Evidence map›Paper›PMID 11053126›Full record

ArticleBiophysical journal2000

Divergent functional properties of ryanodine receptor types 1 and 3 expressed in a myogenic cell line.

J D Fessenden, Y Wang, R A Moore, S R Chen, P D Allen, I N Pessah

Abstract read
In one paragraph

Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
–field-weighted citation impact
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

56 citing papers in PubMed.

  1. Effects of aging on calcium channels in skeletal muscle.Frontiers in molecular biosciences · 2025
    Review
  2. Article
  3. Article
  4. Regulatory mechanisms of ryanodine receptor/CaJournal of muscle research and cell motility · 2021
    Review
  5. Physiological and Pathological Relevance of Selective and Nonselective CaAdvances in experimental medicine and biology · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Alteration of Ryanodine-receptors in Cultured Rat Aortic Smooth Muscle Cells.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2011
    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

6 authors.

J D FessendenDepartment of Molecular Biosciences, School of Veterinary Medicine, University of California Davis, Davis, California 95616, USA.
Y Wang
R A Moore
S R Chen
P D Allen
I N Pessah

Funding

Structure Function Studies of RyR1 in a Myogenic KnockoutR01AR043140 · NIAMS · CHILDREN'S HOSPITAL BOSTON · PI ALLEN, PAUL D · 1996 to 2010
$4.8M
NIAMS NIH HHS 1PO AR1760NIAMS NIH HHS 1RO1AR43140
6 · The paper itself

Abstract

Of the three known ryanodine receptor (RyR) isoforms expressed in muscle, RyR1 and RyR2 have well-defined roles in contraction. However, studies on mammalian RyR3 have been difficult because of low expression levels relative to RyR1 or RyR2. Using the herpes simplex virus 1 (HSV-1) helper-free amplicon system, we expressed either RyR1 or RyR3 in 1B5 RyR-deficient myotubes. Western blot analysis revealed that RyR1- or RyR3-transduced cells expressed the appropriate RyR isoform of the correct molecular mass. Although RyR1 channels exhibited the expected unitary conductance for Cs(+) in bilayer lipid membranes, 74 of 88 RyR3 channels exhibited pronounced subconductance behavior. Western blot analysis with an FKBP12/12.6-selective antibody reveals that differences in gating behavior exhibited by RyR1 and RyR3 may be, in part, the result of lower affinity of RyR3 for FKBP12. In calcium imaging studies, RyR1 restored skeletal-type excitation-contraction coupling, whereas RyR3 did not. Although RyR3-expressing myotubes were more sensitive to caffeine than those expressing RyR1, they were much less sensitive to 4-chloro-m-cresol (CMC). In RyR1-expressing cells, regenerative calcium oscillations were observed in response to caffeine and CMC but were never seen in RyR3-expressing 1B5 cells. In [(3)H]ryanodine binding studies, only RyR1 exhibited sensitivity to CMC, but both RyR isoforms responded to caffeine. These functional differences between RyR1 and RyR3 expressed in a mammalian muscle context may reflect differences in association with accessory proteins, especially FKBP12, as well as structural differences in modulator binding sites.

Indexed as

AnimalsBiophysical PhenomenaBiophysicsCaffeineCalcium SignalingCell LineCresolsElectrophysiologyGene ExpressionHerpesvirus 1, HumanMiceMuscle ContractionMuscle, SkeletalProtein IsoformsRecombinant ProteinsRyanodine Receptor Calcium Release ChannelCaffeinechlorocresolCresolsProtein IsoformsRecombinant ProteinsRyanodine Receptor Calcium Release ChannelTacrolimus Binding Protein 1A

Identifiers

PMID11053126
PMCPMC1301134

What OpenQuestion holds

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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.