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Matches in Nanopublications for { ?s ?p "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." ?g. }

• _6 value "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." provenance.
• _7 value "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." provenance.
• _5 value "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." provenance.
• _6 value "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." provenance.
• _7 value "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." provenance.
• _5 value "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." provenance.
• _6 value "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." provenance.
• _6 value "In this light, JDP2 could be used as a general inhibitor involved in cell cycle arrest and terminal differentiation and, like Mad, may have tumor suppressor activity The in vitro interaction of JDP2 with JunB and JunD was also examined (Fig. 5C). JDP2 formed heterodimeric complexes with both proteins. The stability of the JDP2-JunB and JDP2-JunD dimers is comparable to that of the c-Jun-JDP2 dimers (Fig. 5C). These results demonstrate that JDP1 and JDP2 are indeed bona fide members of the AP-1 group that heterodimerize with c-Jun or other Jun proteins." provenance.