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Crystal structure of an Hsp90 - Geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
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Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
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Schulte, T. W.; Akinaga, S.; Soga, S.; Sullivan, W.; Stensgard, B.; Toft, D.; Neckers, L. M. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 1998, 2, 100-108.
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A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
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Synthesis and application of functionally diverse 2,6,9-trisubstituted purine libraries as CDK inhibitors
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Studies of tautomers and protonation of adenine and its derivatives by nitrogen-15 nuclear magnetic resonance
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Synthesis of 8-alkyl derivatives of 9-methyl adenine
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In contrast, we found that the cyclization of 1-(4-butylamino-6-methoxy-5-yl)-3-(4-methoxyphenyl)propan-2-one occurred in high yields using this method
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In contrast, we found that the cyclization of 1-(4-butylamino-6-methoxy-5-yl)-3-(4-methoxyphenyl)propan-2-one occurred in high yields using this method.
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12
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Purines: Reaction and synthesis
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Mills, K.2
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0041727023
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Alkylation of adenine or 8-butyl-9H-purin-6-ylamine under Mitsunobu conditions gave mostly 9-N-alkylated product and small amounts of 7-N-alkylated product
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Alkylation of adenine or 8-butyl-9H-purin-6-ylamine under Mitsunobu conditions gave mostly 9-N-alkylated product and small amounts of 7-N-alkylated product.
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