• protein glycosylation
  • His research has largely focused on molecular cell biology and, in particular, how protein glycosylation contributes to the mechanisms of health and common diseases including diabetes, sepsis, inflammatory diseases, and autoimmunity. (wikipedia.org)
  • Marth's use of Cre-Lox conditional mutagenesis established the presence and functions of multiple and in some cases previously unknown enzymes participating in protein glycosylation, an area of research that has become a focus of exploration in how common diseases originate in the absence of discernible pathogenic genetic variation. (wikipedia.org)
  • Marth's laboratory has also taken a close look at the molecular and cellular bases of type 2 diabetes and the role that protein glycosylation has in the origin of the disease. (wikipedia.org)
  • enzymes
  • 7-10 The enzymes involved transfer lipid-linked glycans, generated en masse in the cytoplasm, to protein targets in the periplasm. (rsc.org)
  • 1 As a consequence, there exists a high degree of functional redundancy such that null mutations in individual enzymes do not cause a glycosylation defect. (pubmedcentralcanada.ca)
  • Null mutations in enzymes that create less common types of O-linkages, however, result in embryonic lethality. (pubmedcentralcanada.ca)
  • Therefore, the type of N-glycan synthesised, depends on its accessibility to the different enzymes present within these cellular compartments. (wikipedia.org)
  • nascent
  • Prior to this, the glycan was co-translationally attached to a nascent protein by the oligosaccharyltransferase complex. (wikipedia.org)
  • There are three conditions to fulfill before a glycan is transferred to a nascent polypeptide: Asparagine must be located in a specific consensus sequence in the primary structure (Asn-X-Ser or Asn-X-Thr or in rare instances Asn-X-Cys). (wikipedia.org)
  • Following full assembly, the glycan is transferred en bloc by the glycosyltransferase oligosaccharyltransferase to a nascent peptide chain, within the reticular lumen. (wikipedia.org)
  • biosynthesis
  • Its affinities for donors of acceptors are lower than that of MGAT4A so it is suggested that it is not the main contributor in N-glycan biosynthesis. (wikipedia.org)
  • alterations
  • Marth's lab further discovered relationships between aberrant glycan linkages and autoimmune diseases including the fact that alterations of glycan linkages could initiate chronic inflammation in the development of autoimmunity. (wikipedia.org)
  • Alterations in glycosylation are often acquired in cases of cancer and inflammation, which may have important functional consequences. (wikipedia.org)
  • acceptor
  • Oligosaccharyltransferase is the enzyme responsible for the recognition of the consensus sequence and the transfer of the precursor glycan to a polypeptide acceptor which is being translated in the endoplasmic reticulum lumen. (wikipedia.org)
  • heterogeneity
  • This immunological role may well have driven the diversification of glycan heterogeneity and creates a barrier to zoonotic transmission of viruses. (wikipedia.org)
  • chains
  • Since there already is an array of aldehyde-specific reagents commercially available (such as aminooxy or hydrazide reagents), possible applications are diverse and include the conjugation of fluorophores, glycans, PEG (polyethylene glycol) chains or reactive groups for further synthesis (see applications). (wikipedia.org)
  • The interactions between the active site of sucrase-isomaltase and the following compounds have been identified: Man2GlcNAc2 glycan: Within the active site, Man2GlcNAc2 hydrogen bonds with hydroxyl side chains of Asp231 and Asp571. (wikipedia.org)
  • glycogen
  • A similar rate of hydrolysis of isomaltose by both isozymes was found indicating that the reduced catalytic activity of the variant isozyme toward glycogen is not the result of a reduced ability of this enzyme to cleave the alpha-1,6 linkages of glycogen. (worldwidescience.org)
  • This enzyme catalyses the following chemical reaction Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by enzyme EC 3.2.1.1. (wikipedia.org)
  • molecule
  • The energy required for this linkage comes from the hydrolysis of a pyrophosphate molecule. (wikipedia.org)
  • This reaction is driven by the energy released from the cleavage of the pyrophosphate bond between the dolichol-glycan molecule. (wikipedia.org)
  • immune system
  • Within the immune system the N-linked glycans on an immune cell's surface will help dictate that migration pattern of the cell, e.g. immune cells that migrate to the skin have specific glycosylations that favor homing to that site. (wikipedia.org)
  • serum
  • Ethyl esterification derivatization combined with MALDI-TOF MS analysis was employed for the comprehensive serum glycomic analysis in order to investigate glycan markers that would indicate the onset and progression of gastric cancer. (jcancer.org)
  • We comprehensively evaluate the serum glycan changes in different stages of GC patients including peritoneal metastasis for the first time. (jcancer.org)
  • At the C- lobe, human serum has two N-glycans while the hen ovotransferrin has a single N-glycan. (wikipedia.org)
  • Consequently, structurally this protein differs from its serum counterpart because of its glycosylation pattern. (wikipedia.org)
  • dolichol
  • N-linked glycosylation requires participation of a special lipid called dolichol phosphate. (wikipedia.org)
  • Sugar molecules are attached to the dolichol through a pyrophosphate linkage (one phosphate was originally linked to dolichol, and the second phosphate came from the nucleotide sugar). (wikipedia.org)
  • cleave
  • Eukaryotic MOGS does not cleave simple substrates such as p-nitrophenyl glucose, and it also shows no activity to the α(1→3) linkage present at the terminus of Glc1-2Man9GlcNAc2. (wikipedia.org)