Evidence map›Paper›PMID 30082313›Full record

ArticleThe Journal of biological chemistry2018

Structural and functional effects of myosin-binding protein-C phosphorylation in heart muscle are not mimicked by serine-to-aspartate substitutions.

Thomas Kampourakis, Saraswathi Ponnam, Yin-Biao Sun, Ivanka Sevrieva, Malcolm Irving

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. From bedside to bench: A multimodal approach uncovering the molecular basis of theProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  4. In situ FRET-based localization of the N terminus of myosin binding protein-C in heart muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  12. MyBP-C: one protein to govern them all.Journal of muscle research and cell motility · 2020
    Review
  13. Article
  14. Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Cardiac myosin binding protein-C phosphorylation regulates the super-relaxed state of myosin.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019
    Review
  17. 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

5 authors at 1 institution in 1 country.

Thomas KampourakisFrom the Randall Centre for Cell and Molecular Biophysics and British Heart Foundation Centre of Research Excellence, School of Basic and Medical Biosciences, King's College London, London SE1 1UL, United Kingdom thomas.kampourakis@kcl.ac.uk.
Saraswathi PonnamFrom the Randall Centre for Cell and Molecular Biophysics and British Heart Foundation Centre of Research Excellence, School of Basic and Medical Biosciences, King's College London, London SE1 1UL, United Kingdom.
Yin-Biao SunFrom the Randall Centre for Cell and Molecular Biophysics and British Heart Foundation Centre of Research Excellence, School of Basic and Medical Biosciences, King's College London, London SE1 1UL, United Kingdom.
Ivanka SevrievaFrom the Randall Centre for Cell and Molecular Biophysics and British Heart Foundation Centre of Research Excellence, School of Basic and Medical Biosciences, King's College London, London SE1 1UL, United Kingdom.
Malcolm IrvingFrom the Randall Centre for Cell and Molecular Biophysics and British Heart Foundation Centre of Research Excellence, School of Basic and Medical Biosciences, King's College London, London SE1 1UL, United Kingdom.
British Heart Foundation · GB

Funding

British Heart Foundation FS/15/1/31071British Heart Foundation FS/16/3/31887British Heart Foundation PG/12/52/29713British Heart Foundation PG/16/19/32072Medical Research Council G0601065Medical Research Council MR/M026655/1
6 · The paper itself

Abstract

Myosin-binding protein-C (cMyBP-C) is a key regulator of contractility in heart muscle, and its regulatory function is controlled in turn by phosphorylation of multiple serines in its m-domain. The structural and functional effects of m-domain phosphorylation have often been inferred from those of the corresponding serine-to-aspartate (Ser-Asp) substitutions, in both

Indexed as

Amino Acid SubstitutionAmino Acid SequenceAnimalsAspartic AcidCalciumCarrier ProteinsKineticsMaleMusclesMyocardiumMyosin Binding Protein CMyosinsPhosphorylationProtein BindingRatsRats, WistarAspartic AcidCalciumCarrier ProteinsMyosin Binding Protein CMyosinsSerinecardiac musclecardiac muscle regulationmusclemyofibrilmyosinmyosin-binding protein-Cphosphomimeticphosphorylationpolarized fluorescence muscle fiberprotein phosphorylationtris-phosphorylation

Identifiers

PMID30082313
PMCPMC6139572
OpenAlexW2887893790

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.