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 DNA Binding and Conformational Variation in Temperature Sensitive p53 Cancer Mutants Using QM-MM Simulations.

PloS one - 1 Jan 2015

Koulgi Shruti, Achalere Archana, Sonavane Uddhavesh, Joshi Rajendra

Abstract excerpt

The tp53 gene is found to be mutated in 50% of all the cancers. The p53 protein, a product of tp53 gene, is a multi-domain protein. It consists of a core DNA binding domain (DBD) which is responsible for its binding and transcription of downstream target genes. The mutations in p53 protein are responsible for creating cancerous conditions and are found to be occurring at a high frequency in the DBD region of p53....

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Mutant Proteins
Share to Principal Component Analysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Stability

Share to Quantum Theory

Share to Solvents

Share to Temperature

Share to Tumor Suppressor Protein p53

Source

Open in PubMed Open full text

Identifiers

PMID: 26579714
DOI: 10.1371/journal.pone.0143065
PMCID: PMC4651507

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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 DNA Binding and Conformational Variation in Temperature Sensitive p53 Cancer Mutants Using QM-MM Simulations.PMID 26579714Read ↗

QM-MM simulations on p53-DNA complex: a study of hot spot and rescue mutants.Semantic 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 ↗

Unraveling the Structural Changes in the DNA-Binding Region of Tumor Protein p53 (TP53) upon Hotspot Mutation p53 Arg248 by Comparative Computational Approach.Semantic proximity Read ↗

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

Impact of Arg175His mutation on the dynamical patterns of full-length human p53 proteinSemantic 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 ↗

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

Estimating the Effect of Single-Point Mutations on Protein Thermodynamic Stability and Analyzing the Mutation Landscape of the p53 Protein.Semantic proximity Read ↗

Investigation of the impact of R273H and R273C mutations on the DNA binding domain of P53 protein through molecular dynamic simulation.Semantic proximity Read ↗

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

Variable Mutations at the p53-R273 Oncogenic Hotspot Position Leads to Altered PropertiesSemantic proximity Read ↗

Factors governing loss and rescue of DNA binding upon single and double mutations in the p53 core domain.Semantic proximity Read ↗

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