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April 1, 1988Journal of Biological ChemistryOpen Access

Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding.

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Authors

CMCarolyn E. MachamerJohns Hopkins UniversityJRJ K RoseYale University

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Machamer et al. (1988) studied this question.

synapsesocial.com/papers/6a22fc90c650520b07cb1dd3https://doi.org/10.1016/s0021-9258(18)60659-3
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane.1988 · 91 citations
  2. 2Specific Intermediates in the Folding Reactions of Small Proteins and the Mechanism of Protein Folding1982 · 1,042 citations
  3. 3A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface.1985 · 157 citations
  4. 4A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein1985 · 160 citations
  5. 5Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers.1987 · 286 citations