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- W1992505890 abstract "The cover picture shows how distinct glycoclusters can interfere with the activity of human adhesion/growth-regulatory proteins. The three human lectins of medical relevance (Gal-1, Gal-3 and Gal-4) selectively bind to multivalent calixarene glycoconjugates, neutralizing lectin activity. Of note is that the sugar ligands are presented with different spatial topology. This diversity is depicted as generated from an ancient Calix, the etymological origin of the name of these macrocycles. The orange ellipses on the cell surface and on the macrocycle scaffolds (in blue) represent sugar units that compete for lectin binding. In vitro bioassays indicate clear intergalectin selectivity of inhibition that depends on the conformational properties of the calix[n]arene scaffold and on the valency of the glycoclusters. The assays also reveal the potent reactivity of the glycoclusters towards a plant toxin from Viscum album L., akin to ricin. Further details can be found in the article by H.-J. Gabius, R. Ungaro, et al. on p. 1649 ff." @default.
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- W1992505890 date "2008-06-23" @default.
- W1992505890 modified "2023-10-16" @default.
- W1992505890 title "Cover Picture: Calix[<i>n</i>]arene‐Based Glycoclusters: Bioactivity of Thiourea‐Linked Galactose/Lactose Moieties as Inhibitors of Binding of Medically Relevant Lectins to a Glycoprotein and Cell‐Surface Glycoconjugates and Selectivity among Human Adhesion/Growth‐Regulatory Galectins (ChemBioChem 10/2008)" @default.
- W1992505890 doi "https://doi.org/10.1002/cbic.200890036" @default.
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