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Open AccessJournal ArticleDOI

The synthesis of complex-type oligosaccharides. I. Structure of the lipid-linked oligosaccharide precursor of the complex-type oligosaccharides of the vesicular stomatitis virus G protein.

E. Li, +2 more
- 10 Nov 1978 - 
- Vol. 253, Iss: 21, pp 7762-7770
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TLDR
The synthesis of the complex-type oligosaccharide unit of the vesicular stomatitis virus G protein is initiated by the en bloc transfer of a high molecular weight oligosACcharide from a lipid carrier to the nascent polypeptide.
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This article is published in Journal of Biological Chemistry.The article was published on 1978-11-10 and is currently open access. It has received 398 citations till now. The article focuses on the topics: Oligosaccharide & Mannose.

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Journal ArticleDOI

Biological Roles of Glycans

TL;DR: It is time for the diverse functional roles of glycans to be fully incorporated into the mainstream of biological sciences, as they are no different from other major macromolecular building blocks of life, simply more rapidly evolving and complex.
Journal ArticleDOI

Inhibitors of the Biosynthesis and Processing of N-Linked Oligosaccharide Chains

TL;DR: A number of inhibitors have been identified that interfere with glycoprotein biosynthesis, processing, or transport, such as tunicamycin, tridecaptin, and flavomycin this paper.

Inhibitors of the biosynthesis and processing of n-linked

TL;DR: A number of glycoproteins have oligosaccharides linked to protein in a GlcNAc----asparagine bond that are either of the complex, the high-mannose or the hybrid structure and a number of inhibitors have been identified that interfere with glycoprotein biosynthesis, processing, or transport.
Journal ArticleDOI

The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant.

TL;DR: Glycopeptide binding to lentil lectin-Sepharose was enhanced by the exposure of terminal N-acetylglucosamine residues on the glycopeptides, whereas binding to pea lectin -Sepharoses was enhancedBy the exposure to terminal mannose residues, and the differences in carbohydrate binding specificity were exploited to fractionate a mixture of [2-3H]mannose-labeled glycoproteins derived from mouse lymphoma cell gly
Book ChapterDOI

Primary structure of glycoprotein glycans: basis for the molecular biology of glycoproteins.

TL;DR: This chapter elaborates the primary structure and metabolism of the N -linked glycans, and presents the hypothesis that the catabolism of N -acetyl-lactosainine glycans starts by the action of endo-2-acetamido- 2-deoxy-β- D -glucosidases in liberating oligosaccharides that are then degraded by exoglycosidases.
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