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Matches in Nanopublications for { ?s ?p "Because these residues are required for enhanced MEF2C activity in monocytic cells, we tested whether MyoD activation of Gal4-MEF2C required the same amino acids. The combined mutation of both Thr293 and Thr300 to alanine (T293;300A) did not affect the basal activity of Gal4-MEF2C (Figure 3b, compare columns 3 and 5), but did enhance the activity of Gal4-MEF2C when MyoD+E12 were co-expressed (Figure 3b, compare columns 4 and 6). In contrast, mutation of Ser387 to alanine (S387A) decreased the basal activity of Gal4-MEF2C and completely eliminated its activation by co-transfected MyoD+E12 (Figure 3b, columns 7,8). Importantly, activation of the p38 kinase pathway did stimulate the function of the S387A Gal4-MEF2C mutant (data not shown; see also [25,27]), indicating that this mutation does not simply inactivate the protein. Therefore, MyoD activation of the MEF2C TAD requires Ser387, but neither Thr293 nor Thr300, of MEF2C." ?g. }

• _5 value "Because these residues are required for enhanced MEF2C activity in monocytic cells, we tested whether MyoD activation of Gal4-MEF2C required the same amino acids. The combined mutation of both Thr293 and Thr300 to alanine (T293;300A) did not affect the basal activity of Gal4-MEF2C (Figure 3b, compare columns 3 and 5), but did enhance the activity of Gal4-MEF2C when MyoD+E12 were co-expressed (Figure 3b, compare columns 4 and 6). In contrast, mutation of Ser387 to alanine (S387A) decreased the basal activity of Gal4-MEF2C and completely eliminated its activation by co-transfected MyoD+E12 (Figure 3b, columns 7,8). Importantly, activation of the p38 kinase pathway did stimulate the function of the S387A Gal4-MEF2C mutant (data not shown; see also [25,27]), indicating that this mutation does not simply inactivate the protein. Therefore, MyoD activation of the MEF2C TAD requires Ser387, but neither Thr293 nor Thr300, of MEF2C." provenance.
• _5 value "Because these residues are required for enhanced MEF2C activity in monocytic cells, we tested whether MyoD activation of Gal4-MEF2C required the same amino acids. The combined mutation of both Thr293 and Thr300 to alanine (T293;300A) did not affect the basal activity of Gal4-MEF2C (Figure 3b, compare columns 3 and 5), but did enhance the activity of Gal4-MEF2C when MyoD+E12 were co-expressed (Figure 3b, compare columns 4 and 6). In contrast, mutation of Ser387 to alanine (S387A) decreased the basal activity of Gal4-MEF2C and completely eliminated its activation by co-transfected MyoD+E12 (Figure 3b, columns 7,8). Importantly, activation of the p38 kinase pathway did stimulate the function of the S387A Gal4-MEF2C mutant (data not shown; see also [25,27]), indicating that this mutation does not simply inactivate the protein. Therefore, MyoD activation of the MEF2C TAD requires Ser387, but neither Thr293 nor Thr300, of MEF2C." provenance.
• _5 value "Because these residues are required for enhanced MEF2C activity in monocytic cells, we tested whether MyoD activation of Gal4-MEF2C required the same amino acids. The combined mutation of both Thr293 and Thr300 to alanine (T293;300A) did not affect the basal activity of Gal4-MEF2C (Figure 3b, compare columns 3 and 5), but did enhance the activity of Gal4-MEF2C when MyoD+E12 were co-expressed (Figure 3b, compare columns 4 and 6). In contrast, mutation of Ser387 to alanine (S387A) decreased the basal activity of Gal4-MEF2C and completely eliminated its activation by co-transfected MyoD+E12 (Figure 3b, columns 7,8). Importantly, activation of the p38 kinase pathway did stimulate the function of the S387A Gal4-MEF2C mutant (data not shown; see also [25,27]), indicating that this mutation does not simply inactivate the protein. Therefore, MyoD activation of the MEF2C TAD requires Ser387, but neither Thr293 nor Thr300, of MEF2C." provenance.
• _5 value "Because these residues are required for enhanced MEF2C activity in monocytic cells, we tested whether MyoD activation of Gal4-MEF2C required the same amino acids. The combined mutation of both Thr293 and Thr300 to alanine (T293;300A) did not affect the basal activity of Gal4-MEF2C (Figure 3b, compare columns 3 and 5), but did enhance the activity of Gal4-MEF2C when MyoD+E12 were co-expressed (Figure 3b, compare columns 4 and 6). In contrast, mutation of Ser387 to alanine (S387A) decreased the basal activity of Gal4-MEF2C and completely eliminated its activation by co-transfected MyoD+E12 (Figure 3b, columns 7,8). Importantly, activation of the p38 kinase pathway did stimulate the function of the S387A Gal4-MEF2C mutant (data not shown; see also [25,27]), indicating that this mutation does not simply inactivate the protein. Therefore, MyoD activation of the MEF2C TAD requires Ser387, but neither Thr293 nor Thr300, of MEF2C." provenance.