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

A stable human p53 heterotetramer based on constructive charge interactions within the tetramerization domain.

The Journal of biological chemistry - 24 Jan 2003

Brokx Richard D, Bolewska-Pedyczak Eleonora, Gariépy Jean

Abstract excerpt

The human p53 tetramerization domain (called p53tet; residues 325-355) spontaneously forms a dimer of dimers in solution. Hydrophobic interactions play a major role in stabilizing the p53 tetramer. However, the distinctive arrangement of charged residues at the dimer-dimer interface suggests that they also contribute to tetramer stability. Charge-reversal mutations at positions 343, 346, and 351 within the...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Dimerization
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Protein Structure, Secondary

Share to Temperature

Share to Tumor Suppressor Protein p53

Share to Ultracentrifugation

Source

Identifiers

PMID: 12433927
DOI: 10.1074/jbc.M208528200

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

A stable human p53 heterotetramer based on constructive charge interactions within the tetramerization domain.PMID 12433927Read ↗

Cancer-associated p53 tetramerization domain mutants: quantitative analysis reveals a low threshold for tumor suppressor inactivation.Semantic proximity Read ↗

Structural Basis of Mutation-Dependent p53 Tetramerization Deficiency.Semantic proximity Read ↗

Structural evolution of p53, p63, and p73: implication for heterotetramer formation.Semantic proximity Read ↗

Structural Basis of Mutation-Dependent p53 Tetramerization DeficiencySemantic proximity Read ↗

Unfolding, aggregation, and amyloid formation by the tetramerization domain from mutant p53 associated with lung cancer.Semantic proximity Read ↗

The role of tetramerization in p53 function.Semantic proximity Read ↗

Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization.Semantic proximity Read ↗

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

Characterization of p53 mutants identified in human tumors with a missense mutation in the tetramerization domain.Semantic proximity Read ↗

Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53--a structural and combinatorial approach.Semantic proximity Read ↗

An engineered four-stranded coiled coil substitutes for the tetramerization domain of wild-type p53 and alleviates transdominant inhibition by tumor-derived p53 mutants.Semantic proximity Read ↗

Structure and functionality of a designed p53 dimer.Semantic proximity Read ↗

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