Evidence map›Paper›PMID 37480427›Full record

ArticleJournal of muscle research and cell motility2023

Zebrafish as a model for cardiac disease; Cryo-EM structure of native cardiac thin filaments from Danio Rerio.

Marston Bradshaw, John M Squire, Edward Morris, Georgia Atkinson, Rebecca Richardson, Jon Lees, Massimo Caputo, Giulia M Bigotti, Danielle M Paul

Open access · hybridAbstract read
In one paragraph

Article in Journal of muscle research and cell motility, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

9 authors at 2 institutions in 1 country.

Marston BradshawPhysiology, Pharmacology and Neuroscience, University of Bristol, Bristol, UK.ORCID 0000-0002-9842-4869
John M SquirePhysiology, Pharmacology and Neuroscience, University of Bristol, Bristol, UK.ORCID 0000-0001-6656-7390
Edward MorrisUniversity of Glasgow, Glasgow, UK.ORCID 0000-0003-3544-0041
Georgia AtkinsonTranslational Health Sciences, University of Bristol, Bristol, UK.ORCID 0000-0002-3454-7034
Rebecca RichardsonPhysiology, Pharmacology and Neuroscience, University of Bristol, Bristol, UK.ORCID 0000-0002-4701-8713
Jon LeesTranslational Health Sciences, University of Bristol, Bristol, UK.ORCID 0000-0003-3925-1424
Massimo CaputoTranslational Health Sciences, University of Bristol, Bristol, UK.ORCID 0000-0001-7508-0891
Giulia M BigottiTranslational Health Sciences, University of Bristol, Bristol, UK.ORCID 0000-0001-9595-3338
Danielle M PaulPhysiology, Pharmacology and Neuroscience, University of Bristol, Bristol, UK. danielle.paul@bristol.ac.uk.ORCID 0000-0002-7327-0023
University of Bristol · GBInstitute of Cancer Research · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R000484/1British Heart Foundation CH/17/1/32804British Heart Foundation FS/14/18/3071British Heart Foundation FS/15/2/31225British Heart Foundation FS/20/5/34973Medical Research Council MR/W003309/1Medical Research Council MR/W003309/2Wellcome TrustWellcome Trust 202904/Z/16/ZWellcome Trust 206181/Z/17/Z
6 · The paper itself

Abstract

Actin, tropomyosin and troponin, the proteins that comprise the contractile apparatus of the cardiac thin filament, are highly conserved across species. We have used cryo-EM to study the three-dimensional structure of the zebrafish cardiac thin and actin filaments. With 70% of human genes having an obvious zebrafish orthologue, and conservation of 85% of disease-causing genes, zebrafish are a good animal model for the study of human disease. Our structure of the zebrafish thin filament reveals the molecular interactions between the constituent proteins, showing that the fundamental organisation of the complex is the same as that reported in the human reconstituted thin filament. A reconstruction of zebrafish cardiac F-actin demonstrates no deviations from human cardiac actin over an extended length of 14 actin subunits. Modelling zebrafish homology models into our maps enabled us to compare, in detail, the similarity with human models. The structural similarities of troponin-T in particular, a region known to contain a hypertrophic cardiomyopathy 'hotspot', confirm the suitability of zebrafish to study these disease-causing mutations.

Indexed as

Cardiomyopathy, HypertrophicZebrafishActin CytoskeletonActinsAnimalsCalciumCryoelectron MicroscopyHumansTropomyosinActinsCalciumTropomyosinActinCryo-EMThin filamentTropomyosinTroponinZebrafish

Identifiers

PMID37480427
PMCPMC10542308
OpenAlexW4385073959

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.