Matches in Nanopublications for { ?s ?p "even though this fusion protein efficiently prevented BrdU uptake in MCK-CAT-positive cells (Figure 4h-j). As E2F1-pRb(SP) retained the anti-proliferative property of pRb but did not fully activate myogenesis on its own, we tested whether it could cooperate with MEF2C-VP16 in our myogenesis assays. The combination of MyoD+E12, MEF2C-VP16, and E2F1-pRb(SP) activated MCK-luciferase expression to a level equal to or greater than that achieved following co-transfection of MyoD+E12 with pRb (Figure 4a, compare columns 3 and 7), and led to the appearance of numerous cells in the culture that displayed very high levels of CAT staining and no BrdU incorporation (Figure 4k-m), very similar to what was observed following transfection of MyoD with pRb (Figure 4b-d). Cotransfection of E2F1-pRb(SP) and MEF2C-VP16 in the absence of MyoD did not induce the expression of MCK-CAT (data not shown). Thus, we were able to fully substitute for the loss of pRb by cotransfecting MyoD with an activated form of MEF2 and the cell-cycle-arresting molecule E2F1-pRb(SP)." ?g. }
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- _4 value "even though this fusion protein efficiently prevented BrdU uptake in MCK-CAT-positive cells (Figure 4h-j). As E2F1-pRb(SP) retained the anti-proliferative property of pRb but did not fully activate myogenesis on its own, we tested whether it could cooperate with MEF2C-VP16 in our myogenesis assays. The combination of MyoD+E12, MEF2C-VP16, and E2F1-pRb(SP) activated MCK-luciferase expression to a level equal to or greater than that achieved following co-transfection of MyoD+E12 with pRb (Figure 4a, compare columns 3 and 7), and led to the appearance of numerous cells in the culture that displayed very high levels of CAT staining and no BrdU incorporation (Figure 4k-m), very similar to what was observed following transfection of MyoD with pRb (Figure 4b-d). Cotransfection of E2F1-pRb(SP) and MEF2C-VP16 in the absence of MyoD did not induce the expression of MCK-CAT (data not shown). Thus, we were able to fully substitute for the loss of pRb by cotransfecting MyoD with an activated form of MEF2 and the cell-cycle-arresting molecule E2F1-pRb(SP)." provenance.
- _4 value "even though this fusion protein efficiently prevented BrdU uptake in MCK-CAT-positive cells (Figure 4h-j). As E2F1-pRb(SP) retained the anti-proliferative property of pRb but did not fully activate myogenesis on its own, we tested whether it could cooperate with MEF2C-VP16 in our myogenesis assays. The combination of MyoD+E12, MEF2C-VP16, and E2F1-pRb(SP) activated MCK-luciferase expression to a level equal to or greater than that achieved following co-transfection of MyoD+E12 with pRb (Figure 4a, compare columns 3 and 7), and led to the appearance of numerous cells in the culture that displayed very high levels of CAT staining and no BrdU incorporation (Figure 4k-m), very similar to what was observed following transfection of MyoD with pRb (Figure 4b-d). Cotransfection of E2F1-pRb(SP) and MEF2C-VP16 in the absence of MyoD did not induce the expression of MCK-CAT (data not shown). Thus, we were able to fully substitute for the loss of pRb by cotransfecting MyoD with an activated form of MEF2 and the cell-cycle-arresting molecule E2F1-pRb(SP)." provenance.