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HIV-1 envelope glycoprotein

Jiang S, Lin K, Strick N, Neurath AR (1993) Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41. Biochem Biophys Res Commun 195 533-538... [Pg.196]

Cormier EG, Persuh M, Thompson DA, et al. Specific interaction of CCR5 amino-terminal domain peptides containing sulfotyrosines with HIV-1 envelope glycoprotein gpl20. Proc Natl Acad Sci U S A 2000 97(ll) 5762-5767. [Pg.51]

Wyatt R, Sodroski J. The HIV-1 envelope glycoproteins fusogens, antigens, and immunogens. Science 1998 280(5371) 1884-1888. [Pg.277]

The major breakthrough in our structural knowledge of the HIV-1 envelope glycoprotein came in 1997 when the X-ray structure of the fusion-active form of gp41 was reported (35-37). Because it is inherently difficult to crystallize envelope glycoproteins, a protein-dissection approach was applied to derive substructures from the N- and C-terminal regions of the ectodomain termed N-36 and C-34. The structure indicates that the N-36/C-34 complex forms a hexahelical bundle consisting of a parallel trimeric coil-coil... [Pg.192]

Jiang S, Lin K, Lu M (1998) A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the HIV-1 envelope glycoprotein. J Virol 72 10213-10217... [Pg.204]

Milligan, E.D., O Connor, K.A., Nguyen, K.T. et al. (2001). Intrathecal HIV-1 envelope glycoprotein gpl20 induces enhanced pain states mediated by spinal cord proinflammatory cytokines. J. Neurosci. 21 2808-19. [Pg.196]

Wexler-Cohen Y, Ashkenazi A, Viard M et al (2010) Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain. FASEB J 24 4196-4202... [Pg.159]

Vives RR, Imberty A, Sattentau QJ, Lortat-Jacob H. Heparan sulfate targets the HIV-1 envelope glycoprotein gpl20 coreceptor binding site. J Biol Chem 2005 280 21353-21357. [Pg.247]

Balabanian, K., Harriague, J., Decrion, C., Lagane, B., Shorte, S., Baleux, F., et al. 2004. CXCR4-tropic HIV-1 envelope glycoprotein functions as a viral chemokine in unstimulated primary CD4+ T lymphocytes. J. Immunol. 173,7150-7160. [Pg.320]

Dimitrov AS, Xiao X, Dimitrov DS, Blumenthal R. Early intermediates in HIV-1 envelope glycoprotein-mediated fusion triggered by CD4 and coreceptor complexes. J Biol Chem 2001 7 7. [Pg.184]

Cormier, E. G., Persuh, M., Thompson, D. A., Lin, S. W., Sakmar, T. P., Olson, W. C., et al. (2000). Specific interaction ofCCRS amino-terminal domain peptides containing sulfotyrosines with HIV-1 envelope glycoprotein gpl20. Proceedings of the National Academy of Sciences of the United States of America, 97(11), 5762—5767. [Pg.385]

Navenot, J.M. et al. (2001) Molecular anatomy of CCR5 engagement by physiologic and viral chemokines and HIV-1 envelope glycoproteins differences in primary structural requirements for RANTES, MIP-1 alpha, and vM IP-II Binding. Journal of Molecular Biology, 313 (5), 1181-1193. [Pg.231]

Broder, C. C., Dimitrov, D. S., Blumenthal, R., and Berger, E. A. (1993) The block to HIV-1 envelope glycoprotein-mediated membrane fusion in animal cells expressing human CD4 can be overcome by a human cell component(s). Virology 193, 483-491. [Pg.261]

Puri A, Hug P, Munoz-Barroso I, Blumenthal R. Human erythrocyte glycolipids promote HIV-1 envelope glycoprotein-mediated fusion of CD4+ cells. Biochem Biophys Res Commun. 1998 242(l) 219-225. [Pg.312]

Ciardo A, Meldolesi J. Effects of the HIV-1 envelope glycoprotein gpl20 in cerebellar cultures. [Ca ]i increases in a glial cell subpopulation. Eur / Neurosci. 1993 5(12) 1711-1718. [Pg.359]

O. Andersen, A. M. Sorensen, S. E. Svehag, E. Fenouillet, Conglutinin binds the HIV-1 envelope glycoprotein gp 160 and inhibits its interaction with cell membrane CD4. Scand J. Immunol 1991,33, 81-88. [Pg.1959]


See other pages where HIV-1 envelope glycoprotein is mentioned: [Pg.360]    [Pg.145]    [Pg.195]    [Pg.277]    [Pg.259]    [Pg.289]    [Pg.217]    [Pg.190]    [Pg.202]    [Pg.414]    [Pg.360]    [Pg.440]    [Pg.386]    [Pg.8]    [Pg.146]    [Pg.125]    [Pg.209]    [Pg.113]    [Pg.123]    [Pg.523]    [Pg.440]    [Pg.261]    [Pg.173]    [Pg.94]    [Pg.259]    [Pg.85]    [Pg.270]    [Pg.297]   
See also in sourсe #XX -- [ Pg.297 ]




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Envelope glycoprotein

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