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

Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion.

Prion - 1 Jan 2000

Bardill J Patrick, Dulle Jennifer E, Fisher Jonathan R, True Heather L

Abstract excerpt

The formation and maintenance of prions in the yeast Saccharomyces cerevisiae is highly regulated by the cellular chaperone machinery. The most important player in this regulation is Hsp104p, which is required for the maintenance of all known prions. The requirements for other chaperones, such as...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Heat-Shock Proteins
Share to Hot Temperature

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP40 Heat-Shock Proteins

Share to Hydrolysis

Share to Molecular Chaperones

Share to Prions

Share to Recombinant Fusion Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19770577
DOI: 10.4161/pri.3.3.9662
PMCID: PMC2802780

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19770577-2026-09-02.2. 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

Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion.PMID 19770577Read ↗

Importance of the Hsp70 ATPase domain in yeast prion propagation.Semantic proximity Read ↗

Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity.Semantic proximity Read ↗

[PSI(+)] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast.Semantic proximity Read ↗

A systematic evaluation of the function of the protein-remodeling factor Hsp104 in [PSI+] prion propagation in S. cerevisiae by comprehensive chromosomal mutations.Semantic proximity Read ↗

Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding.Semantic proximity Read ↗

Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+].Semantic proximity Read ↗

Biochemical and genetic methods for characterization of [PIN+] prions in yeast.Semantic proximity Read ↗

Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.Semantic proximity Read ↗

Chaperone-dependent amyloid assembly protects cells from prion toxicity.Semantic proximity Read ↗

N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression.Semantic proximity Read ↗

Selfish prion of Rnq1 mutant in yeast.Semantic proximity Read ↗

Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 in Saccharomyces cerevisiae.Semantic proximity Read ↗

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