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  2. N-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/N-linked_glycosylation

    The different types of lipid-linked oligosaccharide (LLO) precursor produced in different organisms.. N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called N-glycosylation, studied in ...

  3. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    N-linked glycosylation is a very prevalent form of glycosylation and is important for the folding of many eukaryotic glycoproteins and for cell–cell and cell–extracellular matrix attachment. The N-linked glycosylation process occurs in eukaryotes in the lumen of the endoplasmic reticulum and widely in archaea, but very rarely in bacteria.

  4. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The most common method of glycosylation of N-linked glycoproteins is through the reaction between a protected glycan and a protected Asparagine. [5] Similarly, an O-linked glycoprotein can be formed through the addition of a glycosyl donor with a protected Serine or Threonine. [5] These two methods are examples of natural linkage. [5]

  5. Unfolded protein response - Wikipedia

    en.wikipedia.org/wiki/Unfolded_protein_response

    The most important of these to note are N-linked glycosylation and disulfide bond formation. N-linked glycosylation occurs as soon as the protein sequence passes into the ER through the translocon, where it is glycosylated with a sugar molecule that forms the key ligand for the lectin molecules calreticulin (CRT; soluble in ER lumen) and ...

  6. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    N-Linked glycosylation involves oligosaccharide attachment to asparagine via a beta linkage to the amine nitrogen of the side chain. [7] The process of N -linked glycosylation occurs cotranslationally, or concurrently while the proteins are being translated.

  7. Protein biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Protein_biosynthesis

    N-linked glycosylation starts in the endoplasmic reticulum with the addition of a precursor glycan. The precursor glycan is modified in the Golgi apparatus to produce complex glycan bound covalently to the nitrogen in an asparagine amino acid. In contrast, O-linked glycosylation is the sequential covalent addition of individual sugars onto the ...

  8. N-glycosyltransferase - Wikipedia

    en.wikipedia.org/wiki/N-glycosyltransferase

    N-linked glycosylation is an important process, especially in eukaryotes where over half of all proteins have N-linked sugars attached [13] and where it is the most common form of glycosylation. [23] The processes are also important in prokaryotes [13] and archaeans. [24]

  9. Congenital disorder of glycosylation - Wikipedia

    en.wikipedia.org/wiki/Congenital_disorder_of...

    All N-linked oligosaccharides originate from a common lipid-linked oligosaccharide (LLO) precursor, synthesized in the ER on a dolichol-phosphate (Dol-P) anchor. The mature LLO is transferred co-translationally to consensus sequence Asn residues in the nascent protein, and is further modified by trimming and re-building in the Golgi. [9]