NGI-1 (ML414) is primarily used in biochemical and pharmacological research for its ability to inhibit N-linked glycosylation, a critical post-translational modification process in proteins. It targets the oligosaccharyltransferase (OST) complex, making it a valuable tool for studying protein folding, endoplasmic reticulum stress, and the unfolded protein response. Due to its role in disrupting glycosylation, NGI-1 has shown potential in antiviral research, particularly against enveloped viruses that rely on properly glycosylated proteins for entry and infectivity, such as Zika, dengue, and hepatitis C virus. Additionally, it is investigated for its anticancer properties, as abnormal glycosylation is commonly observed in tumor cells and can influence cell adhesion, signaling, and immune evasion. Its selectivity and cell permeability make it suitable for in vitro and cellular assays aimed at understanding glycosylation-dependent pathways and developing therapeutic strategies.