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

Hsp40/70/110 chaperones adapt nuclear protein quality control to serve cytosolic clients.

The Journal of cell biology - 4 Jun 2018

Prasad Rupali, Xu Chengchao, Ng Davis T W

Abstract excerpt

Misfolded cytosolic proteins are degraded by the ubiquitin proteasome system through quality control (QC) pathways defined by E3 ubiquitin ligases and associated chaperones. Although they work together as a comprehensive system to monitor cytosolic protein folding, their respective contributions remain unclear. To bridge existing gaps, the pathways mediated by the San1 and Ubr1 E3 ligases were studied...

Read the complete abstract on PubMed

Topics

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

Share to Active Transport, Cell Nucleus
Share to Cell Nucleus
Share to Cytosol

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Nuclear Proteins

Share to Protein Folding

Share to Protein Transport

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 29653997
DOI: 10.1083/jcb.201706091
PMCID: PMC5987712

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

Hsp40/70/110 chaperones adapt nuclear protein quality control to serve cytosolic clients.PMID 29653997Read ↗

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

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

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

The Nuclear SUMO-Targeted Ubiquitin Quality Control Network Regulates the Dynamics of Cytoplasmic Stress Granules.Semantic proximity Read ↗

Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.Semantic proximity Read ↗

San1p, checking up on nuclear proteins.Semantic proximity Read ↗

Chaperone-mediated assembly of the proteasome core particle – recent developments and structural insightsSemantic proximity Read ↗

An Hsp90 co-chaperone links protein folding and degradation and is part of a conserved protein quality control.Semantic proximity Read ↗

Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases.Semantic proximity Read ↗

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

Protein quality control: chaperones culling corrupt conformations.Semantic proximity Read ↗

The Cdc48 Complex Alleviates the Cytotoxicity of Misfolded Proteins by Regulating Ubiquitin Homeostasis.Semantic proximity Read ↗

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