ArticleFrontiers in immunology2016
Evidence of an Antimicrobial Peptide Signature Encrypted in HECT E3 Ubiquitin Ligases.
Article in Frontiers in immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 10 citations in OpenAlex.
- Two Tachykinin-Related Peptides with Antimicrobial Activity Isolated fromMicrobiology insights · 2020Article
- The Role of Peptide Signals Hidden in the Structure of Functional Proteins in Plant Immune Responses.International journal of molecular sciences · 2019Review
- Article
- Antimicrobial peptide similarity and classification through rough set theory using physicochemical boundaries.BMC bioinformatics · 2018Article
- Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitin-proteasome pathway (UPP) is a hallmark of the eukaryotic cell. In jawed vertebrates, it has been co-opted by the adaptive immune system, where proteasomal degradation produces endogenous peptides for major histocompatibility complex class I antigen presentation. However, proteolytic products are also necessary for the phylogenetically widespread innate immune system, as they often play a role as host defense peptides (HDPs), pivotal effectors against pathogens. Here, we report the identification of the arachnid HDP oligoventin, which shares homology to a core member of the UPP, E3 ubiquitin ligases. Oligoventin has broad antimicrobial activity and shows strong synergy with lysozymes. Using computational and phylogenetic approaches, we show high conservation of the oligoventin signature in HECT E3s.
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Registered trials
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