ArticleJournal of insect science (Online)2018
Transcriptomics-Based Identification of Aquaporin Diversity in the House Dust Mite Dermatophagoides farinae (Acariformes: Pyroglyphidae).
Article in Journal of insect science (Online), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 12 citations in OpenAlex.
- A Chromosomal-Level Genome ofInternational journal of genomics · 2024Article
- Article
- Lineage-level divergence of copepod glycerol transporters and the emergence of isoform-specific trafficking regulation.Communications biology · 2021Article
- Identification of LincRNA from Dermatophagoides farinae (Acari: Pyroglyphidae) for Potential Allergen-Related Targets.Genetics and molecular biology · 2020Article
- Molecular Dynamics Simulations of Mite Aquaporin DerfAQP1 from the Dust MiteBioMed research international · 2020Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin water channel proteins are highly conserved across many diverse species. Some evidence indicates that aquaporins in insects may contribute to insect-related mammalian diseases and inflammation, and thus these proteins may represent viable therapeutic targets. Here, we used RNA sequencing and bioinformatics to identify putative aquaporins from the house dust mite, Dermatophagoides farinae. Six putative aquaporins were identified based on sequence similarity with aquaporins from other species. These putative aquaporins, deposited in GenBank and named DerfAQP1-4 (KY231248, KY231249, KY231250, and KY231251, respectively), DerfAQP5.01, and DerfAQP5.02 (KY231252 and KY231253), were successfully cloned into a bacterial plasmid. The identification of full-length aquaporin sequences from D. farinae provides a foundation for future molecular and biochemical studies of these proteins in D. farinae and related species.
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