Evidence map›Paper›PMID 33288678›Full record

ArticleThe Journal of biological chemistry

Single-molecule fluorescence-based approach reveals novel mechanistic insights into human small heat shock protein chaperone function.

Caitlin L Johnston, Nicholas R Marzano, Bishnu P Paudel, George Wright, Justin L P Benesch, Antoine M van Oijen, Heath Ecroyd

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

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  9. Article
  10. Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches.Computational and structural biotechnology journal · 2021
    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

7 authors at 2 institutions in 2 countries.

Caitlin L JohnstonMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, New South Wales, Australia; Illawarra Health & Medical Research Institute, Wollongong, New South Wales, Australia.
Nicholas R MarzanoMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, New South Wales, Australia; Illawarra Health & Medical Research Institute, Wollongong, New South Wales, Australia.
Bishnu P PaudelMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, New South Wales, Australia; Illawarra Health & Medical Research Institute, Wollongong, New South Wales, Australia.
George WrightDepartment of Chemistry, Physical and Theoretical Chemistry, University of Oxford, Oxford, UK.
Justin L P BeneschDepartment of Chemistry, Physical and Theoretical Chemistry, University of Oxford, Oxford, UK.
Antoine M van OijenMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, New South Wales, Australia; Illawarra Health & Medical Research Institute, Wollongong, New South Wales, Australia. Electronic address: vanoijen@uow.edu.au.
Heath EcroydMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, New South Wales, Australia; Illawarra Health & Medical Research Institute, Wollongong, New South Wales, Australia. Electronic address: heathe@uow.edu.au.
University of Wollongong · AUUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small heat shock proteins (sHsps) are a family of ubiquitous intracellular molecular chaperones; some sHsp family members are upregulated under stress conditions and play a vital role in protein homeostasis (proteostasis). It is commonly accepted that these chaperones work by trapping misfolded proteins to prevent their aggregation; however, fundamental questions regarding the molecular mechanism by which sHsps interact with misfolded proteins remain unanswered. The dynamic and polydisperse nature of sHsp oligomers has made studying them challenging using traditional biochemical approaches. Therefore, we have utilized a single-molecule fluorescence-based approach to observe the chaperone action of human alphaB-crystallin (αBc, HSPB5). Using this approach we have, for the first time, determined the stoichiometries of complexes formed between αBc and a model client protein, chloride intracellular channel 1. By examining the dispersity and stoichiometries of these complexes over time, and in response to different concentrations of αBc, we have uncovered unique and important insights into a two-step mechanism by which αBc interacts with misfolded client proteins to prevent their aggregation.

Indexed as

alpha-Crystallin B ChainBinding SitesCarbocyaninesChloride ChannelsCloning, MolecularEscherichia coliFluorescence Resonance Energy TransferFluorescent DyesGene ExpressionGenetic VectorsHumansProtein BindingProtein FoldingRecombinant ProteinsRhodaminesSingle Molecule ImagingAlexa Fluor 555Alexa Fluor 647alpha-Crystallin B ChainCarbocyaninesChloride ChannelsCLIC1 protein, humanCRYAB protein, humanFluorescent DyesRecombinant ProteinsRhodaminesSolutionsSulfonic AcidsalphaB-crystallinchloride intracellular channel 1mass photometrymolecular chaperoneoligomersprotein aggregationprotein complexestotal internal reflection fluorescence microscopy

Identifiers

PMID33288678
PMCPMC7921601
OpenAlexW3111756506

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.