Evidence map›Paper›PMID 20837775›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2011

Myosin cleft closure determines the energetics of the actomyosin interaction.

Balázs Takács, Elizabeth O'Neall-Hennessey, Csaba Hetényi, József Kardos, Andrew G Szent-Györgyi, Mihály Kovács

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Homologous mutations in human β, embryonic, and perinatal muscle myosins have divergent effects on molecular power generation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  4. Article
  5. Molecular mechanisms underlying deoxy-ADP.Pi activation of pre-powerstroke myosin.Protein science : a publication of the Protein Society · 2017
    Article
  6. Article
  7. Cell shape regulation through mechanosensory feedback control.Journal of the Royal Society, Interface · 2015
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

6 authors at 2 institutions in 2 countries.

Balázs TakácsDepartment of Biochemistry, Eötvös University, Pázmány Péter sétány 1/c, H-1117 Budapest, Hungary.
Elizabeth O'Neall-Hennessey
Csaba Hetényi
József Kardos
Andrew G Szent-Györgyi
Mihály Kovács
Eötvös Loránd University · HUBrandeis University · US

Funding

Emerging New Types of MotilityR01TW007241 · FIC · EOTVOS LORAND UNIVERSITY · PI KOVACS, MIHALY · 2005 to 2009
$260k
FIC NIH HHS 1 R01-TW-007241FIC NIH HHS R01 TW007241Howard Hughes Medical Institute
6 · The paper itself

Abstract

Formation of the strong binding interaction between actin and myosin is essential for force generation in muscle and in cytoskeletal motor systems. To clarify the role of the closure of myosin's actin-binding cleft in the actomyosin interaction, we performed rapid kinetic, spectroscopic, and calorimetric experiments and atomic-level energetic calculations on a variety of myosin isoforms for which atomic structures are available. Surprisingly, we found that the endothermic actin-binding profile of vertebrate skeletal muscle myosin subfragment-1 is unique among studied myosins. We show that the diverse propensity of myosins for cleft closure determines different energetic profiles as well as structural and kinetic pathways of actin binding. Depending on the type of myosin, strong actin binding may occur via induced-fit or conformational preselection mechanisms. However, cleft closure does not directly determine the kinetics and affinity of actin binding. We also show that cleft closure is enthalpically unfavorable, reflecting the development of an internal strain within myosin in order to adopt precise steric complementarity to the actin filament. We propose that cleft closure leads to an increase in the torsional strain of myosin's central β-sheet that has been proposed to serve as an allosteric energy-transducing spring during force generation.

Indexed as

ActinsActomyosinAnimalsBinding SitesCalorimetryKineticsMuscle, SkeletalMyosinsMyosin SubfragmentsProtein BindingRabbitsSpectrometry, FluorescenceTemperatureActinsActomyosinMyosinsMyosin Subfragments

Identifiers

PMID20837775
PMCPMC3005428
OpenAlexW2004332434

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.