Related Experiment Video
Updated: Jun 11, 2026

08:16
Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
Published on: February 7, 2025
Metabolically incorporated photocrosslinking sialic acid covalently captures a ganglioside-protein complex
Michelle R Bond1, Chad M Whitman, Jennifer J Kohler
1Division of Translational Research, Department of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9185, USA. jennifer.kohler@utsouthwestern.edu
Molecular Biosystems
|July 14, 2010
Abstract:
When photoirradiated, an unnatural sialic acid analog can covalently capture the complex formed by ganglioside GM1 and cholera toxin subunit B.
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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