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

San1p, checking up on nuclear proteins.

Cell - 25 Mar 2005

Sommer Thomas, Hirsch Christian

Abstract excerpt

Cellular quality control mechanisms perform vital tasks by ensuring that the proteome reflects precisely the information encoded by the genome. In this issue of Cell, Gardner et al. (2005) report the discovery of a novel protein quality control system that resides in the nucleus. Central to this system is the E3 ligase San1p, which monitors nuclear proteins and targets aberrant species for destruction.

Read the complete abstract on PubMed

Topics

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

Share to Cell Nucleus
Share to Genome
Share to Nuclear Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proteome

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Share to Signal Transduction

Share to Ubiquitin-Protein Ligases

Source

Identifiers

PMID: 15797374
DOI: 10.1016/j.cell.2005.03.003

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

San1p, checking up on nuclear proteins.PMID 15797374Read ↗

Degradation-mediated protein quality control in the nucleus.Semantic proximity Read ↗

Hsp40/70/110 chaperones adapt nuclear protein quality control to serve cytosolic clients.Semantic proximity Read ↗

The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate.Semantic proximity Read ↗

BAG6 and RNF126 are broadly involved in protein quality control of non-native missense protein variantsSemantic proximity Read ↗

At the nucleus of the problem: nuclear proteins and disease.Semantic proximity Read ↗

The co-chaperone DNAJA2 buffers proteasomal degradation of cytosolic proteins with missense mutationsSemantic proximity Read ↗

Bioinformatics analysis identifies several intrinsically disordered human E3 ubiquitin-protein ligasesSemantic proximity Read ↗

Spatial proteomic mapping of human nuclear bodies reveals new functional insights into RNA regulationSemantic proximity Read ↗

BAG6 and RNF126 promote the degradation of cytosolic misfolded proteins that contain buried degron motifsSemantic proximity Read ↗

Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase.Semantic proximity Read ↗

Proteome Stability as a Key Factor of Genome IntegritySemantic proximity Read ↗

SON and SRRM2 form nuclear speckles in human cellsSemantic proximity Read ↗

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