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

A synthetic defect in protein degradation caused by loss of Ufd4 and Rad23.

Biochemical and biophysical research communications - 10 Mar 2006

Ju Donghong, Xie Youming

Abstract excerpt

The UFD (ubiquitin fusion degradation) pathway is responsible for multiubiquitination of the fusion proteins that bear a "non-removable" N-terminal ubiquitin moiety. Previous reports have shown that the UFD pathway is conserved from yeast to human. The essential elements of the UFD pathway have a...

Read the complete abstract on PubMed

Topics

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

Share to DNA Repair
Share to Dose-Response Relationship, Drug
Share to Gene Deletion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Fungal

Share to Saccharomyces cerevisiae Proteins

Share to Two-Hybrid System Techniques

Share to Ubiquitin

Share to Ubiquitin-Protein Ligases

Source

Identifiers

PMID: 16430867
DOI: 10.1016/j.bbrc.2006.01.013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16430867-2026-09-02.2. 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

A synthetic defect in protein degradation caused by loss of Ufd4 and Rad23.PMID 16430867Read ↗

A proteolytic pathway that recognizes ubiquitin as a degradation signal.Semantic proximity Read ↗

Concerted action of the ubiquitin-fusion degradation protein 1 (Ufd1) and Sumo-targeted ubiquitin ligases (STUbLs) in the DNA-damage response.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 ↗

An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation.Semantic proximity Read ↗

The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway.Semantic proximity Read ↗

The structure and function of deubiquitinases: lessons from budding yeastSemantic proximity Read ↗

Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.Semantic proximity Read ↗

Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding.Semantic proximity Read ↗

E3 ligases: a ubiquitous link between DNA repair, DNA replication and human diseaseSemantic proximity Read ↗

A guide to UFMylation, an emerging posttranslational modificationSemantic proximity Read ↗

Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae.Semantic proximity Read ↗

Inactivation of the VID27 gene prevents suppression of the doa4 degradation defect in doa4Δ did3Δ double mutant.Semantic proximity Read ↗

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