ArticleMethods in molecular biology (Clifton, N.J.)2023
Tyrosine Phosphorylation Screening on the Yeast Surface by Magnetic Bead Selection and FACS.
Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 0 citations in OpenAlex.
- A tethered yeast surface display system facilitates enriching epitope-specific binding interactions.Protein engineering, design & selection : PEDS · 2026Article
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2 authors at 1 institution in 1 country.
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Abstract
The ability to understand and characterize phosphorylation is important to the study of cell signaling and to synthetic biology approaches. Current methods for characterizing kinase-substrate interactions are limited by their inherently low throughput and the heterogeneity of samples analyzed. Recent advances in yeast surface display techniques provide new opportunities for studying individual kinase-substrate interactions in a stimulus-independent fashion. Here, we describe techniques for building substrate libraries into full-length domains of interest that, when co-localized intracellularly with individual kinases, result in the display of phosphorylated domains on the yeast surface, as well as fluorescence-activated cell sorting and magnetic bead selection techniques for enriching from these libraries based on phosphorylation state.
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