Evidence map›Paper›PMID 18059477›Full record

ArticleThe EMBO journal2008

Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin.

Nikos Pinotsis, Stephan Lange, Jean-Claude Perriard, Dmitri I Svergun, Matthias Wilmanns

Abstract readValidation Study
In one paragraph

Article in The EMBO journal, 2008. 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
–field-weighted citation impact
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.

  1. Review
  2. Article
  3. Article
  4. The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Force-induced remodelling of proteins and their complexes.Current opinion in structural biology · 2015
    Review
  10. Article
  11. Stable single α-helices are constant force springs in proteins.The Journal of biological chemistry · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Structural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

5 authors.

Nikos PinotsisEMBL-Hamburg c/o DESY, Hamburg, Germany.
Stephan Lange
Jean-Claude Perriard
Dmitri I Svergun
Matthias Wilmanns

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sarcomeric filament proteins display extraordinary properties in terms of protein length and mechanical elasticity, requiring specific anchoring and assembly mechanisms. To establish the molecular basis of terminal filament assembly, we have selected the sarcomeric M-band protein myomesin as a prototypic filament model. The crystal structure of the myomesin C-terminus, comprising a tandem array of two immunoglobulin (Ig) domains My12 and My13, reveals a dimeric end-to-end filament of 14.3 nm length. Although the two domains share the same fold, an unexpected rearrangement of one beta-strand reveals how they are evolved into unrelated functions, terminal filament assembly (My13) and filament propagation (My12). The two domains are connected by a six-turn alpha-helix, of which two turns are void of any interactions with other protein parts. Thus, the overall structure of the assembled myomesin C-terminus resembles a three-body beads-on-the-string model with potentially elastic properties. We predict that the found My12-helix-My13 domain topology may provide a structural template for the filament architecture of the entire C-terminal Ig domain array My9-My13 of myomesin.

Indexed as

Amino Acid SequenceConnectinCrystallography, X-RayCytoskeletonHumansModels, MolecularMolecular Sequence DataMuscle ProteinsPeptide FragmentsSarcomeresConnectinMuscle ProteinsPeptide Fragments

Identifiers

PMID18059477
PMCPMC2206126

What OpenQuestion holds

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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.