Evidence map›Paper›PMID 30641143›Full record

ArticleJournal of structural biology2019

The FKBP12 subunit modifies the long-range allosterism of the ryanodine receptor.

Tyler W E Steele, Montserrat Samsó

Abstract read
In one paragraph

Article in Journal of structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Interplay between MgNature communications · 2024
    Article
  7. Review
  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. Review
  11. Molecular mechanism of the severe MH/CCD mutation Y522S in skeletal ryanodine receptor (RyR1) by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. CaeLife · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. 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

2 authors.

Tyler W E SteeleDepartment of Physiology and Biophysics, Virginia Commonwealth University, Richmond, VA 23298, United States.
Montserrat SamsóDepartment of Physiology and Biophysics, Virginia Commonwealth University, Richmond, VA 23298, United States. Electronic address: montserrat.samso@vcuhealth.org.

Funding

RyR architecture and gatekeeping of internal calcium storesR01AR068431 · NIAMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI SAMSO, MONTSERRAT · 2017 to 2021
$2.0M
Mechanistic Insight of Premature Ventricular Contractions-induced CardiomyopathyR56HL133182 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI HUIZAR, JOSE FRANCISCO · 2016 to 2016
$507k
NHLBI NIH HHS R56 HL133182NIAMS NIH HHS R01 AR068431
6 · The paper itself

Abstract

Ryanodine receptors (RyRs) are large conductance intracellular channels controlling intracellular calcium homeostasis in myocytes, neurons, and other cell types. Loss of RyR's constitutive cytoplasmic partner FKBP results in channel sensitization, dominant subconductance states, and increased cytoplasmic Ca

Indexed as

AnimalsCryoelectron MicroscopyHumansProtein BindingRyanodine Receptor Calcium Release ChannelTacrolimus Binding Protein 1ARyanodine Receptor Calcium Release ChannelTacrolimus Binding Protein 1ACalciumCryo-electron microscopyExcitation-contraction couplingFKBP12Ryanodine receptor

Identifiers

PMID30641143
PMCPMC6494473

What OpenQuestion holds

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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.