ArticleApplied and environmental microbiology2023
Cadherin Is a Binding Protein but Not a Functional Receptor of Bacillus thuringiensis Cry2Ab in Helicoverpa armigera.
Article in Applied and environmental microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Novel codon-optimized cry1Ac34 gene from Indian Bt isolate confers resistance against Helicoverpa armigera in Transgenic tobacco.Archives of microbiology · 2026Article
- Interactions between insecticidal cry toxins and their receptors.Current genetics · 2025Review
- Transcriptomic Analysis of the Response of theInternational journal of molecular sciences · 2024Article
- Utilization of Diverse Molecules as Receptors by Cry Toxin and the Promiscuous Nature of Receptor-Binding Sites Which Accounts for the Diversity.Biomolecules · 2024Review
- An overview of the production and use ofOpen life sciences · 2024Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Midgut receptors play a critical role in the specificity of Cry toxins for individual insect species. Cadherin proteins are essential putative receptors of Cry1A toxins in lepidopteran larvae. Cry2A family members share common binding sites in Helicoverpa armigera, and one of them, Cry2Aa, has been widely reported to interact with midgut cadherin. Here, we studied the binding interaction and functional role of
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Registered trials
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