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Showing 1 to 8 of 8 for “"Oligosaccharyltransferase"”.

  1. ENGINEERING WATER-SOLUBLE VARIANTS OF THE SINGLE-SUBUNIT OLIGOSACCHARYLTRANSFERASE

    Oligosaccharyltransferase (OST) is a key enzyme in the asparagine-linked (N-linked) protein glycosylation pathway. OSTs exist in all domains of life and are capable of transferring a preassembled glycan from lipid carrier to an acceptor peptide. Bacterial OSTs are an single-subunit enzyme that are …

    cornell Repository record for ENGINEERING WATER-SOLUBLE VARIANTS OF THE SINGLE-SUBUNIT OLIGOSACCHARYLTRANSFERASE (opens in a new tab)

  2. Investigating asparagine-linked glycosylation substrate : specificity and effects on protein folding

    … expression including a single subunit oligosaccharyltransferase. To probe the bacterial N-linked glycosylation machinery, a chemo-enzymatic synthesis for each of the glycan intermediates within this pathway was developed, which are impractical to obtain from the host organism. …

    mit Repository record for Investigating asparagine-linked glycosylation substrate : specificity and effects on protein folding (opens in a new tab)

  3. Engineered Oligosaccharyltransferases With Unique N-Glycosylation Site Preferences

    … been one of the well-studied asparagine-linked oligosaccharyltransferase (OST) in bacterial glycoengineering area. While C. jejuni PglB performs well in transferring different glycans, the acceptor sites it can recognize are limited. We provided a thorough investigation into Desulfovibrio …

    cornell Repository record for Engineered Oligosaccharyltransferases With Unique N-Glycosylation Site Preferences (opens in a new tab)

  4. IMPROVING GLYCOSYLATION EFFICIENCY IN ESCHERICHIA COLI BY MAMMALIAN-CELL-INSPIRED PROTEIN-PROTEIN INTERACTIONS

    … glycans onto asparagine residues is called the oligosaccharyltransferase (OST). In mammalian cells, most proteins are N-glycosylated cotranslationally, mediated by protein-protein interactions between the OST and the general secretion (Sec) pathway. This mechanism is important for efficient …

    cornell Repository record for IMPROVING GLYCOSYLATION EFFICIENCY IN ESCHERICHIA COLI BY MAMMALIAN-CELL-INSPIRED PROTEIN-PROTEIN INTERACTIONS (opens in a new tab)

  5. Biochemical and biophysical investigations of N-linked glycosylation pathways in archaea

    … eukaryotes and selected bacteria, in which the oligosaccharyltransferase (OTase) carries out the en bloc transfer of glycans from polyprenyl-PP-linked donors onto asparagine side chains of acceptor proteins. The first aim of this thesis is to elucidate the biochemical details of archaeal …

    mit Repository record for Biochemical and biophysical investigations of N-linked glycosylation pathways in archaea (opens in a new tab)

  6. Polyprenyl-dependent glycan assembly pathways in microbial pathogens

    … The final glycan transfer is performed by an oligosaccharyltransferase (OTase), and specificity studies of O-linked and Nlinked bacterial OTases suggest that both enzymes prefer their native glycans under in vitro assay conditions. This work represents the first biochemical characterization of …

    mit Repository record for Polyprenyl-dependent glycan assembly pathways in microbial pathogens (opens in a new tab)

  7. TREX1 C-Terminus Regulates Oligosaccharyltransfererase to Prevent the Accumulation of an Endogenous Bioactive Disaccharide Associated with Autoimmune Disorders

    … I identified that TREX1 interacts with the oligosaccharyltransferase subunits Ribophorin 1 (RPN1) and DDOST. This interaction was dependent solely on TREX1 C-terminus. Furthermore, TREX1 C-terminus modulates OST's preference to hydrolyze lipid-linked oligosaccharides (LLOs) into bioactive …

    utswmed Repository record for TREX1 C-Terminus Regulates Oligosaccharyltransfererase to Prevent the Accumulation of an Endogenous Bioactive Disaccharide Associated with Autoimmune Disorders (opens in a new tab)