ArticleBiotechnology letters2012
Virus-binding activity of the truncated C subunit of porcine aminopeptidase N expressed in Escherichia coli.
Article in Biotechnology letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
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.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Review
- Resistance to coronavirus infection in amino peptidase N-deficient pigs.Transgenic research · 2019Article
- Screening and antiviral analysis of phages that display peptides with an affinity to subunit C of porcine aminopeptidase.Monoclonal antibodies in immunodiagnosis and immunotherapy · 2013Article
- Expression and Purification of the scFv from hybridoma cells secreting a monoclonal antibody against S PROTEIN of PEDV.Monoclonal antibodies in immunodiagnosis and immunotherapy · 2013Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Seven overlapping truncated forms of the C subunit of porcine aminopeptidase N (pAPN-C) were expressed in Escherichia coli. By western blotting and ELISA test, all recombinant proteins were recognized by the antibody against native porcine aminopeptidase N. Recombinant proteins, rpAPN-C2 (aa 623-722) and rpAPN-C3 (aa 673-772), had the highest binding activity with swine transmissible gastroenteritis virus among the truncated pAPN-C recombinant proteins. The overlapping region (aa 673-722) between rpAPN-C2 and rpAPN-C3 is indicated to play a key role in viral binding.
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Registered trials
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