Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/95658
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Changes in tau phosphorylation in hibernating rodents |
Autor: | León-Espinosa, G. CSIC ORCID; García, Esther; García-Escudero, Vega CSIC ORCID CVN; Hernández Pérez, Félix CSIC ORCID; DeFelipe, Javier CSIC ORCID ; Ávila, Jesús CSIC ORCID | Palabras clave: | Phosphorylation Hibernation Syrian hamster Tau |
Fecha de publicación: | 2013 | Editor: | John Wiley & Sons | Citación: | Journal of Neuroscience Research 91: 954- 962 (2013) | Resumen: | Tau is a cytoskeletal protein present mainly in the neurons of vertebrates. By comparing the sequence of tau molecule among different vertebrates, it was found that the variability of the N-terminal sequence in tau protein is higher than that of the C-terminal region. The N-terminal region is involved mainly in the binding of tau to cellular membranes, whereas the C-terminal region of the tau molecule contains the microtubule-binding sites. We have compared the sequence of Syrian hamster tau with the sequences of other hibernating and nonhibernating rodents and investigated how differences in the N-terminal region of tau could affect the phosphorylation level and tau binding to cell membranes. We also describe a change, in tau phosphorylation, on a casein kinase 1 (ck1)-dependent site that is found only in hibernating rodents. This ck1 site seems to play an important role in the regulation of tau binding to membranes. © 2013 Wiley Periodicals, Inc. | URI: | http://hdl.handle.net/10261/95658 | DOI: | 10.1002/jnr.23220 | Identificadores: | doi: 10.1002/jnr.23220 issn: 0360-4012 |
Aparece en las colecciones: | (CBM) Artículos (IC) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
18
checked on 20-abr-2024
WEB OF SCIENCETM
Citations
18
checked on 20-feb-2024
Page view(s)
329
checked on 24-abr-2024
Download(s)
219
checked on 24-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.