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Título: | Polymerization of τ into filaments in the presence of heparin: The minimal sequence required for τ - τ interaction |
Autor: | Pérez, Mar CSIC ORCID; Valpuesta, José M. CSIC ORCID ; Medina, Miguel CSIC ORCID; Montejo de Garcini, Esteban; Ávila, Jesús CSIC ORCID | Fecha de publicación: | 1996 | Editor: | John Wiley & Sons | Citación: | Journal of Neurochemistry 67(3): 1183-1190 (1996) | Resumen: | Paired helical filaments isolated from the brains of patients with Alzheimer's disease are composed of a major protein component, the microtubule-associated protein termed τ, together with other nonprotein components, including heparan, a glycosaminoglycan, the more extensively sulfated form of which is heparin. As some of these nonprotein components may modulate the assembly of τ into filamentous structures, we have analyzed the ability of the whole τ protein or some of its fragments to self-assemble in the presence of heparin. Different τ fragments, all of them containing some sequences of the tubulin-binding motif, can assemble in vitro into filaments. We have also found formation of polymers with the 18-residue-long peptide corresponding to the third tubulin-binding motif of τ. This suggests that the ability of τ for self-assembly could be localized in a short sequence of amino acids present in the tubulin-binding repeats of the τ molecule. | Versión del editor: | https://doi.org/10.1046/j.1471-4159.1996.67031183.x | URI: | http://hdl.handle.net/10261/251995 | DOI: | 10.1046/j.1471-4159.1996.67031183.x | ISSN: | 0022-3042 |
Aparece en las colecciones: | (CBM) Artículos (CNB) Artículos |
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