Results 301 to 310 of about 333,854 (331)
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Nuclear protein tyrosine kinases
Trends in Biochemical Sciences, 1994Protein tyrosine phosphorylation plays an important role in the transduction of extracellular signals. The prototypical protein tyrosine kinases are localized at the plasma membrane and are coupled to receptors that bind extracellular factors. Thus, protein tyrosine phosphorylation was previously thought to occur only in the cytoplasm. However, several
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Protein Tyrosine Kinase Structure and Function
Annual Review of Biochemistry, 2000▪ Abstract Tyrosine phosphorylation is one of the key covalent modifications that occurs in multicellular organisms as a result of intercellular communication during embryogenesis and maintenance of adult tissues. The enzymes that carry out this modification are the protein tyrosine kinases (PTKs), which catalyze the transfer of the γ phosphate of ...
S R, Hubbard, J H, Till
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Regulation of protein tyrosine kinases in platelets
Trends in Biochemical Sciences, 1994Platelet activation is accompanied by a dramatic increase in tyrosine phosphorylation of many cellular proteins. Phosphorylation of these proteins occurs in successive waves during the activation process, suggesting that several distinct mechanisms, occurring in a temporal order, regulate protein tyrosine kinases and/or phosphatases in activated ...
E A, Clark, S J, Shattil, J S, Brugge
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Fertilization signalling and protein-tyrosine kinases
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2000Fertilization is initiated by species-specific gamete cell recognition, i.e. sperm-egg interaction, followed by a rapid and sustained activation of multiple cellular and biochemical events, collectively called 'egg activation', which is indispensable for successful formation of zygotic nucleus and later embryogenesis.
K, Sato, A A, Tokmakov, Y, Fukami
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Protein tyrosine kinases in thymocyte development
Current Opinion in Immunology, 1997Much has been learned over the past few years about how protein tyrosine kinases mediate pre-TCR and mature alphabetaTCR function. The highlights include understanding the roles and the distinct effects of the Src and Syk families of protein tyrosine kinases in thymocyte development and function.
A M, Cheng, A C, Chan
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Protein Tyrosine Kinase Activity Assays
Current Protocols in Pharmacology, 1999AbstractProtein tyrosine kinases (PTKs) are ubiquitous enzymes that are integrally involved in the regulation of transformation mechanisms, normal and pathological growth, cell cycle regulation, immune responses, and a variety of intracellular signaling mechanisms.
B E, Hawes, T, van Biesen
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Protein tyrosine kinase–substrate interactions
Current Opinion in Structural Biology, 2006Protein 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.
Ron, Bose +3 more
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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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Protein tyrosine kinases in malignant melanoma
Melanoma Research, 2000Protein tyrosyl phosphorylation is an essential component in intracellular signalling, with diverse and crucial functions including mediation of cell proliferation, survival, death, differentiation, migration and attachment. It is regulated by the balance between the activities of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases.
D J, Easty, D C, Bennett
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Structural biology of protein tyrosine kinases
Cellular and Molecular Life Sciences, 2006Our current understanding of the structure, mechanism of action and modes of regulation of the protein tyrosine kinase family owes a great deal to structural biology. Structures are now available for more than 20 different tyrosine kinase domains, many of these in multiple conformational states.
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