Matches in Nanopublications for { ?s ?p "mutations in the Par-4 gene have not been reported in cancer cells. Accordingly, endogenous Par-4 must be bound and functionally inactivated by an antiapoptotic protein, which prevents Par-4 from executing its proapoptotic functions. Indeed, our recent studies reveal that binding of Akt1 to Par-4 results in both Par-4 phosphorylation and inactivation of its proapoptotic potential (7)." ?g. }
Showing items 1 to 4 of
4
with 100 items per page.
- _6 value "mutations in the Par-4 gene have not been reported in cancer cells. Accordingly, endogenous Par-4 must be bound and functionally inactivated by an antiapoptotic protein, which prevents Par-4 from executing its proapoptotic functions. Indeed, our recent studies reveal that binding of Akt1 to Par-4 results in both Par-4 phosphorylation and inactivation of its proapoptotic potential (7)." provenance.
- _6 value "mutations in the Par-4 gene have not been reported in cancer cells. Accordingly, endogenous Par-4 must be bound and functionally inactivated by an antiapoptotic protein, which prevents Par-4 from executing its proapoptotic functions. Indeed, our recent studies reveal that binding of Akt1 to Par-4 results in both Par-4 phosphorylation and inactivation of its proapoptotic potential (7)." provenance.
- _5 value "mutations in the Par-4 gene have not been reported in cancer cells. Accordingly, endogenous Par-4 must be bound and functionally inactivated by an antiapoptotic protein, which prevents Par-4 from executing its proapoptotic functions. Indeed, our recent studies reveal that binding of Akt1 to Par-4 results in both Par-4 phosphorylation and inactivation of its proapoptotic potential (7)." provenance.
- _5 value "mutations in the Par-4 gene have not been reported in cancer cells. Accordingly, endogenous Par-4 must be bound and functionally inactivated by an antiapoptotic protein, which prevents Par-4 from executing its proapoptotic functions. Indeed, our recent studies reveal that binding of Akt1 to Par-4 results in both Par-4 phosphorylation and inactivation of its proapoptotic potential (7)." provenance.