Evidence map›Paper›PMID 10692315›Full record

ArticleBiophysical journal2000

Molecular cloning of cDNA encoding a drosophila ryanodine receptor and functional studies of the carboxyl-terminal calcium release channel.

X Xu, M B Bhat, M Nishi, H Takeshima, J Ma

Open access · bronzeAbstract 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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. eLife · 2026
    Article
  3. Article
  4. Modeling traveling calcium waves in cellular structures.Journal of computational neuroscience · 2025
    Article
  5. Article
  6. Maintenance of hematopoietic stem cell niche homeostasis requires gap junction-mediated calcium signaling.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Unnatural verticilide enantiomer inhibits type 2 ryanodine receptor-mediated calcium leak and is antiarrhythmic.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Dynamics expression ofCell & bioscience · 2019
    Article
  16. Article
  17. Review
  18. Article
  19. 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

5 authors at 2 institutions in 2 countries.

X XuDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
M B Bhat
M Nishi
H Takeshima
J Ma
University School · USThe University of Tokyo · JP

Funding

RYANODINE RECEPTOR OF E/C COUPLING IN STRIATED MUSCLESR01AG015556 · NIA · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI MA, JIANJIE · 1997 to 2006
$2.6M
NIA NIH HHS R01-AG15556
6 · The paper itself

Abstract

Ryanodine is a plant alkaloid that was originally used as an insecticide. To study the function and regulation of the ryanodine receptor (RyR) from insect cells, we have cloned the entire cDNA sequence of RyR from the fruit fly Drosophila melanogaster. The primary sequence of the Drosophila RyR contains 5134 amino acids, which shares approximately 45% identity with RyRs from mammalian cells, with a large cytoplasmic domain at the amino-terminal end and a small transmembrane domain at the carboxyl-terminal end. To characterize the Ca(2+) release channel activity of the cloned Drosophila RyR, we expressed both full-length and a deletion mutant of Drosophila RyR lacking amino acids 277-3650 (Drosophila RyR-C) in Chinese hamster ovary cells. For subcellular localization of the expressed Drosophila RyR and Drosophila RyR-C proteins, green fluorescent protein (GFP)-Drosophila RyR and GFP-Drosophila RyR-C fusion constructs were generated. Confocal microscopic imaging identified GFP-Drosophila RyR and GFP-Drosophila RyR-C on the endoplasmic reticulum membranes of transfected cells. Upon reconstitution into the lipid bilayer membrane, Drosophila RyR-C formed a large conductance cation-selective channel, which was sensitive to modulation by ryanodine. Opening of the Drosophila RyR-C channel required the presence of microM concentration of Ca(2+) in the cytosolic solution, but the channel was insensitive to inhibition by Ca(2+) at concentrations as high as 20 mM. Our data are consistent with our previous observation with the mammalian RyR that the conduction pore of the calcium release channel resides within the carboxyl-terminal end of the protein and further demonstrate that structural and functional features are essentially shared by mammalian and insect RyRs.

Indexed as

Amino Acid SequenceAnimalsCHO CellsCloning, MolecularCricetinaeDNA, ComplementaryDNA PrimersDrosophila melanogasterGreen Fluorescent ProteinsIntracellular MembranesKineticsLuminescent ProteinsMammalsMembrane PotentialsMicrosomesMutagenesis, Site-DirectedDNA, ComplementaryDNA PrimersGreen Fluorescent ProteinsLuminescent ProteinsRecombinant Fusion ProteinsRecombinant ProteinsRyanodineRyanodine Receptor Calcium Release Channel

Identifiers

PMID10692315
PMCPMC1300728
OpenAlexW2079637246

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.