Evidence map›Paper›PMID 16572728›Full record

ArticleCell stress & chaperones2006

Heat shock protein 70 binds its own messenger ribonucleic acid as part of a gene expression self-limiting mechanism.

Karthik Balakrishnan, Antonio De Maio

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

13 citing papers in PubMed, 33 citations in OpenAlex.

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  11. Magnetic field-controlled gene expression in encapsulated cells.Journal of controlled release : official journal of the Controlled Release Society · 2012
    Article
  12. Effects of simulated weightlessness on liver Hsp70 and Hsp70mRNA expression in rats.International journal of clinical and experimental medicine · 2010
    Article
  13. Article
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

2 authors at 2 institutions in 1 country.

Karthik BalakrishnanDepartment of Surgery, Division of Pediatric Surgery, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Antonio De Maio
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

Mechanisms of cytoprotection induced by stress proteinsR01GM050878 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DE MAIO, ANTONIO · 1994 to 2008
$2.3M
NIGMS NIH HHS GM 50878NIGMS NIH HHS R01 GM050878
6 · The paper itself

Abstract

Expression of heat shock proteins is a cellular response to a variety of stressors. HSP70, the major stress-induced heat shock protein, is involved in repair and protection after the insult. However, the prolonged presence of this protein is detrimental. Consequently, Hsp70 expression must be tightly regulated. We have previously shown an increase in the degradation of Hsp70 messenger ribonucleic acid (mRNA) paralleling the accumulation of HSP70. Incubation of cells with transcriptional and translational inhibitors after heat shock resulted in a significant reduction in Hsp70 mRNA degradation. These observations suggest that newly synthesized, stress-induced factors might be involved in the decay of Hsp70 mRNA. We found that HSP70 binds directly to Hsp70 mRNA, as demonstrated by immunoprecipitation. This observation was confirmed by RNA gel-shift assays. These results are evidence for a novel and likely direct interaction between HSP70 and Hsp70 mRNA in cells after stress. This interaction may be part of a self-limiting mechanism to reduce HSP70 production, thus avoiding potential toxic effects of this protein in the absence of stress.

Indexed as

Gene Expression RegulationHeat-Shock ResponseBlotting, NorthernCarcinoma, HepatocellularCell Line, TumorCycloheximideDactinomycinElectrophoretic Mobility Shift AssayHeLa CellsHSP70 Heat-Shock ProteinsHumansLiver NeoplasmsPrecipitin TestsProtein Synthesis InhibitorsPuromycinRNA, MessengerCycloheximideDactinomycinHSP70 Heat-Shock ProteinsProtein Synthesis InhibitorsPuromycinRNA, Messenger

Identifiers

PMID16572728
PMCPMC1400612
OpenAlexW2114506767

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.