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- W4311671429 endingPage "102233" @default.
- W4311671429 startingPage "102233" @default.
- W4311671429 abstract "Glycosylation is a ubiquitous post-translational modification read by glycan-binding proteins (GBP) to encode important functions, but a robust understanding of these interactions and their consequences can be challenging to uncover. Glycan-GBP interactions are transient and weak, making them difficult to capture, and glycosylation is dynamic and heterogenous, necessitating study in native cellular environments to identify endogenous ligands. Proximity labeling, an experimental innovation that labels biomolecules close to a protein of interest, has recently emerged as a powerful strategy to overcome these limitations, allowing interactors to be tagged in cells for subsequent enrichment and identification by mass spectrometry-based proteomics. We will describe this nascent technique and discuss its applications in the last five years with different GBP classes, including Siglecs, galectins, and non-human lectins." @default.
- W4311671429 created "2022-12-28" @default.
- W4311671429 creator A5020889163 @default.
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- W4311671429 date "2023-02-01" @default.
- W4311671429 modified "2023-10-16" @default.
- W4311671429 title "Proximity labeling technologies to illuminate glycan–protein interactions" @default.
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- W4311671429 doi "https://doi.org/10.1016/j.cbpa.2022.102233" @default.
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