Evidence map›Paper›PMID 35948542›Full record

ArticleNature communications2022

Identification of a HTT-specific binding motif in DNAJB1 essential for suppression and disaggregation of HTT.

S M Ayala Mariscal, M L Pigazzini, Y Richter, M Özel, I L Grothaus, J Protze, K Ziege, M Kulke, M ElBediwi, J V Vermaas and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Chaperone-mediated remodelling of mutant huntingtin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Review
  3. Article
  4. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. DnaJB1 chaperone inhibits tau aggregation by recognizing its N-terminus.bioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Factors affecting protein recovery during Hsp40 affinity profiling.Analytical and bioanalytical chemistry · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. 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

14 authors at 3 institutions in 2 countries.

S M Ayala MariscalLeibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP), Berlin, Germany.
M L PigazziniLeibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP), Berlin, Germany.
Y RichterDepartment of Cell Biology, University of Bremen, Bremen, Germany.
M ÖzelDepartment of Cell Biology, University of Bremen, Bremen, Germany.
I L GrothausHybrid Materials Interfaces Group, Faculty of Production Engineering and Bremen Center for Computational Materials Science, University of Bremen, Bremen, Germany.ORCID 0000-0002-0441-3860
J ProtzeLeibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP), Berlin, Germany.ORCID 0000-0002-1506-9831
K ZiegeLeibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP), Berlin, Germany.
M KulkeMSU-DOE-Plant Research Laboratory, Michigan State University, 612 Wilson Road, East Lansing, MI, 48824, USA.ORCID 0000-0002-2689-2428
M ElBediwiDepartment of Cell Biology, University of Bremen, Bremen, Germany.ORCID 0000-0001-9086-5996
J V VermaasMSU-DOE-Plant Research Laboratory, Michigan State University, 612 Wilson Road, East Lansing, MI, 48824, USA.ORCID 0000-0003-3139-6469
L Colombi CiacchiHybrid Materials Interfaces Group, Faculty of Production Engineering and Bremen Center for Computational Materials Science, University of Bremen, Bremen, Germany.
S KöppenHybrid Materials Interfaces Group, Faculty of Production Engineering and Bremen Center for Computational Materials Science, University of Bremen, Bremen, Germany.ORCID 0000-0001-7626-9936
F LiuLeibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP), Berlin, Germany.ORCID 0000-0002-2358-549X
J KirsteinLeibniz Research Institute for Molecular Pharmacology (FMP) im Forschungsverbund Berlin e.V. (FMP), Berlin, Germany. kirstein@uni-bremen.de.ORCID 0000-0003-4990-2497
University of Bremen · DEForschungsverbund Berlin · DEMichigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Huntington's disease is a neurodegenerative disease caused by an expanded polyQ stretch within Huntingtin (HTT) that renders the protein aggregation-prone, ultimately resulting in the formation of amyloid fibrils. A trimeric chaperone complex composed of Hsc70, DNAJB1 and Apg2 can suppress and reverse the aggregation of HTTExon1Q

Indexed as

Huntington DiseaseNeurodegenerative DiseasesAmyloidHEK293 CellsHSP40 Heat-Shock ProteinsHumansHuntingtin ProteinMolecular ChaperonesProtein AggregatesAmyloidDNAJB1 protein, humanHSP40 Heat-Shock ProteinsHTT protein, humanHuntingtin ProteinMolecular ChaperonesProtein Aggregates

Identifiers

PMID35948542
PMCPMC9365803
OpenAlexW4290989221

What OpenQuestion holds

Textmetadata
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.