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Non-receptor protein tyrosine kinases
Frontiers in Bioscience, 2003The 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 ...
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B61 is a ligand for the ECK receptor protein-tyrosine kinase
Nature, 1994A protein ligand for the ECK receptor protein-tyrosine kinase has been isolated by using the extracellular domain (ECK-X) of the receptor as an affinity reagent. Initially, concentrated cell culture supernatants were screened for receptor binding activity using immobilized ECK-X in a surface plasmon resonance detection system.
Timothy D. Bartley +19 more
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Comparative characterization of receptor and non-receptor associated protein tyrosine kinases
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989By using poly(Glu: Tyr, 4:1) as an exogenous substrate, the characteristics of insulin receptor associated protein tyrosine kinase (PTK) from rabbit skeletal muscle has been compared with a growth factor-independent non-receptor PTK partially purified from rat lung particulate fraction.
A K, Srivastava, J L, Chiasson
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Control of Lymphopoiesis by Non-Receptor Protein Tyrosine Kinases
1994Maintenance of a satisfactory immune system requires the daily generation of millions of lymphocytes from immature progenitor cells that reside (in adult mammals) in the bone marrow. Three fundamental processes underlie lymphopoiesis. First, a small population of hematopoietic stem cells (estimated to represent something less than 0.1% of bone marrow ...
R M, Perlmutter, S J, Anderson
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The ErbB/HER receptor protein-tyrosine kinases and cancer
Biochemical and Biophysical Research Communications, 2004The 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.
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Regulation of antigen receptor signal transduction by protein tyrosine kinases
Current Opinion in Immunology, 1996The past two years have seen further clarification of the early events occurring in antigen receptor signal transduction that are mediated by the immunoreceptor tyrosine-based activation motif (ITAM). The ITAM was shown to be a specific binding site for the ZAP-70/Syk protein tyrosine kinases and the structure of this complex was solved.
A C, Chan, A S, Shaw
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Protein tyrosine kinases in the initiation of antigen receptor signaling
Current Opinion in Immunology, 1995Intracellular responses to antigen receptor engagement involve the activation of protein tyrosine kinases and the tyrosine phosphorylation of cellular proteins, including components of the antigen receptor. Phosphorylation of two tyrosine residues within an 18 amino acid segment of the cytoplasmic domain of antigen receptor subunits, and the subsequent
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Non-Receptor Protein Tyrosine Kinases and Phosphatases in Human Platelets
Thrombosis and Haemostasis, 1996There 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.
S P, Jackson +4 more
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VEGF receptor protein–tyrosine kinases: Structure and regulation
Biochemical and Biophysical Research Communications, 2008The 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).
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Non-receptor protein tyrosine kinases as immune targets of viruses
Immunology Today, 1997Abstract Non-receptor protein tyrosine kinases (NRPTKs) are critically involved in signaling pathways that modulate growth, differentiation and (mature) cell function. Here, Yves Collette and Daniel Olive reviaw the recently identified interactions of virus proteins from Herpesviridae, Retroviridae and Papavaviridae with NRPTKs, mid propose that these
Y, Collette, D, Olive
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