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- W2801162528 endingPage "4972" @default.
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- W2801162528 abstract "Selectins are a class of cell adhesion molecules that play a critical role during the initial steps of inflammation. The N-terminal domain of P-selectin glycoprotein ligand-1 (PSGL-1) binds to all selectins, but with the highest affinity to P-selectin. Recent evidence suggests that the blockade of P-selectin/PSGL-1 interactions provides a viable therapeutic option for the treatment of many inflammatory diseases. Herein, we report the total synthesis of threonine bearing sialyl LewisX (sLeX) linked to a Core-1- O-hexasaccharide 1, as a key glycan of the N-terminal domain of PSGL-1. A convergent synthesis using α-selective sialylation and a regioselective [4+2] glycosylation are the key features of this synthesis." @default.
- W2801162528 created "2018-05-17" @default.
- W2801162528 creator A5004697596 @default.
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- W2801162528 date "2018-04-11" @default.
- W2801162528 modified "2023-10-15" @default.
- W2801162528 title "Convergent Synthesis of Sialyl LewisX-O-Core-1 Threonine" @default.
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- W2801162528 doi "https://doi.org/10.1021/acs.joc.7b03117" @default.
- W2801162528 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7648531" @default.
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- W2801162528 hasPublicationYear "2018" @default.
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