NGI-1 (ML414) is an inhibitor of Asparagine (N)-linked glycoslysation.
NGI-1 (ML414) is an inhibitor of Asparagine (N)-linked glycoslysation. NGI-1 inhibits the oligosaccharyltransferase, preventing the attachment to the protein. NGI-1 has been shown to induce senescence in receptor tyrosine kinase dependent tumors.
Asparagine-linked glycosylation involves the sequential assembly of an oligosaccharide onto a polyisoprenyl donor, followed by the en bloc transfer of the glycan to particular asparagine residues within acceptor proteins. These N-linked glycans play a critical role in a wide variety
Nature chemical biology, 12(12), 1023-1030 (2016-10-25)
Asparagine (N)-linked glycosylation is a protein modification critical for glycoprotein folding, stability, and cellular localization. To identify small molecules that inhibit new targets in this biosynthetic pathway, we initiated a cell-based high-throughput screen and lead-compound-optimization campaign that delivered a cell-permeable
In a series of investigations, N-glycosylation has proven to be a key determinant of enzyme secretion, activity, binding affinity and substrate specificity, enabling a protein to fine-tune its activity. In the majority of cases elimination of all putative N-glycosylation sites
Glycans modify lipids and proteins to mediate inter- and intramolecular interactions across all domains of life. RNA is not thought to be a major target of glycosylation. Here, we challenge this view with evidence that mammals use RNA as a
American journal of cancer research, 12(10), 4721-4736 (2022-11-17)
N-linked glycosylation of proteins is one of the post-translational modifications (PTMs) that shield tumor antigens from immune attack. Signaling lymphocytic activation molecule family 7 (SLAMF7) suppresses cancer cell phagocytosis and is an ideal target under clinical development. PTM of SLAMF7
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