Results 11 to 20 of about 396,884 (345)
Characterization of B61, the Ligand for the Eck Receptor Protein-Tyrosine Kinase (*) [PDF]
Journal of Biological Chemistry, 1995 B61 was originally described as a novel secreted tumor necrosis factor-Ī±-inducible gene product in endothelial cells (Holzman, L. B., Marks, R. M., and Dixit, V. M.(1990) Mol. Cell. Biol. 10, 5830-5838).
H. Shao +4 more
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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
semanticscholar +3 more sources
Activation of receptor protein-tyrosine kinases from the cytoplasmic compartment. [PDF]
Journal of Biochemistry, 2012 It is widely accepted that receptor protein-tyrosine kinases (RTKs) are activated upon dimerization by binding to their extracellular ligands. However, EGF receptor (EGFR) dimerization per se does not require ligand binding. Instead, its cytoplasmic kinase domains have to form characteristic head-to-tail asymmetric dimers to become active, where one ...
Y. Yamanashi +2 more
semanticscholar +4 more sources
Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk.
Proceedings of the National Academy of Sciences of the United States of America, 1995 Betsy D. Bennett +6 more
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Tyrosine 402 phosphorylation of Pyk2 is involved in ionomycin-induced neurotransmitter release. [PDF]
PLoS ONE, 2014 Protein tyrosine kinases, which are highly expressed in the central nervous system, are implicated in many neural processes. However, the relationship between protein tyrosine kinases and neurotransmitter release remains unknown.
Zhao Zhang +9 more
doaj +1 more source
Association of the erythropoietin receptor with protein tyrosine kinase activity. [PDF]
Proceedings of the National Academy of Sciences, 1992 We have examined the signal transduction mechanism of the hematopoietic growth factor erythropoietin (Epo). Epo stimulation of Ba/F3 cells transfected with the Epo receptor resulted in increases in tyrosine phosphorylation of proteins of 97, 75, and 55 kDa.
William L. Farrar +3 more
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Frontiers in Plant Science, 2012 In metazoans, receptor kinases control many essential processes related to growth and development and response to the environment. The receptor kinases in plants and animals are structurally similar but evolutionarily distinct and thus while most animal ...
Man-Ho eOh +3 more
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Grb2 binding induces phosphorylation-independent activation of Shp2
Communications Biology, 2021 Lin et al. investigate the interactions between adaptor protein, Grb2, and the ubiquitously expressed protein tyrosine phosphatase, Shp2. They find that monomericĀ Grb2 can activate Shp2 and its downstream signalling in the absence of up-regulation of ...
Chi-Chuan Lin +5 more
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Cells, 2020 Helicobacter pylori, a stomach-colonizing Gram-negative bacterium, is the main etiological factor of various gastroduodenal diseases, including gastric adenocarcinoma. By establishing a life-long infection of the gastric mucosa, H.
Marina Leite +8 more
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Substrate Specificity of R3 Receptor-like Protein-tyrosine Phosphatase Subfamily toward Receptor Protein-tyrosine Kinases [PDF]
Journal of Biological Chemistry, 2013 Receptor-like protein-tyrosine phosphatases (RPTPs) are involved in various aspects of cellular functions, such as proliferation, differentiation, survival, migration, and metabolism. A small number of RPTPs have been reported to regulate activities of some cellular proteins including receptor protein-tyrosine kinases (RPTKs).
Juichi Sakuraba +7 more
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