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Glycosylation is one of the most complex and functionally diverse biomolecular modifications, shaping protein folding, trafficking, and cell communication. Using our newly developed LODES/MSⁿ method, we established a systematic workflow for de novo glycan sequencing and uncovered several uncommon N-glycan structures in human cells that are not explained by canonical multicellular biosynthetic pathways. This advance expands the structural space of known glycans and allows precise decoding beyond traditional biosynthetic assumptions. In my postdoctoral research, I applied this approach to investigate how the loss of the AAA+ ATPase p97 affects glycoprotein processing in HeLa cells. Integrating proteomic and glycomic data revealed global remodeling of high-mannose and hybrid/complex N-glycans, coupled with altered expression of key glycosyltransferases and ER-associated degradation factors, highlighting the intimate link between proteostasis and glycosylation quality control. Building upon this foundation, my future work aims to extend LODES/MSⁿ-based structural analysis toward understanding GlycoRNA, RNA molecules covalently modified with glycans, and to explore how glycan modifications on RNA may contribute to molecular communication and regulation. Together, these studies aim to uncover new layers of glycobiological complexity at the interface of proteins and RNA.