A5039897946- Glycosylation and Glycoproteins Research
- Ubiquitin and proteasome pathways
- Peptidase Inhibition and Analysis
- Carbohydrate Chemistry and Synthesis
- Click Chemistry and Applications
- Cancer Research and Treatments
- Particle accelerators and beam dynamics
- Monoclonal and Polyclonal Antibodies Research
- Particle Accelerators and Free-Electron Lasers
Stanford University
2019-2021
Studying posttranslational modifications classically relies on experimental strategies that oversimplify the complex biosynthetic machineries of living cells. Protein glycosylation contributes to essential biological processes, but correlating glycan structure, underlying protein, and disease-relevant regulation is currently elusive. Here, we engineer cells tag glycans with editable chemical functionalities while providing information biosynthesis, physiological context, fine structure. We...
Significance Most human secreted and cell surface proteins are modified by Ser/Thr(O)-linked glycosylation with N -acetylgalactosamine (O-GalNAc). While of fundamental importance in health disease, O-GalNAcglycosylation is technically challenging to study because a lack specific tools for biological assays. Here, we design an O-GalNAc–specific reporter molecule termed uridine diphosphate (UDP)– -( S )-azidopropionylgalactosamine (GalNAzMe) selectively label O-GalNAc glycoproteins living...
Metabolic oligosaccharide engineering (MOE) has fundamentally contributed to our understanding of protein glycosylation. Efficient MOE reagents are activated into nucleotide-sugars by cellular biosynthetic machineries, introduced glycoproteins and traceable bioorthogonal chemistry. Despite their widespread use, the metabolic fate many is only beginning be mapped. While interconnectivity can affect probe specificity, poor uptake salvage pathways may impact sensitivity trigger side reactions....
Abstract Studying posttranslational modifications classically relies on experimental strategies that oversimplify the complex biosynthetic machineries of living cells. Protein glycosylation contributes to essential biological processes, but correlating glycan structure, underlying protein and disease-relevant regulation is currently elusive. Here, we engineer cells tag glycans with editable chemical functionalities while providing information biosynthesis, physiological context fine...
Abstract Protein glycosylation events that happen early in the secretory pathway are often dysregulated during tumorigenesis. These can be probed, principle, by monosaccharides with bioorthogonal tags would ideally specific for distinct glycan subtypes. However, metabolic interconversion into other drastically reduces such specificity living cell. Here, we use a structure-based design process to develop monosaccharide probe GalNAzMe is cancer-relevant Ser/Thr- N -acetylgalactosamine...
Metabolic oligosaccharide engineering (MOE) has fundamentally contributed to our understanding of protein glycosylation. Efficient MOE reagents are activated into nucleotide-sugars by cellular biosynthetic machineries, introduced glycoproteins and traceable bioorthogonal chemistry. Despite their widespread use, the metabolic fate many is only beginning be mapped. While interconnectivity can affect probe specificity, poor uptake salvage pathways may impact sensitivity trigger side reactions....
Metabolic oligosaccharide engineering (MOE) has fundamentally contributed to our understanding of protein glycosylation. Efficient MOE reagents are activated into nucleotide-sugars by cellular biosynthetic machineries, introduced glycoproteins and traceable bioorthogonal chemistry. Despite their widespread use, the metabolic fate many is only beginning be mapped. While interconnectivity can affect probe specificity, poor uptake salvage pathways may impact sensitivity trigger side reactions....