5-Chloroindoloyl glycine amide inhibitors of glycogen phosphorylase: synthesis, in vitro, in vivo, and X-ray crystallographic characterization.
Article Details
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Wright SW, Rath VL, Genereux PE, Hageman DL, Levy CB, McClure LD, McCoid SC, McPherson RK, Schelhorn TM, Wilder DE, Zavadoski WJ, Gibbs EM, Treadway JL
5-Chloroindoloyl glycine amide inhibitors of glycogen phosphorylase: synthesis, in vitro, in vivo, and X-ray crystallographic characterization.
Bioorg Med Chem Lett. 2005 Jan 17;15(2):459-65.
- PubMed ID
- 15603973 [ View in PubMed]
- Abstract
The synthesis, in vitro, and in vivo biological characterization of a series of achiral 5-chloroindoloyl glycine amide inhibitors of human liver glycogen phosphorylase A are described. Improved potency over previously reported compounds in cellular and in vivo assays was observed. The allosteric binding site of these compounds was shown by X-ray crystallography to be the same as that reported previously for 5-chloroindoloyl norstatine amides.
DrugBank Data that Cites this Article
- Binding Properties
Drug Target Property Measurement pH Temperature (°C) 5-Chloro-1h-Indole-2-Carboxylic Acid{[Cyclopentyl-(2-Hydroxy-Ethyl)-Carbamoyl]-Methyl}-Amide Glycogen phosphorylase, liver form IC 50 (nM) 570 N/A N/A Details