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

Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome.

Physiological genomics - 10 Oct 2001

Cagney G, Uetz P, Fields S

Abstract excerpt

A two-hybrid screen against an activation domain array of Saccharomyces cerevisiae proteins was carried out for 31 yeast proteasome proteins. Fifty-five putative interactions were identified: 21 between components of the proteasome complex and 34 between proteasome proteins and other proteins. Many of these latter interactions involved either proteins of the ubiquitin pathway, cell cycle proteins, protein kinases...

Read the complete abstract on PubMed

Topics

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

Share to Peptide Hydrolases
Share to Proteasome Endopeptidase Complex
Share to Protein Subunits

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Gene Library

Share to Macromolecular Substances

Share to Two-Hybrid System Techniques

Share to Ubiquitin

Source

Identifiers

PMID: 11595789
DOI: 10.1152/physiolgenomics.2001.7.1.27

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

Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome.PMID 11595789Read ↗

Biogenesis, structure and function of the yeast 20S proteasome.Semantic proximity Read ↗

Species-specific protein-protein interactions govern the humanization of the 20S proteasome in yeastSemantic proximity Read ↗

Proteasome subunit α1 overexpression preferentially drives canonical proteasome biogenesis and enhances stress tolerance in yeastSemantic proximity Read ↗

A multimeric assembly factor controls the formation of alternative 20S proteasomes.Semantic proximity Read ↗

Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae.Semantic proximity Read ↗

Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes.Semantic proximity Read ↗

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1.Semantic proximity Read ↗

A Split-Ubiquitin Based Strategy Selecting for Protein Complex-Interfering Mutations.Semantic proximity Read ↗

Loss of a 20S proteasome activator in Saccharomyces cerevisiae downregulates genes important for genomic integrity, increases DNA damage, and selectively sensitizes cells to agents with diverse mechanisms of action.Semantic proximity Read ↗

A genetic suppressor of two dominant temperature-sensitive lethal proteasome mutants of Drosophila melanogaster is itself a mutated proteasome subunit gene.Semantic proximity Read ↗

Identification of genes affecting the toxicity of anti-cancer drug bortezomib by genome-wide screening in S. pombe.Semantic proximity Read ↗

Probing the effects of double mutations on the versatile protein ubiquitin in Saccharomyces cerevisiae.Semantic proximity Read ↗

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