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Updated: Feb 8, 2026

Mass Histology to Quantify Neurodegeneration in Drosophila
Published on: December 15, 2016
The sulfation code for propagation of neurodegeneration
Masahito Yamada1, Tsuyoshi Hamaguchi2
1From the Department of Neurology and Neurobiology of Aging, Kanazawa University Graduate School of Medical Sciences, Kanazawa 920-8640, Japan m-yamada@med.kanazawa-u.ac.jp.
Abstract:
Prion-like propagation of protein aggregates is thought to be an essential feature in many neurodegenerative diseases, but the mechanisms underlying transcellular transfer of protein aggregates remain unclear. Stopschinski et al. now demonstrate that the cellular uptake of tau, Aβ, and α-synuclein aggregates mediated by heparan sulfate proteoglycans (HSPGs) varies with distinct glycosaminoglycan chain length and sulfation patterns. The results help us to understand how different protein aggregates propagate, leading to distinct neurodegenerative pathologies.
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