Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Autoinhibition of MDMX by intramolecular p53 mimicry.

Proceedings of the National Academy of Sciences of the United States of America - 14 Apr 2015

Chen Lihong, Borcherds Wade, Wu Shaofang, Becker Andreas, Schonbrunn Ernst, Daughdrill Gary W, Chen Jiandong

Abstract excerpt

The p53 inhibitor MDMX is controlled by multiple stress signaling pathways. Using a proteolytic fragment release (PFR) assay, we detected an intramolecular interaction in MDMX that mechanistically mimics the interaction with p53, resulting in autoinhibition of MDMX. This mimicry is mediated by a hydrophobic peptide located in a long disordered central segment of MDMX that has sequence similarity to the p53...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Cycle Proteins
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Molecular Mimicry

Share to Peptides

Share to Proteolysis

Share to Proto-Oncogene Proteins c-mdm2

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 25825738
DOI: 10.1073/pnas.1420833112
PMCID: PMC4403185

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Autoinhibition of MDMX by intramolecular p53 mimicry.PMID 25825738Read ↗

Wild-type and cancer-related p53 proteins are preferentially degraded by MDM2 as dimers rather than tetramers.Semantic proximity Read ↗

Effect of the Flexible Regions of the Oncoprotein Mouse Double Minute X on Inhibitor Binding Affinity.Semantic proximity Read ↗

Structure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activation.Semantic proximity Read ↗

Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.Semantic proximity Read ↗

Functional analysis and consequences of Mdm2 E3 ligase inhibition in human tumor cells.Semantic proximity Read ↗

Simulating molecular mechanisms of the MDM2-mediated regulatory interactions: a conformational selection model of the MDM2 lid dynamics.Semantic proximity Read ↗

Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms.Semantic proximity Read ↗

The α-helical FXXΦΦ motif in p53: TAF interaction and discrimination by MDM2Semantic proximity Read ↗

Molecular mechanism of the interaction between MDM2 and p53.Semantic proximity Read ↗

Conserved Helix-Flanking Prolines Modulate Intrinsically Disordered Protein:Target Affinity by Altering the Lifetime of the Bound Complex.Semantic proximity Read ↗

The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo.Semantic proximity Read ↗

Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.