Isolation and characterization of the hydrophobic COOH-terminal domains of the Sindbis virion glycoproteins
- 1 January 1982
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 154 (2) , 355-378
- https://doi.org/10.1016/0022-2836(82)90069-9
Abstract
No abstract availableThis publication has 48 references indexed in Scilit:
- Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteinsNature, 1980
- The mechanism of protein secretion across membranesNature, 1980
- Purification and amino acid compositions of the structural proteins of sindbis virusVirology, 1979
- Membrane biogenesis. In vitro cleavage, core glycosylation, and integration into microsomal membranes of sindbis virus glycoproteins.The Journal of cell biology, 1979
- Assembly of the semliki forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitroJournal of Molecular Biology, 1978
- The amphiphilic membrane glycoproteins of Semliki forest virus are attached to the lipid bilayer by their COOH-terminal endsJournal of Molecular Biology, 1978
- Initiation sites for translation of sindbis virus 42S and 26S messenger RNAsCell, 1975
- Isolation and characterization of the membrane proteins of Semliki Forest virusVirology, 1974
- A Film Detection Method for Tritium‐Labelled Proteins and Nucleic Acids in Polyacrylamide GelsEuropean Journal of Biochemistry, 1974
- Location of the Glycoprotein in the Membrane of Sindbis VirusNature New Biology, 1971