A Chimeric Protein of Simian Immunodeficiency Virus Envelope Glycoprotein gp140 and Escherichia coli Aspartate Transcarbamoylase
Harrison, Stephen C.
Reinherz, Ellis L.
Skehel, John J.
Wiley, Don C.
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CitationChen, B., Y. Cheng, L. Calder, S. C. Harrison, E. L. Reinherz, J. J. Skehel, and D. C. Wiley. 2004. “A Chimeric Protein of Simian Immunodeficiency Virus Envelope Glycoprotein Gp140 and Escherichia Coli Aspartate Transcarbamoylase.” Journal of Virology 78 (9): 4508–16. doi:10.1128/JVI.78.9.4508-4516.2004.
AbstractThe envelope glycoproteins of the human immunodeficiency virus and the related simian immunodeficiency virus (SIV) mediate viral entry into host cells by fusing viral and target cell membranes. We have reported expression, purification, and characterization of gp140 (also called gp160e), the soluble, trimeric ectodomain of the SIV envelope glycoprotein, gp160 (B. Chen et al., J. Biol. Chem. 275:34946-34953, 2000). We have now expressed and purified chimeric proteins of SIV gp140 and its variants with the catalytic subunit
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