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

Interaction of p53 with MDM2 is independent of E6 and does not mediate wild type transformation suppressor function.

Oncogene - 1 Sept 1994

Marston N J, Crook T, Vousden K H

Abstract excerpt

Using a new series of p53 mutants targeting the conserved regions we have analysed the relationship of various activities of the protein. Mdm-2 and human papillomavirus (HPV) E6, two proteins which interact with and abrogate p53 function, were shown to bind independently. Deletion of the conserved regions of the protein in which most of the naturally occurring mutations are found (boxes II-V) abrogated...

Read the complete abstract on PubMed

Topics

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

Share to Cell Transformation, Neoplastic
Share to Mutation
Share to Neoplasm Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Nuclear Proteins

Share to Phosphorylation

Share to Proto-Oncogene Proteins

Share to Repressor Proteins

Share to Tumor Suppressor Protein p53

Source

Identifiers

PMID: 8058335

Genes

MDM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interaction of p53 with MDM2 is independent of E6 and does not mediate wild type transformation suppressor function.PMID 8058335Read ↗

The ability of human papillomavirus E6 proteins to target p53 for degradation in vivo correlates with their ability to abrogate actinomycin D-induced growth arrestSemantic proximity Read ↗

Complete switch from Mdm2 to human papillomavirus E6-mediated degradation of p53 in cervical cancer cellsSemantic proximity Read ↗

Interaction of HPV E6 with p53 and associated proteins.Semantic proximity Read ↗

Sensitivity of p53 lysine mutants to ubiquitin-directed degradation targeted by human papillomavirus E6.Semantic proximity Read ↗

Functional inactivation of p73, a homolog of p53 tumor suppressor protein, by human papillomavirus E6 proteins.Semantic proximity Read ↗

Human papillomavirus E6 proteins bind p53 in vivo and abrogate p53‐mediated repression of transcription.Semantic proximity Read ↗

Inhibition of serum- and calcium-induced terminal differentiation of human keratinocytes by HPV 16 E6: study of the association with p53 degradation, inhibition of p53 transactivation, and binding to E6BP.Semantic proximity Read ↗

Interaction of the human papillomavirus type 16 E6 oncoprotein with wild-type and mutant human p53 proteinsSemantic proximity Read ↗

High-risk human papillomavirus E6 protein has two distinct binding sites within p53, of which only one determines degradationSemantic proximity Read ↗

Mutant p53 can substitute for human papillomavirus type 16 E6 in immortalization of human keratinocytes but does not have E6-associated trans-activation or transforming activity.Semantic proximity Read ↗

Induction of apoptosis by p53 is independent of its oligomeric state and can be abolished by HPV-18 E6 through ubiquitin mediated degradation.Semantic proximity Read ↗

Inhibition of Serum- and Calcium-Induced Differentiation of Human Keratinocytes by HPV16 E6 Oncoprotein: Role of p53 InactivationSemantic proximity Read ↗

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