Concanavalin A targets phylogenetically conserved N-linked glycans on coronavirus spike proteins for broad-spectrum antiviral activity. [PDF]
Guo D +10 more
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CGL, a Lectin from <i>Crenomytilus grayanus</i>, Exhibits Antibiofilm and Synergistic Antibacterial Activity Against <i>Escherichia coli</i> and <i>Staphylococcus aureus</i>. [PDF]
Chikalovets IV +7 more
europepmc +1 more source
A Pancreatic Ductal Adenocarcinoma Diagnostic System Using Serum Extracellular Vesicle Detection with Optimized Lectin Combination Using Machine Learning. [PDF]
Kawakami T +18 more
europepmc +1 more source
Histochemical Properties of the Vomeronasal System in Hokkaido Sika Deer (<i>Cervus nippon yesoensis</i>). [PDF]
Kondoh D +5 more
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Neuraminidase of influenza A viruses induces global desialylation of host cells via its intracellular function. [PDF]
Kobayashi D, Hiono T, Isoda N, Sakoda Y.
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C-type lectins are the largest and most diverse family of mammalian carbohydrate-binding proteins. They share a common protein fold, which provides the unifying basis for calcium-mediated carbohydrate recognition. Their involvement in a multitude of biological functions is remarkable.
Keller, B., Rademacher, C.
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C-Type Lectin Receptors in Phagocytosis
2020C-type lectin receptors (CLRs) are a family of transmembrane proteins having at least one C-type lectin-like domain (CTLD) on the cell surface and either a short intracellular signaling tail or a transmembrane domain that facilitates interaction with a second protein, often the Fc receptor common gamma chain (FcRγ), that mediates signaling.
Kai, Li, David M, Underhill
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Genomic analysis of C-type lectins
Biochemical Society Symposia, 2002Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate ...
Kurt, Drickamer, Andrew J, Fadden
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C-type lectins belong to a superfamily of receptors that share structural homology in their carbohydrate recognition domains and often bind to carbohydrates in a Ca-dependent fashion. Whereas endocytic C-type lectin receptors (CLRs) trigger the receptor-mediated endocytosis of soluble ligands, myeloid CLRs in innate immunity act as pattern recognition ...
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