Evidence map›Paper›PMID 15111414›Full record

ArticleBiophysical journal2004

Structural and functional roles of desmin in mouse skeletal muscle during passive deformation.

Sameer B Shah, Jennifer Davis, Noah Weisleder, Ioanna Kostavassili, Andrew D McCulloch, Evelyn Ralston, Yassemi Capetanaki, Richard L Lieber

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
3.0field-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

67 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Desmin Knock-Out Cardiomyopathy: A Heart on the Verge of Metabolic Crisis.International journal of molecular sciences · 2022
    Article
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  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

7 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Sameer B ShahDepartments of Bioengineering and Orthopaedics, Biomedical Sciences Graduate Group, University of California and Veterans Administration Medical Centers, San Diego, California 92161, USA.
Jennifer Davis
Noah Weisleder
Ioanna Kostavassili
Andrew D McCulloch
Evelyn Ralston
Yassemi Capetanaki
Richard L Lieber
Academy of Athens · GRNational Institutes of Health · US

Funding

CARDIOVASCULAR SURGERY/BIOENGINEERING TRAININGT32HL007089 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHIEN, SHU · 1985 to 2009
$9.3M
Regulation of Subcellular Organization in Skeletal MuscleZIAAR041132 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI RALSTON, EVELYN · 2010 to 2019
$4.5M
REGULATION OF SUBCELLULAR ORGANIZATION IN SKELETAL MUSCLEZ01AR041132 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI RALSTON, EVELYN · 2002 to 2008
$2.9M
Skeletal Muscle Injury: Mechanism Prevention &TreatmentR01AR040050 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LIEBER, RICHARD L · 1989 to 2007
$1.6M
REGULATION OF SUBCELLULAR ORGANIZATION IN SKELETAL MUSCLEZICAR041132 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI RALSTON, EVELYN · 2009 to 2009
$1.2M
NHLBI NIH HHS T32 HL007089NHLBI NIH HHS T32HL07089NIAMS NIH HHS AR40050NIAMS NIH HHS R01 AR040050
6 · The paper itself

Abstract

Mechanical interactions between desmin and Z-disks, costameres, and nuclei were measured during passive deformation of single muscle cells. Image processing and continuum kinematics were used to quantify the structural connectivity among these structures. Analysis of both wild-type and desmin-null fibers revealed that the costamere protein talin colocalized with the Z-disk protein alpha-actinin, even at very high strains and stresses. These data indicate that desmin is not essential for mechanical coupling of the costamere complex and the sarcomere lattice. Within the sarcomere lattice, significant differences in myofibrillar connectivity were revealed between passively deformed wild-type and desmin-null fibers. Connectivity in wild-type fibers was significantly greater compared to desmin-null fibers, demonstrating a significant functional connection between myofibrils that requires desmin. Passive mechanical analysis revealed that desmin may be partially responsible for regulating fiber volume, and consequently, fiber mechanical properties. Kinematic analysis of alpha-actinin strain fields revealed that knockout fibers transmitted less shear strain compared to wild-type fibers and experienced a slight increase in fiber volume. Finally, linkage of desmin intermediate filaments to muscle nuclei was strongly suggested based on extensive loss of nuclei positioning in the absence of desmin during passive fiber loading.

Indexed as

ActininAnimalsBiomechanical PhenomenaBiophysical PhenomenaBiophysicsCell NucleusDesminIntermediate FilamentsMiceMice, KnockoutMice, TransgenicModels, StatisticalModels, TheoreticalMusclesMuscle, SkeletalMyofibrilsActininDesminTalin

Identifiers

PMID15111414
PMCPMC1304166
OpenAlexW1968058435

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.