ArticleToxins2019
Structural Domains of the
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.
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
19 citing papers in PubMed.
- Amino Acid Substitutions in the C-Terminal Domains of Vip3Aa Enhance Insecticidal Toxicity.Biology · 2026Article
- Biophysical Analysis of Vip3Aa Toxin Mutants Before and After Activation.International journal of molecular sciences · 2024Article
- N-Terminal α-Helices in Domain I ofToxins · 2024Article
- Domain IIIToxins · 2024Article
- A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency.Engineering microbiology · 2023Article
- Functional characterization of Vip3Aa from Bacillus thuringiensis reveals the contributions of specific domains to its insecticidal activity.The Journal of biological chemistry · 2023Article
- Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis.Microbial biotechnology · 2022Article
- In vivo competition assays between Vip3 proteins confirm the occurrence of shared binding sites in Spodoptera littoralis.Scientific reports · 2022Article
- Antifungal Mechanism of Vip3Aa, a Vegetative Insecticidal Protein, against Pathogenic Fungal Strains.Antibiotics (Basel, Switzerland) · 2021Article
- Critical Domains in the Specific Binding of Radiolabeled Vip3Af Insecticidal Protein to Brush Border Membrane Vesicles fromApplied and environmental microbiology · 2021Article
- How DoesToxins · 2021Review
- Response Mechanisms of Invertebrates toMicrobiology and molecular biology reviews : MMBR · 2021Review
- Vegetative Insecticidal Protein (Vip): A Potential Contender FromFrontiers in microbiology · 2021Review
- Current Insights on Vegetative Insecticidal Proteins (Vip) as Next Generation Pest Killers.Toxins · 2020Review
- Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis.Nature communications · 2020Article
- Structural and Functional Insights into the C-terminal Fragment of Insecticidal Vip3A Toxin ofToxins · 2020Article
- Oligomer Formation and Insecticidal Activity ofToxins · 2020Article
- Insecticidal Activity of 11 Bt toxins and 3 Transgenic Maize Events Expressing Vip3Aa19 to Black Cutworm,Insects · 2020Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vip3 proteins are increasingly used in insect control in transgenic crops. To shed light on the structure of these proteins, we used the approach of the trypsin fragmentation of mutants altering the conformation of the Vip3Af protein. From an alanine scanning of Vip3Af, we selected mutants with an altered proteolytic pattern. Based on protease digestion patterns, their effect on oligomer formation, and theoretical cleavage sites, we generated a map of the Vip3Af protein with five domains which match some of the domains proposed independently by two in silico models. Domain I ranges amino acids (aa) 12-198, domain II aa199-313, domain III aa314-526, domain IV aa527-668, and domain V aa669-788. The effect of some mutations on the ability to form a tetrameric molecule revealed that domains I-II are required for tetramerization, while domain V is not. The involvement of domain IV in the tetramer formation is not clear. Some mutations distributed from near the end of domain I up to the end of domain II affect the stability of the first three domains of the protein and destroy the tetrameric form upon trypsin treatment. Because of the high sequence similarity among Vip3 proteins, we propose that our domain map can be extended to the Vip3 family of proteins.
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.