Evidence map›Paper›PMID 32619437›Full record

ArticleJournal of molecular biology2020

The Axial Alignment of Titin on the Muscle Thick Filament Supports Its Role as a Molecular Ruler.

Pauline Bennett, Martin Rees, Mathias Gautel

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  11. Review
  12. Obscurin Maintains Myofiber Identity in Extraocular Muscles.Investigative ophthalmology & visual science · 2024
    Article
  13. Titin: roles in cardiac function and diseases.Frontiers in physiology · 2024
    Review
  14. Article
  15. Molecular insights into titin's A-band.Journal of muscle research and cell motility · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Titin activates myosin filaments in skeletal muscle by switching from an extensible spring to a mechanical rectifier.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

3 authors at 1 institution in 1 country.

Pauline BennettThe Randall Centre for Cell & Molecular Biophysics, School of Basic and Medical Biosciences, New Hunt's House, Guy's Campus, King's College London, London, UK. Electronic address: pauline.bennett@kcl.ac.uk.
Martin ReesThe Randall Centre for Cell & Molecular Biophysics, School of Basic and Medical Biosciences, New Hunt's House, Guy's Campus, King's College London, London, UK. Electronic address: martin.rees@kcl.ac.uk.
Mathias GautelThe Randall Centre for Cell & Molecular Biophysics, School of Basic and Medical Biosciences, New Hunt's House, Guy's Campus, King's College London, London, UK. Electronic address: mathias.gautel@kcl.ac.uk.
King's College London · GB

Funding

British Heart Foundation BHF-RG/15/8/31480British Heart Foundation CH/08/001/25300Medical Research Council MR/K015664/1Wellcome Trust 201543/Z/16/Z
6 · The paper itself

Abstract

The giant protein titin is expressed in vertebrate striated muscle where it spans half a sarcomere from the Z-disc to the M-band and is essential for muscle organisation, activity and health. The C-terminal portion of titin is closely associated with the thick, myosin-containing filament and exhibits a complex pattern of immunoglobulin and fibronectin domains. This pattern reflects features of the filament organisation suggesting that it acts as a molecular ruler and template, but the exact axial disposition of the molecule has not been determined. Here, we present data that allow us to precisely locate titin domains axially along the thick filament from its tip to the edge of the bare zone. We find that the domains are regularly distributed along the filament at 4-nm intervals and we can determine the domains that associate with features of the filament, such as the 11 stripes of accessory proteins. We confirm that the nine stripes ascribed to myosin binding protein-C are not related to the titin sequence previously assumed; rather, they relate to positions approximately 18 domains further towards the C terminus along titin. This disposition also allows a subgroup of titin domains comprising two or three fibronectin domains to associate with each of the 49 levels of myosin heads in each half filament. The results strongly support the role of titin as a blueprint for the thick filament and the arrangement of the myosin motor domains.

Indexed as

AnimalsCarrier ProteinsConnectinMiceMuscle, SkeletalMutationMyosin Binding Protein CProtein BindingProtein DomainsProtein KinasesRabbitsCarrier ProteinsConnectinMyosin Binding Protein CProtein Kinasestitin protein, mouseMyBP-CMyBP-HSTEDSTORM

Identifiers

PMID32619437
PMCPMC7427331
OpenAlexW3038731780

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.