Evidence map›Paper›PMID 18350308›Full record

ArticleHistochemistry and cell biology2008

New aspects of obscurin in human striated muscles.

Lena Carlsson, Ji-Guo Yu, Lars-Eric Thornell

Abstract read
PubMed Publisher
In one paragraph

Article in Histochemistry and cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.4field-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

30 citing papers in PubMed, 40 citations in OpenAlex.

  1. Trial
  2. Review
  3. Obscurin Maintains Myofiber Identity in Extraocular Muscles.Investigative ophthalmology & visual science · 2024
    Article
  4. Obscurin regulates ankyrin macromolecular complex formation.Journal of molecular and cellular cardiology · 2022
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Biophysical characterization of naturally occurring titin M10 mutations.Protein science : a publication of the Protein Society · 2015
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. The kinase domains of obscurin interact with intercellular adhesion proteins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  17. Article
  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 1 institution in 1 country.

Lena CarlssonDepartment of Integrative Medical Biology, Section for Anatomy, Umeå University, Umeå, Sweden. lena.carlsson@anatomy.umu.se
Ji-Guo Yu
Lars-Eric Thornell
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Obscurin is a giant protein (700-800 kDa) present in both skeletal muscles and myocardium. According to animal studies, obscurin interacts with myofibrillar Z-discs during early muscle development, but is translocalised to be predominantly associated with the M-bands in mature muscles. The proposed function for obscurin is in the assembly and organisation of myosin into regular A-bands during formation of new sarcomeres. In the present study, the precise localisation of obscurin in developing and mature normal human striated muscle is presented for the first time. We show that obscurin surrounded myofibrils at the M-band level in both developing and mature human skeletal and heart muscles, which is partly at variance with that observed in animals. At maturity, obscurin also formed links between the peripheral myofibrils and the sarcolemma, and was a distinct component of the neuromuscular junctions. Obscurin should therefore be regarded as an additional component of the extrasarcomeric cytoskeleton. To test this function of obscurin, biopsies from subjects with exercise-induced delayed onset muscle soreness (DOMS) were examined. In these subjects, myofibrillar alterations related to sarcomerogenesis are observed. Our immunohistochemical analysis revealed that obscurin was never lacking in myofibrillar alterations, but was either preserved at the M-band level or diffusely spread over the sarcomeres. As myosin was absent in such areas but later reincorporated in the newly formed sarcomeres, our results support that obscurin also might play an important role in the formation and maintenance of A-bands.

Indexed as

AdultAnimalsFetusGuanine Nucleotide Exchange FactorsHeartHumansMicroscopy, ImmunoelectronMuscle ProteinsMuscle, StriatedMyocardiumProtein Serine-Threonine KinasesRho Guanine Nucleotide Exchange FactorsSarcomeresGuanine Nucleotide Exchange FactorsMuscle ProteinsOBSCN protein, humanProtein Serine-Threonine KinasesRho Guanine Nucleotide Exchange Factors

Identifiers

PMID18350308
OpenAlexW2170476464

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.