A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits
- 1 June 1988
- Vol. 53 (5), 743-752
- https://doi.org/10.1016/0092-8674(88)90092-x
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- Deletion of the cytoplasmic domain of the polymeric immunoglobulin receptor prevents basolateral localization and endocytosisCell, 1986
- 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 transportCell, 1986
- Heterologous transmembrane and cytoplasmic domains direct functional chimeric influenza virus hemagglutinins into the endocytic pathway.The Journal of cell biology, 1986
- Receptor-Mediated Endocytosis: Concepts Emerging from the LDL Receptor SystemAnnual Review of Cell Biology, 1985
- Signal sequencesJournal of Molecular Biology, 1985
- Internalization-defective LDL receptors produced by genes with nonsense and frameshift mutations that truncate the cytoplasmic domainCell, 1985
- Mutations in the cytoplasmic domain of the influenza virus hemagglutinin affect different stages of intracellular transport.The Journal of cell biology, 1985
- EndosomesTrends in Biochemical Sciences, 1983
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970