Evidence map›Paper›PMID 26793121›Full record

ReviewFrontiers in physiology2015

Critical Role of Intracellular RyR1 Calcium Release Channels in Skeletal Muscle Function and Disease.

Erick O Hernández-Ochoa, Stephen J P Pratt, Richard M Lovering, Martin F Schneider

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 75 citations in OpenAlex.

  1. Trial
  2. Review
  3. NMJ-associated transcriptomic remodeling correlates with disease severity in juvenile dermatomyositis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Phosphorylation of RYR1 at SerScience signaling · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Therapeutic advances in neurological disorders · 2025
    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

4 authors at 1 institution in 1 country.

Erick O Hernández-OchoaDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine Baltimore, MD, USA.
Stephen J P PrattDepartment of Orthopaedics, University of Maryland School of Medicine Baltimore, MD, USA.
Richard M LoveringDepartment of Orthopaedics, University of Maryland School of Medicine Baltimore, MD, USA.
Martin F SchneiderDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine Baltimore, MD, USA.
University of Maryland, Baltimore · US

Funding

Roles of voltage sensor, S100A1 and calmodulin in skeletal muscle Ca2+ signalingR37AR055099 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI SCHNEIDER, MARTIN F · 2012 to 2021
$3.5M
NIAMS NIH HHS R37 AR055099
6 · The paper itself

Abstract

The skeletal muscle Ca(2+) release channel, also known as ryanodine receptor type 1 (RyR1), is the largest ion channel protein known and is crucial for effective skeletal muscle contractile activation. RyR1 function is controlled by Cav1.1, a voltage gated Ca(2+) channel that works mainly as a voltage sensor for RyR1 activity during skeletal muscle contraction and is also fine-tuned by Ca(2+), several intracellular compounds (e.g., ATP), and modulatory proteins (e.g., calmodulin). Dominant and recessive mutations in RyR1, as well as acquired channel alterations, are the underlying cause of various skeletal muscle diseases. The aim of this mini review is to summarize several current aspects of RyR1 function, structure, regulation, and to describe the most common diseases caused by hereditary or acquired RyR1 malfunction.

Indexed as

Ca2+ release channelexcitation-contraction couplingryanodine receptor type 1RyR1 dysfunction and diseaseRyR1-related mutationssarcolemmasarcoplasmic reticulumskeletal muscle

Identifiers

PMID26793121
PMCPMC4709859
OpenAlexW2270508964

What OpenQuestion holds

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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.