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

Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway.

Nucleic acids research - 1 Jan 2004

Ortolan Tatiana G, Chen Li, Tongaonkar Prasad, Madura Kiran

Abstract excerpt

Rad23 protein interacts with the nucleotide excision-repair (NER) factor Rad4, and the dimer can bind damaged DNA. Rad23 also binds ubiquitinated proteins and promotes their degradation by the proteasome. Rad23/proteasome interaction is required for efficient NER, although the specific role of th...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to DNA Repair
Share to Proteasome Endopeptidase Complex

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Structure, Tertiary

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Share to Ubiquitin-Conjugating Enzymes

Share to Ultraviolet Rays

Source

Open in PubMed Open full text

Identifiers

PMID: 15601997
DOI: 10.1093/nar/gkh987
PMCID: PMC545455

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-15601997-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway.PMID 15601997Read ↗

The moonlighting of RAD23 in DNA repair and protein degradation.Semantic proximity Read ↗

Roles of Rad23 protein in yeast nucleotide excision repair.Semantic proximity Read ↗

Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.Semantic proximity Read ↗

The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair.Semantic proximity Read ↗

Investigating the importance of proteasome-interaction for Rad23 function.Semantic proximity Read ↗

Proteolysis of a nucleotide excision repair protein by the 26 S proteasome.Semantic proximity Read ↗

Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain.Semantic proximity Read ↗

The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis.Semantic proximity Read ↗

The 26S proteasome negatively regulates the level of overall genomic nucleotide excision repair.Semantic proximity Read ↗

The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stabilitySemantic proximity Read ↗

Rad23 promotes the targeting of proteolytic substrates to the proteasome.Semantic proximity Read ↗

The deubiquitylating enzyme Ubp12 regulates Rad23-dependent proteasomal degradation.Semantic proximity Read ↗

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