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

Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins.

BMC biochemistry - 30 Jan 2008

Goh Amanda M, Walters Kylie J, Elsasser Suzanne, Verma Rati, Deshaies Raymond J, Finley Daniel, Howley Peter M

Abstract excerpt

BACKGROUND: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step in the regulation of the ubiquitin-proteasome pathway, yet the mechanisms underlying this step are not understood in detail. The Rad23 family of proteins is known to bind ubiquitinated proteins through its two ubiquitin-associated (UBA) domains, and may participate in the delivery of ubiquitinated proteins to the...

Read the complete abstract on PubMed

Topics

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

Share to Binding, Competitive
Share to DNA Repair Enzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Polyubiquitin

Share to Proteasome Endopeptidase Complex

Share to Protein Structure, Tertiary

Share to Ubiquitin

Share to Ubiquitin-Protein Ligases

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 18234089
DOI: 10.1186/1471-2091-9-4
PMCID: PMC2267792

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins.PMID 18234089Read ↗

Binding Surface Mapping of Intra- and Interdomain Interactions among hHR23B, Ubiquitin, and Polyubiquitin Binding Site 2 of S5aSemantic proximity Read ↗

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

The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain.Semantic proximity Read ↗

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

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

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

Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins.Semantic proximity Read ↗

Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathway.Semantic proximity Read ↗

Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome.Semantic proximity Read ↗

Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains.Semantic proximity Read ↗

Biochemical and Structural Analysis of the Interaction between the UBA(2) Domain of the DNA Repair Protein HHR23A and HIV-1 VprSemantic proximity Read ↗

Protein-protein interactions within an E2-RING finger complex. Implications for ubiquitin-dependent DNA damage repair.Semantic proximity Read ↗

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