Evidence map›Paper›PMID 22375125›Full record

ArticleFrontiers in physiology2012

The sarcomeric protein nebulin: another multifunctional giant in charge of muscle strength optimization.

Coen A C Ottenheijm, Henk Granzier, Siegfried Labeit

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2012. 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
2.7field-weighted citation impact, top 9% 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. Article
  3. Article
  4. Review
  5. Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023
    Review
  6. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Nebulin: big protein with big responsibilities.Journal of muscle research and cell motility · 2020
    Review
  10. Article
  11. Article
  12. Nemaline myopathies: a current view.Journal of muscle research and cell motility · 2019
    Review
  13. Article
  14. Article
  15. Adaptations to Endurance and Strength Training.Cold Spring Harbor perspectives in medicine · 2018
    Review
  16. Effects of aging, exercise, and disease on force transfer in skeletal muscle.American journal of physiology. Endocrinology and metabolism · 2015
    Review
  17. Review
  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

3 authors at 2 institutions in 3 countries.

Coen A C OttenheijmDepartment of Physiology, Institute for Cardiovascular Research, VU University Medical Center Amsterdam, Netherlands.
Henk Granzier
Siegfried Labeit
University of Arizona · USHeidelberg University · DE

Funding

Roles of Nebulin in Structure and Function of Striated MuscleR01AR053897 · NIAMS · UNIVERSITY OF ARIZONA · PI Henk L. GRANZIER · 2007 to 2026
$7.4M
NIAMS NIH HHS R01 AR053897
6 · The paper itself

Abstract

The sliding filament model of the sarcomere was developed more than half a century ago. This model, consisting only of thin and thick filaments, has been successful in explaining many, but not all, features of skeletal muscle. Work during the 1980s revealed the existence of two additional filaments: the giant filamentous proteins titin and nebulin. Whereas the role of titin rapidly progressed, nebulin's role in muscle structure and function remained long nebulous. An important feature of muscle structure and function that has remained relatively obscure concerns the mechanisms that are involved in regulating thin filament length. Filament length is an important aspect of muscle function as force production is proportional to the amount of overlap between thick and thin filaments. Recent advances, due in part to the generation of nebulin KO models, reveal that nebulin plays an important role in the regulation of thin filament length, most likely by stabilizing F-actin assemblies. Another structural feature of skeletal muscle that has been incompletely understood concerns the mechanisms involved in maintaining Z-disk structure and the regular lateral alignment of adjacent sarcomeres during contraction. Recent studies indicate that nebulin is part of a protein complex that mechanically links adjacent myofibrils. In addition to these structural roles in support of myofibrillar force generation, nebulin has been also shown to regulate directly muscle contraction at the level of individual crossbridges: cycling kinetics and the calcium sensitivity of force producing crossbridges is enhanced in the presence of nebulin. Thus, these recent data all point to nebulin being important for muscle force optimization. Consequently, muscle weakness as the lead symptom develops in the case of patients with nemaline myopathy that have mutations in the nebulin gene. Here, we discuss these important novel insights into the role of nebulin in skeletal muscle function.

Indexed as

nebulinskeletal musclethin filament

Identifiers

PMID22375125
PMCPMC3286824
OpenAlexW2103082980

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.