Evidence map›Paper›PMID 22045734›Full record

ArticleJournal of cell science2011

Integrity of the network sarcoplasmic reticulum in skeletal muscle requires small ankyrin 1.

Maegen A Ackermann, Andrew P Ziman, John Strong, Yinghua Zhang, April K Hartford, Christopher W Ward, William R Randall, Aikaterini Kontrogianni-Konstantopoulos, Robert J Bloch

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

23 citing papers in PubMed, 29 citations in OpenAlex.

  1. Genome writing and Targeted Delivery of thebioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Obscurin regulates ankyrin macromolecular complex formation.Journal of molecular and cellular cardiology · 2022
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Skeletal muscle: A review of molecular structure and function, in health and disease.Wiley interdisciplinary reviews. Systems biology and medicine · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Electron tomography of rabbit cardiomyocyte three-dimensional ultrastructure.Progress in biophysics and molecular biology · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

9 authors at 1 institution in 1 country.

Maegen A AckermannDepartment of Biochemistry and Molecular Biology, Therapeutics University of Maryland, Baltimore, MD 21201, USA.
Andrew P Ziman
John Strong
Yinghua Zhang
April K Hartford
Christopher W Ward
William R Randall
Aikaterini Kontrogianni-Konstantopoulos
Robert J Bloch
University of Maryland, Baltimore · US

Funding

SMALL ANKYRINS IN EXCITABLE CELLSR01HL064304 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI BLOCH, ROBERT J · 1999 to 2009
$2.3M
Organization of Sarcoplasmic Reticulum in Skeletal MuscleR01AR056330 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI BLOCH, ROBERT J · 2008 to 2012
$1.5M
M-Line Proteins and A-Band Assembly in Skeletal MuscleR01AR052768 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI KONTROGIANNI-KONSTANTOPOULOS, AIKATERINI · 2006 to 2010
$1.4M
The Role of Small Ankyrin 1 in the Sarcoplasmic Reticulum in Skeletal MuscleF32AR057647 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI ZIMAN, ANDREW P. · 2010 to 2011
$107k
NHLBI NIH HHS R01 HL064304NHLBI NIH HHS R01 HL64304NIAMS NIH HHS F32 AR057647NIAMS NIH HHS F32 AR52768NIAMS NIH HHS R01 AR052768NIAMS NIH HHS R01 AR056330NIAMS NIH HHS R01 AR52768NIAMS NIH HHS R01 AR56330
6 · The paper itself

Abstract

Small ankyrin 1 (sAnk1; Ank1.5) is a ~20 kDa protein of striated muscle that concentrates in the network compartment of the sarcoplasmic reticulum (nSR). We used siRNA targeted to sAnk1 to assess its role in organizing the sarcoplasmic reticulum (SR) of skeletal myofibers in vitro. siRNA reduced sAnk1 mRNA and protein levels and disrupted the organization of the remaining sAnk1. Sarcomeric proteins were unchanged, but two other proteins of the nSR, SERCA and sarcolipin, decreased significantly in amount and segregated into distinct structures containing sarcolipin and sAnk1, and SERCA, respectively. Exogenous sAnk1 restored SERCA to its normal distribution. Ryanodine receptors and calsequestrin in the junctional SR, and L-type Ca(2+) channels in the transverse tubules were not reduced, although their striated organization was mildly altered. Consistent with the loss of SERCA, uptake and release of Ca(2+) were significantly inhibited. Our results show that sAnk1 stabilizes the nSR and that its absence causes the nSR to fragment into distinct membrane compartments.

Indexed as

AnimalsAnkyrinsMuscle ProteinsMuscle, SkeletalProteolipidsRatsSarcoplasmic ReticulumSarcoplasmic Reticulum Calcium-Transporting ATPasesAnk1 protein, ratAnkyrinsAtp2a1 protein, ratMuscle ProteinsProteolipidssarcolipinSarcoplasmic Reticulum Calcium-Transporting ATPases

Identifiers

PMID22045734
PMCPMC3215573
OpenAlexW2155274466

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.