Evidence map›Paper›PMID 8947029›Full record

ArticleThe EMBO journal1996

Myosin motors with artificial lever arms.

M Anson, M A Geeves, S E Kurzawa, D J Manstein

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

45 citing papers in PubMed, 146 citations in OpenAlex.

  1. Kidney international reports · 2026
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  6. Review
  7. Phenamacril is a reversible and noncompetitive inhibitor ofThe Journal of biological chemistry · 2019
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Nonmuscle myosin-2: mix and match.Cellular and molecular life sciences : CMLS · 2013
    Review
  15. Article
  16. Article
  17. Article
  18. Functional characterization of the human myosin-7a motor domain.Cellular and molecular life sciences : CMLS · 2012
    Article
  19. Article
  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

4 authors at 1 institution in 1 country.

M AnsonNational Institute for Medical Research, London, UK.
M A Geeves
S E Kurzawa
D J Manstein
Max Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The myosin head consists of a globular catalytic domain and a light chain binding domain (LCBD). The coupling efficiency between ATP hydrolysis and myosin-induced actin movement is known to decline as the LCBD is truncated or destabilized. However, it was not clear whether the observed alteration in the production of force and movement reflects only the mechanical changes to the length of the LCBD or whether these changes also affect the kinetic properties of the catalytic domain. Here we show that replacement of the LCBD with genetically engineered domains of similar rigidity and dimensions produces functional molecular motors with unchanged kinetic properties. The resulting single-chain, single-headed motors were produced in Dictyostelium discoideum and obtained after purification from a standard peptone-based growth medium at levels of up to 12 mg/l. Their actin motility properties are similar or greater than those of native myosin. Rates of 2.5 and 3.3 microm/s were observed for motor domains fused to one or two of these domains, respectively. Their kinetic and functional similarity to the extensively studied myosin subfragment 1 (S1) and their accessibility to molecular genetic approaches makes these simple constructs ideal models for the investigation of chemo-mechanical coupling in the myosin motor.

Indexed as

Actin CytoskeletonActininActinsAdenosine TriphosphateAnimalsDictyosteliumKineticsMass SpectrometryModels, MolecularMyosin Light ChainsProtein BindingProtein FoldingRecombinant ProteinsSpectrometry, FluorescenceActininActinsAdenosine TriphosphateMyosin Light ChainsRecombinant Proteins

Identifiers

PMID8947029
PMCPMC452428
OpenAlexW1514691814

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.