Evidence map›Paper›PMID 8994600›Full record

ArticleBiophysical journal1997

Subconductance states in single-channel activity of skeletal muscle ryanodine receptors after removal of FKBP12.

G P Ahern, P R Junankar, A F Dulhunty

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

55 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. FKBP12 binds to the cardiac ryanodine receptor with negative cooperativity: implications for heart muscle physiology in health and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  10. How does flecainide impact RyR2 channel function?The Journal of general physiology · 2022
    Article
  11. Review
  12. Article
  13. SR CaThe Journal of general physiology · 2019
    Article
  14. Dysregulated mitochondrial CaArchives of biochemistry and biophysics · 2019
    Review
  15. Article
  16. Changes in Redox Signaling in the Skeletal Muscle with Aging.Oxidative medicine and cellular longevity · 2019
    Review
  17. Article
  18. Review
  19. Article
  20. A guide to the 3D structure of the ryanodine receptor type 1 by cryoEM.Protein science : a publication of the Protein Society · 2017
    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

3 authors at 1 institution in 1 country.

G P AhernDivision of Neuroscience, John Curtin School of Medical Research, Australian National University, Canberra, Australia.
P R Junankar
A F Dulhunty
Australian National University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FKBP12 was removed from ryanodine receptors (RyRs) by incubation of rabbit skeletal muscle terminal cisternae membranes with rapamycin. The extent of FKBP12 removal was estimated by immunostaining Western blots of terminal cisternae proteins. Single FKBP12-depleted RyR channels, incorporated into planar lipid bilayers, were modulated by Ca2+, ATP, ryanodine, and ruthenium red in the cis chamber and opened frequently to the normal maximum conductance of approximately 230 pS and to substate levels of approximately 0.25, approximately 0.5, and approximately 0.75 of the maximum conductance. Substate activity was rarely seen in native RyRs. Ryanodine did not after the number of conductance levels in FKBP12-depleted channels, but, at a membrane potential of +40 mV, reduced both the maximum and the substate conductances by approximately 50%. FKBP12-stripped channels were activated by a 10-fold-lower [Ca2+] and inhibited by a 10-fold-higher [Ca2+], than RyRs from control-incubated and native terminal cisternae vesicles. The open probability (Po) of these FKBP12-deficient channels was greater than that of control channels at 0.1 microM and 1 mM cis Ca2+ but no different at 10 microM cis Ca2+, where channels showed maximal Ca2+ activation. The approximately 0.25 substate was less sensitive than the maximum conductance to inhibition by Ca2+ and was the dominant level in channels inhibited by 1 mM cis Ca2+. The results show that FKBP12 coordinates the gating of channel activity in control and ryanodine-modified RyRs.

Indexed as

Lipid BilayersAdenosine TriphosphateAmino Acid SequenceAnimalsAntibodiesBlotting, WesternCalciumCalcium ChannelsCarrier ProteinsDNA-Binding ProteinsElectric ConductivityHeat-Shock ProteinsHumansImmunosuppressive AgentsIon Channel GatingMembrane PotentialsAdenosine TriphosphateAntibodiesCalciumCalcium ChannelsCarrier ProteinsDNA-Binding ProteinsHeat-Shock ProteinsImmunosuppressive AgentsLipid BilayersMuscle ProteinsPeptide FragmentsPolyenesRecombinant ProteinsRuthenium RedRyanodineRyanodine Receptor Calcium Release ChannelSirolimusTacrolimus Binding Proteins

Identifiers

PMID8994600
PMCPMC1184304
OpenAlexW1963674209

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.