Evidence map›Paper›PMID 37279443›Full record

ReviewFEMS microbiology reviews2023

The role of glycoconjugates as receptors for insecticidal proteins.

Hannah L Best, Lainey J Williamson, Emily A Heath, Helen Waller-Evans, Emyr Lloyd-Evans, Colin Berry

Abstract readReview
In one paragraph

Review in FEMS microbiology reviews, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. A second locus associated with high-level resistance to Bt Cry1Ac inApplied and environmental microbiology · 2026
    Article
  2. Article
  3. Article
  4. Downregulation of APN1 andApplied and environmental microbiology · 2024
    Article
  5. Article
  6. Biomolecules · 2023
    Article
  7. Structure of theProceedings of the National Academy of Sciences of the United States of America · 2023
    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

6 authors.

Hannah L BestSchool of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, United Kingdom.ORCID 0000-0002-2612-2749
Lainey J WilliamsonSchool of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, United Kingdom.ORCID 0000-0003-3575-5078
Emily A HeathSchool of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, United Kingdom.ORCID 0000-0002-6061-5790
Helen Waller-EvansMedicines Discovery Institute, Cardiff University, Park Place, Cardiff CF10 3AT, United Kingdom.ORCID 0000-0003-4133-6064
Emyr Lloyd-EvansSchool of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, United Kingdom.ORCID 0000-0002-3626-1611
Colin BerrySchool of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, United Kingdom.ORCID 0000-0002-9943-548X

Funding

Biotechnology and Biological Sciences Research Council BB/M009122/1Biotechnology and Biological Sciences Research Council BB/S002774/1
6 · The paper itself

Abstract

Bacillus thuringiensis (Bt) proteins are an environmentally safe and effective alternative to chemical pesticides and have been used as biopesticides, with great commercial success, for over 50 years. Global agricultural production is predicted to require a 70% increase until 2050 to provide for an increasing population. In addition to agriculture, Bt proteins are utilized to control human vectors of disease-namely mosquitoes-which account for >700 000 deaths annually. The evolution of resistance to Bt pesticial toxins threatens the progression of sustainable agriculture. Whilst Bt protein toxins are heavily utilized, the exact mechanisms behind receptor binding and toxicity are unknown. It is critical to gain a better understanding of these mechanisms in order to engineer novel toxin variants and to predict, and prevent, future resistance evolution. This review focuses on the role of carbohydrate binding in the toxicity of the most utilized group of Bt pesticidal proteins-three domain Cry (3D-Cry) toxins.

Indexed as

Bacillus thuringiensisInsecticidesAnimalsBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsGlycoconjugatesHemolysin ProteinsHumansMosquito VectorsBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsGlycoconjugatesHemolysin ProteinsInsecticidesBacillus thuringiensisglycobiologyinsecticidalpesticidaltoxins

Identifiers

PMID37279443
PMCPMC10337751

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.