The characterisation of p53 binding phage isolated from phage peptide display libraries.

doi:10.1016/0022-2836(94)90038-8

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Article

The characterisation of p53 binding phage isolated from phage peptide display libraries.

Journal of molecular biology - 4 Nov 1994

Daniels D A, Lane D P

Abstract excerpt

Peptide phage display libraries were screened for peptides that bind to the tumour suppressor protein, human p53. Three p53 binding peptides were isolated respectively from hexamer (6-mer), dodecamer (12-mer) and icosomer (20-mer) libraries. We have characterised their interaction with p53 in detail. The phage appear to bind regions on native p53 common between mouse and man. Two conformation-specific anti-p53...

Topics

Amino Acid Sequence
Animals
Antibodies, Monoclonal
Antibody Specificity
Antigen-Antibody Complex
Antigens, Viral, Tumor
Bacteriophages
Baculoviridae
Binding, Competitive
Conserved Sequence
Enzyme-Linked Immunosorbent Assay

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Genomic Library

Humans

Mice

Molecular Sequence Data

Mutation

Peptides

Polymers

Source

Open in PubMed

Identifiers

PMID: 7966288
DOI: 10.1016/0022-2836(94)90038-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7966288-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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