Evidence map›Paper›PMID 32424160›Full record

ArticleScientific reports2020

Co-chaperones DNAJA1 and DNAJB6 are critical for regulation of polyglutamine aggregation.

Claudio Rodríguez-González, Shiying Lin, Sertan Arkan, Christian Hansen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. DNAJB6: A guardian against neurodegeneration.Neural regeneration research · 2026
    Article
  4. Article
  5. Article
  6. Review
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  8. Review
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  14. Evidence for ~12-h ultradian gene programs in humans.Npj biological timing and sleep · 2024
    Article
  15. DnaJs are enriched in tau regulators.International journal of biological macromolecules · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The roles of HSP40/DNAJ protein family in neurodegenerative diseases.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2022
    Review
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

4 authors at 1 institution in 1 country.

Claudio Rodríguez-GonzálezMolecular Neurobiology, Department of Experimental Medical Science, Lund University, BMC B11, 22184, Lund, Sweden.
Shiying LinMolecular Neurobiology, Department of Experimental Medical Science, Lund University, BMC B11, 22184, Lund, Sweden.
Sertan ArkanMolecular Neurobiology, Department of Experimental Medical Science, Lund University, BMC B11, 22184, Lund, Sweden.
Christian HansenMolecular Neurobiology, Department of Experimental Medical Science, Lund University, BMC B11, 22184, Lund, Sweden. christian.hansen@med.lu.se.
Lund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Huntington's disease (HD) is caused by CAG repeat expansion in the huntingtin gene. The expanded polyglutamine (polyQ) repeat of the encoded protein leads to protein misfolding and aggregation, resulting in increased neuronal cell death. DNAJ co-chaperones play a crucial role in transferring misfolded/unfolded proteins to HSP70 chaperones, which play an essential role for protein folding. Here, we investigated the effect of knock out (KO) of three individual DNAJ genes in HEK293 cells expressing polyglutamine74exon1 huntingtin (polyQ74htt). Flourescence microscopy analysis revealed that KO of DNAJB6 resulted in a 5-fold increase in polyQ74htt aggregation and that DNAJA1 KO resulted in a 4-fold decrease of polyQ74htt aggregation. KO of DNAJB1 did not change the propensity of polyQ74htt to aggregate in cells. These findings where confirmed both by fluorescence microscopy analysis and filter trap assay (FTA). DNAJB6 KO cells displayed an increased rate of cell death as assessed by trypan blue exclusion and propidium iodide (PI) uptake assays. These results demonstrate that the DNAJ proteins DNAJA1 and DNAJB6 can modulate polyQ aggregation in opposite manners, and thus that fine-tuning the cellular levels of DNAJ proteins is critical for suppression of polyQ aggregation and cell survival.

Indexed as

HEK293 CellsHSP40 Heat-Shock ProteinsHumansHuntingtin ProteinHuntington DiseaseMolecular ChaperonesNerve Tissue ProteinsPeptidesProtein AggregatesDNAJA1 protein, humanDNAJB6 protein, humanHSP40 Heat-Shock ProteinsHTT protein, humanHuntingtin ProteinMolecular ChaperonesNerve Tissue ProteinsPeptidespolyglutamineProtein Aggregates

Identifiers

PMID32424160
PMCPMC7235262
OpenAlexW3025700325

What OpenQuestion holds

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Registered trials

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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.