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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. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    The process of N-linked glycosylation occurs cotranslationally, or concurrently while the proteins are being translated. Since it is added cotranslationally, it is believed that N -linked glycosylation helps determine the folding of polypeptides due to the hydrophilic nature of sugars.

  5. Galectin - Wikipedia

    en.wikipedia.org/wiki/Galectin

    Structure of human galectin-9 in complex with N-acetyllactosamine dimer, clearly showing the two carbohydrate binding sites. Galectins are a class of proteins that bind specifically to β-galactoside sugars, such as N-acetyllactosamine (Galβ1-3GlcNAc or Galβ1-4GlcNAc), which can be bound to proteins by either N-linked or O-linked glycosylation.

  6. GCS1 - Wikipedia

    en.wikipedia.org/wiki/GCS1

    7841 57377 Ensembl n/a ENSMUSG00000030036 UniProt Q13724 Q80UM7 RefSeq (mRNA) NM_006302 NM_001146158 NM_020619 RefSeq (protein) NP_001139630 NP_006293 NP_065644 Location (UCSC) n/a Chr 6: 83.09 – 83.1 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Mannosyl-oligosaccharide glucosidase is an enzyme that in humans is encoded by the MOGS gene. Glucosidase I is the first enzyme in the ...

  7. 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 ...

  8. N-glycosyltransferase - Wikipedia

    en.wikipedia.org/wiki/N-glycosyltransferase

    N-glycosyltransferases are an unusual [a] type of glycosyltransferase which joins single hexoses to the target protein. [6] [7] [4] Attachment of sugars to the nitrogen atom in an amide group — such as the amide group of an asparagine — requires an enzyme, as the electrons of the nitrogen are delocalized in a pi-electron system with the carbon of the amide.

  9. GroEL - Wikipedia

    en.wikipedia.org/wiki/GroEL

    There are also three N-linked glycosylation sites at positions 104, 230, 436. [9] The sequence and secondary structure for the mitochondrial protein are illustrated in the above image obtained from the Protein Data Bank. Newer information has begun to suggest that the HSP60 found in the mitochondria differs from that of the cytoplasm.