Evidence map›Paper›PMID 19679637›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2009

Nebulin plays a direct role in promoting strong actin-myosin interactions.

Marie-Louise Bang, Marco Caremani, Elisabetta Brunello, Ryan Littlefield, Richard L Lieber, Ju Chen, Vincenzo Lombardi, Marco Linari

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Panorama of the distal myopathies.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2020
    Review
  6. Article
  7. Nebulin: big protein with big responsibilities.Journal of muscle research and cell motility · 2020
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Overview of the Muscle Cytoskeleton.Comprehensive Physiology · 2017
    Review
  17. Identification of 2 Potentially Relevant Gene Mutations Involved in Strabismus Using Whole-Exome Sequencing.Medical science monitor : international medical journal of experimental and clinical research · 2017
    Article
  18. Article
  19. Nebulin, a multi-functional giant.The Journal of experimental biology · 2016
    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

8 authors at 4 institutions in 2 countries.

Marie-Louise BangIstituto Tecnologie Biomediche-Consiglio Nazionale delle Ricerche (ITB-CNR), Via Fratelli Cervi 93, 20090 Segrate, Milan, Italy. m.bang@itb.cnr.it
Marco Caremani
Elisabetta Brunello
Ryan Littlefield
Richard L Lieber
Ju Chen
Vincenzo Lombardi
Marco Linari
University of Florence · ITUniversity of California, San Diego · USDulbecco Telethon Institute · ITLuxel (United States) · US

Funding

The molecular mechanism of muscle contractionR01AR049033 · NIAMS · UNIVERSITY OF FLORENCE · PI LOMBARDI, VINCENZO · 2003 to 2006
$422k
NIAMS NIH HHS R01 AR049033NIAMS NIH HHS R01 AR49033Telethon TCP07006
6 · The paper itself

Abstract

The role of the actin filament-associated protein nebulin on mechanical and kinetic properties of the actomyosin motor was investigated in skeletal muscle of wild-type (wt) and nebulin-deficient (nebulin(-)(/)(-)) mice that were 1 d old, an age at which sarcomeric structure is still well preserved. In Ca2+-activated skinned fibers from psoas muscle, we determined the Ca2+ dependence of isometric force and stiffness, the rate of force redevelopment after unloaded shortening (k(TR)), the power during isotonic shortening, and the unloaded shortening velocity (V(0)). Our results show a 65% reduction in isometric force in nebulin(-)(/)(-) fibers at saturating [Ca2+], whereas neither thin-filament length nor the Ca2+ sensitivity of the contractile system is affected. Stiffness measurements indicate that the reduction in isometric force is due to a reduction in the number of actin-attached myosin motors, whereas the force of the motor is unchanged. Furthermore, in nebulin(-)(/)(-) fibers, k(TR) is decreased by 57%, V(0) is increased by 63%, and the maximum power is decreased by 80%. These results indicate that, in the absence of nebulin, the attachment probability of the myosin motors to actin is decreased, revealing a direct role for nebulin in promoting strong actomyosin interactions responsible for force and power production.

Indexed as

ActinsAnimalsAnimals, NewbornCalciumMiceMice, KnockoutMuscle ContractionMuscle ProteinsMuscle, SkeletalMyosinsActinsCalciumMuscle ProteinsMyosinsnebulin

Identifiers

PMID19679637
PMCPMC2812046
OpenAlexW2059118657

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.