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  2. 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.

  3. 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 ...

  4. Chemical glycosylation - Wikipedia

    en.wikipedia.org/wiki/Chemical_glycosylation

    A chemical glycosylation reaction involves the coupling of a glycosyl donor, to a glycosyl acceptor forming a glycoside. [1] [2] [3] If both the donor and acceptor are sugars, then the product is an oligosaccharide. The reaction requires activation with a suitable activating reagent.

  5. DNA glycosylase - Wikipedia

    en.wikipedia.org/wiki/DNA_glycosylase

    DNA glycosylases catalyze the first step of this process. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. This is accomplished by flipping the damaged base out of the double helix followed by cleavage of the N-glycosidic bond. [1]

  6. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The process of glycosylation (binding a carbohydrate to a protein) is a post-translational modification, meaning it happens after the production of the protein. [3] Glycosylation is a process that roughly half of all human proteins undergo and heavily influences the properties and functions of the protein. [3]

  7. AP site - Wikipedia

    en.wikipedia.org/wiki/AP_site

    AP site formation can also be caused by various base-modifying chemicals. Alkylation, deamination, and oxidation of individual bases can all lead to the weakening of the glycosyl bond, so exposure to agents that cause those modifications can encourage AP site formation. [2] Ionizing radiation can also lead to AP site formation. Irradiated ...

  8. Glycation - Wikipedia

    en.wikipedia.org/wiki/Glycation

    Glycation is the non-enzymatic process responsible for many (e.g. micro and macrovascular) complications in diabetes mellitus and is implicated in some diseases and in aging. [ 2 ] [ 3 ] [ 4 ] Glycation end products are believed to play a causative role in the vascular complications of diabetes mellitus .

  9. O-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/O-linked_glycosylation

    O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O -glycosylation is a post-translational modification that occurs after the protein has been synthesised.