Evidence map›Paper›PMID 23349863›Full record

ArticlePloS one2013

The SIRT1 modulators AROS and DBC1 regulate HSF1 activity and the heat shock response.

Rachel Raynes, Kathleen M Pombier, Kevin Nguyen, Jessica Brunquell, Jamie E Mendez, Sandy D Westerheide

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.5field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 53 citations in OpenAlex.

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  13. Heat Shock Proteins and HSF1 in Cancer.Frontiers in oncology · 2022
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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

6 authors at 1 institution in 1 country.

Rachel RaynesThe Department of Cell Biology, Microbiology and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, Florida, USA.
Kathleen M Pombier
Kevin Nguyen
Jessica Brunquell
Jamie E Mendez
Sandy D Westerheide
University of South Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The heat shock response, the cellular response to protein damaging stress, is critical in maintaining proteostasis. The heat shock response is regulated by the transcription factor HSF1, which is activated upon heat shock and other stresses to induce the expression of molecular chaperones. SIRT1 has previously been shown to activate HSF1 by deacetylating it, leading to increased DNA binding ability. We have investigated how the heat shock response may be controlled by factors influencing SIRT1 activity. We found that heat shock results in an increase in the cellular NAD(+)/NADH ratio and an increase in recruitment of SIRT1 to the hsp70 promoter. Furthermore, we found that the SIRT1 modulators AROS and DBC1 have an impact on hsp70 transcription, HSF1 acetylation status, and HSF1 recruitment to the hsp70 promoter. Therefore, AROS and DBC1 are now two new targets available for therapeutic regulation of the heat shock response.

Indexed as

AcetylationCell Cycle ProteinsDNA-Binding ProteinsHeat-Shock ResponseHeat Shock Transcription FactorsHEK293 CellsHeLa CellsHot TemperatureHSP70 Heat-Shock ProteinsHumansNADNerve Tissue ProteinsNuclear ProteinsPromoter Regions, GeneticSirtuin 1Transcription FactorsBRINP1 protein, humanCell Cycle ProteinsDNA-Binding ProteinsHeat Shock Transcription FactorsHSF1 protein, humanHSP70 Heat-Shock ProteinsNADNerve Tissue ProteinsNuclear ProteinsRPS19BP1 protein, humanSIRT1 protein, humanSirtuin 1Transcription FactorsTumor Suppressor Proteins

Identifiers

PMID23349863
PMCPMC3548779
OpenAlexW1989635548

What OpenQuestion holds

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LicenceCC BY
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.