Synthesis and photophysical properties of a fluorescent cyanoquinoline probe for profiling ERBB2 kinase inhibitor response

2017 ◽  
Vol 25 (21) ◽  
pp. 6016-6023 ◽  
Author(s):  
Heajin Lee ◽  
Ralf Landgraf ◽  
James N. Wilson
Keyword(s):  
Kinase Inhibitor ◽  
Photophysical Properties

scholarly journals Binding-induced, turn-on fluorescence of the EGFR/ERBB kinase inhibitor, lapatinib

2015 ◽  
Vol 13 (17) ◽  
pp. 5006-5011 ◽  
Author(s):  
James N. Wilson ◽  
Wenjun Liu ◽  
Adrienne S. Brown ◽  
Ralf Landgraf
Keyword(s):  
Fluorescence Imaging ◽  
Cellular Uptake ◽  
Kinase Inhibitor ◽  
Photophysical Properties ◽  
Turn On

The photophysical properties, fluorescence imaging, cellular uptake and distribution of lapatinib, an EGFR/ERBB inhibitor are reported.

947: Chemopreventive Effects of COX-2 Inhibitor and Epidermal Growth Factor (EGF)-Receptor Kinase Inhibitor on Rat Urinary Bladder Tumorigenesis

2004 ◽  
Vol 171 (4S) ◽  
pp. 251-251
Author(s):  
Kazunori Hattori ◽  
Katsuyuki Iida ◽  
Akira Johraku ◽  
Sadamu Tsukamoto ◽  
Taeko Asano ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Urinary Bladder ◽  
Egf Receptor ◽  
Kinase Inhibitor ◽  
Receptor Kinase ◽  
Rat Urinary Bladder ◽  
Epidermal Growth ◽  
Cox 2

Pro-apoptotic and anti-proliferative mechanisms of the kinase inhibitor tivantinib (ARQ 197)

2013 ◽  
Vol 51 (09) ◽  
Author(s):  
EN De Toni ◽  
S Lu ◽  
A Rizzani ◽  
F Kolligs ◽  
E Gallmeier ◽  
...  
Keyword(s):  
Kinase Inhibitor ◽  
Arq 197

Protein-tyrosine Kinase p72 syk Is Activated by Platelet Activating Factor in Platelets

1994 ◽  
Vol 72 (06) ◽  
pp. 937-941 ◽  
Author(s):  
Karim Rezaul ◽  
Shigeru Yanagi ◽  
Kiyonao Sada ◽  
Takanobu Taniguchi ◽  
Hirohei Yamamura
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Kinase ◽  
Kinase Inhibitor ◽  
Critical Role ◽  
Platelet Activating Factor ◽  
Kinase Assay ◽  
Potential Candidate ◽  
Protein Tyrosine ◽  
Induced Aggregation

SummaryIt has been demonstrated that activation of platelets by platelet-activating factor (PAF) results in a dramatic increase in tyrosine phosphorylation of several cellular proteins. We report here that p72 syk is a potential candidate for the protein-tyrosine phosphorylation following PAF stimulation in porcine platelets. Immunoprecipitation kinase assay revealed that PAF stimulation resulted in a rapid activation of p72 syk which peaked at 10 s. The level of activation was found to be dose dependent and could be completely inhibited by the PAF receptor antagonist, CV3988. Phosphorylation at the tyrosine residues of p72 syk coincided with activation of yllsyk. Pretreatment of platelets with aspirin and apyrase did not affect PAF induced activation of p72 syk .Furthermore, genistein, a potent protein-tyrosine-kinase inhibitor, diminished PAF-induced p72 syk activation and Ca2+ mobilization as well as platelet aggregation. These results suggest that p72 syk may play a critical role in PAF-induced aggregation, possibly through regulation of Ca2+ mobilization.

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