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Article

20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1.

Molecular cell - 4 Mar 2005

Asher Gad, Bercovich Zippi, Tsvetkov Peter, Shaul Yosef, Kahana Chaim

Abstract excerpt

Ornithine decarboxylase (ODC), a key enzyme in the biosynthesis of polyamines, is a very labile protein. ODC is a homodimeric enzyme that undergoes ubiquitin-independent proteasomal degradation via direct interaction with antizyme, a polyamine-induced protein. Binding of antizyme promotes the dissociation of ODC homodimers and marks ODC for degradation by the 26S proteasomes. We describe here an alternative...

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Share to Dimerization
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to NAD(P)H Dehydrogenase (Quinone)

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Source

Identifiers

PMID: 15749015
DOI: 10.1016/j.molcel.2005.01.020

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.

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