Evidence map›Paper›PMID 31242582›Full record

ArticleToxins2019

Pore-Forming Proteins from Cnidarians and Arachnids as Potential Biotechnological Tools.

Esperanza Rivera-de-Torre, Juan Palacios-Ortega, José G Gavilanes, Álvaro Martínez-Del-Pozo, Sara García-Linares

Abstract read
In one paragraph

Article in Toxins, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Cnidarian toxins: omics approaches and recombinant proteins.The journal of venomous animals and toxins including tropical diseases · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Sea Anemones, Actinoporins, and Cholesterol.International journal of molecular sciences · 2022
    Review
  12. Article
  13. Article
  14. Widow spiders in the New World: a review onThe journal of venomous animals and toxins including tropical diseases · 2021
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
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.

Esperanza Rivera-de-TorreDepartamento de Bioquímica y Biología Molecular, Facultad de CC. Químicas, Universidad Complutense de Madrid, 28040 Madrid, Spain. esperanza.rivera.detorre@gmail.com.ORCID 0000-0002-0272-6150
Juan Palacios-OrtegaDepartamento de Bioquímica y Biología Molecular, Facultad de CC. Químicas, Universidad Complutense de Madrid, 28040 Madrid, Spain. juan.palaciosb1a@gmail.com.ORCID 0000-0002-4629-0221
José G GavilanesDepartamento de Bioquímica y Biología Molecular, Facultad de CC. Químicas, Universidad Complutense de Madrid, 28040 Madrid, Spain. jggavila@ucm.es.
Álvaro Martínez-Del-PozoDepartamento de Bioquímica y Biología Molecular, Facultad de CC. Químicas, Universidad Complutense de Madrid, 28040 Madrid, Spain. alvaromp@quim.ucm.es.ORCID 0000-0003-0043-5939
Sara García-LinaresCell Biology Department, Harvard Medical School, Boston, MA 02115, USA. sara_garcialinares@hms.harvard.edu.ORCID 0000-0003-4983-5730

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Animal venoms are complex mixtures of highly specialized toxic molecules. Cnidarians and arachnids produce pore-forming proteins (PFPs) directed against the plasma membrane of their target cells. Among PFPs from cnidarians, actinoporins stand out for their small size and molecular simplicity. While native actinoporins require only sphingomyelin for membrane binding, engineered chimeras containing a recognition antibody-derived domain fused to an actinoporin isoform can nonetheless serve as highly specific immunotoxins. Examples of such constructs targeted against malignant cells have been already reported. However, PFPs from arachnid venoms are less well-studied from a structural and functional point of view. Spiders from the

Indexed as

Cnidarian VenomsPore Forming Cytotoxic ProteinsSpider VenomsAnimalsArachnidaBiotechnologyCnidariaGenomicsHumansCnidarian VenomsPore Forming Cytotoxic ProteinsSpider Venomsactinoporinbioinsecticidesimmunotoxinlatrotoxinpore-forming proteinstranscriptomicsvenomics

Identifiers

PMID31242582
PMCPMC6628452

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.