scholarly journals FRS2β, a potential prognostic gene for non-small cell lung cancer, encodes a feedback inhibitor of EGF receptor family members by ERK binding

Oncogene ◽  
2010 ◽  
Vol 29 (21) ◽  
pp. 3087-3099 ◽  
Author(s):  
D Iejima ◽  
Y Minegishi ◽  
K Takenaka ◽  
A Siswanto ◽  
M Watanabe ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Egf Receptor ◽  
Small Cell ◽  
Small Cell Lung ◽  
Prognostic Gene ◽  
Egf Receptor Family ◽  
Feedback Inhibitor ◽  
Receptor Family

scholarly journals PET imaging of patients with non-small cell lung cancer employing an EGF receptor targeting drug as tracer

2011 ◽  
Vol 105 (12) ◽  
pp. 1850-1855 ◽  
Author(s):  
A A Memon ◽  
B Weber ◽  
M Winterdahl ◽  
S Jakobsen ◽  
P Meldgaard ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Pet Imaging ◽  
Egf Receptor ◽  
Small Cell ◽  
Small Cell Lung ◽  
Receptor Targeting

scholarly journals MA 15.06 ERBB Receptor Feedback Inhibitor-1 Alterations in Non-Small Cell Lung Cancer

2017 ◽  
Vol 12 (11) ◽  
pp. S1863
Author(s):  
J. Schneider ◽  
P. Jain ◽  
K. Schalper ◽  
C. Lovly ◽  
F. Gardner ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Small Cell ◽  
Erbb Receptor ◽  
Small Cell Lung ◽  
Feedback Inhibitor

scholarly journals Structure and Dynamics of the EGF Receptor as Revealed by Experiments and Simulations and Its Relevance to Non-Small Cell Lung Cancer

Cells ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 316 ◽  
Author(s):  
Marisa L. Martin-Fernandez ◽  
David T. Clarke ◽  
Selene K. Roberts ◽  
Laura C. Zanetti-Domingues ◽  
Francesco L. Gervasio
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Structure Function ◽  
Cell Lung Cancer ◽  
Egf Receptor ◽  
Growth Factor Receptor ◽  
Md Simulations ◽  
Small Cell ◽  
Small Cell Lung ◽  
High Resolution Data

The epidermal growth factor receptor (EGFR) is historically the prototypical receptor tyrosine kinase, being the first cloned and the first where the importance of ligand-induced dimer activation was ascertained. However, many years of structure determination has shown that EGFR is not completely understood. One challenge is that the many structure fragments stored at the PDB only provide a partial view because full-length proteins are flexible entities and dynamics play a key role in their functionality. Another challenge is the shortage of high-resolution data on functionally important higher-order complexes. Still, the interest in the structure/function relationships of EGFR remains unabated because of the crucial role played by oncogenic EGFR mutants in driving non-small cell lung cancer (NSCLC). Despite targeted therapies against EGFR setting a milestone in the treatment of this disease, ubiquitous drug resistance inevitably emerges after one year or so of treatment. The magnitude of the challenge has inspired novel strategies. Among these, the combination of multi-disciplinary experiments and molecular dynamic (MD) simulations have been pivotal in revealing the basic nature of EGFR monomers, dimers and multimers, and the structure-function relationships that underpin the mechanisms by which EGFR dysregulation contributes to the onset of NSCLC and resistance to treatment.

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