Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "Strikingly, activation of the MEF2 reporter by a fusion protein consisting of MyoD with the herpesvirus VP16 transactivation domain (MyoD-VP16) remained predominantly pRb-dependent (Figure 1b, columns 4 and 5), even though MyoD-VP16 alone activated the E-box reporter considerably more than did wild-type MyoD and pRb together (Figure 1a, columns 3 and 4). Moreover, MyoD-VP16 did not activate the MEF2 reporter to significantly greater levels in either the absence or the presence of pRb than did wild-type MyoD (Figure 1b, compare columns 2 and 3 with columns 4 and 5). Together, these findings indicate that pRb is specifically required for MyoD-mediated activation of MEF2 and that this process is not a direct function of the transactivation abilities of MyoD. MEF2 expression, DNA binding, and nuclear localization are not modulated by pRb" ?g. }

• _5 value "Strikingly, activation of the MEF2 reporter by a fusion protein consisting of MyoD with the herpesvirus VP16 transactivation domain (MyoD-VP16) remained predominantly pRb-dependent (Figure 1b, columns 4 and 5), even though MyoD-VP16 alone activated the E-box reporter considerably more than did wild-type MyoD and pRb together (Figure 1a, columns 3 and 4). Moreover, MyoD-VP16 did not activate the MEF2 reporter to significantly greater levels in either the absence or the presence of pRb than did wild-type MyoD (Figure 1b, compare columns 2 and 3 with columns 4 and 5). Together, these findings indicate that pRb is specifically required for MyoD-mediated activation of MEF2 and that this process is not a direct function of the transactivation abilities of MyoD. MEF2 expression, DNA binding, and nuclear localization are not modulated by pRb" provenance.
• _5 value "Strikingly, activation of the MEF2 reporter by a fusion protein consisting of MyoD with the herpesvirus VP16 transactivation domain (MyoD-VP16) remained predominantly pRb-dependent (Figure 1b, columns 4 and 5), even though MyoD-VP16 alone activated the E-box reporter considerably more than did wild-type MyoD and pRb together (Figure 1a, columns 3 and 4). Moreover, MyoD-VP16 did not activate the MEF2 reporter to significantly greater levels in either the absence or the presence of pRb than did wild-type MyoD (Figure 1b, compare columns 2 and 3 with columns 4 and 5). Together, these findings indicate that pRb is specifically required for MyoD-mediated activation of MEF2 and that this process is not a direct function of the transactivation abilities of MyoD. MEF2 expression, DNA binding, and nuclear localization are not modulated by pRb" provenance.