Evidence map›Paper›PMID 22562659›Full record

ReviewInvertebrate neuroscience : IN2012

Bacterial pore-forming proteins as anthelmintics.

Yan Hu, Raffi V Aroian

Abstract readReview
In one paragraph

Review in Invertebrate neuroscience : IN, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Frontiers in microbiology · 2020
    Article
  5. Repertoire of theToxins · 2019
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

2 authors.

Yan HuSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, 9500 Gilman Drive, Mail Code 0322, La Jolla, CA 92093-0322, USA. yahu@ucsd.edu
Raffi V Aroian

Funding

Function/optimization of a nematicidal Cry toxin arsenalR01AI056189 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI RAFFI V AROIAN · 2005 to 2026
$11.0M
NIAID NIH HHS R01 AI056189
6 · The paper itself

Abstract

Crystal (Cry) proteins are made by the Gram-positive bacterium Bacillus thuringiensis (Bt). Cry proteins are pore-forming proteins and are the most widely used biological insecticides in the world. Our laboratory found some Cry proteins are highly effective against a broad range of nematodes (roundworms). Here, we discuss our results of Cry protein activity against intestinal roundworms. Both Cry5B and Cry21A have therapeutic activities against infections of the roundworm Heligmosomoides polygyrus bakeri in mice. Cry5B also shows highly therapeutic activity against Ancylostoma ceylanicum infection in hamsters. A. ceylanicum is a minor hookworm parasite of humans, and it is closely related to the more prevalent Ancylostoma duodenale. In addition, Cry proteins show excellent combinatorial therapeutic properties with nicotinic acetylcholine receptor (nAChR) agonists, one of the two classes of compounds approved by the World Health Organization for the treatment for intestinal roundworms in humans. Given their non-toxicity to humans and their broad spectrum of nematicidal action, Cry proteins show great potential as next-generation anthelmintics.

Indexed as

AnimalsAntinematodal AgentsBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsHemolysin ProteinsNematodaAntinematodal AgentsBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsHemolysin Proteinsinsecticidal crystal protein, Bacillus Thuringiensis

Identifiers

PMID22562659
PMCPMC3889471

What OpenQuestion holds

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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.