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dc.contributor.authorChen, Bing
dc.contributor.authorCheng, Yifan
dc.contributor.authorCalder, Lesley
dc.contributor.authorHarrison, Stephen C.
dc.contributor.authorReinherz, Ellis L.
dc.contributor.authorSkehel, John J.
dc.contributor.authorWiley, Don C.
dc.date.accessioned2019-10-13T16:03:38Z
dc.date.issued2004
dc.identifier.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.
dc.identifier.issn0022-538X
dc.identifier.issn1070-6321
dc.identifier.issn1098-5514
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41542815*
dc.description.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
dc.language.isoen_US
dc.publisherAmerican Society for Microbiology
dash.licenseLAA
dc.titleA Chimeric Protein of Simian Immunodeficiency Virus Envelope Glycoprotein gp140 and Escherichia coli Aspartate Transcarbamoylase
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalJournal of Virology
dash.depositing.authorHarrison, Stephen::29356e859c6d3698df98e8184352069e::600
dc.date.available2019-10-13T16:03:38Z
dash.workflow.comments1Science Serial ID 62846
dc.identifier.doi10.1128/JVI.78.9.4508-4516.2004
dash.source.volume78;9
dash.source.page4508


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