1,721,088 research outputs found
Determination of the Volume Changes Induced by Ligand Binding to Hsp90 Using High Pressure Denaturation
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X-Ray Crystallographic Structures of High-Affinity and High-Selectivity Inhibitor Complexes with CA IX That Plays a Special Role in Cancer
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Organic Synthesis of Substituted Fluorinated Benzenesulfonamides as Selective Inhibitors of CA IX and Other Isoforms
No full textBinding of Natural and Synthetic Inhibitors to Human Heat Shock Protein 90 and Their Clinical Application
No full textThis review describes the recent progress in the field of heat shock protein 90 (Hsp90) inhibitor design. Hsp90 is a heat shock protein with a molecular weight of approximately 90 kDa. Hsp90 is considered a good anticancer target because its inhibition leads to inactivation of its numerous client proteins participating in various signaling and other processes involved in cancer progression. Numerous Hsp90 inhibitors-leads currently tested in clinical trials are presented in this review. Furthermore, this review emphasizes the application of biophysical binding assays in the development of Hsp90 inhibitors. The binding of designed lead compounds to various Hsp90 constructs is measured by isothermal titration calorimetry and thermal shift assay. These assays provide a detailed energetic insight of the binding reaction, including the enthalpy, entropy, heat capacity, and the Gibbs free energy. A detailed description of the binding energetics helps to extend our knowledge of structure-activity relationships in the design of more potent inhibitors. The most active compounds are then tested for their absorption, distribution, metabolism, elimination, toxicity, and activity against cancer cell lines.</jats:p
Intrinsic thermodynamics of trifluoromethanesulfonamide and ethoxzolamide binding to human carbonic anhydrase VII
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