Evidence map›Paper›PMID 24689030›Full record

ReviewGlobal cardiology science & practice2013

Three-dimensional structure of the human myosin thick filament: clinical implications.

Hind A Al-Khayat

Open access · diamondAbstract readReview
In one paragraph

Review in Global cardiology science & practice, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact, top 81% 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

20 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Hybrid method for representing ions in implicit solvation calculations.Computational and structural biotechnology journal · 2021
    Article
  15. Review
  16. Article
  17. Ordering of myosin II filaments driven by mechanical forces: experiments and theory.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  18. Review
  19. Structure of the fission yeast actomyosin ring during constriction.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. 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

1 author at 1 institution in 1 country.

Hind A Al-KhayatQatar Cardiovascular Research Centre, Qatar Foundation, PO Box 5825, Doha, Qatar.
Qatar Foundation · QA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High resolution information about the three-dimensional (3D) structure of myosin filaments has always been hard to obtain. Solving the 3D structure of myosin filaments is very important because mutations in human cardiac muscle myosin and its associated proteins (e.g. titin and myosin binding protein C) are known to be associated with a number of familial human cardiomyopathies (e.g. hypertrophic cardiomyopathy and dilated cardiomyopathy). In order to understand how normal heart muscle works and how it fails, as well as the effects of the known mutations on muscle contractility, it is essential to properly understand myosin filament 3D structure and properties in both healthy and diseased hearts. The aim of this review is firstly to provide a general overview of the 3D structure of myosin thick filaments, as studied so far in both vertebrates and invertebrate striated muscles. Knowledge of this 3D structure is the starting point from which myosin filaments isolated from human cardiomyopathic samples, with known mutations in either myosin or its associated proteins (titin or C-protein), can be studied in detail. This should, in turn, enable us to relate the structure of myosin thick filament to its function and to understanding the disease process. A long term objective of this research would be to assist the design of possible therapeutic solutions to genetic myosin-related human cardiomyopathies.

Indexed as

human cardiomyopathiesmyosin thick filamentssingle particle image analysisthree-dimensional reconstructiontransmission electron microscopy

Identifiers

PMID24689030
PMCPMC3963759
OpenAlexW2160251433

What OpenQuestion holds

Textmetadata
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.