THE EVIDENCE OF NON N-GLYCAN LINKED MANNOSE IN EXOCHITINASE (42 kDa) FROM Trichoderma harzianum BIO10671 GLYCOSYLATION

Evidence for N-linked glycosylation in Toxoplasma gondii.

In this paper we report experiments demonstrating the presence of N-linked oligosaccharide structures in Toxoplasma gondii tachyzoites, providing the first direct biochemical evidence that this sporozoan parasite is capable of synthesizing N-linked glycans. The tachyzoite surface glycoprotein gp23 was metabolically labelled with [3H]glucosamine and [3H]mannose. Gel-filtration chromatography on ...

Congenital disorders of glycosylation caused by defects in mannose addition during N-linked oligosaccharide assembly.

Trichoderma harzianum peritonitis in peritoneal dialysis.

Galactosyltransferase 4 is a major control point for glycan branching in N-linked glycosylation

Protein N-glycosylation is a common post-translational modification that produces a complex array of branched glycan structures. The levels of branching, or antennarity, give rise to differential biological activities for single glycoproteins. However, the precise mechanism controlling the glycan branching and glycosylation network is unknown. Here, we constructed quantitative mathematical mode...

Molecular imaging of N-linked glycosylation suggests glycan biosynthesis is a novel target for cancer therapy.

PURPOSE Redundant receptor tyrosine kinase (RTK) signaling is a mechanism for therapeutic resistance to epidermal growth factor receptor (EGFR) inhibition. A strategy to reduce parallel signaling by coexpressed RTKs is inhibition of N-linked glycosylation (NLG), an endoplasmic reticulum (ER) cotranslational protein modification required for receptor maturation and cell surface expression. We th...