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- W2053235095 endingPage "94" @default.
- W2053235095 startingPage "81" @default.
- W2053235095 abstract "Protein phosphorylation is a central regulatory mechanism of cell signaling pathways. This highly controlled biochemical process is involved in most cellular functions, and defects in protein kinases and phosphatases have been implicated in many diseases, highlighting the importance of understanding phosphorylation-mediated signaling networks. However, phosphorylation is a transient modification, and phosphorylated proteins are often less abundant. Therefore, the large-scale identification and quantification of phosphoproteins and their phosphorylation sites under different conditions are one of the most interesting and challenging tasks in the field of proteomics. Both 2D gel electrophoresis and liquid chromatography-tandem mass spectrometry serve as key phosphoproteomic technologies in combination with prefractionation, such as enrichment of phosphorylated proteins/peptides. Recently, new possibilities for quantitative phosphoproteomic analysis have been offered by technical advances in sample preparation, enrichment, separation, instrumentation, quantification and informatics. In this article, we present an overview of several strategies for quantitative phosphoproteomics and discuss how phosphoproteomic analysis can help to elucidate signaling pathways that regulate various cellular processes." @default.
- W2053235095 created "2016-06-24" @default.
- W2053235095 creator A5026964301 @default.
- W2053235095 creator A5044106619 @default.
- W2053235095 date "2011-02-01" @default.
- W2053235095 modified "2023-09-25" @default.
- W2053235095 title "Quantitative phosphoproteomics strategies for understanding protein kinase-mediated signal transduction pathways" @default.
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