Evidence map›Paper›PMID 15497499›Full record

ReviewCell stress & chaperones2004

On mechanisms that control heat shock transcription factor activity in metazoan cells.

Richard Voellmy

Open access · greenAbstract readReview
In one paragraph

Review in Cell stress & chaperones, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
7.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

114 citing papers in PubMed, 278 citations in OpenAlex.

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54 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Richard VoellmyDepartment of Biochemistry and Molecular Biology, University of Miami, Gautier Building, Room 403, 1011 NW 15th Street, Miami, FL 33136, USA. rvoellmy@molbio.med.miami.edu
University of Miami · US

Funding

NIGMS NIH HHS GM31125
6 · The paper itself

Abstract

Heat shock factor Hsf in nonvertebrate animals and homologous heat shock factor Hsf1 in vertebrate animals are key transcriptional regulators of the stress protein response. Hsf/Hsf1 is constitutively present in cells but is, typically, only active during periods during which cells are experiencing a physical or chemical proteotoxic stress. It has become increasingly clear that regulation of Hsf/Hsf1 activity occurs at multiple levels: the oligomeric status of Hsf/Hsf1, its DNA-binding ability, posttranslational modification, transcriptional competence, nuclear/ subnuclear localization, as well as its interactions with regulatory cofactors or other transcription factors all appear to be carefully controlled. This review emphasizes work reported over the past several years suggesting that regulation at several of these levels is mediated by repressive interactions of Hsp90-containing multichaperone complexes and/or individual chaperones and Hsf/Hsf1.

Indexed as

Transcription, GeneticAmino Acid SequenceAnimalsBase SequenceDNA-Binding ProteinsGene Expression RegulationHeat Shock Transcription FactorsHSP90 Heat-Shock ProteinsHumansModels, BiologicalProtein Processing, Post-TranslationalTranscription FactorsDNA-Binding ProteinsHeat Shock Transcription FactorsHSF1 protein, humanHSP90 Heat-Shock ProteinsTranscription Factors

Identifiers

PMID15497499
PMCPMC1065292
OpenAlexW2118292263

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.