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Because glycosylation is known to be critical for numerous immune-related proteins, these patients likely present with additional abnormalities including hemolytic anemia, hepatosplenomegaly, and neutropenia. An immunologic mechanism to explain the link between glycosylation abnormalities and the immune dysregulation has not yet been established.
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.
A congenital disorder of glycosylation (previously called carbohydrate-deficient glycoprotein syndrome) is one of several rare inborn errors of metabolism in which glycosylation of a variety of tissue proteins and/or lipids is deficient or defective. Congenital disorders of glycosylation are sometimes known as CDG syndromes.
SRD5A3-CDG (also known as CDG syndrome type Iq, CDG-Iq, CDG1Q or Congenital disorder of glycosylation type 1q) is a rare, non X-linked congenital disorder of glycosylation (CDG) [1] due to a mutation in the steroid 5 alpha reductase type 3 gene. It is one of over 150 documented types of Congenital disorders of Glycosylation. [2]
ALG1-CDG is an autosomal recessive congenital disorder of glycosylation caused by biallelic pathogenic variants in ALG1. The first cases of ALG1-CDG were described in 2004, and the causative gene was identified at the same time. This disorder was originally designated CDG-IK, under earlier nomenclature for congenital disorders of glycosylation. [1]
NGLY1 deficiency is a very rare genetic disorder caused by biallelic pathogenic variants in NGLY1.It is an autosomal recessive disorder. Errors in deglycosylation are responsible for the symptoms of this condition. [1]
Tunicamycin blocks N-linked glycosylation (N-glycans) and treatment of cultured human cells with tunicamycin causes cell cycle arrest in G1 phase. It is used as an experimental tool in biology, e.g. to induce unfolded protein response. [2] Tunicamycin is produced by several bacteria, including Streptomyces clavuligerus and Streptomyces ...
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]