Article
Molecular basis of 1-deoxygalactonojirimycin arylthiourea binding to human α-galactosidase a: pharmacological chaperoning efficacy on Fabry disease mutants.
ACS chemical biology - 18 Jul 2014
Yu Yi, Mena-Barragán Teresa, Higaki Katsumi, Johnson Jennifer L, Drury Jason E, Lieberman Raquel L, Nakasone Naoe, Ninomiya Haruaki, Tsukimura Takahiro, Sakuraba Hitoshi, Suzuki Yoshiyuki, Nanba Eiji, Mellet Carmen Ortiz, García Fernández José M, Ohno Kousaku
Abstract excerpt
Fabry disease (FD) is an X-linked lysosomal storage disorder caused by mutations in the GLA gene often leading to missense α-galactosidase A (α-Gal A) variants that undergo premature endoplasmic reticulum-associated degradation due to folding defects. We have synthesized and characterized a new family of neutral amphiphilic pharmacological chaperones, namely 1-deoxygalactonojirimycin-arylthioureas (DGJ-ArTs),...
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