N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression.-Reference-Cited by-同舟云学术

N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression.

Published:1992-05 Issue:15 Volume:267 Page:10690-10698
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Shakin-Eshleman S.H.,Remaley A.T.,Eshleman J.R.,Wunner W.H.,Spitalnik S.L.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference60 articles.

1. ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDES

2. Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane.

3. Glycosylation at specific sites of erythropoietin is essential for biosynthesis, secretion, and biological function.

4. In vitro expression and site-specific mutagenesis of the cloned human lipoprotein lipase gene. Potential N-linked glycosylation site asparagine 43 is important for both enzyme activity and secretion.

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