Evidence map›Paper›PMID 24520162›Full record

ArticleeLife2014

Small molecule-mediated refolding and activation of myosin motor function.

Michael B Radke, Manuel H Taft, Britta Stapel, Denise Hilfiker-Kleiner, Matthias Preller, Dietmar J Manstein

Abstract readVideo-Audio Media
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Understanding hypertrophic cardiomyopathy and its regulation by myosin drugs.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Predominant myosin superrelaxed state in canine myocardium with naturally occurring dilated cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2023
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Treatments targeting inotropy.European heart journal · 2019
    Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Michael B RadkeInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Manuel H Taft
Britta Stapel
Denise Hilfiker-Kleiner
Matthias Preller
Dietmar J Manstein

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small molecule EMD 57033 has been shown to stimulate the actomyosin ATPase activity and contractility of myofilaments. Here, we show that EMD 57033 binds to an allosteric pocket in the myosin motor domain. EMD 57033-binding protects myosin against heat stress and thermal denaturation. In the presence of EMD 57033, ATP hydrolysis, coupling between actin and nucleotide binding sites, and actin affinity in the presence of ATP are increased more than 10-fold. Addition of EMD 57033 to heat-inactivated β-cardiac myosin is followed by refolding and reactivation of ATPase and motile activities. In heat-stressed cardiomyocytes expression of the stress-marker atrial natriuretic peptide is suppressed by EMD 57033. Thus, EMD 57033 displays a much wider spectrum of activities than those previously associated with small, drug-like compounds. Allosteric effectors that mediate refolding and enhance enzymatic function have the potential to improve the treatment of heart failure, myopathies, and protein misfolding diseases. DOI: http://dx.doi.org/10.7554/eLife.01603.001.

Indexed as

ActinsAdenosine TriphosphateAllosteric RegulationAnimalsAnimals, NewbornBinding SitesCardiac MyosinsCardiotonic AgentsCatalytic DomainCells, CulturedDictyosteliumDose-Response Relationship, DrugEnzyme ActivationEnzyme ActivatorsHumansHydrolysisActinsAdenosine TriphosphateCardiac MyosinsCardiotonic AgentsEMD 53998Enzyme ActivatorsQuinolinesRecombinant ProteinsThiadiazinesallosterymyosinpharmacological chaperoneprotein folding

Identifiers

PMID24520162
PMCPMC3920478

What OpenQuestion holds

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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.