| Author | dc.contributor.author | Reyes Parada, Miguel | |
| Author | dc.contributor.author | Fierro, A. | es_CL |
| Author | dc.contributor.author | Iturriaga-Vásquez, Patricio | es_CL |
| Author | dc.contributor.author | Cassels Niven, Bruce | es_CL |
| Admission date | dc.date.accessioned | 2012-06-08T15:17:32Z | |
| Available date | dc.date.available | 2012-06-08T15:17:32Z | |
| Publication date | dc.date.issued | 2004-11-25 | |
| Cita de ítem | dc.identifier.citation | Current Enzyme Inhibition, Vol. 1, p. 85-95, 2005. | es_CL |
| Identifier | dc.identifier.issn | 1573-4080 | |
| Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/119468 | |
| Abstract | dc.description.abstract | The recent description of the crystal structures of rat MAO-A and human MAO-B provides an
unprecedented framework to elucidate the mechanisms underlying the selective interactions between these
proteins and their ligands. The analysis of previous and emerging data, in the light of the structural similarities
and differences between both isozymes, allows a better understanding of the requirements that determine the
affinity and selectivity of substrates and inhibitors. This augurs a new impulse for the rational design of potent
and selective MAO inhibitors with therapeutic potential. | es_CL |
| Patrocinador | dc.description.sponsorship | The support of
FONDECYT grant 1000776 and DICYT-USACH is
gratefully acknowledged. | es_CL |
| Lenguage | dc.language.iso | en | es_CL |
| Publisher | dc.publisher | Bentham Science Publishers Ltd. | es_CL |
| Keywords | dc.subject | Monoamine oxidase | es_CL |
| Título | dc.title | Monoamine Oxidase Inhibition In the Light of New Structural Data | es_CL |
| Document type | dc.type | Artículo de revista | |
