ArticleACS medicinal chemistry letters2014
Acyclic tethers mimicking subunits of polysaccharide ligands: selectin antagonists.
Article in ACS medicinal chemistry letters, 2014. 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Synthesis of and characterization of differentially sulfated disaccharide repeating units of keratan sulfate.Glycoscience & therapy · 2026Article
- Sialyl LewisACS medicinal chemistry letters · 2025Article
- Pan-selectin inhibitors as potential therapeutics for COVID-19 treatment: in silico screening study.Glycobiology · 2021Article
- Developing a Library of Mannose-Based Mono- and Disaccharides: A General Chemoenzymatic Approach to Monohydroxylated Building Blocks.Molecules (Basel, Switzerland) · 2020Article
- Selectins-The Two Dr. Jekyll and Mr. Hyde Faces of Adhesion Molecules-A Review.Molecules (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report on the design and synthesis of molecules having E- and P-selectins blocking activity both in vitro and in vivo. The GlcNAc component of the selectin ligand sialyl Lewis(X) was replaced by an acyclic tether that links two saccharide units. The minimization of intramolecular dipole-dipole interactions and the gauche effect would be at the origin of the conformational bias imposed by this acyclic tether. The stereoselective synthesis of these molecules, their biochemical and biological evaluations using surface plasmon resonance spectroscopy (SPR), and in vivo assays are described. Because the structure of our analogues differs from the most potent E-selectin antagonists reported, our acyclic analogues offer new opportunities for chemical diversity.
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