Evidence map›Paper›PMID 11157756›Full record

ArticleThe EMBO journal2001

Modulation of Drosophila heat shock transcription factor activity by the molecular chaperone DROJ1.

G Marchler, C Wu

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 85 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

G MarchlerLaboratory of Molecular Cell Biology, National Cancer Institute, National Institutes of Health, Building 37, Room 5E-26, Bethesda, MD 20892, USA.
C Wu
National Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock transcription factors (HSFs) play important roles in the cellular response to physiological stress signals. To examine the control of HSF activity, we undertook a yeast two-hybrid screen for proteins interacting with Drosophila HSF. DROJ1, the fly counterpart of the human heat shock protein HSP40/HDJ1, was identified as the dominant interacting protein (15 independent isolates from 58 candidates). Overexpression of DROJ1 in Drosophila SL2 cells delays the onset of the heat shock response. Moreover, RNA interference involving transfection of SL2 cells with double-stranded droj1 RNA depletes the endogenous level of DROJ1 protein, leading to constitutive activation of endogenous heat shock genes. The induction level, modest when DROJ1 was depleted alone, reached maximal levels when DROJ1 and HSP70/HSC70, or DROJ1 and HSP90, were depleted concurrently. Chaperone co-depletion was also correlated with strong induction of the DNA binding activity of HSF. Our findings support a model in which synergistic interactions between DROJ1 and the HSP70/HSC70 and HSP90 chaperones modulate HSF activity by feedback repression.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCell NucleusCytoplasmDrosophilaDrosophila ProteinsHeat-Shock ProteinsHeat-Shock ResponseHSP40 Heat-Shock ProteinsHumansInsect ProteinsMolecular ChaperonesMolecular Sequence DataRecombinant Fusion ProteinsSequence Homology, Amino AcidDnaJ-1 protein, DrosophilaDNAJB1 protein, humanDrosophila ProteinsHeat-Shock ProteinsHSP40 Heat-Shock ProteinsInsect ProteinsMolecular ChaperonesRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID11157756
PMCPMC133474
OpenAlexW2051286072

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.