Evidence map›Paper›PMID 22347812›Full record

ArticlePLoS biology2012

Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties.

Nikos Pinotsis, Spyros D Chatziefthimiou, Felix Berkemeier, Fabienne Beuron, Irene M Mavridis, Petr V Konarev, Dmitri I Svergun, Edward Morris, Matthias Rief, Matthias Wilmanns

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Nanosurgical Manipulation of Titin and Its M-Complex.Nanomaterials (Basel, Switzerland) · 2022
    Article
  6. Article
  7. Article
  8. Article
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  10. The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Force-induced remodelling of proteins and their complexes.Current opinion in structural biology · 2015
    Review
  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

10 authors at 4 institutions in 3 countries.

Nikos PinotsisEuropean Molecular Biology Laboratory Hamburg, Hamburg, Germany.
Spyros D Chatziefthimiou
Felix Berkemeier
Fabienne Beuron
Irene M Mavridis
Petr V Konarev
Dmitri I Svergun
Edward Morris
Matthias Rief
Matthias Wilmanns
European Molecular Biology Laboratory · DECenter for Integrated Protein Science Munich · DEInstitute of Cancer Research · GBNational Centre of Scientific Research "Demokritos" · GR

Funding

British Heart Foundation PG/07/076/23480
6 · The paper itself

Abstract

Active muscles generate substantial mechanical forces by the contraction/relaxation cycle, and, to maintain an ordered state, they require molecular structures of extraordinary stability. These forces are sensed and buffered by unusually long and elastic filament proteins with highly repetitive domain arrays. Members of the myomesin protein family function as molecular bridges that connect major filament systems in the central M-band of muscle sarcomeres, which is a central locus of passive stress sensing. To unravel the mechanism of molecular elasticity in such filament-connecting proteins, we have determined the overall architecture of the complete C-terminal immunoglobulin domain array of myomesin by X-ray crystallography, electron microscopy, solution X-ray scattering, and atomic force microscopy. Our data reveal a dimeric tail-to-tail filament structure of about 360 Å in length, which is folded into an irregular superhelical coil arrangement of almost identical α-helix/domain modules. The myomesin filament can be stretched to about 2.5-fold its original length by reversible unfolding of these linkers, a mechanism that to our knowledge has not been observed previously. Our data explain how myomesin could act as a highly elastic ribbon to maintain the overall structural organization of the sarcomeric M-band. In general terms, our data demonstrate how repetitive domain modules such as those found in myomesin could generate highly elastic protein structures in highly organized cell systems such as muscle sarcomeres.

Indexed as

ElasticityConnectinCrystallography, X-RayMicroscopy, Atomic ForceMicroscopy, Electron, TransmissionModels, MolecularMuscle ProteinsProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiarySarcomeresScattering, Small AngleConnectinMuscle Proteins

Identifiers

PMID22347812
PMCPMC3279516
OpenAlexW2074332558

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.