Results 281 to 290 of about 938,417 (319)

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 ...
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Protein tyrosine kinase–substrate interactions

Current Opinion in Structural Biology, 2006
Protein tyrosine kinases (PTKs) are enzymes that catalyze the phosphorylation of tyrosyl residues. They are important in physiological and pathophysiological processes. Protein substrates of PTKs are often difficult to discern, but recently reported methods have helped to identify targets and characterize their structural interactions with kinases.
Philip A. Cole, Kerry A. Pickin, Marc A. Holbert, Ron Bose   +3 more
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Tec protein‐tyrosine kinase is an effector molecule of Lyn proteni‐tyroenie kinase

The FASEB Journal, 1996
The Tec family is a recently emerging subfamily among nonreceptor type protein-tyrosine kinases (PTKs) consisting of Tec, Txk, Btk, Bmx, and Itk/Tsk/Emt. They have a long amino-terminal unique region containing a pleckstrin homology domain and a Tec-homology domain.
Yasusada Miura, Yoshihiro Yamashita, Akkra Miyazato, Keiya Ozawa, Hiroyuki Mano   +4 more
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Mechanisms of Transformation by Protein-Tyrosine Kinases

1988
In multicellular organisms there must be stringent control over the processes of cellular proliferation and differentiation. Thus sophisticated networks of regulatory molecules have evolved to sense and transmit signals within and between normal cells.
William H. Colledge, Michael J. Fry, John C. Bell, Michael G. Sargent, J. Gordon Foulkes, A. Raymond Frackelton, Louis Mahadevan   +6 more
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src-related protein tyrosine kinases

1989
Tyrosine protein kinases (TPKs) catalyze the transfer of phosphate groups from nucleotide triphosphates to tyrosine residues on proteins and peptides. While phosphorylation of proteins on tyrosine residues is a well-known post-radiational event detected in different regulatory systems, only a small number of cellular proteins are known substrates for ...
Joseph B. Bolen, André Veillette
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In vitro substrate specificity of protein tyrosine kinases

Molecular and Cellular Biochemistry, 1993
Synthetic peptides such as P60src autophosphorylation site peptides and angiotensin are indiscriminately phosphorylated by protein tyrosine kinases. The observation has led to the general belief that protein tyrosine kinases are highly promiscuous, displaying little in vitro site specificity.
Heung-Chin Cheng, Jerry H. Wang, Isao Matsuura   +2 more
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Butein, a Specific Protein Tyrosine Kinase Inhibitor

Biochemical and Biophysical Research Communications, 1998
Butein, a plant polyphenol, was shown to be a specific protein tyrosine kinase inhibitor. This compound inhibited not only the epidermal growth factor (EGF)-stimulated auto-phosphotyrosine level of EGF receptor in HepG2 cells but also tyrosine-specific protein kinase activities of EGF receptor (IC50 = 65 microM) and p60c-src (IC50 = 65 microM) in vitro.
Yang, E.-B., Zhang, K., Mack, P., Cheng, L.Y.   +3 more
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Structure and function of the protein tyrosine kinases

Progress in Growth Factor Research, 1990
The protein tyrosine kinases (PTKs) are a large and structurally diverse family of enzymes. The conserved catalytic domain held in common by each member of this family is a self-contained 250-300 amino acid unit bearing sixteen highly conserved linear sequence elements, several of which have been shown to be important to the catalytic activity of this ...
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Src-Related Protein Tyrosine Kinases in Hematopoiesis

Blood, 1999
T HE PROLIFERATION and differentiation of blood cell progenitors and precursors are tightly regulated by approximately a dozen different growth factors, which act primarily on hematopoietic cells.[1][1] In addition, growth factors that stimulate a wider variety of cell types, such as insulin ...
Steven M. Anderson, Seth J. Corey
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Proximal protein tyrosine kinases in immunoreceptor signaling

Current Opinion in Immunology, 2001
Immunoreceptor engagement results in the sequential activation of several classes of protein tyrosine kinases, including the Src and Syk/Zap-70 families. Recent progress has been made in our understanding of the regulation and function of these molecules. First, it was revealed that membrane compartmentation of protein tyrosine kinases may be essential
Sylvain Latour, André Veillette
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