ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2026
Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Abstract
This short review discusses the structural and molecular events at the origin of diverse debilitating neurodegenerative diseases. The pathological consequences owing to the primary, secondary, tertiary and quaternary structural diversity of alpha-synuclein and tau proteins and the aggregates they form are presented. The crosstalk between alpha-synuclein and tau proteins aggregates structural heterogeneity and cellular homeostasis, and more precisely the proteostasis network is next considered. Overall, the proteostasis network appears as the master regulator of distinct synucleinopathies and tauopathies progression depending on its capacity to clear and/or disassemble to completion structurally diverse alpha-synuclein or tau fibrillar aggregates or not. This article is part of the Theo Murphy meeting issue 'ProteostaSys: a systems view of proteostasis'.
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