ReviewToxins2014
Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxins.
Review in Toxins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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.
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.
Who cites it
65 citing papers in PubMed, 168 citations in OpenAlex.
- Interaction with theApplied and environmental microbiology · 2026Article
- Structure-Function Analysis of Individual Reversion Variants of the Engineered Mpp46Aa1 (PS2Aa1) N65 Protein.Cancers · 2026Article
- Bacillus thuringiensis as a factory producing parasporin toxins with promising anticancer properties: a review.Microbial cell factories · 2026Review
- Structure Elucidation, Biological and Molecular Docking Studies of the δ‑Endotoxin Cry1Ca17 fromACS omega · 2025Article
- Interactions between insecticidal cry toxins and their receptors.Current genetics · 2025Review
- Article
- Update of the list of qualified presumption of safety (QPS) recommended microbiological agents intentionally added to food or feed as notified to EFSA 21: Suitability of taxonomic units notified to EFSA until September 2024.EFSA journal. European Food Safety Authority · 2025Article
- Insights into the structural changes that trigger receptor binding upon proteolytic activation of Bacillus thuringiensis Vip3Aa insecticidal protein.PLoS pathogens · 2024Article
- Enhancing the Cytotoxicity and Apoptotic Efficacy of Parasporin-2-Derived Variants (Mpp46Aa1) on Cancer Cell Lines.Toxins · 2024Article
- A fusion protein designed for soluble expression, rapid purification, and enhanced stability of parasporin-2 with potential therapeutic applications.Biotechnology reports (Amsterdam, Netherlands) · 2024Article
- Exploratory comparative transcriptomic analysis reveals potential gene targets associated with Cry1A.105 and Cry2Ab2 resistance in fall armyworm (Spodoptera frugiperda).Functional & integrative genomics · 2024Article
- Review
- Cry1Ac toxin binding in the velvetbean caterpillarFrontiers in physiology · 2024Article
- Random Mutational Analysis Targeting Residue KBiology · 2023Article
- Novel insecticidal proteins from ferns resemble insecticidal proteins fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Diversity of transgenes in sustainable management of insect pests.Transgenic research · 2023Review
- MultipleInternational journal of molecular sciences · 2023Article
- Article
- Development of a cypovirus protein microcrystal-encapsulated Bacillus thuringiensis UV-tolerant and mosquitocidal δ-endotoxin.Biology open · 2022Article
- The crystal structure of Cry78Aa from Bacillus thuringiensis provides insights into its insecticidal activity.Communications biology · 2022Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Since the first X-ray structure of Cry3Aa was revealed in 1991, numerous structures of B. thuringiensis toxins have been determined and published. In recent years, functional studies on the mode of action and resistance mechanism have been proposed, which notably promoted the developments of biological insecticides and insect-resistant transgenic crops. With the exploration of known pore-forming toxins (PFTs) structures, similarities between PFTs and B. thuringiensis toxins have provided great insights into receptor binding interactions and conformational changes from water-soluble to membrane pore-forming state of B. thuringiensis toxins. This review mainly focuses on the latest discoveries of the toxin working mechanism, with the emphasis on structural related progress. Based on the structural features, B. thuringiensis Cry, Cyt and parasporin toxins could be divided into three categories: three-domain type α-PFTs, Cyt toxin type β-PFTs and aerolysin type β-PFTs. Structures from each group are elucidated and discussed in relation to the latest data, respectively.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.