133284-48-7

Upstream product

• 97009-67-1 1-(4-fluorophenyl)cyclopropane-1-carbonitrile 
• 1455028-72-4 N-(2,4-dimethoxybenzyl)-1-(4-fluorophenyl)cyclopropanecarboxamide 
• 773100-29-1 1-(4-fluorophenyl)cyclopropane-1-carboxylic acid 
• 1176030-00-4 C₁₀H₈ClFO 
• 459-22-3 4-fluorophenylacetonitrile 

Downstream Products

• 773100-29-1 1-(4-fluorophenyl)cyclopropane-1-carboxylic acid 
• 75180-46-0 (1-(4-fluorophenyl)cyclopropyl)methanamine 

Relevant academic research and scientific papers

MODULATORS OF INDOLEAMINE 2,3-DIOXYGENASE

Provided are IDO inhibitor compounds of Formula I and pharmaceutically acceptable salts thereof, their pharmaceutical compositions, their methods of preparation, and methods for their use in the prevention and/or treatment of diseases. Formula I

Positive Allosteric Modulators of MGLUR2

The disclosure generally relates to compounds of formula I, including their salts, as well as compositions and methods of using the compounds. The compounds modulate the mGluR2 receptor and may be useful for the treatment of various disorders of the centr

Distinctive molecular inhibition mechanisms for selective inhibitors of human 11β-hydroxysteroid dehydrogenase type 1

11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1) catalyzes the NADPH dependent interconversion of inactive cortisone to active cortisol. Excess 11β-HSD1 or cortisol leads to insulin resistance and metabolic syndrome in animal models and in humans. Inhibiting 11β-HSD1 activity signifies a promising therapeutic strategy in the treatment of Type 2 diabetes and related diseases. Herein, we report two highly potent and selective small molecule inhibitors of human 11β-HSD1. While compound 1, a sulfonamide, functions as a simple substrate competitive inhibitor, compound 2, a triazole, shows the kinetic profile of a mixed inhibitor. Co-crystal structures reveal that both compounds occupy the 11β-HSD1 catalytic site, but present distinct molecular interactions with the protein. Strikingly, compound 2 interacts much closer to the cofactor NADP+ and likely modifies its binding. Together, the structural and kinetic analyses demonstrate two distinctive molecular inhibition mechanisms, providing valuable information for future inhibitor design.