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Antigen processing of a short viral antigen by proteasomes

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dc.contributor.authorLopez, Daniel
dc.contributor.authorCalero, Olga
dc.contributor.authorJimenez, Mercedes
dc.contributor.authorGarcía-Calvo, Margarita
dc.contributor.authorDel Val, Margarita
dc.contributor.funderInstituto de Salud Carlos III
dc.contributor.funderComunidad de Madrid (España)
dc.contributor.funderMinisterio de Educación y Ciencia (España)
dc.date.accessioned2020-04-23T06:59:43Z
dc.date.available2020-04-23T06:59:43Z
dc.date.issued2006-10-13
dc.description.abstractMass spectrometry (MS)-based methods coupled to reverse phase chromatography separation are a useful technology to analyze complex peptide pools that are comprised of different peptides with unrelated sequences. In antigen presentation, proteasomes generate a set of short peptides that are closely related and overlapping and in some instances may even have identical retention times and identical masses. In these situations, micro-liquid chromatography-MS/MS focused on each theoretical parent ion followed by manual interpretation optimizes the identification of generated peptides. The results suggest that the degradation of short antigens by the proteasome occurs by sequential cleavage.es_ES
dc.description.peerreviewedSíes_ES
dc.description.sponsorshipThis work was supported by grants from the Programa Ramón y Cajal, Comunidad de Madrid, Instituto de Salud Carlos III, Fundación FIPSE, and Fondo de Investigaciones Sanitarias de la SS (to D. L.) and from the Ministerio de Educación y Ciencia, Comunidad de Madrid, and Instituto de Salud Carlos III (to M. D. V.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.es_ES
dc.format.number41es_ES
dc.format.page30315-8es_ES
dc.format.volume281es_ES
dc.identifier.citationJ Biol Chem. 2006 Oct 13;281(41):30315-8. Epub 2006 Jul 21.es_ES
dc.identifier.doi10.1074/jbc.M605973200es_ES
dc.identifier.issn0021-9258es_ES
dc.identifier.journalThe Journal of biological chemistryes_ES
dc.identifier.pubmedID16861221es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/9696
dc.language.isoenges_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biology (ASBMB)es_ES
dc.relation.publisherversionhttps://doi.org/10.1074/jbc.M605973200es_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsopen accesses_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAmino Acid Sequencees_ES
dc.subject.meshAnimalses_ES
dc.subject.meshAntigen Presentationes_ES
dc.subject.meshAntigens, Virales_ES
dc.subject.meshChromatographyes_ES
dc.subject.meshChromatography, Liquides_ES
dc.subject.meshMass Spectrometryes_ES
dc.subject.meshMolecular Sequence Dataes_ES
dc.subject.meshPeptideses_ES
dc.subject.meshProteasome Endopeptidase Complexes_ES
dc.subject.meshRabbitses_ES
dc.titleAntigen processing of a short viral antigen by proteasomeses_ES
dc.typejournal articlees_ES
dc.type.hasVersionVoRes_ES
dspace.entity.typePublication
relation.isAuthorOfPublicatione96d76f3-57bc-46bd-82f0-175b493cef6c
relation.isAuthorOfPublication096634d2-d4e9-4562-ac2d-5fcd90848fae
relation.isAuthorOfPublication1cacaac4-2f79-4c26-8770-a36de8770a19
relation.isAuthorOfPublication.latestForDiscoverye96d76f3-57bc-46bd-82f0-175b493cef6c

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