ArticleMolecular biology reports2014
New insights into the allergenicity of tropomyosin: a bioinformatics approach.
Article in Molecular biology reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed, 15 citations in OpenAlex.
- Effect of pressure cooking alone and in combination with other treatments on shrimp allergic protein, tropomyosin.Journal of food science and technology · 2022Article
- Molecular and allergenic characterization of recombinant tropomyosin from mud crab Scylla olivacea.Molecular biology reports · 2021Article
- Article
- Allergy in an Evolutionary Framework.Journal of molecular evolution · 2020Review
- Article
- Cross-reactivity between aeroallergens and food allergens.World journal of methodology · 2015Article
- Carbohydrate Structure Database: tools for statistical analysis of bacterial, plant and fungal glycomes.Database : the journal of biological databases and curation · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The invertebrate panallergen tropomyosin is a protein with an extremely simple folding. This makes it a perfect target for investigating structural differences between invertebrate and vertebrate tropomyosins, which are not considered allergenic. Phylogenetic and sequence analyses were conducted in order to explore the differences in primary structure between several tropomyosins and to promote an experimental development in the field of food allergy, based on the study of tropomyosin. The phylogenetic analyses showed that tropomyosin is a useful evolutionary marker. The phylogenetic trees obtained with tropomyosin were not always phylogenetically correct, but they might be useful for allergen avoidance by tropomyosin allergic individuals. Sequence analyses revealed that the probability of alpha helix folding in invertebrate tropomyosins was lower than in all the studied vertebrate ones, except for the Atlantic bluefin tuna Thunnus thynnus tropomyosin. This suggested that the lack of alpha helix folding may be involved in the immunogenicity of tropomyosins. More specifically, the regions adjacent to the positions 133-135 and 201 of the invertebrate tropomyosins, presented lower probability of alpha helix folding than those of vertebrates and are candidates to be responsible for their allergenicity.
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Registered trials
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