Evidence map›Paper›PMID 24967648›Full record

ReviewSmall GTPases2014

Importance of RhoGTPases in formation, characteristics, and functions of invadosomes.

Pirjo Spuul, Paolo Ciufici, Véronique Veillat, Anne Leclercq, Thomas Daubon, IJsbrand Kramer, Elisabeth Génot

Open access · bronzeAbstract readReview
In one paragraph

Review in Small GTPases, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
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  5. Article
  6. Article
  7. Review
  8. Article
  9. Amoeboid migration in health and disease: Immune responsesFrontiers in cell and developmental biology · 2022
    Review
  10. Review
  11. Review
  12. Review
  13. Recycling the Purpose of Old Drugs to Treat Ovarian Cancer.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  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

7 authors at 1 institution in 1 country.

Pirjo SpuulUniversité de Bordeaux; Bordeaux, France; INSERM U1045; Bordeaux, France; IECB; European Institute of Chemistry and Biology; Pessac, France.
Paolo CiuficiUniversité de Bordeaux; Bordeaux, France; INSERM U1045; Bordeaux, France; IECB; European Institute of Chemistry and Biology; Pessac, France.
Véronique VeillatUniversité de Bordeaux; Bordeaux, France; INSERM U1045; Bordeaux, France; IECB; European Institute of Chemistry and Biology; Pessac, France.
Anne LeclercqUniversité de Bordeaux; Bordeaux, France; INSERM U1045; Bordeaux, France; IECB; European Institute of Chemistry and Biology; Pessac, France.
Thomas DaubonUniversité de Bordeaux; Bordeaux, France; INSERM U1045; Bordeaux, France; IECB; European Institute of Chemistry and Biology; Pessac, France.
IJsbrand KramerUniversité de Bordeaux; Bordeaux, France; INSERM U1045; Bordeaux, France; IECB; European Institute of Chemistry and Biology; Pessac, France.
Elisabeth GénotUniversité de Bordeaux; Bordeaux, France; INSERM U1045; Bordeaux, France; IECB; European Institute of Chemistry and Biology; Pessac, France.
Université de Bordeaux · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Podosomes and invadopodia (collectively known as invadosomes) are specialized plasma-membrane actin-based microdomains that combine adhesive properties with matrix degrading and/or mechanosensor activities. These organelles have been extensively studied in vitro and current concerted efforts aim at establishing their physiological relevance and subsequent association with human diseases. Proper functioning of the bone, immune, and vascular systems is likely to depend on these structures while their occurrence in cancer cells appears to be linked to tumor metastasis. The elucidation of the mechanisms driving invadosome assembly is a prerequisite to understanding their role in vivo and ultimately to controlling their functions. Adhesive and soluble ligands act via transmembrane receptors that propagate signals to the cytoskeleton via small G proteins of the Rho family, assisted by tyrosine kinases and scaffold proteins to induce invadosome formation and rearrangements. Oncogene expression and cell-cell interactions may also trigger their assembly. Manipulation of the signals that regulate invadosome formation and dynamics could therefore be a strategy to interfere with their functions in a multitude of pathological settings, such as excessive bone breakdown, infections, vascular remodeling, transendothelial diapedesis, and metastasis.

Indexed as

Actin CytoskeletonAnimalscdc42 GTP-Binding ProteinExtracellular MatrixHumansrac GTP-Binding ProteinsrhoA GTP-Binding Proteinrho GTP-Binding ProteinsWiskott-Aldrich Syndrome Proteincdc42 GTP-Binding Proteinrac GTP-Binding ProteinsrhoA GTP-Binding Proteinrho GTP-Binding ProteinsWiskott-Aldrich Syndrome Proteincytoskeletonextracellular matrixinvadopodiainvadosomespodosomesRhoGTPases

Identifiers

PMID24967648
PMCPMC4114929
OpenAlexW1985143502

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.