Evidence map›Paper›PMID 2143196›Full record

ArticleThe Journal of cell biology1990

Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin.

D H Schwyter, S J Kron, Y Y Toyoshima, J A Spudich, E Reisler

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

29 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. International journal of molecular sciences · 2022
    Article
  3. Article
  4. Article
  5. Actin filaments as tension sensors.Current biology : CB · 2012
    Review
  6. Remodeling of actin filaments by ADF/cofilin proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  7. Article
  8. Structural polymorphism in F-actin.Nature structural & molecular biology · 2010
    Article
  9. Article
  10. Article
  11. Article
  12. Large-scale models reveal the two-component mechanics of striated muscle.International journal of molecular sciences · 2008
    Article
  13. Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

5 authors at 1 institution in 1 country.

D H SchwyterDepartment of Chemistry and Biochemistry, University of California, Los Angeles 90024.
S J Kron
Y Y Toyoshima
J A Spudich
E Reisler
University of California, Los Angeles · US

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
DYNAMIC EVENTS IN MYOSIN DURING CONTRACTION OF MUSCLER01AR022031 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 1986 to 2004
$2.5M
NIAMS NIH HHS AR 22031NIAMS NIH HHS R01 AR022031NIGMS NIH HHS GM 33289
6 · The paper itself

Abstract

Subtilisin cleaved actin was shown to retain several properties of intact actin including the binding of heavy meromyosin (HMM), the dissociation from HMM by ATP, and the activation of HMM ATPase activity. Similar Vmax but different Km values were obtained for acto-HMM ATPase with the cleaved and intact actins. The ATPase activity of HMM stimulated by copolymers of intact and cleaved actin showed a linear dependence on the fraction of intact actin in the copolymer. The most important difference between the intact and cleaved actin was observed in an in vitro motility assay for actin sliding movement over an HMM coated surface. Only 30% of the cleaved actin filaments appeared mobile in this assay and moreover, the velocity of the mobile filaments was approximately 30% that of intact actin filaments. These results suggest that the motility of actin filaments can be uncoupled from the activation of myosin ATPase activity and is dependent on the structural integrity of actin and perhaps, dynamic changes in the actin molecule.

Indexed as

Actin CytoskeletonActinsCytoskeletonEnzyme ActivationKineticsLightMicroscopy, ElectronMyosinsMyosin SubfragmentsProtein BindingScattering, RadiationSubtilisinsActinsMyosinsMyosin SubfragmentsSubtilisins

Identifiers

PMID2143196
PMCPMC2116201
OpenAlexW2151191962

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.