Evidence map›Paper›PMID 12719246›Full record

ArticleBiophysical journal2003

Cooperative regulation of myosin-actin interactions by a continuous flexible chain II: actin-tropomyosin-troponin and regulation by calcium.

D A Smith, M A Geeves

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.8field-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

58 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Effect of Myosin Isoforms on Cardiac Muscle Twitch of Mice, Rats and Humans.International journal of molecular sciences · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Spectrum ofGenes · 2021
    Article
  10. Mechanical contribution to muscle thin filament activation.The Journal of biological chemistry · 2020
    Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. High-speed AFM reveals subsecond dynamics of cardiac thin filaments upon CaProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Article
  18. Article
  19. Review
  20. 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

2 authors at 2 institutions in 1 country.

D A SmithRandall Centre, King's College London, Guy's Campus, London SE1 1UL, UK.
M A Geeves
King's College London · GBUniversity of Kent · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The model of myosin regulation by a continuous tropomyosin chain is generalized to a chain of tropomyosin-troponin units. Myosin binding to regulated actin is cooperative and initially inhibited by the chain as before. In the absence of calcium, myosin is further inhibited by the binding of troponin-I to actin, which through the whole of troponin pins the tropomyosin chain in a blocking position; myosin and TnI compete for actin and induce oppositely-directed chain kinks. The model predicts equilibrium binding curves for myosin-S1 and TnI as a function of their first-order affinities K(S1) and L(TI). Myosin is detached by the actin binding of TnI, but TnI is more efficiently detached by myosin when the kink size (typically nine to ten actin sites) spans the seven-site spacing between adjacent TnI molecules. An allosteric mechanism is used for coupling the detachment of TnI to calcium binding by TnC. With thermally activated TnI kinks (kink energy B approximately k(B)T), TnI also binds cooperatively to actin, producing cooperative detachment of myosin and biphasic myosin-calcium Hill plots, with Hill coefficients of 2 at high calcium and 4-6 at low calcium as observed in striated muscle. The theory also predicts the cooperative effects observed in the calcium loading of TnC.

Indexed as

Models, BiologicalActinsBinding SitesCalciumComputer SimulationFeedbackHomeostasisMacromolecular SubstancesModels, ChemicalModels, MolecularMolecular Motor ProteinsMotionMuscle ContractionMyosinsProtein BindingProtein ConformationActinsCalciumMacromolecular SubstancesMolecular Motor ProteinsMyosinsTropomyosinTroponin

Identifiers

PMID12719246
PMCPMC1302877
OpenAlexW1999457478

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.