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dc.contributor.authorPons, Guillemes_ES
dc.contributor.authorRiba, Danieles_ES
dc.contributor.authorCasasampere, Mireiaes_ES
dc.contributor.authorIzquierdo, Eduardoes_ES
dc.contributor.authorAbad, José Luises_ES
dc.contributor.authorFabriàs, Gemmaes_ES
dc.contributor.authorRodríguez Ortega, Pilar G.es_ES
dc.contributor.authorMontejo, Manueles_ES
dc.contributor.authorLópez González, Juan J.es_ES
dc.contributor.authorCasas, Josefinaes_ES
dc.contributor.authorDelgado Cirilo, Antonioes_ES
dc.date.accessioned2020-05-26T14:52:29Z-
dc.date.available2020-05-26T14:52:29Z-
dc.date.issued2020-01-17-
dc.identifier.citationJournal of Organic Chemistry 85 (2): 419-429 (2020)es_ES
dc.identifier.urihttp://hdl.handle.net/10261/212234-
dc.description.abstractThe synthesis of a series of vinylated analogues of sphingosine-1-phosphate together with their unambiguous configurational assignment by VCD methods is reported. Among them, compound RBM10-8 can irreversibly inhibit human sphingosine-1-phosphate lyase (hS1PL) while behaving also as an enzyme substrate. These findings, together with the postulated mechanism for S1PL activity, reinforce the role of RBM10-8 as a new mechanism-based hS1PL inhibitor. Copyright © 2019 American Chemical Society.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Chemical Societyes_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectSphingosineses_ES
dc.subjectAlkanolamineses_ES
dc.subjectEnzyme substrateses_ES
dc.titleA Mechanism-Based Sphingosine-1-phosphate Lyase Inhibitores_ES
dc.typeartículoes_ES
dc.identifier.doi10.1021/acs.joc.9b02420-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversion10.1021/acs.joc.9b02420es_ES
dc.embargo.terms2021-01-17es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.contributor.orcidAbad, José Luís [0000-0002-8343-9611]es_ES
dc.contributor.orcidFabriàs, Gemma [0000-0001-7162-3772]es_ES
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
item.cerifentitytypePublications-
item.openairetypeartículo-
item.languageiso639-1en-
item.grantfulltextopen-
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