Please use this identifier to cite or link to this item: https://www.um.edu.mt/library/oar/handle/123456789/22587
Title: Tau protein hyperphosphorylation and aggregation in Alzheimer's disease and other tauopathies, and possible neuroprotective strategies
Authors: Simic, Goran
Babic Leko, Mirjana
Wray, Selina
Harrington, Charles
Delalle, Ivana
Jovanov-Milosevic, Natasa
Bazadona, Danira
Buee, Luc
Silva, Rohan de
Di Giovanni, Giuseppe
Wischik, Claude
Hof, Patrick R.
Keywords: Alzheimer's disease
Amyloid beta-protein
Nervous system -- Diseases
Nervous system -- Degeneration
Tau proteins
Issue Date: 2016
Publisher: MDPIAG
Citation: Šimić, G., Babić Leko, M., Wray, S., Harrington, C., Delalle, I., Jovanov-Milošević, N...,Hof, P. R. (2016). Tau protein hyperphosphorylation and aggregation in Alzheimer's disease and other tauopathies, and possible neuroprotective strategies. Biomolecules, 6, 1.
Abstract: Abnormal deposition of misprocessed and aggregated proteins is a common final pathway of most neurodegenerative diseases, including Alzheimer’s disease (AD). AD is characterized by the extraneuronal deposition of the amyloid β (Aβ) protein in the form of plaques and the intraneuronal aggregation of the microtubule-associated protein tau in the form of filaments. Based on the biochemically diverse range of pathological tau proteins, a number of approaches have been proposed to develop new potential therapeutics. Here we discuss some of the most promising ones: inhibition of tau phosphorylation, proteolysis and aggregation, promotion of intra- and extracellular tau clearance, and stabilization of microtubules. We also emphasize the need to achieve a full understanding of the biological roles and post-translational modifications of normal tau, as well as the molecular events responsible for selective neuronal vulnerability to tau pathology and its propagation. It is concluded that answering key questions on the relationship between Aβ and tau pathology should lead to a better understanding of the nature of secondary tauopathies, especially AD, and open new therapeutic targets and strategies.
URI: https://www.um.edu.mt/library/oar//handle/123456789/22587
Appears in Collections:Scholarly Works - FacM&SPB

Files in This Item:
File Description SizeFormat 
biomolecules-06-00006-v2.pdf3.84 MBAdobe PDFView/Open


Items in OAR@UM are protected by copyright, with all rights reserved, unless otherwise indicated.