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• W2416902139 abstract "The identification of proteins that interact specifically with posttranslational modifications such as phosphorylation is often necessary to understand cellular signaling pathways. Numerous methods for identifying proteins that interact with posttranslational modifications have been utilized, including affinity-based purification and analysis, protein microarrays, phage display, and tethered catalysis. Although these techniques have been used successfully, each has limitations. Recently, yeast surface-displayed human proteome libraries have been utilized to identify protein fragments with affinity for various target molecules, including phosphorylated peptides. When coupled with fluorescently activated cell sorting and high throughput methods for the analysis of selection outputs, yeast surface-displayed human proteome libraries can rapidly and efficiently identify protein fragments with affinity for any soluble ligand that can be fluorescently detected, including posttranslational modifications. In this review we compare the use of yeast surface display libraries to other methods for the identification of interactions between proteins and posttranslational modifications and discuss future applications of the technology." @default.
• W2416902139 created "2016-06-24" @default.
• W2416902139 creator A5035923646 @default.
• W2416902139 creator A5048826252 @default.
• W2416902139 date "2015-01-01" @default.
• W2416902139 modified "2023-09-23" @default.
• W2416902139 title "Identification of Posttranslational Modification-Dependent Protein Interactions Using Yeast Surface Displayed Human Proteome Libraries" @default.
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• W2416902139 doi "https://doi.org/10.1007/978-1-4939-2748-7_10" @default.
• W2416902139 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4839784" @default.
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