Influenza virus ts61S hemagglutinin is significantly defective in polypeptide folding and intracellular transport at the permissive temperature

This publication has 17 references indexed in Scilit:

• Intracellular maturation and transport of the SV5 type II glycoprotein hemagglutinin-neuraminidase: specific and transient association with GRP78-BiP in the endoplasmic reticulum and extensive internalization from the cell surface.
  The Journal of cell biology, 1989
• Regulation of Protein Export From the Endoplasmic Reticulum
  Annual Review of Cell Biology, 1988
• A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits
  Cell, 1988
• Assembly of influenza hemagglutinin trimers and its role in intracellular transport.
  The Journal of cell biology, 1986
• Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
  Cell, 1986
• Temperature-sensitive mutants of fowl plague virus defective in the intracellular transport of the hemagglutinin
  Virus Research, 1986
• Mutations in the cytoplasmic domain of the influenza virus hemagglutinin affect different stages of intracellular transport.
  The Journal of cell biology, 1985
• Polarized delivery of viral glycoproteins to the apical and basolateral plasma membranes of Madin-Darby canine kidney cells infected with temperature-sensitive viruses.
  The Journal of cell biology, 1985
• Physiological Characterization of Influenza Virus Temperature-sensitive Mutants Defective in the Haemagglutinin Gene
  Journal of General Virology, 1984
• Intracellular transport of influenza virus hemagglutinin to the apical surface of Madin-Darby canine kidney cells.
  The Journal of cell biology, 1984