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Port, we show that soluble mimics of CD4 inhibit HIV-1 infection by prematurely triggering the viral envelope glycoproteins. The unstable activated state of the virus lasts only a few minutes, after which the virus loses the ability to infect cells. This novel strategy for inhibition may be generally applicable to other viruses besides HIV-1, some of which are also activated by binding to their re
Port, we show that soluble mimics of CD4 inhibit HIV-1 infection by prematurely triggering the viral envelope glycoproteins. The unstable activated state of the virus lasts only a few minutes, after which the virus loses the ability to infect cells. This novel strategy for inhibition may be generally applicable to other viruses besides HIV-1, some of which are also activated by binding to their re
D role functioning (perfect score = 100) favoured the CXT arm (median change HAART = 0, CXT = +17; p=0.011). Improvement in pain (perfect score = 0, median change HAART = -16.7, CXT = -33.3; p=0.1) and overall QOL (median change HAART = 12.5, CXT = 16.7; p=0.08) were also greater in the CXT arm. Comparisons between arms were not statistically significant.NIH-PA Author Manuscript NIH-PA Author Manu
Tagonist `Compound A' [4-nitrobenzyl 1-(3(N-methylphenylsulfonamido)-3-phenylbutyl)piperidin-4-yl(vinyl)carbamate] [41,42] was kindly provided by Dr. Martin Springer at Merck Research Laboratories, Rahway, NJ. The anti-gp120 monoclonal antibody 48d, which recognizes an epitope that overlaps the coreceptor-binding site, was kindly provided by Dr. James Robinson (Tulane University Medical Center) [4
Infection in vitro, this protein was tested for clinical efficacy in HIV-1-infected individuals; however, no effect on plasma viral loads was observed [13]. Further examination revealed that doses of sCD4 that were significantly higher than those achieved in the clinical trial were required to neutralize primary clinical isolates of HIV-1, in contrast to the relatively sensitive, laboratory-adapte