Evidence map›Paper›PMID 22089698›Full record

ReviewJournal of muscle research and cell motility2012

cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.

Sonya C Bardswell, Friederike Cuello, Jonathan C Kentish, Metin Avkiran

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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
  10. Article
  11. Cardiac myosin binding protein-C SerScience advances · 2017
    Article
  12. Article
  13. Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. Myosin light chain phosphorylation enhances contraction of heart muscle via structural changes in both thick and thin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  17. The genetic basis of hypertrophic cardiomyopathy in cats and humans.Journal of veterinary cardiology : the official journal of the European Society of Veterinary Cardiology · 2015
    Review
  18. Review
  19. Article
  20. 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

4 authors.

Sonya C BardswellCardiovascular Division, King's College London British Heart Foundation Centre of Research Excellence, The Rayne Institute, St Thomas' Hospital, London, UK.
Friederike Cuello
Jonathan C Kentish
Metin Avkiran

Funding

British Heart Foundation FS/03/091British Heart Foundation PG/03/053British Heart Foundation PG/05/043British Heart Foundation PG/07/056/23150British Heart Foundation PG/08/064/25398British Heart Foundation PG/11/100/29211British Heart Foundation PG/11/9/28705Medical Research Council G0001112Medical Research Council G0001227Medical Research Council G0300052Medical Research Council G0800206
6 · The paper itself

Abstract

It is now generally accepted that phosphorylation of cMyBP-C is critically important in maintaining normal cardiac function. Although much of the work to date on phospho-regulation of cMyBP-C has focused on the role of protein kinase A (PKA, also known as cAMP-dependent protein kinase), recent evidence suggests that a number of non-PKA serine/threonine kinases, such as Ca(2+)/calmodulin-dependent protein kinase II, protein kinase C, protein kinase D and the 90-kDa ribosomal S6 kinase are also capable of targeting this key regulatory sarcomeric protein. This article reviews such evidence and proposes a hypothetical role for some of the pertinent signalling pathways in phospho-regulation of cMyBP-C in the setting of heart failure.

Indexed as

Signal TransductionAnimalsBinding SitesCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Carrier ProteinsCyclic AMP-Dependent Protein KinasesHeart FailureHumansMyofibrilsMyosin Binding Protein CPhosphorylationProtein Kinase CRibosomal Protein S6 Kinases, 90-kDaSubstrate SpecificityCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Carrier ProteinsCyclic AMP-Dependent Protein KinasesMyosin Binding Protein CProtein Kinase Cprotein kinase DRibosomal Protein S6 Kinases, 90-kDa

Identifiers

What OpenQuestion holds

Textmetadata
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.