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Murakami, T., Freed, E. O. (2000) The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions. Proceedings of the National Academy of Sciences, 97 (1) 343-348 doi:10.1073/pnas.97.1.343

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Reference TypeJournal (article/letter/editorial)
TitleThe long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions
JournalProceedings of the National Academy of Sciences
AuthorsMurakami, T.Author
Freed, E. O.Author
Year2000 (January 4)Volume97
Issue1
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.97.1.343Search in ResearchGate
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Mindat Ref. ID1639145Long-form Identifiermindat:1:5:1639145:7
GUID0
Full ReferenceMurakami, T., Freed, E. O. (2000) The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions. Proceedings of the National Academy of Sciences, 97 (1) 343-348 doi:10.1073/pnas.97.1.343
Plain TextMurakami, T., Freed, E. O. (2000) The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions. Proceedings of the National Academy of Sciences, 97 (1) 343-348 doi:10.1073/pnas.97.1.343
In(2000, January) Proceedings of the National Academy of Sciences Vol. 97 (1) Proceedings of the National Academy of Sciences

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Qi, Mingli, Chu, Hin, Chen, Xuemin, Choi, Junghwa, Wen, Xiaoyun, Hammonds, Jason, Ding, Lingmei, Hunter, Eric, Spearman, Paul (2015) A tyrosine-based motif in the HIV-1 envelope glycoprotein tail mediates cell-type– and Rab11-FIP1C–dependent incorporation into virions. Proceedings of the National Academy of Sciences, 112 (24) 7575-7580 doi:10.1073/pnas.1504174112
Freed, E. O., Myers, D. J., Risser, R. (1990) Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proceedings of the National Academy of Sciences, 87 (12) 4650-4654 doi:10.1073/pnas.87.12.4650
Salzwedel, K., Berger, E. A. (2000) Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: Functional complementation of specific defects in gp120 and gp41. Proceedings of the National Academy of Sciences, 97 (23) 12794-12799 doi:10.1073/pnas.230438497
Tedbury, Philip R., Novikova, Mariia, Ablan, Sherimay D., Freed, Eric O. (2016) Biochemical evidence of a role for matrix trimerization in HIV-1 envelope glycoprotein incorporation. Proceedings of the National Academy of Sciences, 113 (2) doi:10.1073/pnas.1516618113
Lopez-Verges, S., Camus, G., Blot, G., Beauvoir, R., Benarous, R., Berlioz-Torrent, C. (2006) Tail-interacting protein TIP47 is a connector between Gag and Env and is required for Env incorporation into HIV-1 virions. Proceedings of the National Academy of Sciences, 103 (40) 14947-14952 doi:10.1073/pnas.0602941103
Freed, E. O., Delwart, E. L., Buchschacher, G. L., Panganiban, A. T. (1992) A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proceedings of the National Academy of Sciences, 89 (1) 70-74 doi:10.1073/pnas.89.1.70
Rousso, I., Mixon, M. B., Chen, B. K., Kim, P. S. (2000) Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity. Proceedings of the National Academy of Sciences, 97 (25) 13523-13525 doi:10.1073/pnas.240459697
Pritsker, M., Jones, P., Blumenthal, R., Shai, Y. (1998) A synthetic all D-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion. Proceedings of the National Academy of Sciences, 95 (13) 7287-7292 doi:10.1073/pnas.95.13.7287
Verrier, F. C., Charneau, P., Altmeyer, R., Laurent, S., Borman, A. M., Girard, M. (1997) Antibodies to several conformation-dependent epitopes of gp120/gp41 inhibit CCR-5-dependent cell-to-cell fusion mediated by the native envelope glycoprotein of a primary macrophage-tropic HIV-1 isolate. Proceedings of the National Academy of Sciences, 94 (17) 9326-9331 doi:10.1073/pnas.94.17.9326
Schrager, J. A., Marsh, J. W. (1999) HIV-1 Nef increases T cell activation in a stimulus-dependent manner. Proceedings of the National Academy of Sciences, 96 (14) 8167-8172 doi:10.1073/pnas.96.14.8167
Broder, C. C., Berger, E. A. (1995) Fusogenic selectivity of the envelope glycoprotein is a major determinant of human immunodeficiency virus type 1 tropism for CD4+ T-cell lines vs. primary macrophages. Proceedings of the National Academy of Sciences, 92 (19) 9004-9008 doi:10.1073/pnas.92.19.9004
 
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