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

Purification and properties of Hsp104 from yeast.

Methods in enzymology - 1 Jan 1998

Schirmer E C, Lindquist S

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Cloning, Molecular
Share to Fungal Proteins
Share to Heat-Shock Proteins

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

Share to Plasmids

Share to Protein Conformation

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 9534180
DOI: 10.1016/s0076-6879(98)90036-2

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

Purification and properties of Hsp104 from yeast.PMID 9534180Read ↗

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

Hsp104 is required for tolerance to many forms of stress.Semantic proximity Read ↗

The role of Hsp104 in stress tolerance and [PSI+] propagation in Saccharomyces cerevisiae.Semantic proximity Read ↗

HSP104 required for induced thermotolerance.Semantic proximity Read ↗

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

Suppression of aggregate and amyloid formation by a novel intrinsically disordered region in metazoan Hsp110 chaperonesSemantic proximity Read ↗

Hsp104 as a key modulator of prion-mediated oxidative stress in Saccharomyces cerevisiae.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 ↗

Expression of a putative ATPase suppresses the growth defect of a yeast potassium transport mutant: identification of a mammalian member of the Clp/HSP104 family.Semantic proximity Read ↗

Processing of proteins by the molecular chaperone Hsp104.Semantic proximity Read ↗

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation.Semantic proximity Read ↗

Protein disaggregation mediated by heat-shock protein Hsp104.Semantic proximity Read ↗

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