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Tyrosine Phosphorylation of Rab Proteins
2005Tyrosine phosphorylation is a fundamental mechanism for regulating the functions of numerous proteins in eukaryotic cells. It has been known for some time that several members of the Rab GTPase family can undergo phosphorylation on serine or threonine residues, but the potential for tyrosine phosphorylation has been appreciated only recently, based on ...
Jean H, Overmeyer, William A, Maltese
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Study of Tyrosine Kinases and Protein Tyrosine Phosphorylation
2004In recent years, our increased understanding of the complex signal transduction mechanisms that regulate cellular function has fueled huge advances in all aspects of biomedical science and cell biology. Platelet and megakaryocyte function is no exception to this. In the last 10 yr our understanding of the receptor biochemistry and the systems that they
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Negative Regulation of a Protein Tyrosine Phosphatase by Tyrosine Phosphorylation
Journal of the American Chemical Society, 2006The low molecular weight protein tyrosine phosphatase (LMW-PTP) is a ubiquitously expressed enzyme with several proposed roles in cell signaling. Previously, two tyrosine phosphorylation modifications of LMW-PTP at sites Tyr-131 and Tyr-132 in response to growth factor stimulation have been mapped and suggested to stimulate LMW-PTP phosphatase activity.
Dirk, Schwarzer +3 more
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Regulation of Tyrosine Kinases by Tyrosine Phosphorylation
1991Protein kinases can be classified according to whether they phosphorylate phenolic (tyrosine) or aliphatic (serine and threonine) hydroxyl groups (Hunter and Cooper, 1985). Although there are now a few examples of kinases that seemingly break the rule (Howell et al., 1990), most tyrosine kinases differ from the serine/threonine kinases in their primary
Jonathan A. Cooper +2 more
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A Quantitative Assay for Tyrosine Sulfation and Tyrosine Phosphorylation in Peptides
Biological Chemistry Hoppe-Seyler, 1990A method was developed to measure sulfation and phosphorylation of tyrosine in proteins after alkaline hydrolysis, ion-exchange chromatography, reaction with [3H]dinitrofluorobenzene and subsequent thin-layer chromatography. The method allows the detection of 10-20 pmol of modified tyrosine and was applied to determine the content of tyrosine-phosphate
H, Blode, T, Heinrich, H, Diringer
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Phosphorylation of tyrosine in cultured human placenta
Biochimica et Biophysica Acta (BBA) - General Subjects, 1983The [32P]phosphoamino acids in proteins of first trimester and term-cultured human placentas have been separated and their relative amounts were measured. A significant phosphorylation of tyrosine residues could be detected in the cultured placental tissue at different stages of gestation.
H, Galski +3 more
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Integrin tyrosine phosphorylation in platelet signaling
Current Opinion in Cell Biology, 2001The beta 3 integrin cytoplasmic tyrosine (ICY) motif of alpha IIb beta 3 becomes tyrosine phosphorylated during platelet aggregation, causing Shc and myosin to interact with the beta-integrin cytoplasmic domain. Platelets from mice lacking beta 3 ICY motif tyrosines formed defective aggregates and poorly retracted clots, establishing integrin tyrosine ...
D R, Phillips +4 more
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Protein tyrosine phosphorylation in cardiovascular system
Molecular and Cellular Biochemistry, 1995Protein tyrosine phosphorylation is believed to play a central role in signaling pathways initiated by growth factor receptor activation. Recent studies have shown that various vasoactive peptides, in addition to eliciting a contractile response, also serve as growth factors for vascular smooth muscle ans stimulate tyrosyl phosphorylation of several ...
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American Journal of Therapeutics, 1995
Danuta Rzymkiewicz, Aubrey R. Morrison
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Danuta Rzymkiewicz, Aubrey R. Morrison
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