Sawkar, Anu R. published the artcileGaucher Disease-Associated Glucocerebrosidases Show Mutation-Dependent Chemical Chaperoning Profiles, Category: alcohols-buliding-blocks, the publication is Chemistry & Biology (Cambridge, MA, United States) (2005), 12(11), 1235-1244, database is CAplus and MEDLINE.
Summary: Gaucher disease is a lysosomal storage disorder caused by deficient glucocerebrosidase activity. We have previously shown that the cellular activity of the most common Gaucher disease-associated glucocerebrosidase variant, N370S, is increased when patient-derived cells are cultured with the chem. chaperone N-nonyl-deoxynojirimycin. Chem. chaperones stabilize proteins against misfolding, enabling their trafficking from the endoplasmic reticulum. Herein, the generality of this therapeutic strategy is evaluated with other glucocerebrosidase variants and with addnl. candidate chem. chaperones. Improved chem. chaperones are identified for N370S glucocerebrosidase. Moreover, we demonstrate that G202R, a glucocerebrosidase variant that is known to be retained in the endoplasmic reticulum, is also amenable to chem. chaperoning. The L444P variant is not chaperoned by any of the active site-directed mols. tested, likely because this mutation destabilizes a domain distinct from the catalytic domain.
Chemistry & Biology (Cambridge, MA, United States) published new progress about 85618-21-9. 85618-21-9 belongs to alcohols-buliding-blocks, auxiliary class Tetrahydropyran,Chiral,sulfides,Alcohol, name is (2R,3S,4S,5R,6S)-2-(Hydroxymethyl)-6-(octylthio)tetrahydro-2H-pyran-3,4,5-triol, and the molecular formula is C14H28O5S, Category: alcohols-buliding-blocks.
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