CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

Right arrow Help viewing high resolution images
Right arrow Return to article
Click on image to view larger version.



Fig. 6. Farnesylated, but not unprenylated, RhoA(63L) retains the ability to antagonize HIV-1 replication and gene expression. A, the ability of the RhoA(63L) protein to block the transient replication of HIV-1 was assessed by cotransfecting the HIV-1 provirus pNL4-3 with pcDNA3 expression plasmids encoding the indicated proteins in 293T cells. At 40–50 h after transfection, HIV-1 virions in the culture supernatant were measured by reverse transcriptase activity ({square}) or by quantification of infectious units ({blacksquare}). The relative HIV-1 replication is presented as a percentage of vector controls (100%). B, the ability of RhoA(63L) protein to inhibit gene expression was assessed by cotransfecting pNL4-3-Luciferase plasmid with pcDNA3 expression plasmids encoding the RhoA proteins in Jurkat T cells. The level of luciferase expression (relative light units) was measured 48 h after transfection. Data points are the means of three independent measurements; bars, SE. Data shown are representative of two independent experiments.





Right arrow Return to article


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation