Brain homogenates from human tauopathies induce tau inclusions in mouse brain
By F. Clavaguera, H. Akatsu, G. Fraser, R. Crowther, S. Frank, J. Hench, A. Probst, D. Winkler, Julia Reichwald, M. Staufenbiel and 3 more. Proceedings of the National Academy of Sciences of the United States of America, 2013
718 citations recorded by the source corpus.
Subfields: Molecular Biology, Neurology, Physiology
View Paper: https://www.semanticscholar.org/paper/a083f0d7beb17b8d2ea9382342fed5dcfc38bf00
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In Molecular Biology
- John Q. Trojanowski
- D. Thal
- V. Lee
- D. Holtzman
- K. Del Tredici
- A. Serrano‐Pozo
- E. Masliah
- Guy C. Brown
In Neurology
- Dennis W. Dickson
- V. Lee
- John Q. Trojanowski
- D. Holtzman
- E. Masliah
- Thomas Wisniewski
- D. Thal
- J. Attems
In Physiology
- Dennis W. Dickson
- D. Holtzman
- V. Lee
- John Q. Trojanowski
- Thomas Wisniewski
- E. Masliah
- D. Thal
- J. Attems
Citations in the corpus
- Neuronal Cell Death. (2018, positive): “In keeping with this observation, tau aggregates derived from non-AD tauopathies injected into mice spread throughout distinct regions of the brain that were different from those derived from AD brains (120).”
- Distinct tau prion strains propagate in cells and mice and define different tauopathies (2014, background): “With respect to prion-like intracellular amyloids in humans, recent data indicate that homogenates from distinct tauopathies might reproduce certain pathological features of the diseases in transgenic mice, which is consistent with strain behavior (Clavaguera et al., 2013a).”
- Alzheimer’s and Parkinson’s diseases: The prion concept in relation to assembled Aβ, tau, and α-synuclein (2015, neutral): “Tauopathy was also observed in wild-type mice after seeding with human brain aggregates, although there was a lower density of aggregates than after seeding in transgenic human tau mice (81).”
- Proteopathic tau seeding predicts tauopathy in vivo (2014, background): “Several reports have implicated prion-like seeding as a key mechanism for driving tauopathy disease progression (8, 9, 18, 34, 35).”
- Reconsideration of Amyloid Hypothesis and Tau Hypothesis in Alzheimer's Disease (2018, background): “Microtubule binding regions R3 and R4 form the core of tau fibrils (PHF and SF) (Taniguchi-Watanabe et al., 2016; Fitzpatrick et al., 2017). cells (Clavaguera et al., 2009, 2013; Nonaka et al., 2010; Hasegawa, 2016; Goedert and Spillantini, 2017).”
- Spreading of pathology in neurodegenerative diseases: a focus on human studies (2015, background): “For tauopathies, Clavaguera et al.(26) showed the induction of tau pathology in”
- Primary age-related tauopathy (PART): a common pathology associated with human aging (2014, background): “Theoretically, given experimental findings that tau pathology might be propagated trans-synaptically [34, 35, 38, 46, 47, 57, 91], it is notable that PART-type pathology generally does not progress to the isocortical Braak stages (i.e., V–VI), remaining relatively restricted neuroanatomically even…”