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 chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.

The Journal of biological chemistry - 24 Jun 2005

Cashikar Anil G, Duennwald Martin, Lindquist Susan L

Abstract excerpt

Cellular protein folding is challenged by environmental stress and aging, which lead to aberrant protein conformations and aggregation. One way to antagonize the detrimental consequences of protein misfolding is to reactivate vital proteins from aggregates. In the yeast Saccharomyces cerevisiae, Hsp104 facilitates disaggregation and reactivates aggregated proteins with assistance from Hsp70 (Ssa1) and Hsp40...

Read the complete abstract on PubMed

Topics

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

Share to Heat-Shock Proteins
Share to Heat-Shock Response

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Chaperones

Share to Mutation

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Share to Sequence Deletion

Share to Solubility

Source

Open in PubMed Open full text

Identifiers

PMID: 15845535
DOI: 10.1074/jbc.M502854200
PMCID: PMC1391974

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.PMID 15845535Read ↗

Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Semantic proximity Read ↗

Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.Semantic proximity Read ↗

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

A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.Semantic proximity Read ↗

Structure and function of the molecular chaperone Hsp104 from yeast.Semantic proximity Read ↗

Specific protein homeostatic functions of small heat‐shock proteins increase lifespanSemantic proximity Read ↗

Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae.Semantic proximity Read ↗

Sub-stoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of a yeast prion proteinSemantic proximity Read ↗

Disaggregating chaperones: an unfolding story.Semantic proximity Read ↗

Redox regulation of yeast Hsp70 modulates protein quality control while directly triggering an Hsf1-dependent cytoprotective responseSemantic proximity Read ↗

Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunitiesSemantic proximity Read ↗

Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.Semantic proximity Read ↗

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