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Article

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

Biochemistry - 14 Feb 2006

Higashimoto Yuichiro, Asanomi Yuya, Takakusagi Satoru, Lewis Marc S, Uosaki Kohei, Durell Stewart R, Anderson Carl W, Appella Ettore, Sakaguchi Kazuyasu

Abstract excerpt

The p53 tumor suppressor is a tetrameric transcriptional enhancer, and its activity is compromised by mutations that cause amino acid substitutions in its tetramerization domain. Here we analyze the biochemical and biophysical properties of peptides corresponding to amino acids 319-358 of wild-type human p53, which includes the tetramerization domain, and that of a cancer-derived mutant with valine substituted...

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Identifiers

PMID: 16460008
DOI: 10.1021/bi051192j
PMCID: PMC2536691

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.

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