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dc.contributor.authorBernardo Ordiz, David 
dc.contributor.authorGarrote Adrados, José Antonio 
dc.contributor.authorNadal, I.
dc.contributor.authorLeón, Alberto José
dc.contributor.authorCalvo Romero, María Del Carmen 
dc.contributor.authorFernández Salazar, Luis Ignacio 
dc.contributor.authorBlanco Quiros, Alfredo 
dc.contributor.authorSanz, Y.
dc.contributor.authorArranz Sanz, Eduardo 
dc.date.accessioned2014-02-27T09:26:13Z
dc.date.available2014-02-27T09:26:13Z
dc.date.issued2009
dc.identifier.citationGut, 2009, vol. 58, n. 6, p. 886-887.es
dc.identifier.urihttp://uvadoc.uva.es/handle/10324/4436
dc.description.abstractProlyl-endopeptidase supplementation has been proposed to favour gliadin degradation as an alternative treatment for coeliac disease (CD), although the real usefulness of this therapy in vivo is still under discussion. 1 However, our data point to alternative treatments aiming to modify the intestinal microbiota in patients with CD by the use of probiotics and/or prebiotics. We propose that the induction of gliadin proteolysis in the human gut might not be the solution but the origin of CD.es
dc.format.mimetypeapplication/pdfes
dc.language.isoenges
dc.publisherBMJes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectEnfermedad celíacaes
dc.subjectGliadinaes
dc.subjectIntestinos - Enfermedadeses
dc.titleIs it true coeliacs do not digest gliadin? Degradation pattern of gliadin in coeliac disease small intestinal mucosaes
dc.typeinfo:eu-repo/semantics/articlees
dc.identifier.doi10.1136/gut.2008.167296
dc.relation.publisherversionhttps://gut.bmj.com/content/58/6/886
dc.identifier.publicationfirstpage886es
dc.identifier.publicationissue6es
dc.identifier.publicationlastpage887es
dc.identifier.publicationtitleGutes
dc.identifier.publicationvolume58es
dc.peerreviewedSIes
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International
dc.type.hasVersioninfo:eu-repo/semantics/acceptedVersion


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