation statements)
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“…The EGFR gene is amplified in 40% of glioblastomas; these tumors also show additional genomic rearrangements of EGFR gene, resulting in the expression of a truncated receptor that shows constitutive tyrosine kinase activity (Voldborg et al, 1997;Seghal, 1998) and aberrant receptor signaling and processing (Nagane at el., 2001). The most common rearrangement of the EGFR gene is type III mutation, an in-frame deletion of 801 bp, spanning exons 2-7 in the mRNA (Nishikawa et al, 1994).…”
Section: Introductionmentioning
confidence: 99%
“…The EGFR gene is amplified in 40% of glioblastomas; these tumors also show additional genomic rearrangements of EGFR gene, resulting in the expression of a truncated receptor that shows constitutive tyrosine kinase activity (Voldborg et al, 1997;Seghal, 1998) and aberrant receptor signaling and processing (Nagane at el., 2001). The most common rearrangement of the EGFR gene is type III mutation, an in-frame deletion of 801 bp, spanning exons 2-7 in the mRNA (Nishikawa et al, 1994).…”
Section: Introductionmentioning
confidence: 99%
“…At the end of the study, 15 of the 54 patients were still alive (27.77%). The median follow-up was 8 months (range [3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20]. The median survival time was 6 months (95% CI 1.7-10.3).…”
Section: Resultsmentioning
confidence: 99%
“…The binding of a ligand to the EGFR induces conformational changes within the receptor that increases the catalytic activity of its intrinsic tyrosine kinase, resulting in autophosphorylation which is necessary for biological activity (11,12). Protein tyrosine kinase activity plays a key role in the regulation of cell proliferation and differentiation (13). A large number of deletions of the EGFR in RNA have been observed in a number of neoplasias such as glioblastoma in non-small cell lung carcinomas, breast cancer, pediatric gliomas, medulloblastomas and ovarian carcinomas (13).…”
Section: Discussionmentioning
confidence: 99%
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“…The type III truncated EGFR lacks elements of the extracellular domain and is consequently unable to bind a ligand. Despite this, it displays constitutive kinase activity (3). These unique features make the mutant-EGFRvIII a potential target for antitumor intervention.…”
Section: Introductionmentioning
confidence: 99%