Your browser doesn't support javascript.
loading
Medicinal chemistry of catechol O-methyltransferase (COMT) inhibitors and their therapeutic utility.
Kiss, László E; Soares-da-Silva, Patrício.
Afiliación
  • Kiss LE; Department of Research & Development, BIAL - Portela & Ca, S.A. , À Avenida da Siderurgia Nacional, 4745-457 S. Mamede do Coronado, Portugal.
J Med Chem ; 57(21): 8692-717, 2014 Nov 13.
Article en En | MEDLINE | ID: mdl-25080080
Catechol O-methyltransferase (COMT) is the enzyme responsible for the O-methylation of endogenous neurotransmitters and of xenobiotic substances and hormones incorporating catecholic structures. COMT is a druggable biological target for the treatment of various central and peripheral nervous system disorders, including Parkinson's disease, depression, schizophrenia, and other dopamine deficiency-related diseases. The purpose of this perspective is fourfold: (i) to summarize the physiological role of COMT inhibitors in central and peripheral nervous system disorders; (ii) to provide the history and perspective of the medicinal chemistry behind the discovery and development of COMT inhibitors; (iii) to discuss how the physicochemical properties of recognized COMT inhibitors are understood to exert influence over their pharmacological properties; and (iv) to evaluate the clinical benefits of the most relevant COMT inhibitors.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catecol O-Metiltransferasa / Inhibidores de Catecol O-Metiltransferasa Tipo de estudio: Prognostic_studies Límite: Animals / Humans / Male Idioma: En Revista: J Med Chem Asunto de la revista: QUIMICA Año: 2014 Tipo del documento: Article País de afiliación: Portugal Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catecol O-Metiltransferasa / Inhibidores de Catecol O-Metiltransferasa Tipo de estudio: Prognostic_studies Límite: Animals / Humans / Male Idioma: En Revista: J Med Chem Asunto de la revista: QUIMICA Año: 2014 Tipo del documento: Article País de afiliación: Portugal Pais de publicación: Estados Unidos