22387-37-7Relevant articles and documents
Discovery of Orally Bioavailable Purine-Based Inhibitors of the Low-Molecular-Weight Protein Tyrosine Phosphatase
Stanford, Stephanie M.,Diaz, Michael A.,Ardecky, Robert J.,Zou, Jiwen,Roosild, Tarmo,Holmes, Zachary J.,Nguyen, Tiffany P.,Hedrick, Michael P.,Rodiles, Socorro,Guan, April,Grotegut, Stefan,Santelli, Eugenio,Chung, Thomas D. Y.,Jackson, Michael R.,Bottini, Nunzio,Pinkerton, Anthony B.
supporting information, p. 5645 - 5653 (2021/05/31)
Obesity-associated insulin resistance plays a central role in the pathogenesis of type 2 diabetes. A promising approach to decrease insulin resistance in obesity is to inhibit the protein tyrosine phosphatases that negatively regulate insulin receptor signaling. The low-molecular-weight protein tyrosine phosphatase (LMPTP) acts as a critical promoter of insulin resistance in obesity by inhibiting phosphorylation of the liver insulin receptor activation motif. Here, we report development of a novel purine-based chemical series of LMPTP inhibitors. These compounds inhibit LMPTP with an uncompetitive mechanism and are highly selective for LMPTP over other protein tyrosine phosphatases. We also report the generation of a highly orally bioavailable purine-based analogue that reverses obesity-induced diabetes in mice.
Dichotomy in regioselective cross-coupling reactions of 6,8-dichloropurines with phenylboronic acid and methylmagnesium chloride: Synthesis of 6,8-di-substituted purines
Hocek, Michal,Hockova, Dana,Dvorakova, Hana
, p. 889 - 894 (2007/10/03)
Pd-catalyzed cross-coupling reaction of 6,8-dichloro-9-(tetrahydropyran-2- yl)purine with one equivalent of phenylboronic acid proceeded regioselectively to give 8-chloro-6-phenylpurine, while the analogous Fe-catalyzed reaction with methylmagnesium chlor
Purine Derivatives as Competitive Inhibitors of Human Erythrocyte Membrane Phosphatidylinositol 4-Kinase
Young, Rodney C.,Jones, Martin,Milliner, Kevin J.,Rana, Kishore K.,Ward, John G.
, p. 2073 - 2080 (2007/10/02)
The possibility of deriving a potent, cell-penetrating inhibitor of human erythrocyte PI 4-kinase, competitive with respect to ATP, has been investigated in a series of purine derivatives and analogues.The purine nucleus is not essential for binding to th