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- W2034350788 abstract "Further optimization efforts on the previously disclosed PTP-1B inhibitor 1 a led to the discovery of a new series of potent compounds, for example derivative 33, which targeted the second phosphotyrosine binding pocket near the catalytic site. In the new series, the N-sulfonylpiperidine group of 1 a was replaced with a smaller substituent, capable of forming a new hydrogen bond interaction with arginine 24. The series reported here maintains the binding mode of 1 a and has the added advantages of a lower molecular weight, smaller polar surface area, and fewer rotatable bonds." @default.
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- W2034350788 date "2008-10-10" @default.
- W2034350788 modified "2023-10-18" @default.
- W2034350788 title "Structure-Based Optimization of Protein Tyrosine Phosphatase-1 B Inhibitors: Capturing Interactions with Arginine 24" @default.
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- W2034350788 doi "https://doi.org/10.1002/cmdc.200800188" @default.
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