Discovery of Pteridin-7(8H)-one-Based Irreversible Inhibitors Targeting the Epidermal Growth Factor Receptor (EGFR) Kinase T790M/L858R Mutant

2013 ◽  
Vol 56 (20) ◽  
pp. 7821-7837 ◽  
Author(s):  
Wei Zhou ◽  
Xiaofeng Liu ◽  
Zhengchao Tu ◽  
Lianwen Zhang ◽  
Xin Ku ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Irreversible Inhibitors ◽  
Epidermal Growth ◽  
Egfr Kinase

Dual inhibitors of epidermal growth factor receptor and topoisomerase IIα derived from a quinoline scaffold

RSC Advances ◽  
2016 ◽  
Vol 6 (81) ◽  
pp. 77717-77734 ◽  
Author(s):  
Monika Chauhan ◽  
Gaurav Joshi ◽  
Harveen Kler ◽  
Archana Kashyap ◽  
Suyog M. Amrutkar ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Anticancer Activities ◽  
Topoisomerase Iiα ◽  
Dual Inhibitors ◽  
Epidermal Growth ◽  
Egfr Kinase

Based on the quinazoline bearing EGFR inhibitors, a series of thirty four compounds having a quinoline scaffold were synthesized and evaluated in vitro for EGFR kinase inhibitory and anticancer activities.

scholarly journals Platination of cysteine by an epidermal growth factor receptor kinase-targeted hybrid agent

2018 ◽  
Vol 54 (54) ◽  
pp. 7479-7482 ◽  
Author(s):  
Mu Yang ◽  
Hanzhi Wu ◽  
Julie Chu ◽  
Lucas A. Gabriel ◽  
Y. Kim ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Kinase Inhibitors ◽  
Growth Factor Receptor ◽  
Cysteine Residue ◽  
Receptor Kinase ◽  
Epidermal Growth ◽  
Hybrid Agent ◽  
Egfr Kinase

Platinum-modified tyrosine kinase inhibitors show strong and selective EGFR kinase binding and form adducts with a pharmacologically relevant cysteine residue.

scholarly journals Absence of Mutations in the Epidermal Growth Factor Receptor (EGFR) Kinase Domain in Patients with Mesothelioma

2009 ◽  
Vol 4 (4) ◽  
pp. 559 ◽  
Author(s):  
Vamsidhar Velcheti ◽  
Yumi Kasai ◽  
Avinash K. Viswanathan ◽  
Jon Ritter ◽  
Ramaswamy Govindan
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Kinase Domain ◽  
Epidermal Growth ◽  
Egfr Kinase

scholarly journals Epidermal Growth Factor Receptor Is Not Required for Human Cytomegalovirus Entry or Signaling

2007 ◽  
Vol 81 (12) ◽  
pp. 6241-6247 ◽  
Author(s):  
Marisa K. Isaacson ◽  
Adam L. Feire ◽  
Teresa Compton
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Endothelial Cell ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Lines ◽  
Virus Entry ◽  
Growth Factor Receptor ◽  
Negative Cell ◽  
Epidermal Growth ◽  
Egfr Kinase

ABSTRACT Human cytomegalovirus (HCMV) can bind, fuse, and initiate gene expression in a diverse range of vertebrate cell types. This broad cellular tropism suggests that multiple receptors and/or universally distributed receptors mediate HCMV entry. Our laboratory has recently discovered that certain β1 and β3 integrin heterodimers are critical mediators of HCMV entry into permissive fibroblasts (A. L. Feire, H. Koss, and T. Compton, Proc. Natl. Acad. Sci. USA 101:15470-15475, 2004). It has also been reported that epidermal growth factor receptor (EGFR) is necessary for HCMV-mediated signaling and entry (X. Wang, S. M. Huong, M. L. Chiu, N. Raab-Traub, and E. E. Huang, Nature 424:456-461, 2003). Integrins are known to signal synergistically with growth factor receptors, and this coordination was recently reported for EGFR and β3 integrins in the context of HCMV entry (X. Wang, D. Y. Huang, S. M. Huong, and E. S. Huang, Nat. Med. 11:515-521, 2005). However, EGFR-negative cell lines, such as hematopoietic cells, are known to be infected by HCMV. Therefore, we wished to confirm a role for EGFR in HCMV entry and then examine any interaction between β1 integrins and EGFR during the entry process. Surprisingly, we were unable to detect any role for EGFR in the process of HCMV entry into fibroblast, epithelial, or endothelial cell lines. Additionally, HCMV did not activate the EGFR kinase in fibroblast cell lines. We first examined HCMV entry into two EGFR-positive or -negative cell lines but observed no increase in entry when EGFR was expressed to high levels. Physically blocking EGFR with a neutralizing antibody in fibroblast, epithelial, or endothelial cell lines or blocking EGFR kinase signaling with a chemical inhibitor in fibroblast cells did not inhibit virus entry. Lastly, we were unable to detect phosphorylation of EGFR in fibroblasts cells in response to HCMV stimulation. Our findings demonstrate that EGFR does not play a significant role in HCMV entry or signaling. These results suggest that specific integrin heterodimers either act alone as the primary entry receptors or interact in conjunction with an additional receptor(s), other than EGFR, to facilitate virus entry.

scholarly journals Tumor Cell Killing Mechanisms of Epidermal Growth Factor Receptor (EGFR) Antibodies Are Not Affected by Lung Cancer-Associated EGFR Kinase Mutations

2008 ◽  
Vol 180 (6) ◽  
pp. 4338-4345 ◽  
Author(s):  
Matthias Peipp ◽  
Tanja Schneider-Merck ◽  
Michael Dechant ◽  
Thomas Beyer ◽  
Jeroen J. Lammerts van Bueren ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tumor Cell ◽  
Growth Factor Receptor ◽  
Cell Killing ◽  
Epidermal Growth ◽  
Tumor Cell Killing ◽  
Egfr Kinase
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