Evidence map›Paper›PMID 10051521›Full record

ArticleThe Journal of general physiology1999

Local control models of cardiac excitation-contraction coupling. A possible role for allosteric interactions between ryanodine receptors.

M D Stern, L S Song, H Cheng, J S Sham, H T Yang, K R Boheler, E Ríos

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.

0numbers the graph read from it
0cells of the map it votes in
159citing papers in PubMed
6.4field-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

159 citing papers in PubMed, 273 citations in OpenAlex.

  1. Article
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  5. Decreased RYR2 Cluster Size and Abnormal SR CaAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  14. How does flecainide impact RyR2 channel function?The Journal of general physiology · 2022
    Article
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  16. Review
  17. Review
  18. Article
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  20. Article

99 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

M D SternLaboratory of Cardiovascular Science, National Institute on Aging, National Institutes of Health, Baltimore, Maryland 21224, USA. sternM@grc.nia.nih.gov
L S Song
H Cheng
J S Sham
H T Yang
K R Boheler
E Ríos
Johns Hopkins University · USNational Institute on Aging · US

Funding

CA INDUCED CA RELEASE FROM STRIATED MUSCLER01AR041526 · NIAMS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI PALADE, PHILIP T. · 1996 to 2000
$256k
NIAMS NIH HHS AR41526
6 · The paper itself

Abstract

In cardiac muscle, release of activator calcium from the sarcoplasmic reticulum occurs by calcium- induced calcium release through ryanodine receptors (RyRs), which are clustered in a dense, regular, two-dimensional lattice array at the diad junction. We simulated numerically the stochastic dynamics of RyRs and L-type sarcolemmal calcium channels interacting via calcium nano-domains in the junctional cleft. Four putative RyR gating schemes based on single-channel measurements in lipid bilayers all failed to give stable excitation-contraction coupling, due either to insufficiently strong inactivation to terminate locally regenerative calcium-induced calcium release or insufficient cooperativity to discriminate against RyR activation by background calcium. If the ryanodine receptor was represented, instead, by a phenomenological four-state gating scheme, with channel opening resulting from simultaneous binding of two Ca2+ ions, and either calcium-dependent or activation-linked inactivation, the simulations gave a good semiquantitative accounting for the macroscopic features of excitation-contraction coupling. It was possible to restore stability to a model based on a bilayer-derived gating scheme, by introducing allosteric interactions between nearest-neighbor RyRs so as to stabilize the inactivated state and produce cooperativity among calcium binding sites on different RyRs. Such allosteric coupling between RyRs may be a function of the foot process and lattice array, explaining their conservation during evolution.

Indexed as

AlgorithmsAnimalsCalcium ChannelsCalcium Channels, L-TypeComputer SimulationEnergy MetabolismHeartIon Channel GatingModels, BiologicalMonte Carlo MethodMuscle ProteinsMyocardial ContractionRatsRyanodine Receptor Calcium Release ChannelSarcoplasmic ReticulumCalcium ChannelsCalcium Channels, L-TypeMuscle ProteinsRyanodine Receptor Calcium Release Channel

Identifiers

PMID10051521
PMCPMC2222895
OpenAlexW2163736419

What OpenQuestion holds

Texttitle and abstract
LicenceCC BY-NC-SA
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.