Evidence map›Paper›PMID 24739166›Full record

ArticleBiophysical journal2014

Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure.

Maryví González-Solá, Hind A Al-Khayat, Martine Behra, Robert W Kensler

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Structure of mavacamten-free human cardiac thick filaments within the sarcomere by cryoelectron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Variants of the myosin interacting-heads motif.The Journal of general physiology · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Review
  15. Article
  16. Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Article
  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

4 authors at 2 institutions in 2 countries.

Maryví González-SoláDepartment of Anatomy and Neurobiology, University of Puerto Rico Medical School, San Juan, Puerto Rico. Electronic address: maryvi.gonzalez@upr.edu.
Hind A Al-KhayatNational Heart and Lung Institute, Faculty of Medicine, Imperial College London, London, United Kingdom.
Martine BehraDepartment of Anatomy and Neurobiology, University of Puerto Rico Medical School, San Juan, Puerto Rico.
Robert W KenslerDepartment of Anatomy and Neurobiology, University of Puerto Rico Medical School, San Juan, Puerto Rico.
University of Puerto Rico, Medical Sciences Campus · PRImperial College London · GB

Funding

RISE Option III: MBRS RISE at the UPR Medical Sciences CampusR25GM061838 · NIGMS · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI CADILLA, CARMEN LYDIA · 2000 to 2021
$25.5M
Cardiac Muscle: Functional Role of Myosin - Binding Protein C in ContractionSC1HL096017 · NHLBI · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI KENSLER, ROBERT W. · 2008 to 2011
$750k
British Heart Foundation FS/07/017/22951NHLBI NIH HHS SC1 HL096017NIGMS NIH HHS R25 GM061838
6 · The paper itself

Abstract

To understand how mutations in thick filament proteins such as cardiac myosin binding protein-C or titin, cause familial hypertrophic cardiomyopathies, it is important to determine the structure of the cardiac thick filament. Techniques for the genetic manipulation of the zebrafish are well established and it has become a major model for the study of the cardiovascular system. Our goal is to develop zebrafish as an alternative system to the mammalian heart model for the study of the structure of the cardiac thick filaments and the proteins that form it. We have successfully isolated thick filaments from zebrafish cardiac muscle, using a procedure similar to those for mammalian heart, and analyzed their structure by negative-staining and electron microscopy. The isolated filaments appear well ordered with the characteristic 42.9 nm quasi-helical repeat of the myosin heads expected from x-ray diffraction. We have performed single particle image analysis on the collected electron microscopy images for the C-zone region of these filaments and obtained a three-dimensional reconstruction at 3.5 nm resolution. This reconstruction reveals structure similar to the mammalian thick filament, and demonstrates that zebrafish may provide a useful model for the study of the changes in the cardiac thick filament associated with disease processes.

Indexed as

AnimalsCarrier ProteinsConnectinFourier AnalysisImaging, Three-DimensionalModels, MolecularMyocardiumMyosin Binding Protein CMyosinsZebrafishCarrier ProteinsConnectinMyosin Binding Protein CMyosins

Identifiers

PMID24739166
PMCPMC4008832
OpenAlexW2068898864

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.