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http://hdl.handle.net/10261/251999
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Medina, Miguel | es_ES |
dc.contributor.author | García-Rocha, Mar | es_ES |
dc.contributor.author | Padilla, Rodolfo | es_ES |
dc.contributor.author | Pérez, Mar | es_ES |
dc.contributor.author | Montejo de Garcini, Esteban | es_ES |
dc.contributor.author | Ávila, Jesús | es_ES |
dc.date.accessioned | 2021-10-11T10:23:58Z | - |
dc.date.available | 2021-10-11T10:23:58Z | - |
dc.date.issued | 1996 | - |
dc.identifier.citation | Biochimica et Biophysica Acta - Molecular Basis of Disease 1316(1): 43-50 (1996) | es_ES |
dc.identifier.issn | 0925-4439 | - |
dc.identifier.issn | https://doi.org/10.1016/0925-4439(96)00018-X | - |
dc.identifier.uri | http://hdl.handle.net/10261/251999 | - |
dc.description.abstract | Human tau phosphorylation has been studied in transfected COS-1 cells. Treatment with okadaic acid alters the electrophoretic mobility of human tau protein transiently expressed in transfected cells, due to an increase in the level of phosphorylation. Treatment with okadaic acid also results in an increased phosphorylation of Alzheimer's disease-type phosphoepitopes. Tau phosphorylation within COS-1 cells is partially inhibited by in vivo treatment with DRB, a protein kinase inhibitor. Double treatment of transfected cells with okadaic acid and DRB reveals that phosphorylation of tau protein at the AT8 epitope is achieved by a DRB-resistant protein kinase which is different from that responsible for tau phosphorylation at the SMI-31 epitope, which appears to be sensitive to DRB. | es_ES |
dc.description.sponsorship | This work has been supported in part by Spanish CICYT, Fundacion Cajamadrid, Comunidad de Madrid, Glaxo- Wellcome, Spain and an institutional grant from Fundacion Ramon Areces. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Elsevier | es_ES |
dc.relation.isversionof | Publisher's version | es_ES |
dc.rights | openAccess | es_ES |
dc.subject | Tau protein | es_ES |
dc.subject | DRB | es_ES |
dc.subject | Protein kinase | es_ES |
dc.subject | Phosphorylation | es_ES |
dc.subject | Alzheimer's disease | es_ES |
dc.title | Protein kinases involved in the phosphorylation of human tau protein in transfected COS-1 cells | es_ES |
dc.type | artículo | es_ES |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | https://doi.org/10.1016/0925-4439(96)00018-X | es_ES |
dc.rights.license | https://www.elsevier.com/open-access/userlicense/1.0/ | es_ES |
dc.contributor.funder | Fundación Ramón Areces | es_ES |
dc.contributor.funder | Comunidad de Madrid | es_ES |
dc.contributor.funder | Comisión Interministerial de Ciencia y Tecnología, CICYT (España) | es_ES |
dc.contributor.funder | Fundación Caja Madrid | es_ES |
dc.relation.csic | Sí | es_ES |
oprm.item.hasRevision | no ko 0 false | * |
dc.identifier.funder | http://dx.doi.org/10.13039/100012818 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003403 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/100008054 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100007273 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.languageiso639-1 | en | - |
item.fulltext | With Fulltext | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
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