Critical structural elements and multitarget protein interactions of the transcriptional activator AF-1 of hepatocyte nuclear factor 4.

TL;DR: It can be demonstrated that specific mutational changes in liver-enriched transcription factors lead to altered intermolecular interactions with the consequence of human disease.

TL;DR: 2b can be considered as a new prodrug prototype that prevents in vivo p53-triggered cell death in several neuropathologies and possibly reduces cancer therapy side effects.

TL;DR: It is suggested that HNF4α can functionally interact with both a coactivator and a corepressor without altering the status of any putative ligand and that the presence of the F domain may play a role in discriminating between the different coregulators.

TL;DR: It is shown that the N-terminal activation function (AF)-1 of HNF4α1 possesses significant activity that can be enhanced through interaction with glucocorticoid receptor-interacting protein 1 (GRIP-1) and cAMP response element-binding protein- binding protein (CBP).

TL;DR: The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-Residue transactivation domain peptide of p53 revealed that MDM 2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic α helix, supporting the hypothesis thatMDM2 inactivates p53 by concealing its transactivationdomain.

TL;DR: It is shown that CBP has intrinsic HAT activity, and Targeting CBP-associated H AT activity to specific promoters may be a mechanism by which E1A acts as a transcriptional activator.

TL;DR: Fluorescence anisotropy measurements are used to define the equi-librium binding parameters of the phosphoCREB:CBP interaction and report here that CBP can activate transcription through a region in its carboxy terminus.

TL;DR: It is shown that MODY1 is the gene encoding HNF-4α (gene symbol, TCP14), a member of the steroid/thyroid hormone receptor superfamily and an upstream regulator of H NF-1α expression9–11.