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 small synthetic peptide, which inhibits the p53-hdm2 interaction, stimulates the p53 pathway in tumour cell lines.

Journal of molecular biology - 26 May 2000

Chène P, Fuchs J, Bohn J, García-Echeverría C, Furet P, Fabbro D

Abstract excerpt

The hdm2 protein negatively regulates p53 tumour suppressor activity. Upon binding to p53, hdm2 stimulates p53 degradation and inhibits its transcriptional activity. Moreover, the hdm2 protein is overexpressed in various tumours inactivating p53. We report here that an octamer synthetic peptide derived from p53 inhibits the p53-hdm2 interaction in vitro. In cellular assays, this untagged peptide penetrates tumour...

Read the complete abstract on PubMed

Topics

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

Share to Caspase 3
Share to Caspase Inhibitors
Share to Caspases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cisplatin

Share to Cyclin-Dependent Kinase Inhibitor p21

Share to Cyclins

Share to Enzyme Induction

Share to Proto-Oncogene Proteins c-mdm2

Source

Identifiers

PMID: 10860736
DOI: 10.1006/jmbi.2000.3738

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 small synthetic peptide, which inhibits the p53-hdm2 interaction, stimulates the p53 pathway in tumour cell lines.PMID 10860736Read ↗

Helping the Released Guardian: Drug Combinations for Supporting the Anticancer Activity of HDM2 (MDM2) AntagonistsSemantic proximity Read ↗

Targeting the p53–MDM2 interaction to treat cancerSemantic proximity Read ↗

Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo.Semantic proximity Read ↗

Inhibition of nutlin-resistant HDM2 mutants by stapled peptides.Semantic proximity Read ↗

Preferential induction of necrosis in human breast cancer cells by a p53 peptide derived from the MDM2 binding site.Semantic proximity Read ↗

Peptide and protein chemistry approaches to study the tumor suppressor protein p53.Semantic proximity Read ↗

Small-molecule inhibitors of the p53-HDM2 interaction for the treatment of cancerSemantic proximity Read ↗

Targeting the MDM2 ‐ MDM4 interaction interface reveals an otherwise therapeutically active wild‐type p53 in colorectal cancerSemantic proximity Read ↗

SCH529074, a small molecule activator of mutant p53, which binds p53 DNA binding domain (DBD), restores growth-suppressive function to mutant p53 and interrupts HDM2-mediated ubiquitination of wild type p53.Semantic proximity Read ↗

A stapled peptide inhibitor of MDM2 enables pharmacological activation of p53 in zebrafishSemantic proximity Read ↗

Small Molecule Inhibitors of the p53-MDM2Semantic proximity Read ↗

MDM2 Oncogene as a Novel Target for Human Cancer TherapySemantic proximity Read ↗

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