Amanuel Kehasse

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Protein phosphorylation is a dynamic post-translational modification. Mass spectrometry-based quantitation was performed to determine the phosphoproteome profile of epithelial cells in response to injury, nucleotide, or epidermal growth factor. Phosphotyrosine enrichment used immunoprecipitation and immobilized metal affinity chromatography. Nucleotides(More)
The release of nucleotides after injury activates purinergic receptors, leading to phosphorylation of site-specific residues on epidermal growth factor receptor (EGFR). To elucidate the differences between the injury-induced response and that induced by exogenous EGF, we examined recruitment of docking proteins, internalization of EGFR, and migration after(More)
There is an increasing interest in the identification and characterization of protein posttranslational modifications (PTMs). The vast amount of information obtained within a typical differential proteomics makes the measure of PTMs challenging. We have begun to explore counting methods for differential analysis of PTM changes in proteomes. We have(More)
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