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

Investigating Conformational Dynamics and Allostery in the p53 DNA-Binding Domain Using Molecular Simulations.

Methods in molecular biology (Clifton, N.J.) - 1 Jan 2021

Papaleo Elena

Abstract excerpt

The p53 tumor suppressor is a multifaceted context-dependent protein, which is involved in multiple cellular pathways, with the ability to either keep the cells alive or to kill them through mechanisms such as apoptosis. To complicate this picture, cancer cells that express mutant p53 becomes addicted to the mutant activity, so that the mutant variant features a myriad of gain-of-function activities, opening...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Binding Sites
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Conformation

Share to Molecular Dynamics Simulation

Share to Protein Binding

Share to Protein Domains

Share to Tumor Suppressor Protein p53

Source

Identifiers

PMID: 33315226
DOI: 10.1007/978-1-0716-1154-8_13

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

Investigating Conformational Dynamics and Allostery in the p53 DNA-Binding Domain Using Molecular Simulations.PMID 33315226Read ↗

Unraveling the allosteric mechanism and mechanical stability of partial and complete loss-of-function mutations in p53 DNA-binding domain.Semantic proximity Read ↗

Navigating the complexity of p53-DNA binding: implications for cancer therapySemantic proximity Read ↗

Structural and sequential context of p53: A review of experimental and theoretical evidence.Semantic proximity Read ↗

Towards In Situ Dynamics of DNA-bound Full-Length p53 TetramerSemantic proximity Read ↗

Thermodynamic resilience of wild-type p53 DNA-binding domain and its disruption by the R273H hotspot mutation: insights from REMD simulations.Semantic proximity Read ↗

Molecular Dynamic Simulation Insights into the Normal State and Restoration of p53 FunctionSemantic proximity Read ↗

Allosteric and Dominant-Negative Effects in a p53 Core Heterotetramer.Semantic proximity Read ↗

Unraveling the Allosteric Mechanism of Four Cancer-related Mutations in the Disruption of p53-DNA Interaction.Semantic proximity Read ↗

Insights into the Effect of the G245S Single Point Mutation on the Structure of p53 and the Binding of the Protein to DNASemantic proximity Read ↗

Effects of temperature on the p53-DNA binding interactions and their dynamical behavior: comparing the wild type to the R248Q mutant.Semantic proximity Read ↗

Cancer-Associated Mutations Perturb the Disordered Ensemble and Interactions of the Intrinsically Disordered p53 Transactivation Domain.Semantic proximity Read ↗

Roles of computational modelling in understanding p53 structure, biology, and its therapeutic targetingSemantic proximity Read ↗

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