Angewandte Chemie International Edition · 2005 · 100 citations · 14 references
Hydrophobic Binding SitesGlycobiologyPeptide SciencePharmacotherapySubstrate Reduction TherapyCarbohydrate-protein InteractionPharmaceutical ChemistryMolecular PharmacologyMedicinal ChemistryRational DesignInhibitory ActivityGlycosylationGaucher DiseaseBiochemistry6-Nonyl IsofagomineDrug DevelopmentPharmacologyMolecular ModelingNatural SciencesMedicineLysosomal Storage DiseaseDrug Discovery
Highly potent human β-glucocerebrosidase inhibitors have been synthesized that appear to recognize both carbohydrate and hydrophobic binding sites. The most potent inhibitor, 6-nonyl isofagomine (see formula), shows an IC50 value at subnanomolar concentrations. These compounds are potential candidates for the development of small-molecule drugs for the treatment of Gaucher disease. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2005/z502662_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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Naoki Asano, Haruhisa Kizu, Kyoko Ikeda et al. · European Journal of Biochemistry · 2000 · 240 citations · Full text
Intracellular Enhancement, Enzymatic Modification, Cellular Physiology +16