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dc.contributor.authorÁvila de Grado, Jesúses_ES
dc.contributor.authorJiménez, Juan S.es_ES
dc.contributor.authorSayas, Carmen L.es_ES
dc.contributor.authorBolós, Martaes_ES
dc.contributor.authorZabala Otaño, Juan Carlos es_ES
dc.contributor.authorRivas, Germánes_ES
dc.contributor.authorHernández, Félixes_ES
dc.contributor.otherUniversidad de Cantabriaes_ES
dc.date.accessioned2017-05-18T10:03:22Z
dc.date.available2017-05-18T10:03:22Z
dc.date.issued2016-11es_ES
dc.identifier.issn1663-4365es_ES
dc.identifier.urihttp://hdl.handle.net/10902/10999
dc.description.abstractTau is a microtubule-associated protein that plays an important role in axonal stabilization, neuronal development, and neuronal polarity. In this review, we focus on the primary, secondary, tertiary, and quaternary tau structures. We describe the structure of tau from its specific residues until its conformation in dimers, oligomers, and larger polymers in physiological and pathological situations.es_ES
dc.format.extent10 p.es_ES
dc.language.isoenges_ES
dc.publisherFrontiers Research Foundationes_ES
dc.rights© 2016 Avila, Jiménez, Sayas, Bolós, Zabala, Rivas and Hernández. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY).es_ES
dc.sourceFront. Aging Neurosci., 08 November 2016 Volume 8 Article 262es_ES
dc.titleTau Structureses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.accessRightsopenAccesses_ES
dc.identifier.DOI10.3389/fnagi.2016.00262es_ES
dc.type.versionpublishedVersiones_ES


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