Evidence map›Paper›PMID 30928430›Full record

ArticleJournal of molecular and cellular cardiology2019

Calmodulin inhibition of human RyR2 channels requires phosphorylation of RyR2-S2808 or RyR2-S2814.

Kafa Walweel, Nieves Gomez-Hurtado, Robyn T Rebbeck, Ye Wint Oo, Nicole A Beard, Peter Molenaar, Cris Dos Remedios, Dirk F van Helden, Razvan L Cornea, Björn C Knollmann and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular and cellular cardiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. βNaunyn-Schmiedeberg's archives of pharmacology · 2026
    Article
  2. Review
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  4. Article
  5. Article
  6. Article
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  8. Article
  9. Targeting p21-activated kinase 1 for development of a novel anti-arrhythmic drug class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  10. Role of CaArchives of toxicology · 2023
    Review
  11. Article
  12. Article
  13. Synergistic FRET assays for drug discovery targeting RyR2 channels.Journal of molecular and cellular cardiology · 2022
    Article
  14. Article
  15. Review
  16. Review
  17. Calmodulin Mutations Associated with Heart Arrhythmia: A Status Report.International journal of molecular sciences · 2020
    Review
  18. 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

11 authors at 6 institutions in 2 countries.

Kafa WalweelSchool of Biomedical Sciences and Pharmacy, University of Newcastle and Hunter Medical Research Institute, Callaghan, NSW 2308, Australia. Electronic address: kwalweel2002@yahoo.com.
Nieves Gomez-HurtadoVanderbilt Center for Arrhythmia Research and Therapeutics, Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA. Electronic address: mlngomez@ucm.es.
Robyn T RebbeckDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, USA. Electronic address: rrebbeck@umn.edu.
Ye Wint OoSchool of Biomedical Sciences and Pharmacy, University of Newcastle and Hunter Medical Research Institute, Callaghan, NSW 2308, Australia.
Nicole A BeardFaculty of Science and Technology, University of Canberra, Bruce, ACT 2617, Australia. Electronic address: nicole.beard@canberra.edu.au.
Peter MolenaarSchool of Biomedical Sciences, Queensland University of Technology, Brisbane, QLD 4000, Australia; Northside Clinical School of Medicine, University of Queensland, Cardio-vascular Molecular & Therapeutics Translational Research Group, The Prince Charles Hospital, Chermside, QLD 4032. Australia. Electronic address: peter.molenaar@qut.edu.au.
Cris Dos RemediosBosch Institute, Discipline of Anatomy, University of Sydney, Sydney, New South Wales 2006, Australia. Electronic address: crisdos@anatomy.usyd.edu.au.
Dirk F van HeldenSchool of Biomedical Sciences and Pharmacy, University of Newcastle and Hunter Medical Research Institute, Callaghan, NSW 2308, Australia. Electronic address: dirk.vanhelden@newcastle.edu.au.
Razvan L CorneaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, USA. Electronic address: corne002@umn.edu.
Björn C KnollmannVanderbilt Center for Arrhythmia Research and Therapeutics, Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA. Electronic address: bjorn.knollmann@vanderbilt.edu.
Derek R LaverSchool of Biomedical Sciences and Pharmacy, University of Newcastle and Hunter Medical Research Institute, Callaghan, NSW 2308, Australia. Electronic address: Derek.Laver@newcastle.edu.au.
Hunter Medical Research Institute · AUUniversity of Minnesota · USVanderbilt University Medical Center · USQueensland University of Technology · AUThe University of Sydney · AUUniversity of Canberra · AU

Funding

Pathophysiological Regulation of Cardiac Myocyte RyR ChannelR01HL092097 · NHLBI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Donald M Bers, Robyn T Rebbeck · 2010 to 2026
$9.3M
Toward a Mechanism-Based Approach to Treating Cardiac ArrhythmiaR35HL144980 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI KNOLLMANN, BJORN C · 2019 to 2025
$7.1M
High-Throughput Screens to Discover Novel Inhibitors of Leaky RyR2 for Heart Failure TherapyR01HL138539 · NHLBI · UNIVERSITY OF MINNESOTA · PI BERS, DONALD M, CORNEA, RAZVAN LIVIU · 2018 to 2021
$3.1M
Toward a Mechanism-Based Approach to Treating Atrial FibrillationR01HL124935 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI KNOLLMANN, BJORN C · 2015 to 2019
$2.8M
NHLBI NIH HHS R01 HL092097NHLBI NIH HHS R01 HL124935NHLBI NIH HHS R01 HL138539NHLBI NIH HHS R35 HL144980
6 · The paper itself

Abstract

Calmodulin (CaM) is a Ca-binding protein that binds to, and can directly inhibit cardiac ryanodine receptor calcium release channels (RyR2). Animal studies have shown that RyR2 hyperphosphorylation reduces CaM binding to RyR2 in failing hearts, but data are lacking on how CaM regulates human RyR2 and how this regulation is affected by RyR2 phosphorylation. Physiological concentrations of CaM (100 nM) inhibited the diastolic activity of RyR2 isolated from failing human hearts by ~50% but had no effect on RyR2 from healthy human hearts. Using FRET between donor-FKBP12.6 and acceptor-CaM bound to RyR2, we determined that CaM binds to RyR2 from healthy human heart with a K

Indexed as

Calcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinCyclic AMP-Dependent Protein KinasesHeart FailureHumansMyocytes, CardiacPhosphorylationProtein BindingRyanodine Receptor Calcium Release ChannelCalcium-Calmodulin-Dependent Protein Kinase Type 2CalmodulinCyclic AMP-Dependent Protein KinasesRyanodine Receptor Calcium Release ChannelRyR2 protein, humanCalcium sparksCalmodulinCardiomyopathyLipid bilayerPhosphorylationRyanodine receptor

Identifiers

PMID30928430
PMCPMC6791359
OpenAlexW2922771874

What OpenQuestion holds

Textmetadata
LicenceTDM
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.