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Article

Distinct glycosaminoglycan chain length and sulfation patterns required for cellular uptake of Tau, Aβ, and α-Synuclein

2017-10-21

Abstract excerpt

Transcellular propagation of aggregate “seeds” has been proposed to mediate progression of neurodegenerative diseases in tauopathies and α-synucleinopathies. We have previously determined that tau and α-synuclein aggregates bind heparan sulfate proteoglycans (HSPGs) on the cell surface. This mediates uptake and intracellular seeding. The specificity and mode of binding to HSPGs has been unknown. We used modified h...

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Identifiers and source

Literature Corpus work
6e31f32d-805f-547b-8873-bddf4b805cb7
DOI
10.1101/207035
Open publication

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Distinct glycosaminoglycan chain length and sulfation patterns required for cellular uptake of Tau, Aβ, and α-SynucleinDOI 10.1101/207035
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