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Matches in Nanopublications for { ?s ?p "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." ?g. }

• _6 value "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." provenance.
• _3 value "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." provenance.
• _4 value "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." provenance.
• _4 value "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." provenance.
• _3 value "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." provenance.
• _6 value "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." provenance.
• _3 value "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." provenance.
• _3 value "Despite such multiple target interactions of Akt1, parallel coinhibition of Akt1 and Par-4 expression by RNA interference resulted in the inhibition of apoptosis, indicating the failure of the other Akt1 substrates to induce apoptosis in the absence of Par-4 expression or function. Moreover, coinhibition of Akt1 and other Akt1 substrates did not inhibit apoptosis, implying that the observed apoptosis upon Akt1 inhibition can be ascribed primarily to Par-4. These observations highlight both the significance of Akt1 inhibition of endogenous Par-4 to promote cancer cell survival and the Par-4 dependent nature of apoptosis upon inhibition of Akt1 (Fig. 1B)." provenance.