Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "CBP was initially characterized as a coactivator required for efficient transactivation of cAMP-response elementbinding protein, and p300 was first identified as a coactivator of the adenovirus E1A oncoprotein. CBP and p300 share many functional properties: both of them function as coactivators for multiple nuclear receptors as well as p53 and nuclear factor-eB [9], both possess intrinsic histone acetyltransferase activity, and both can recruit histone acetyltransferase and CBP/p300-associated factor [26]. Besides, CBP/p300 interacts with members of the SRC family and synergizes with SRC-1 in the transactivation of the ER and the PR" ?g. }

• _7 value "CBP was initially characterized as a coactivator required for efficient transactivation of cAMP-response elementbinding protein, and p300 was first identified as a coactivator of the adenovirus E1A oncoprotein. CBP and p300 share many functional properties: both of them function as coactivators for multiple nuclear receptors as well as p53 and nuclear factor-eB [9], both possess intrinsic histone acetyltransferase activity, and both can recruit histone acetyltransferase and CBP/p300-associated factor [26]. Besides, CBP/p300 interacts with members of the SRC family and synergizes with SRC-1 in the transactivation of the ER and the PR" provenance.
• _7 value "CBP was initially characterized as a coactivator required for efficient transactivation of cAMP-response elementbinding protein, and p300 was first identified as a coactivator of the adenovirus E1A oncoprotein. CBP and p300 share many functional properties: both of them function as coactivators for multiple nuclear receptors as well as p53 and nuclear factor-eB [9], both possess intrinsic histone acetyltransferase activity, and both can recruit histone acetyltransferase and CBP/p300-associated factor [26]. Besides, CBP/p300 interacts with members of the SRC family and synergizes with SRC-1 in the transactivation of the ER and the PR" provenance.
• _7 value "CBP was initially characterized as a coactivator required for efficient transactivation of cAMP-response elementbinding protein, and p300 was first identified as a coactivator of the adenovirus E1A oncoprotein. CBP and p300 share many functional properties: both of them function as coactivators for multiple nuclear receptors as well as p53 and nuclear factor-eB [9], both possess intrinsic histone acetyltransferase activity, and both can recruit histone acetyltransferase and CBP/p300-associated factor [26]. Besides, CBP/p300 interacts with members of the SRC family and synergizes with SRC-1 in the transactivation of the ER and the PR" provenance.
• _7 value "CBP was initially characterized as a coactivator required for efficient transactivation of cAMP-response elementbinding protein, and p300 was first identified as a coactivator of the adenovirus E1A oncoprotein. CBP and p300 share many functional properties: both of them function as coactivators for multiple nuclear receptors as well as p53 and nuclear factor-eB [9], both possess intrinsic histone acetyltransferase activity, and both can recruit histone acetyltransferase and CBP/p300-associated factor [26]. Besides, CBP/p300 interacts with members of the SRC family and synergizes with SRC-1 in the transactivation of the ER and the PR" provenance.
• _7 value "CBP was initially characterized as a coactivator required for efficient transactivation of cAMP-response elementbinding protein, and p300 was first identified as a coactivator of the adenovirus E1A oncoprotein. CBP and p300 share many functional properties: both of them function as coactivators for multiple nuclear receptors as well as p53 and nuclear factor-eB [9], both possess intrinsic histone acetyltransferase activity, and both can recruit histone acetyltransferase and CBP/p300-associated factor [26]. Besides, CBP/p300 interacts with members of the SRC family and synergizes with SRC-1 in the transactivation of the ER and the PR" provenance.
• _7 value "CBP was initially characterized as a coactivator required for efficient transactivation of cAMP-response elementbinding protein, and p300 was first identified as a coactivator of the adenovirus E1A oncoprotein. CBP and p300 share many functional properties: both of them function as coactivators for multiple nuclear receptors as well as p53 and nuclear factor-eB [9], both possess intrinsic histone acetyltransferase activity, and both can recruit histone acetyltransferase and CBP/p300-associated factor [26]. Besides, CBP/p300 interacts with members of the SRC family and synergizes with SRC-1 in the transactivation of the ER and the PR" provenance.