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- W2128249805 abstract "Protein tyrosine phosphorylation is a fundamental mechanism for controlling many aspects of cellular processes, as well as aspects of human health and diseases. Compared with phosphoserine and phosphothreonine, phosphotyrosine signaling is more tightly regulated, but often more challenging to characterize, due to significantly lower levels of tyrosine phosphorylation (i.e., a relative abundance of 1800:200:1 was estimated for phosphoserine/phosphothreonine/phosphotyrosine in vertebrate cells). In this review, we outline recent advances in analytical methodologies for enrichment, identification and accurate quantitation of tyrosine-phosphorylated proteins and peptides. Advances in antibody-based technologies, capillary liquid chromatography coupled with mass spectrometry, and various stable isotope labeling strategies are discussed, as well as non-mass spectrometry-based methods, such as those using protein/peptide arrays. As a result of these advances, powerful tools now have the power to crack signal transduction codes at the system level, and provide a basis for discovering novel drug targets for human diseases." @default.
- W2128249805 created "2016-06-24" @default.
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- W2128249805 creator A5064658611 @default.
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- W2128249805 date "2007-02-01" @default.
- W2128249805 modified "2023-10-09" @default.
- W2128249805 title "Quantitative proteomic approaches for studying phosphotyrosine signaling" @default.
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- W2128249805 doi "https://doi.org/10.1586/14789450.4.1.13" @default.
- W2128249805 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17288512" @default.
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