Evidence map›Paper›PMID 24376425›Full record

ReviewFrontiers in physiology2013

Structure of giant muscle proteins.

Logan C Meyer, Nathan T Wright

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. The varied functions of the giant muscle scaffold protein obscurin.Frontiers in cell and developmental biology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Titin N2A Domain and Its Interactions at the Sarcomere.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Actin Mutations and Their Role in Disease.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Review
  11. Obscurin is a semi-flexible molecule in solution.Protein science : a publication of the Protein Society · 2019
    Article
  12. Review
  13. Review
  14. Article
  15. TheeLife · 2016
    Article
  16. Article
  17. Review
  18. Article
  19. Fibre typing of intrafusal fibres.Journal of anatomy · 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

2 authors at 1 institution in 1 country.

Logan C MeyerDepartment of Chemistry and Biochemistry, James Madison University Harrisonburg, VA, USA.
Nathan T WrightDepartment of Chemistry and Biochemistry, James Madison University Harrisonburg, VA, USA.
James Madison University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Giant muscle proteins (e.g., titin, nebulin, and obscurin) play a seminal role in muscle elasticity, stretch response, and sarcomeric organization. Each giant protein consists of multiple tandem structural domains, usually arranged in a modular fashion spanning 500 kDa to 4 MDa. Although many of the domains are similar in structure, subtle differences create a unique function of each domain. Recent high and low resolution structural and dynamic studies now suggest more nuanced overall protein structures than previously realized. These findings show that atomic structure, interactions between tandem domains, and intrasarcomeric environment all influence the shape, motion, and therefore function of giant proteins. In this article we will review the current understanding of titin, obscurin, and nebulin structure, from the atomic level through the molecular level.

Indexed as

fibronectin type IIIimmunoglobulinnebulinobscurinstructuretitin

Identifiers

PMID24376425
PMCPMC3859903
OpenAlexW2141676377

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.