Evidence map›Paper›PMID 8134386›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Biochemical evidence for a complex involving dihydropyridine receptor and ryanodine receptor in triad junctions of skeletal muscle.

I Marty, M Robert, M Villaz, K De Jongh, Y Lai, W A Catterall, M Ronjat

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

66 citing papers in PubMed, 156 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Review
  8. Huntingtin regulates calcium fluxes in skeletal muscle.The Journal of general physiology · 2023
    Article
  9. Review
  10. In vivo RyR1 reduction in muscle triggers a core-like myopathy.Acta neuropathologica communications · 2020
    Article
  11. Article
  12. Article
  13. Interplay between Triadin and Calsequestrin in the Pathogenesis of CPVT in the Mouse.Molecular therapy : the journal of the American Society of Gene Therapy · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

6 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 2 countries.

I MartyDépartement de Biologie Moléculaire et Structurale, CENG 85X, Grenoble, France.
M Robert
M Villaz
K De Jongh
Y Lai
W A Catterall
M Ronjat
Laboratoire de Génétique Cellulaire · FRUniversity of Washington · US

Funding

MOLECULAR PROPERTIES OF VOLTAGE-SENSITIVE CHANNELSR01NS022625 · NINDS · UNIVERSITY OF WASHINGTON · PI CATTERALL, WILLIAM A · 1985 to 2019
$6.2M
NINDS NIH HHS NS22625
6 · The paper itself

Abstract

Membrane vesicles enriched in both ryanodine receptor and dihydropyridine receptor were obtained from rabbit skeletal muscle and solubilized with 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate. Analysis of the sedimentation behavior of the solubilized proteins showed the existence of a population of alpha 1 subunits of the dihydropyridine receptor which cosedimented with the ryanodine receptor. Solubilized proteins were immunoprecipitated with antibodies directed against either the ryanodine receptor or the alpha 1, alpha 2, or beta subunits of the dihydropyridine receptor. Immunoprecipitated proteins were identified by Western blot analysis and by specific labeling with [3H]ryanodine or [3H]PN200-110. Immunoprecipitation of the solubilized proteins with antibodies directed against the dihydropyridine receptor led to the coimmunoprecipitation of the ryanodine receptor. Conversely, immunoprecipitation with antibodies directed against the ryanodine receptor led to an immune complex containing both receptors, but these antibodies were unable to precipitate purified dihydropyridine receptor. These results demonstrate that ryanodine receptor and dihydropyridine receptor are present in the triad membrane preparation in a complex which may play an important role in excitation-contraction coupling.

Indexed as

AnimalsBlotting, WesternCalcium ChannelsCalcium Channels, L-TypeMuscle ContractionMuscle ProteinsMusclesPrecipitin TestsRabbitsRyanodine Receptor Calcium Release ChannelSolubilityCalcium ChannelsCalcium Channels, L-TypeMuscle ProteinsRyanodine Receptor Calcium Release Channel

Identifiers

PMID8134386
PMCPMC43352
OpenAlexW1997050207

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.