ArticleBMC biophysics2017
DNA secondary structure formation by DNA shuffling of the conserved domains of the Cry protein of
Article in BMC biophysics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed, 5 citations in OpenAlex.
- Toxic Determination of Cry11 Mutated Proteins Obtained Using Rational Design and Its Computational Analysis.International journal of molecular sciences · 2023Article
- Genetic Modification Approaches for ParasporinsMolecules (Basel, Switzerland) · 2021Review
- Generation of Cry11 Variants ofEvolutionary bioinformatics online · 2020Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Cry toxins, or δ-endotoxins, are a diverse group of proteins produced by
resultsThe results showed a shared thermodynamic pattern for each cluster and relationships among sequences that are phylogenetically close at the protein level. The regions of the
conclusionThese results suggest the presence of thermodynamic variations associated to the formation of secondary structures and an evolutionary relationship with regions that encode highly conserved domains in Cry proteins. The findings of this study may have a role in the
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Registered trials
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