Evidence map›Paper›PMID 32651905›Full record

ReviewBiophysical reviews2020

Disease mutations in striated muscle myosins.

Francine Parker, Michelle Peckham

Open access · hybridAbstract readReview
In one paragraph

Review in Biophysical reviews, 2020. 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
3.9field-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

19 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  8. Atomistic Simulations of Sarcomere Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  9. Article
  10. Structure of theInternational journal of molecular sciences · 2023
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Cardiomyocyte Dysfunction in Inherited Cardiomyopathies.International journal of molecular sciences · 2021
    Review
  17. Article
  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

2 authors at 1 institution in 1 country.

Francine ParkerSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.
Michelle PeckhamSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK. m.peckham@leeds.ac.uk.ORCID http://orcid.org/0000-0002-3754-2028
University of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/T019751/1British Heart Foundation PG/07/095/23743British Heart Foundation PG/15/2/31208Medical Research Council MR/R009406/1Medical Research Council MR/S023593/1
6 · The paper itself

Abstract

Over 1000 disease-causing missense mutations have been found in human β-cardiac, α-cardiac, embryonic and adult fast myosin 2a myosin heavy chains. Most of these are found in human β-cardiac myosin heavy chain. Mutations in β-cardiac myosin cause hypertrophic cardiomyopathy predominantly, whereas those in α-cardiac are associated with many types of heart disease, of which the most common is dilated cardiomyopathy. Mutations in embryonic and fast myosin 2a affect skeletal muscle function. This review provides a short overview of the mutations in the different myosin isoforms and their disease-causing effects.

Indexed as

Cardiac diseaseEmbryonic myosinMissense mutationSkeletal muscle diseaseα-Cardiac myosinβ-Cardiac myosin

Identifiers

PMID32651905
PMCPMC7429545
OpenAlexW3041148217

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.