Discovery of novel quinoline-based estrogen receptor ligands using peptide interaction profiling.
J Med Chem
; 48(6): 2243-7, 2005 Mar 24.
Article
en En
| MEDLINE
| ID: mdl-15771467
Traditional approaches to discovery of selective estrogen receptor modulators (SERMs) have relied on ER binding and cell-based estrogen response element-driven assays to identify compounds that are osteoprotective but nonproliferative in breast and uterine tissues. To discover new classes of potential SERMs, we have employed a cell-free microsphere-based binding assay to rapidly characterize ERalpha interactions with conformation-sensing cofactor or phage display peptides. Peptide profiles of constrained triarenes were compared to known proliferative and nonproliferative ER ligands to discover potent quinoline-based ligands with minimal Ishikawa cell stimulation.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Quinolinas
/
Receptores de Estrógenos
/
Moduladores Selectivos de los Receptores de Estrógeno
Límite:
Female
/
Humans
Idioma:
En
Revista:
J Med Chem
Asunto de la revista:
QUIMICA
Año:
2005
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Estados Unidos