Evidence map›Paper›PMID 28487364›Full record

ArticleThe Journal of biological chemistry2017

Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1.

Michelle Heirbaut, Frederik Lermyte, Esther M Martin, Steven Beelen, Frank Sobott, Sergei V Strelkov, Stephen D Weeks

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 26 citations in OpenAlex.

  1. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Medicina (Kaunas, Lithuania) · 2023
    Article
  7. Article
  8. Heat shock proteins and metal ions - Reaction or interaction?Computational and structural biotechnology journal · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Mutations in HspB1 and hereditary neuropathies.Cell stress & chaperones · 2020
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

7 authors at 3 institutions in 2 countries.

Michelle HeirbautFrom the Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, 3000 Leuven, Belgium.
Frederik Lermytethe Biomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, 2020 Antwerp, Belgium, and.
Esther M Martinthe Biomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, 2020 Antwerp, Belgium, and.
Steven BeelenFrom the Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, 3000 Leuven, Belgium.
Frank Sobottthe Biomolecular and Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, 2020 Antwerp, Belgium, and.
Sergei V StrelkovFrom the Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, 3000 Leuven, Belgium, sergei.strelkov@kuleuven.be.ORCID 0000-0001-7189-4652
Stephen D WeeksFrom the Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, 3000 Leuven, Belgium, stephen.weeks@kuleuven.be.ORCID 0000-0002-1360-0852
KU Leuven · BEUniversity of Antwerp · BEUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small heat-shock proteins (sHSPs) are a conserved group of molecular chaperones with important roles in cellular proteostasis. Although sHSPs are characterized by their small monomeric weight, they typically assemble into large polydisperse oligomers that vary in both size and shape but are principally composed of dimeric building blocks. These assemblies can include different sHSP orthologues, creating additional complexity that may affect chaperone activity. However, the structural and functional properties of such hetero-oligomers are poorly understood. We became interested in hetero-oligomer formation between human heat-shock protein family B (small) member 1 (HSPB1) and HSPB6, which are both highly expressed in skeletal muscle. When mixed

Indexed as

Models, MolecularAmino Acid MotifsAmino Acid SubstitutionConserved SequenceCross-Linking ReagentsDimerizationGene DeletionHeat-Shock ProteinsHSP20 Heat-Shock ProteinsHSP27 Heat-Shock ProteinsHumansMolecular ChaperonesMutagenesis, Site-DirectedNitrogen IsotopesPeptide FragmentsPoint MutationCross-Linking ReagentsHeat-Shock ProteinsHSP20 Heat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB1 protein, humanHSPB6 protein, humanMolecular ChaperonesNitrogen IsotopesPeptide FragmentsRecombinant Fusion ProteinsRecombinant ProteinsSulfhydryl Reagentschaperonecysteine-mediated cross-linkingHsp20Hsp27mass spectrometry (MS)site-directed mutagenesissmall heat-shock protein (sHsp)

Identifiers

PMID28487364
PMCPMC5473246
OpenAlexW2613815235

What OpenQuestion holds

Textmetadata
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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.