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

P53 hot-spot mutants are resistant to ubiquitin-independent degradation by increased binding to NAD(P)H:quinone oxidoreductase 1.

Proceedings of the National Academy of Sciences of the United States of America - 9 Dec 2003

Asher Gad, Lotem Joseph, Tsvetkov Peter, Reiss Veronica, Sachs Leo, Shaul Yosef

Abstract excerpt

Proteasomal degradation of p53 is mediated by two alternative pathways that are either dependent or independent of both Mdm2 and ubiquitin. The ubiquitin-independent pathway is regulated by NAD(P)H: quinone oxidoreductase 1 (NQO1) that stabilizes p53. The NQO1 inhibitor dicoumarol induces ubiquitin-independent p53 degradation. We now show that, like dicoumarol, several other coumarin and flavone inhibitors of...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Cysteine Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Multienzyme Complexes

Share to NAD(P)H Dehydrogenase (Quinone)

Share to Precipitin Tests

Share to Proteasome Endopeptidase Complex

Share to Proto-Oncogene Proteins c-mdm2

Share to Ubiquitin

Source

Open in PubMed Open full text

Identifiers

PMID: 14634213
DOI: 10.1073/pnas.2436329100
PMCID: PMC299908

Genes

NQO1

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

P53 hot-spot mutants are resistant to ubiquitin-independent degradation by increased binding to NAD(P)H:quinone oxidoreductase 1.PMID 14634213Read ↗

Inhibition of the ubiquitin-proteasome system by an NQO1-activatable compound.Semantic proximity Read ↗

Natural Small Molecules as Stabilizers and Activators of Cancer-Associated NQO1 Polymorphisms.Semantic proximity Read ↗

Inhibition of the ubiquitin-proteasome system by a bioactivatable compoundSemantic proximity Read ↗

Natural (and Unnatural) Small Molecules as Pharmacological Chaperones and Inhibitors in Cancer.Semantic proximity Read ↗

20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1.Semantic proximity Read ↗

Specific regulation of BACH1 by the hotspot mutant p53R175H reveals a distinct gain-of-function mechanism.Semantic proximity Read ↗

Structural basis of the pleiotropic and specific phenotypic consequences of missense mutations in the multifunctional NAD(P)H:quinone oxidoreductase 1 and their pharmacological rescueSemantic proximity Read ↗

Site-to-site interdomain communication may mediate different loss-of-function mechanisms in a cancer-associated NQO1 polymorphism.Semantic proximity Read ↗

Small molecule restoration of wildtype structure and function of mutant p53 using a novel zinc-metallochaperone based mechanism.Semantic proximity Read ↗

Update of the NAD(P)H:quinone oxidoreductase (NQO) gene family.Semantic proximity Read ↗

Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy.Semantic proximity Read ↗

Rapid polyubiquitination and proteasomal degradation of a mutant form of NAD(P)H:quinone oxidoreductase 1.Semantic proximity Read ↗

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