Our Research:
Glycosylation is a critical post-translational modification that regulates numerous biological processes, including protein folding, stability, trafficking, intercellular communication, signaling, molecular recognition, immune responses, and inflammation. Aberrant glycosylation is strongly linked to the progression of diseases such as cancer and neurodegenerative disorders.
Our laboratory is advancing LC-MS/MS-based structural glycoproteomics, integrated with systems biology and bioinformatics, to investigate the structural and functional consequences of aberrant glycosylation. Additionally, we have developed a network biology analysis strategy to systematically analyze glycoform co-expression patterns and map glycoproteomic data into functional networks. Applying this approach to human disease models and patient samples, including cancer and Alzheimer's disease, has allowed us to identify key glycosylation modules involved in critical biological processes and uncover regulatory molecules implicated in disease-related glycosylation changes.
Current Projects Focus on:
Developing structural glycoproteomics techniques for the accurate identification of glycans and glycopeptides, focusing on mapping glycosylation sites and characterizing glycan heterogeneity.
Establishing an integrated approach that combines structural analysis with systems biology and bioinformatics to study how glycosylation affects protein networks and pathways.
Translating structural insights into biomarker discovery and therapeutic targeting by leveraging specific glycan structures associated with disease states, opening new avenues for diagnosis and treatment.