Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding - Machamer, C E; Rose, J K (The Journal of biological chemistry, 1988)
Keywords: Binding Sites; Biological and medical sciences; Biological Transport; Cell Line; Cell Membrane - metabolism; Disulfides - metabolism; DNA, Recombinant; Endoplasmic Reticulum - metabolism; Fluorescent Antibody Technique; Fundamental and applied biological sciences. Psychology; Glycosylation; Hexosaminidases - pharmacology; Immunosorbent Techniques; Iodine Radioisotopes - metabolism; Lactoperoxidase - metabolism; Membrane Glycoproteins - metabolism; Microbiology; Mutation; Oligosaccharides - metabolism; Protein Conformation; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Structure-Activity Relationship; Temperature; Transfection; Vesicular stomatitis Indiana virus; vesicular stomatitis virus; Viral Envelope Proteins; Viral Matrix Proteins - genetics; Viral Matrix Proteins - metabolism; Virology; Virus; Intracellular transport; Vesicular stomatitis virus; Vesiculovirus; Rhabdoviridae; Plasma membrane; Virus replication cycle; Glycosylation; Property structure relationship; Gene expression