scholarly journals The HPV16 E6 Oncoprotein Causes Prolonged Receptor Protein Tyrosine Kinase Signaling and Enhances Internalization of Phosphorylated Receptor Species

2013 ◽  
Vol 9 (3) ◽  
pp. e1003237 ◽  
Author(s):  
Jennifer M. Spangle ◽  
Karl Munger
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Receptor Protein ◽  
Kinase Signaling ◽  
Tyrosine Kinase Signaling ◽  
Hpv16 E6 ◽  
Protein Tyrosine ◽  
E6 Oncoprotein ◽  
Receptor Protein Tyrosine Kinase

scholarly journals Characterization of B61, the Ligand for the Eck Receptor Protein-Tyrosine Kinase

1995 ◽  
Vol 270 (10) ◽  
pp. 5636-5641 ◽  
Author(s):  
Haining Shao ◽  
Akhilesh Pandey ◽  
K. Sue O'Shea ◽  
Michael Seldin ◽  
Vishva M. Dixit
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinase

Control of neuronal pathway selection by a Drosophila receptor protein-tyrosine kinase family member

Nature ◽  
1995 ◽  
Vol 376 (6536) ◽  
pp. 171-174 ◽  
Author(s):  
Christopher A. Callahan ◽  
M. G. Muralidhar ◽  
Scott E. Lundgren ◽  
Audra L. Scully ◽  
John B. Thomas
Keyword(s):  
Tyrosine Kinase ◽  
Family Member ◽  
Protein Tyrosine Kinase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Kinase Family ◽  
Neuronal Pathway ◽  
Receptor Protein Tyrosine Kinase

scholarly journals Biochemical characterization of the protein tyrosine kinase homology domain of the ErbB3 (HER3) receptor protein

1997 ◽  
Vol 322 (3) ◽  
pp. 757-763 ◽  
Author(s):  
Susan L. SIERKE ◽  
Kunrong CHENG ◽  
Hong-Hee KIM ◽  
John G. KOLAND
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Egf Receptor ◽  
Biochemical Characterization ◽  
Cd Spectroscopy ◽  
Receptor Protein ◽  
Tyrosine Kinase Domain ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinase ◽  
Her3 Receptor

The putative protein tyrosine kinase domain (TKD) of the ErbB3 (HER3) receptor protein was generated as a histidine-tagged recombinant protein (hisTKD-B3) and characterized enzymologically. CD spectroscopy indicated that the hisTKD-B3 protein assumed a native conformation with a secondary structure similar to that of the epidermal growth factor (EGF) receptor TKD. However, when compared with the EGF receptor-derived protein, hisTKD-B3 exhibited negligible intrinsic protein tyrosine kinase activity. Immune complex kinase assays of full-length ErbB3 proteins also yielded no evidence of catalytic activity. A fluorescence assay previously used to characterize the nucleotide-binding properties of the EGF receptor indicated that the ErbB3 protein was unable to bind nucleotide. The hisTKD-B3 protein was subsequently found to be an excellent substrate for the EGF receptor protein tyrosine kinase, which suggested that in vivophosphorylation of ErbB3 in response to EGF could be attributed to a direct cross-phosphorylation by the EGF receptor protein tyrosine kinase.

scholarly journals Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk.

1995 ◽  
Vol 92 (6) ◽  
pp. 1866-1870 ◽  
Author(s):  
B. D. Bennett ◽  
F. C. Zeigler ◽  
Q. Gu ◽  
B. Fendly ◽  
A. D. Goddard ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Molecular Cloning ◽  
Protein Tyrosine Kinase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinase
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