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

Reversible amyloid formation by the p53 tetramerization domain and a cancer-associated mutant.

Journal of molecular biology - 28 Mar 2003

Lee Amanda S, Galea Charles, DiGiammarino Enrico L, Jun Bokkyoo, Murti Gopal, Ribeiro Raul C, Zambetti Gerard, Schultz Christian P, Kriwacki Richard W

Abstract excerpt

The tetramerization domain for wild-type p53 (p53tet-wt) and a p53 mutant, R337H (p53tet-R337H), associated with adrenocortical carcinoma (ACC) in children, can be converted from the soluble native state to amyloid-like fibrils under certain conditions. Circular dichroism, Fourier transform infrared spectroscopy and staining with Congo red and thioflavin T showed that p53tet-wt and p53tet-R337H adopt an...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Benzothiazoles

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Coloring Agents

Share to Congo Red

Share to Guanidine

Share to Spectrophotometry

Share to Spectroscopy, Fourier Transform Infrared

Share to Thiazoles

Source

Identifiers

PMID: 12634062
DOI: 10.1016/s0022-2836(03)00175-x

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

Reversible amyloid formation by the p53 tetramerization domain and a cancer-associated mutant.PMID 12634062Read ↗

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

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

Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.Semantic proximity Read ↗

The Status of p53 Oligomeric and Aggregation States in CancerSemantic proximity Read ↗

Targeting the Prion-like Aggregation of Mutant p53 to Combat Cancer.Semantic proximity Read ↗

Amyloidogenicity of p53: A Hidden Link Between Protein Misfolding and CancerSemantic proximity Read ↗

p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis.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 ↗

Amyloidogenicity of p53: a hidden link between protein misfolding and cancer.Semantic proximity Read ↗

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

Evidence for allosteric effects on p53 oligomerization induced by phosphorylation.Semantic proximity Read ↗

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

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