Evidence map›Paper›PMID 26792324›Full record

ReviewThe Journal of experimental biology2016

Nebulin, a multi-functional giant.

Miensheng Chu, Carol C Gregorio, Christopher T Pappas

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of experimental biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The Nebulin Family LIM and SH3 Proteins Regulate Postsynaptic Development and Function.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  19. Review
  20. Actin droplet machine.Royal Society open science · 2019
    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.

Miensheng ChuDepartment of Cellular and Molecular Medicine and the Sarver Molecular Cardiovascular Research Program, The University of Arizona, 1656 East Mabel, MRB315, Tucson, AZ 85724, USA.
Carol C GregorioDepartment of Cellular and Molecular Medicine and the Sarver Molecular Cardiovascular Research Program, The University of Arizona, 1656 East Mabel, MRB315, Tucson, AZ 85724, USA gregorio@email.arizona.edu.
Christopher T PappasDepartment of Cellular and Molecular Medicine and the Sarver Molecular Cardiovascular Research Program, The University of Arizona, 1656 East Mabel, MRB315, Tucson, AZ 85724, USA.
University of Arizona · US

Funding

Deciphering the role of Lmod2 in thin filament length regulation and dilated cardiomyopathyR01HL123078 · NHLBI · UNIVERSITY OF ARIZONA · PI Carol C Gregorio, Shashank Shekhar · 2015 to 2026
$5.6M
Deciphering the role of the RNA-binding protein, FXR1, in cardiac muscle assemblyR01HL108625 · NHLBI · UNIVERSITY OF ARIZONA · PI GREGORIO, CAROL C · 2012 to 2015
$1.9M
NHLBI NIH HHS R01 HL108625NHLBI NIH HHS R01HL108625NHLBI NIH HHS R01 HL123078NHLBI NIH HHS R01HL123078
6 · The paper itself

Abstract

Efficient muscle contraction in skeletal muscle is predicated on the regulation of actin filament lengths. In one long-standing model that was prominent for decades, the giant protein nebulin was proposed to function as a 'molecular ruler' to specify the lengths of the thin filaments. This theory was questioned by many observations, including experiments in which the length of nebulin was manipulated in skeletal myocytes; this approach revealed that nebulin functions to stabilize filamentous actin, allowing thin filaments to reach mature lengths. In addition, more recent data, mostly from in vivo models and identification of new interacting partners, have provided evidence that nebulin is not merely a structural protein. Nebulin plays a role in numerous cellular processes including regulation of muscle contraction, Z-disc formation, and myofibril organization and assembly.

Indexed as

Actin CytoskeletonAnimalsDiseaseHumansMuscle ProteinsMutationProtein BindingMuscle ProteinsnebulinActin filamentSarcomereSkeletal muscle

Identifiers

PMID26792324
PMCPMC6514474
OpenAlexW2263078558

What OpenQuestion holds

Textmetadata
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.