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  2. 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.

  3. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    O-linked glycans attached to the hydroxyl oxygen of serine, threonine, tyrosine, hydroxylysine, or hydroxyproline side-chains, or to oxygens on lipids such as ceramide. Phosphoglycans linked through the phosphate of a phosphoserine. C-linked glycans, a rare form of glycosylation where a sugar is added to a carbon on a tryptophan side-chain.

  4. O-GlcNAc - Wikipedia

    en.wikipedia.org/wiki/O-GlcNAc

    O-GlcNAc differs from other forms of protein glycosylation: (i) O-GlcNAc is not elongated or modified to form more complex glycan structures, (ii) O-GlcNAc is almost exclusively found on nuclear and cytoplasmic proteins rather than membrane proteins and secretory proteins, and (iii) O-GlcNAc is a highly dynamic modification that turns over more ...

  5. Protein O-GlcNAc transferase - Wikipedia

    en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase

    Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme (EC 2.4.1.255) that in humans is encoded by the OGT gene. [ 5 ] [ 6 ] OGT catalyzes the addition of the O -GlcNAc post-translational modification to proteins .

  6. 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]

  7. Protein O-GlcNAcase - Wikipedia

    en.wikipedia.org/wiki/Protein_O-GlcNAcase

    O-GlcNAcylation is a form of glycosylation, the site-specific enzymatic addition of saccharides to proteins and lipids. This form of glycosylation is with O-linked β-N-acetylglucosamine or β-O-linked 2-acetamido-2-deoxy-D-glycopyranose (O-GlcNAc).

  8. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    An example of an O-linked oligosaccharide with β-Galactosyl-(1n3)-α-N-acetylgalactosaminyl-Ser/Thr. Oligosaccharides that participate in O-linked glycosylation are attached to threonine or serine on the hydroxyl group of the side chain. [7]

  9. GALNT13 - Wikipedia

    en.wikipedia.org/wiki/GALNT13

    271786 Ensembl ENSG00000144278 ENSMUSG00000060988 UniProt Q8IUC8 Q8CF93 RefSeq (mRNA) NM_001301627 NM_052917 NM_173030 RefSeq (protein) NP_001288556 NP_443149 NP_001363321 NP_001363323 NP_001363327 NP_001363329 NP_001363330 NP_001363331 NP_001363332 NP_001363333 NP_001363334 NP_766618 Location (UCSC) Chr 2: 153.87 – 154.45 Mb Chr 2: 54.44 – 55.12 Mb PubMed search Wikidata View/Edit Human ...