Intrinsically disordered proteins in cellular signalling and regulation

PE Wright, HJ Dyson - Nature reviews Molecular cell biology, 2015 - nature.com
Intrinsically disordered proteins (IDPs) are important components of the cellular signalling
machinery, allowing the same polypeptide to undertake different interactions with different …

Targeting the p53–MDM2 interaction to treat cancer

C Klein, LT Vassilev - British journal of cancer, 2004 - nature.com
The tumour suppressor p53 is a transcription factor with powerful antitumour activity that is
controlled by its negative regulator MDM2 (mouse double minute 2, also termed HDM2 in …

Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation

CW Lee, JC Ferreon, ACM Ferreon… - Proceedings of the …, 2010 - National Acad Sciences
The transcriptional activity of p53 is regulated by a cascade of posttranslational
modifications. Although acetylation of p53 by CREB-binding protein (CBP)/p300 is known to …

Terphenyl-based helical mimetics that disrupt the p53/HDM2 interaction

H Yin, GI Lee, SP Hyung, GA Payne… - Angewandte …, 2005 - nyuscholars.nyu.edu
Abstract (Chemical Equation Presented) HDM2 regulates p53 by binding to its
transactivation domain and promoting its ubiquitin-dependent degradation. Crystallographic …

New insights into cancer: MDM2 binds to the citrullinating enzyme PADI4

S Araujo‐Abad, B Rizzuti, A Villamarin‐Ortiz… - Protein …, 2023 - Wiley Online Library
PADI4 is one of the human isoforms of a family of enzymes implicated in the conversion of
arginine to citrulline. MDM2 is an E3 ubiquitin ligase which is crucial for down‐regulation of …

[HTML][HTML] Dual-site regulation of MDM2 E3-ubiquitin ligase activity

M Wallace, E Worrall, S Pettersson, TR Hupp, KL Ball - Molecular cell, 2006 - cell.com
The control of p53 ubiquitination by MDM2 provides a model system to define how an E3-
ligase functions on a conformationally flexible substrate. The mechanism of MDM2-mediated …

Structural details on mdm2-p53 interaction

SW Chi, SH Lee, DH Kim, MJ Ahn, JS Kim… - Journal of Biological …, 2005 - ASBMB
Mdm2 is a cellular antagonist of p53 that keeps a balanced cellular level of p53. The two
proteins are linked by a negative regulatory feedback loop and physically bind to each other …

Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding

S Uhrinova, D Uhrin, H Powers, K Watt… - Journal of molecular …, 2005 - Elsevier
Critical to the inhibitory action of the oncogene product, MDM2, on the tumour suppressor,
p53, is association of the N-terminal domain of MDM2 (MDM2N) with the transactivation …

Probing the structural requirements of peptoids that inhibit hDM2− p53 interactions

T Hara, SR Durell, MC Myers… - Journal of the American …, 2006 - ACS Publications
Many cellular processes are controlled by protein− protein interactions, and selective
inhibition of these interactions could lead to the development of new therapies for several …

Structure–activity studies in a family of β‐Hairpin protein epitope mimetic inhibitors of the p53–HDM2 protein–protein interaction

R Fasan, RLA Dias, K Moehle, O Zerbe… - …, 2006 - Wiley Online Library
Inhibitors of the interaction between the p53 tumor‐suppressor protein and its natural human
inhibitor HDM2 are attractive as potential anticancer agents. In earlier work we explored …