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<http://fhircat.org/cord-19/metadata/d710e993d5c0aca81ed537d9462953a234309a1c> fhir_link: <https://fhircat.org/cord-19/fhir/Commercial/d710e993d5c0aca81ed537d9462953a234309a1c> ;
    dc:abstract "To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds, especially from red algae. In fact, man-specific seaweed lectins consist of different structural scaffolds harboring a single or a few carbohydrate-binding sites which specifically recognize mannose-containing glycans. Depending on the structural scaffold, man-specific seaweed lectins belong to five distinct structurally-related lectin families, namely (1) the griffithsin lectin family (β-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (β-barrel scaffold); (3) the legume lectin-like lectin family (β-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (β-prism II scaffold); and, (5) the MFP2-like lectin family (MFP2-like scaffold). Another algal lectin from Ulva pertusa, has been inferred to the methanol dehydrogenase related lectin family, because it displays a rather different GlcNAc-specificity. In spite of these structural discrepancies, all members from the five lectin families share a common ability to specifically recognize man-containing glycans and, especially, high-mannose type glycans. Because of their mannose-binding specificity, these lectins have been used as valuable tools for deciphering and characterizing the complex mannose-containing glycans from the glycocalyx covering both normal and transformed cells, and as diagnostic tools and therapeutic drugs that specifically recognize the altered high-mannose N-glycans occurring at the surface of various cancer cells. In addition to these anti-cancer properties, man-specific seaweed lectins have been widely used as potent human immunodeficiency virus (HIV-1)-inactivating proteins, due to their capacity to specifically interact with the envelope glycoprotein gp120 and prevent the virion infectivity of HIV-1 towards the host CD4+ T-lymphocyte cells in vitro." ;
    dc:creator "['Barre, Annick', 'Simplicien, Mathias', 'Benoist, Hervé', 'Van Damme, Els J.M.', 'Rougé, Pierre']" ;
    dc:identifier <http://dx.doi.org/10.3390/md17080440>,
        <https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6723950>,
        <https://www.ncbi.nlm.nih.gov/pubmed/31357490> ;
    dc:issued "2019-01-01"^^xsd:date ;
    dc:license "CC BY" ;
    dc:title "Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties" ;
    sso:has_full_text "True" ;
    sso:journal "Mar Drugs" ;
    sso:sha "d710e993d5c0aca81ed537d9462953a234309a1c" ;
    sso:source_x "PMC" .

