Evidence map›Paper›PMID 35356048›Full record

ArticleCurrent research in physiology2022

Regulation of cardiac ryanodine receptor function by the cyclic-GMP dependent protein kinase G.

Luis A Gonano, Hamish M Aitken-Buck, Akash D Chakraborty, Luke P I Worthington, Tanya R Cully, Regis R Lamberts, Martin G Vila-Petroff, Peter P Jones

Open access · goldAbstract read
In one paragraph

Article in Current research in physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
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  4. Insulin resistance, CaFrontiers in physiology · 2025
    Review
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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

8 authors at 2 institutions in 2 countries.

Luis A GonanoDepartment of Physiology, HeartOtago, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Hamish M Aitken-BuckDepartment of Physiology, HeartOtago, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Akash D ChakrabortyDepartment of Physiology, HeartOtago, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Luke P I WorthingtonDepartment of Physiology, HeartOtago, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Tanya R CullyDepartment of Physiology, HeartOtago, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Regis R LambertsDepartment of Physiology, HeartOtago, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
Martin G Vila-PetroffCentro de Investigaciones Cardiovasculares Horacio E. Cingolani. CONICET-UNLP, Argentina.
Peter P JonesDepartment of Physiology, HeartOtago, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.
University of Otago · NZCentro de Investigaciones Cardiovasculares · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: The cGMP-dependent protein kinase G (PKG) phosphorylates the cardiac ryanodine receptor (RyR2) Methods: & Results: Human embryonic kidney (HEK293) cells with inducible RyR2 expression were treated with the cGMP analogue 8-Br-cGMP (100 μM) to activate endogenous PKG. In cells transfected with luminal Ca Conclusion: In an intact cell model, activation of endogenous PKG reduces the threshold for RyR2-mediated spontaneous Ca

Indexed as

CalciumCardiac ryanodine receptorKT 5823PhosphorylationProtein kinase GStore overload-induced calcium release

Identifiers

PMID35356048
PMCPMC8958330
OpenAlexW4220967680

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.