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

Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation.

Current biology : CB - 1 Mar 1995

Vogel J L, Parsell D A, Lindquist S

Abstract excerpt

BACKGROUND: The heat-shock protein Hsp104 plays a crucial role in the survival of cells exposed to high temperatures and other severe stresses, but its specific functions and the biological pathways on which it operates have been unclear. Indeed, very little is known about the specific cellular p...

Topics

Fungal Proteins
Gene Expression
Genotype
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
Hot Temperature
Kinetics
Mutation
RNA Splicing
RNA, Messenger
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Species Specificity

Source

Identifiers

PMID: 7780741
DOI: 10.1016/s0960-9822(95)00061-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7780741-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation.PMID 7780741Read ↗

Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae.Semantic proximity Read ↗

Reassembly and protection of small nuclear ribonucleoprotein particles by heat shock proteins in yeast cells.Semantic proximity Read ↗

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

HSP104 required for induced thermotolerance.Semantic proximity Read ↗

Requirements for chromatin reassembly during transcriptional downregulation of a heat shock gene in Saccharomyces cerevisiae.Semantic proximity Read ↗

Upregulation of the Hsp104 chaperone at physiological temperature during recovery from thermal insult.Semantic proximity Read ↗

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

Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation.Semantic proximity Read ↗

Heat-shock protein 104 expression is sufficient for thermotolerance in yeast.Semantic proximity Read ↗

Regulation of mRNA export in response to stress in Saccharomyces cerevisiae.Semantic proximity Read ↗

Nucleocytoplasmic trafficking of the molecular chaperone Hsp104 in unstressed and heat-shocked cells.Semantic proximity Read ↗

Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region.Semantic proximity Read ↗

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