Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

By Brandon B. Holmes, Sarah L. DeVos, Najla Kfoury, Mei Li, R. Jacks, K. Yanamandra, M. Ouidja, F. Brodsky, J. Marasa, Devika P. Bagchi and 4 more. Proceedings of the National Academy of Sciences of the United States of America, 2013

795 citations recorded by the source corpus.

Subfields: Molecular Biology, Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/bdc31d0a20f3916287c4524ad645815a80510ca9

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Citations in the corpus

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “Tau uptake is regulated by HSPGs in neuronal cells, and by Chemokine CX3C receptor1 (CX3CR1) in microglia [262, 263, 265].”
Distinct tau prion strains propagate in cells and mice and define different tauopathies (2014, background): “In the case of tau, fibrils transmit its aggregated state from the outside to the inside of a cell (Frost et al., 2009a; Holmes et al., 2013), suggesting that this mechanism could account for the stereotyped progression of tauopathies.”
Impairment of Glymphatic Pathway Function Promotes Tau Pathology after Traumatic Brain Injury (2014, background): “…tau is taken up into cells of the CNS, and the uptake of interstitial tau aggregates into neurons is now thought to underlie the “prionic” spread of tauopathy in progressive neurodegenerative diseases such as Alzheimer’s disease (Kfoury et al., 2012; Holmes et al., 2013; Walker et al., 2013).”
Proteopathic tau seeding predicts tauopathy in vivo (2014, methodology): “Our laboratory has previously used FRET to quantify protein aggregation in cultured cells (13, 21, 22).”