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- W1571611182 abstract "The value of conformationally constrained analogs rests with the hypothesis that restricting the number of attainable conformations of a flexible, acyclic molecule, such as L-glutamate, should limit the number of glutamate binding sites with which the analog can interact, thereby increasing its selectivity as a pharmacological probe. Pharmacophore models have become tools in the development of the next generation analogs that is used to refine the models and identify more selectively acting agents, such as those that can distinguish among closely related transporter subtypes. This chapter explains the calculation of low energy conformations of acidic amino acids. To compare the structures of the active transport inhibitors, computational libraries of the energetically accessible conformations of each must be generated. From a practical point of view, this task must be carried out using molecular mechanics rather than higher levels of theory." @default.
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- W1571611182 date "1998-01-01" @default.
- W1571611182 modified "2023-10-18" @default.
- W1571611182 title "[12] Design and synthesis of conformationally constrained inhibitors of high-affinity, sodium-dependent glutamate transporters" @default.
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- W1571611182 doi "https://doi.org/10.1016/s0076-6879(98)96014-1" @default.
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