Evidence map›Paper›PMID 27782102›Full record

ArticleNature communications2016

Disulfide-activated protein kinase G Iα regulates cardiac diastolic relaxation and fine-tunes the Frank-Starling response.

Jenna Scotcher, Oleksandra Prysyazhna, Andrii Boguslavskyi, Kornel Kistamas, Natasha Hadgraft, Eva D Martin, Jenny Worthington, Olena Rudyk, Pedro Rodriguez Cutillas, Friederike Cuello and 8 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Targeting PKGIα CysScience advances · 2026
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  6. Review
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  10. Review
  11. cGMP Signaling and Modulation in Heart Failure.Journal of cardiovascular pharmacology · 2020
    Review
  12. Review
  13. Article
  14. Article
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  16. Article
  17. Article
  18. Article
  19. Review
  20. Reduced SERCA activity underlies dysregulation of CaFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    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

18 authors at 7 institutions in 2 countries.

Jenna ScotcherKing's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
Oleksandra PrysyazhnaKing's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
Andrii BoguslavskyiKing's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
Kornel KistamasInstitute of Cardiovascular Sciences, Manchester Academic Health Science Centre, Core Technology Facility, University of Manchester, 46 Grafton Street, Manchester M13 9NT, UK.
Natasha HadgraftBiomedical Research Centre, University of Salford, Peel Building, Salford Crescent M5 4WT, UK.
Eva D MartinKing's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
Jenny WorthingtonInstitute for Women's Health, University College London, Gower Street, London WC1E 6BT, UK.
Olena RudykKing's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
Pedro Rodriguez CutillasBarts Cancer Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK.ORCID 0000-0002-3426-2274
Friederike CuelloDepartment of Experimental Pharmacology and Toxicology, Cardiovascular Research Centre, University Medical Center Hamburg-Eppendorf, Hamburg, DZHK (German Centre for Cardiovascular Research), Partner site Hamburg/Kiel/Lübeck, Hamburg 20246, Germany.
Michael J ShattockKing's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
Michael S MarberKing's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
Maria R ConteRandall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.ORCID 0000-0001-8558-2051
Adam GreensteinInstitute of Cardiovascular Sciences, Manchester Academic Health Science Centre, Core Technology Facility, University of Manchester, 46 Grafton Street, Manchester M13 9NT, UK.
David J GreensmithBiomedical Research Centre, University of Salford, Peel Building, Salford Crescent M5 4WT, UK.
Luigi VenetucciInstitute of Cardiovascular Sciences, Manchester Academic Health Science Centre, Core Technology Facility, University of Manchester, 46 Grafton Street, Manchester M13 9NT, UK.
John F TimmsInstitute for Women's Health, University College London, Gower Street, London WC1E 6BT, UK.
Philip EatonKing's College London, Cardiovascular Division, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, London SE1 7EH, UK.
St Thomas' Hospital · GBManchester Academic Health Science Centre · GBUniversity College London · GBUniversity of Salford · GBKing's College London · GBQueen Mary University of London · GBUniversität Hamburg · DE

Funding

British Heart Foundation FS/10/42/28372British Heart Foundation FS/10/63/28374British Heart Foundation FS/11/68/28821British Heart Foundation FS/12/81/29882British Heart Foundation FS/14/26/30767British Heart Foundation PG/15/109/31931British Heart Foundation RG/12/4/29426European Research CouncilMedical Research Council G0700320Wellcome Trust
6 · The paper itself

Abstract

The Frank-Starling mechanism allows the amount of blood entering the heart from the veins to be precisely matched with the amount pumped out to the arterial circulation. As the heart fills with blood during diastole, the myocardium is stretched and oxidants are produced. Here we show that protein kinase G Iα (PKGIα) is oxidant-activated during stretch and this form of the kinase selectively phosphorylates cardiac phospholamban Ser16-a site important for diastolic relaxation. We find that hearts of Cys42Ser PKGIα knock-in (KI) mice, which are resistant to PKGIα oxidation, have diastolic dysfunction and a diminished ability to couple ventricular filling with cardiac output on a beat-to-beat basis. Intracellular calcium dynamics of ventricular myocytes isolated from KI hearts are altered in a manner consistent with impaired relaxation and contractile function. We conclude that oxidation of PKGIα during myocardial stretch is crucial for diastolic relaxation and fine-tunes the Frank-Starling response.

Indexed as

AnimalsBiomechanical PhenomenaCalciumCalcium-Binding ProteinsCardiac OutputCyclic GMP-Dependent Protein Kinase Type IDiastoleDisulfidesGene Expression ProfilingGene Expression RegulationGene Knock-In TechniquesHeart VentriclesMaleMiceMice, Inbred C57BLMyocardial ContractionCalciumCalcium-Binding ProteinsCyclic GMP-Dependent Protein Kinase Type IDisulfidesPhospholambanSerine

Identifiers

PMID27782102
PMCPMC5095173
OpenAlexW2542799164

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.