Evidence map›Paper›PMID 22043020›Full record

ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2011

Unmasking potential intracellular roles for dysferlin through improved immunolabeling methods.

Joseph A Roche, Lisa W Ru, Andrea M O'Neill, Wendy G Resneck, Richard M Lovering, Robert J Bloch

Open access · bronzeAbstract read
In one paragraph

Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2011. 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
1.3field-weighted citation impact, top 20% 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, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Elevated CaFrontiers in physiology · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Coupling of excitation to CaThe Journal of physiology · 2017
    Article
  15. Article
  16. Membrane fusion in muscle development and repair.Seminars in cell & developmental biology · 2015
    Review
  17. Article
  18. Rapid actin-cytoskeleton-dependent recruitment of plasma membrane-derived dysferlin at wounds is critical for muscle membrane repair.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
  19. Review
  20. Dysferlin stabilizes stress-induced Ca2+ signaling in the transverse tubule membrane.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

6 authors at 1 institution in 1 country.

Joseph A RocheDepartment of Physiology, University of Maryland School of Medicine, Baltimore, USA.
Lisa W Ru
Andrea M O'Neill
Wendy G Resneck
Richard M Lovering
Robert J Bloch
University of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in the DYSF gene that severely reduce the levels of the protein dysferlin are implicated in muscle-wasting syndromes known as dysferlinopathies. Although studies of its function in skeletal muscle have focused on its potential role in repairing the plasma membrane, dysferlin has also been found, albeit inconsistently, in the sarcoplasm of muscle fibers. The aim of this article is to study the localization of dysferlin in skeletal muscle through optimized immunolabeling methods. We studied the localization of dysferlin in control rat skeletal muscle using several different methods of tissue collection and subsequent immunolabeling. We then applied our optimized immunolabeling methods on human cadaveric muscle, control and dystrophic human muscle biopsies, and control and dysferlin-deficient mouse muscle. Our data suggest that dysferlin is present in a reticulum of the sarcoplasm, similar but not identical to those containing the dihydropyridine receptors and distinct from the distribution of the sarcolemmal protein dystrophin. Our data illustrate the importance of tissue fixation and antigen unmasking for proper immunolocalization of dysferlin. They suggest that dysferlin has an important function in the internal membrane systems of skeletal muscle, involved in calcium homeostasis and excitation-contraction coupling.

Indexed as

AnimalsDysferlinFluorescent Antibody TechniqueHumansMaleMembrane ProteinsMiceMuscle ProteinsMuscle, SkeletalMuscular DystrophiesRatsRats, Sprague-DawleyDysferlinDYSF protein, humanDysf protein, mouseDysf protein, ratMembrane ProteinsMuscle Proteins

Identifiers

PMID22043020
PMCPMC3261626
OpenAlexW2100028579

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.