ArticleJournal of insect science (Online)2015
Identification of Core Alpha 1,3-Fucosyltransferase Gene From Silkworm: An Insect Popularly Used to Express Mammalian Proteins.
Article in Journal of insect science (Online), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 11 citations in OpenAlex.
- Egg Cooling After Oviposition Extends the Permissive Period for Microinjection-Mediated Genome Modification inInternational journal of molecular sciences · 2024Article
- Species-SpecificMarine drugs · 2023Article
- VectorMOD: Method for Bottom-Up Proteomic Characterization of rAAV Capsid Post-Translational Modifications and Vector Impurities.Frontiers in immunology · 2021Article
- Glycobiotechnology of the Insect Cell-Baculovirus Expression System Technology.Advances in biochemical engineering/biotechnology · 2021Article
- Production of a correctly assembled fibrinogen using transgenic silkworms.Transgenic research · 2020Article
- Novel recombinant feline interferon carrying N-glycans with reduced allergy risk produced by a transgenic silkworm system.BMC veterinary research · 2018Article
- The underestimated N-glycomes of lepidopteran species.Biochimica et biophysica acta. General subjects · 2017Article
- The fucomic potential of mosquitoes: Fucosylated N-glycan epitopes and their cognate fucosyltransferases.Insect biochemistry and molecular biology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Silkworm has great potential as production system of recombinant mammalian proteins. When the protein products are used for medical purpose, it is required to reduce the risk of an allergy, the content of core alpha 1,3-fucosyl residue attached to the N-glycan of proteins, for example. We isolated the gene of an enzyme responsible for the transfer of core alpha 1,3-fucosyl residue, core alpha 1,3-fucosyltransferase (Fuc-T C3), from silkworm. A candidate cDNA for silkworm Fuc-T C3 was isolated as a homolog of the fruit fly enzyme gene fucTA. The gene was located on chromosome 7 of the silkworm genome and was composed of seven exons, which spanned approximately 10 kb on the genome. The coding region of the gene was 1,350 bp and encoded a 450-amino acid protein with a molecular mass of 52.2 kDa. Deduced amino acid sequence of the coding region showed one transmembrane domain in its N-terminal and typical motifs common to fucosyltransferases including Fuc-T C3s of other organisms in its C-terminal. The extract of CHO cells transfected with the cDNA showed Fuc-T C3 activity using GDP-fucose and DABS-GnGn peptide as substrates. These results showed this cDNA clone actually encodes silkworm Fuc-T C3.
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Registered trials
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