Evidence map›Paper›PMID 1734024›Full record

ArticleThe Journal of cell biology1992

Direct proof that the primary site of action of cytochalasin on cell motility processes is actin.

H Ohmori, S Toyama, S Toyama

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. 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
23.3field-weighted citation impact, top 1% 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, 89 citations in OpenAlex.

  1. IMA fungus · 2025
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Glutamate induces rapid upregulation of astrocyte glutamate transport and cell-surface expression of GLAST.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
  9. Cytochalasin D and latrunculin affect chromosome behaviour during meiosis in crane-fly spermatocytes.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 1998
    Article
  10. Article
  11. Article
  12. Article
  13. Serum protects against azurophil granule dependent down-regulation of complement receptor type 1 (CR1) on human neutrophils.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 1995
    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

3 authors at 1 institution in 1 country.

H OhmoriInstitute for Virus Research, Kyoto University, Japan.
S Toyama
S Toyama
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously described the isolation of a mutant KB cell (Cyt 1 mutant) resistant to the cytotoxic effect of cytochalasin B (CB). The Cyt 1 mutant carries an altered form of beta-actin (beta'-actin) and lacks normal beta-actin (Toyama, S., and S. Toyama. 1984. Cell. 37:609-614). Increased resistance of the Cyt 1 mutant to CB in vivo is reflected in altered properties of beta'-actin in vitro (Toyama, S., and S. Toyama. 1988. J. Cell Biol. 107:1499-1504). Here, we show that the mutation in beta-actin is solely responsible for the cytochalasin-resistant phenotype of the Cyt mutant. We have isolated a cDNA clone encoding beta'-actin from Cyt 1 cells. Sequence analysis reveals two mutations in the coding region that substitute two amino acid residues (Val139----Met and Ala295----Asp). Expression of the beta'-actin cDNA confers cytochalasin resistance upon transformed cytochalasin-sensitive KB cells. Levels of resistance to CB in the transformed cell clones correlate well with amounts of beta'-actin polypeptide. Both of the two mutations in beta'-actin are necessary for the high level expression of cytochalasin resistance. Overall, we conclude that the primary site of action of cytochalasin on cell motility processes in vivo is actin.

Indexed as

Actin CytoskeletonActinsAmino Acid SequenceBase SequenceBlotting, SouthernCell MembraneCell MovementCytochalasin BDNAGenetic VectorsHumansKB CellsMicroscopy, FluorescenceMolecular Sequence DataMutationPhenotypeActinsCytochalasin BDNA

Identifiers

PMID1734024
PMCPMC2289332
OpenAlexW1995573855

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.