41901-72-8Relevant articles and documents
Discovery of novel, potent, selective and cellular active ADC type PTP1B inhibitors via fragment-docking-oriented de novel design
Du, Yongli,Ling, Hao,Zhang, Meng,Shen, Jingkang,Li, Qunyi
, p. 4891 - 4898 (2015)
Fragment-docking-oriented de novel design for both the catalytic site and the C phosphotyrosine binding site led to the discovery of novel scaffold and chemical easy N-(2,5-diethoxy-phenyl)-methanesulfonamide based phosphotyrosine mimetics that when incorporated into ureas are high potent and selective inhibitors of protein tyrosine phosphatase 1B. Among them, compound 15 was shown to be the most potent PTP1B inhibitor with great selectivity over the highly homologous T-cell protein tyrosine phosphatase.
Novel urea protein tyrosine phosphatase 1B inhibitor, and preparation method, pharmaceutical composition and application thereof
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Paragraph 0018, (2017/01/09)
The invention relates to novel urea compounds with a structure as shown in a general formula I in the specification or pharmaceutically acceptable salts thereof, wherein the urea compounds and the pharmaceutically acceptable salts thereof can be used as a novel inhibitor of protein tyrosine phosphatase (PTP) 1B. The invention also relates to a pharmaceutical composition containing the compounds as shown in the general formula I or the pharmaceutically acceptable salts of the compounds. The compounds as shown in the general formula I or the pharmaceutically acceptable salts thereof have the effect of inhibiting the activity of the protein tyrosine phosphatase 1B (PTP1B), and can be applied in preparation of drugs capable of preventing and/or treating symptoms or diseases like hyperglycemia and type 2 diabetes.
Structure-activity relationships of 3-(substituted benzoyl)propionic acids, a new class of antispasmodics for biliary smooth muscle
Murata,Satoh,Nohara,et al.
, p. 17 - 20 (2007/10/09)
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