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

p53 Amino-terminus region (1-125) stabilizes and restores heat denatured p53 wild phenotype.

PloS one - 22 Oct 2009

Sharma Anuj Kumar, Ali Amjad, Gogna Rajan, Singh Amir Kumar, Pati Uttam

Abstract excerpt

BACKGROUND: The intrinsically disordered N-ter domain (NTD) of p53 encompasses approximately hundred amino acids that contain a transactivation domain (1-73) and a proline-rich domain (64-92) and is responsible for transactivation function and apoptosis. It also possesses an auto-inhibitory function as its removal results in remarkable reduction in dissociation of p53 from DNA. PRINCIPAL FINDINGS/METHODOLOGY: In...

Read the complete abstract on PubMed

Topics

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

Share to Cell Nucleus
Share to Circular Dichroism
Share to Cytoplasm

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dose-Response Relationship, Drug

Share to Genes, p53

Share to Hot Temperature

Share to Proline

Share to Protein Denaturation

Source

Open in PubMed Open full text

Identifiers

PMID: 19847292
DOI: 10.1371/journal.pone.0007159
PMCID: PMC2760748

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

p53 Amino-terminus region (1-125) stabilizes and restores heat denatured p53 wild phenotype.PMID 19847292Read ↗

Mutant and wild-type p53 form complexes with p73 upon phosphorylation by the kinase JNK.Semantic proximity Read ↗

Cancer-Associated Mutations Perturb the Structure and Interactions of the Intrinsically Disordered p53 Transactivation DomainSemantic proximity Read ↗

Identification and characterization of the binding sequences and target genes of p53 lacking the 1st transactivation domain.Semantic proximity Read ↗

Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational ModelingSemantic proximity Read ↗

Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational ModelingSemantic proximity Read ↗

P53 TAD2 Domain (38-61) Forms Amyloid-like Aggregates in IsolationSemantic proximity Read ↗

The (1–63) Region of the p53 Transactivation Domain Aggregates In Vitro into Cytotoxic Amyloid AssembliesSemantic proximity Read ↗

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

A C-terminal inhibitory domain controls the activity of p63 by an intramolecular mechanism.Semantic proximity Read ↗

Structural studies on mechanisms to activate mutant p53.Semantic proximity Read ↗

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

Biological significance of a small highly conserved region in the N terminus of the p53 tumour suppressor protein.Semantic proximity Read ↗

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