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

Wild-type p53 adopts a 'mutant'-like conformation when bound to DNA.

The EMBO journal - 1 Mar 1993

Halazonetis T D, Davis L J, Kandil A N

Abstract excerpt

p53 is a negative regulator of cell growth. The majority of human tumors express mutant p53 proteins, which can be distinguished from wild-type by their immuno-reactivity to a panel of conformation-specific monoclonal antibodies, such as PAb421, PAb1620 and PAb246. Wild-type p53 has sequence-spec...

Topics

Animals
Antibodies, Monoclonal
Base Sequence
Cells, Cultured
DNA
Molecular Sequence Data
Mutation
Protein Binding
Protein Conformation
Rats
Tumor Suppressor Protein p53

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Open in PubMed Open full text

Identifiers

PMID: 8458320
DOI: 10.1002/j.1460-2075.1993.tb05743.x
PMCID: PMC413303

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8458320-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Wild-type p53 adopts a 'mutant'-like conformation when bound to DNA.PMID 8458320Read ↗

Reactivation of mutant p53: molecular mechanisms and therapeutic potential.Semantic proximity Read ↗

Structural biology of the tumor suppressor p53 and cancer-associated mutants.Semantic proximity Read ↗

Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants.Semantic proximity Read ↗

Understanding p53 functions through p53 antibodiesSemantic proximity Read ↗

A new set of monoclonal antibodies directed to proline-rich and central regions of p53.Semantic proximity Read ↗

A conformation hypothesis for the suppressor and promoter functions of p53 in cell growth control and in cancer.Semantic proximity Read ↗

Effect of mutation and conformation on the function of p53 in colorectal cancer.Semantic proximity Read ↗

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

Transcriptional Regulation by Wild-Type and Cancer-Related Mutant Forms of p53.Semantic proximity Read ↗

Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A resolution.Semantic proximity Read ↗

Tumorigenic p53 mutants undergo common structural disruptions including conversion to α-sheet structure.Semantic proximity Read ↗

Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human CancerSemantic proximity Read ↗

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