Disulfide bonding controls the processing of retroviral envelope glycoproteins.

This publication has 41 references indexed in Scilit:

• The human immunodeficiency virus type 1 envelope glycoprotein precursor acquires aberrant intermolecular disulfide bonds that may prevent normal proteolytic processing
  Virology, 1990
• Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents
  Nature, 1990
• Regulation of Protein Export From the Endoplasmic Reticulum
  Annual Review of Cell Biology, 1988
• Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteins
  Cell, 1988
• Formation of disulphide-linked µ2ω2 tetramers in pre-B cells by the 18K ω-immunoglobulin light chain
  Nature, 1987
• Structural and immunological similarities between simian sarcoma virus gene product(s) and human platelet-derived growth factor
  Nature, 1983
• S-Aminoethylation of Human Globin Chains Using 2-Bromoethylamine Hydrobromide
  Hemoglobin, 1981
• Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds
  Journal of Molecular Biology, 1980
• Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
  Proceedings of the National Academy of Sciences, 1979
• Diamide, a new reagent for the intracellular oxidation of glutathione to the disulfide
  Biochemical and Biophysical Research Communications, 1969