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Toward a comprehensive characterization of the phosphotyrosine proteome
Cellular Signalling, 2011Tyrosine phosphorylation (pTyr) regulates important cell functions and plays a key role in carcinogenesis. The purpose of this study was to perform a comprehensive study of the phosphotyrosine proteome. Immunoaffinity enriched pTyr proteins and peptides from K562 leukemia cells were analyzed with high-resolving liquid chromatography mass spectrometry ...
Sara, Bergström Lind +6 more
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An alternative method for a fast separation of phosphotyrosine
Analytical Biochemistry, 1990A simple and rapid procedure is described for fully separating phosphotyrosine from phosphoserine and phosphothreonine through one-dimensional thin-layer chromatography. The migration properties of these phosphoamino acids are compared with those of CMP, UMP, ATP, ribose phosphate, and inorganic orthophosphate, considered the most frequent comigrating ...
G, Muñoz, S H, Marshall
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Phosphotyrosine-binding domains in signal transduction
Nature Reviews Molecular Cell Biology, 2002Protein phosphorylation provides molecular control of complex physiological events within cells. In many cases, phosphorylation on specific amino acids directly controls the assembly of multi-protein complexes by recruiting phospho-specific binding modules. Here, the function, structure, and cell biology of phosphotyrosine-binding domains is discussed.
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Biokhimiia (Moscow, Russia), 1990
Protein kinases phosphorylating proteins at tyrosine residues play an essential role in the cell growth regulation and neoplastic transformation. However, the functions of the majority of tyrosine protein kinases are still obscure, thus creating hindrances in the identification and isolation of phosphotyrosine-containing proteins.
A I, Kharitonenkov +2 more
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Protein kinases phosphorylating proteins at tyrosine residues play an essential role in the cell growth regulation and neoplastic transformation. However, the functions of the majority of tyrosine protein kinases are still obscure, thus creating hindrances in the identification and isolation of phosphotyrosine-containing proteins.
A I, Kharitonenkov +2 more
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Phosphotyrosine phosphatase activity in human platelets
Life Sciences, 1991Using O-phosphotyrosine as a substrate, human platelets were shown to contain a highly active phosphotyrosine phosphatase (PTPase) activity. This activity was potently inhibited by vanadate, molybdate, and HgCl2. About 80% of the PTPase activity was particulate. When Triton-solubilized PTPase activity from whole platelets was applied to a DEAE Sephacel
H M, Smilowitz +3 more
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The CD45 phosphotyrosine phosphatase
2003The CD45 transmembrane tyrosine phosphatase is an abundant glycoprotein expressed on all nucleated haematopoietic cells. It plays a critical role in regulating the threshold for signalling via the T and B cell antigen receptors and can also exert positive or negative effects on other receptors in immune cells. Mice and humans lacking CD45 have a severe
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Journal of the American Society for Mass Spectrometry, 2018
Guangming Chen +3 more
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Guangming Chen +3 more
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Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder.
Nature Chemical Biology, 2016Yangyang Bian +13 more
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