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- W2321173906 endingPage "200" @default.
- W2321173906 startingPage "190" @default.
- W2321173906 abstract "The quest for ever more selective kinase inhibitors as potential future drugs has yielded a large repertoire of chemical probes that are selective for specific kinase conformations. These probes have been useful tools to obtain structural snapshots of kinase conformational plasticity. Similarly, kinetic and thermodynamic inhibitor binding experiments provide glimpses at the time scales and energetics of conformational interconversions. These experimental insights are complemented by computational predictions of conformational energy landscapes and simulations of conformational transitions and of the process of inhibitors binding to the protein kinase domain. A picture emerges in which highly selective inhibitors capitalize on the dynamic nature of kinases." @default.
- W2321173906 created "2016-06-24" @default.
- W2321173906 creator A5008590226 @default.
- W2321173906 creator A5076005115 @default.
- W2321173906 date "2014-12-19" @default.
- W2321173906 modified "2023-10-13" @default.
- W2321173906 title "Targeting Conformational Plasticity of Protein Kinases" @default.
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