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Non-receptor protein tyrosine kinases

Frontiers in Bioscience, 2003
The protein tyrosine kinases (PTKs) are enzymes catalyzing the transfer of the gamma-phosphate group of ATP to the hydroxyl groups of specific tyrosine residues in peptides. Although phosphotransfer reactions catalyzed by various PTKs are similar with regard to their basic mechanisms, their biological functions demonstrate a considerable degree of ...
A. Tsygankov
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The ErbB/HER receptor protein-tyrosine kinases and cancer

Biochemical and Biophysical Research Communications, 2004
The ErbB/HER protein-tyrosine kinases, which include the epidermal growth factor receptor, consist of a growth-factor-binding ectodomain, a single transmembrane segment, an intracellular protein-tyrosine kinase catalytic domain, and a tyrosine-containing cytoplasmic tail.
R. Roskoski
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VEGF receptor protein–tyrosine kinases: Structure and regulation

Biochemical and Biophysical Research Communications, 2008
The human VEGF family consists of VEGF (VEGF-A), VEGF-B, VEGF-C, VEGF-D, and placental growth factor (PlGF). The VEGF family of receptors consists of three protein-tyrosine kinases (VEGFR1, VEGFR2, and VEGFR3) and two non-protein kinase co-receptors (neuropilin-1 and neuropilin-2).
R. Roskoski
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Non-Receptor Protein Tyrosine Kinases and Phosphatases in Human Platelets

Thrombosis and Haemostasis, 1996
There is now a large and rapidly growing body of information on the different types of non-receptor tyrosine kinases and phosphatases present within platelets. These enzymes appear to play a critical role in co-ordinating, integrating and amplifying signals from multiple cell surface receptors.
Hatem H. Salem, Shaun P. Jackson, Prasad Cooray, Yuping Yuan, Simone M. Schoenwaelder   +4 more
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Signalling pathways operated by receptor protein tyrosine kinases

2002
The first RTK discovered was the EGFR. It was also the first receptor that provided evidence for a relationship between activating mutations (oncogenes) and cancer. About 90 genes code for protein tyrosine kinases in the human genome, out of which 58 are receptors (rPTK) and are classified into 20 subfamilies.
IJsbrand M. Kramer, Bastien D. Gomperts, Peter E.R. Tatham   +2 more
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Deceiving appearances: signaling by “dead” and “fractured” receptor protein-tyrosine kinases

BioEssays, 2000
The mechanisms by which most receptor protein-tyrosine kinases (RTKs) transmit signals are now well established. Binding of ligand results in the dimerization of receptor monomers followed by transphosphorylation of tyrosine residues within the cytoplasmic domains of the receptors.
Michael A. Miller, Robert Steele, Michael Kroiher   +2 more
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Phosphorylation of the Nicotinic Acetylcholine Receptor by Protein Tyrosine Kinases^a

Annals of the New York Academy of Sciences, 1995
Most neurotransmitter receptors examined to date are either regulated by phosphorylation or contain consensus sequences for phosphorylation by protein kinases. The nicotinic acetylcholine receptor (AChR), which mediates depolarization at the neuromuscular junction, has served as a model for the study of the structure, function, and regulation of ligand-
Richard L. Huganir, Zhican Qu, Sheridan L. Swope   +2 more
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Non-Receptor Protein Tyrosine Kinases

1995
Reversible phosphorylation of proteins has proved to be the most widely-employed regulatory mechanism governing cell behavior. Seminal studies performed in the 1960s by Edwin Krebs and colleagues on the regulation of glucose homeostasis paved the way for the enumeration of literally hundreds of protein kinases acting in species as diverse as bacteria ...
Steven J. Anderson, Roger M. Perlmutter, Mark W. Appleby, Jane A. Gross   +3 more
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