145149-49-1Relevant academic research and scientific papers
SEVEN-MEMBERED SULFONAMIDES AS MODULATORS OF RAR-RELATED ORPHAN RECEPTOR-GAMMA (RORγ, NR1F3)
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Page/Page column 55-56, (2013/05/22)
The invention provides modulators for the orphan nuclear receptor RORγ and methods for treating RORγ mediated diseases by administration of these novel RORγ modulators to a human or a mammal in need thereof. Specifically, the present invention provides compounds of Formula (1) and the enantiomers, diastereomers, tautomers, solvates and pharmaceutically acceptable salts thereof as well as pharmaceutical compositions comprising said compounds as an active ingredient.
Structure-based design of novel human Pin1 inhibitors (II)
Dong, Liming,Marakovits, Joseph,Hou, Xinjun,Guo, Chuangxing,Greasley, Samantha,Dagostino, Eleanor,Ferre, RoseAnn,Johnson, M. Catherine,Kraynov, Eugenia,Thomson, James,Pathak, Ved,Murray, Brion W.
supporting information; experimental part, p. 2210 - 2214 (2010/06/15)
Following the discovery of a novel series of phosphate-containing small molecular Pin1 inhibitors, the drug design strategy shifted to replacement of the phosphate group with an isostere with potential better pharmaceutical properties. The initial loss in potency of carboxylate analogs was likely due to weaker charge-charge interactions in the putative phosphate binding pocket and was subsequently recovered by structure-based optimization of ligand-protein interactions in the proline binding site, leading to the discovery of a sub-micromolar non-phosphate small molecular Pin1 inhibitor.
Syntheses and biological activities of bombesin analogs modified in the C-terminal dipeptide part
Llinares,Devin,Azay,Berge,Fehrentz,Martinez
, p. 767 - 780 (2007/10/03)
Bombesin receptor antagonists are possible therapeutic agents due to their ability to act as inhibitors of cellular proliferation. On the basis of our hypothesis on the mechanism of action of gastrin associating an activating enzyme system to the receptor and on the results reported in the litterature, we have synthesized bombesin analogues which have been modified in the C-terminal Leu13-Leu14 amide part. We have shown that modification in the C-terminal part of the bombesin strongly affected the biological activity in rat pancreatic acini. The most potent compound which is described here, H-D-Phe-Gln-Trp-Ala-Val-Gly-His-Leu-Ψ/(CH2)Leu-NH2, was able to recognize the bombesin receptor on rat pancreatic acini (Ki 4.3 nM) and antagonized the bombesin stimulated amylase secretion (Ki 7.7 nM).
