Evidence map›Paper›PMID 1310994›Full record

ArticleThe Journal of cell biology1992

In vivo analysis of functional domains from villin and gelsolin.

J Finidori, E Friederich, D J Kwiatkowski, D Louvard

Open access · bronzeAbstract readComparative Study
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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 46 citations in OpenAlex.

  1. Actin Bundles in The Pollen Tube.International journal of molecular sciences · 2018
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. The 3D structure of villin as an unusual F-Actin crosslinker.Structure (London, England : 1993) · 2008
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Refined structure of villin 14T and a detailed comparison with other actin-severing domains.Protein science : a publication of the Protein Society · 1997
    Article
  12. Article
  13. Article
  14. Article
  15. Distribution of gelsolin in mouse ovary.Cell and tissue research · 1994
    Article
  16. 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.

J FinidoriUnité de Recherche Associé 1149 Centre National de la Recherche Scientifique, Institut Pasteur, Département de Biologie Moléculaire, Paris, France.
E Friederich
D J Kwiatkowski
D Louvard
Institut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transfected CV1 cells were used to compare the in vivo effects of various domains of villin and gelsolin. These two homologous actin modulating proteins both contain a duplicated severin-like sequence. Villin has in addition a carboxy-terminal domain, the headpiece, which accounts for its bundling activity. The effects of the villin-deleted mutants were compared with those of native villin. Our results show that essential domains of villin required to induce the growth of microvilli and F-actin redistribution are present in the first half of the core and in the headpiece. We also show that the second half of the villin core cannot be exchanged by its homolog in gelsolin. When expressed at high levels of CV1 cells, full length gelsolin completely disrupted stress fibers without change of the cell shape. Addition of the villin headpiece to gelsolin had no effect on the phenotype induced by gelsolin alone. Expression of the first half of gelsolin induced similar modifications as capping proteins and rapid cell mortality; this deleterious effect on the cell structure was also observed when the headpiece was linked to the first half of gelsolin. In cells expressing the second half of gelsolin, a dotted F-actin staining was often seen. Moreover elongated dorsal F-actin structures were observed when the headpiece was linked to the second gelsolin domain. These studies illustrate the patent in vivo severing activity of gelsolin as well as the distinct functional properties of villin core in contrast to gelsolin.

Indexed as

ActinsBinding SitesCalcium-Binding ProteinsCarrier ProteinsCell LineChimeraCytoskeletonDNA, RecombinantGelsolinHumansMicrofilament ProteinsMolecular StructureRecombinant ProteinsTransfectionActinsCalcium-Binding ProteinsCarrier ProteinsDNA, RecombinantGelsolinMicrofilament ProteinsRecombinant Proteinsvillin

Identifiers

PMID1310994
PMCPMC2289362
OpenAlexW2078484801

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.