1380716-22-2Relevant academic research and scientific papers
Discovery, structure - Activity relationship, and biological evaluation of noninhibitory small molecule chaperones of glucocerebrosidase
Patnaik, Samarjit,Zheng, Wei,Choi, Jae H.,Motabar, Omid,Southall, Noel,Westbroek, Wendy,Lea, Wendy A.,Velayati, Arash,Goldin, Ehud,Sidransky, Ellen,Leister, William,Marugan, Juan J.
, p. 5734 - 5748 (2012/08/07)
A major challenge in the field of Gaucher disease has been the development of new therapeutic strategies including molecular chaperones. All previously described chaperones of glucocerebrosidase are enzyme inhibitors, which complicates their clinical development because their chaperone activity must be balanced against the functional inhibition of the enzyme. Using a novel high throughput screening methodology, we identified a chemical series that does not inhibit the enzyme but can still facilitate its translocation to the lysosome as measured by immunostaining of glucocerebrosidase in patient fibroblasts. These compounds provide the basis for the development of a novel approach toward small molecule treatment for patients with Gaucher disease. This article not subject to U.S. Copyright. Published 2012 by the American Chemical Society.
SUBSTITUTED PYRAZOLOPYRIMIDINES AS GLUCOCEREBROSIDASE ACTIVATORS
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Page/Page column 25, (2012/06/30)
Substituted pyrazolopyrimidines and dihydropyrazolopyrimidines and related compounds, their methods of manufacture, compositions containing these compounds, and methods of use of these compounds in treating lysosomal storage disorders such as Gaucher disease are described herein. The compounds are of general Formula (I) in which variables R1-R7 and X are described in the application.
