http://www.cnr.it/ontology/cnr/individuo/prodotto/ID178570
Synthesis of new chiral 1,4-morpholin-2,5-dione derivatives and evaluation as alpha-glucosidase inhibitors. Part 3 (Articolo in rivista)
- Type
- Label
- Synthesis of new chiral 1,4-morpholin-2,5-dione derivatives and evaluation as alpha-glucosidase inhibitors. Part 3 (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.tetasy.2007.02.013 (literal)
- Alternative label
Arcelli Antonio; Balducci Daniele; Estevao Neto Sonia de Fatima; Porzi Gianni; Sandri Monica (2007)
Synthesis of new chiral 1,4-morpholin-2,5-dione derivatives and evaluation as alpha-glucosidase inhibitors. Part 3
in Tetrahedron: asymmetry (Online)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Arcelli Antonio; Balducci Daniele; Estevao Neto Sonia de Fatima; Porzi Gianni; Sandri Monica (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://www.sciencedirect.com/science/article/pii/S0957416607001279 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Dipartimento di Chimica 'G.Ciamician', Università di Bologna, Via Selmi 2, 40126 Bologna, Italy;
Departamento de Quimica e Bioquimica de Faculdade de Ciencias, Campo Grande, 1749-016 Lisboa, Portugal;
ISTEC-CNR, Via Granarolo 64, 48018 Faenza, Italy; (literal)
- Titolo
- Synthesis of new chiral 1,4-morpholin-2,5-dione derivatives and evaluation as alpha-glucosidase inhibitors. Part 3 (literal)
- Abstract
- A series of chiral 1,4-morpholin-2,5-dione derivatives were synthesized starting from chiral synthons 1 and 2, monolactim ethers derived from L- valine, and the absolute configurations of the new stereocentres were assigned. The substrates investigated behave as noncompetitive inhibitors against alpha-glucosidases and Eire inactive towards beta-glucosidase, alpha-mannosidase and alpha-galactosidase. Three of these substrates show very good and specific inhibition abilities towards alpha-glucosidase. (literal)
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