S3‐03‐05: Transmission and Spreading of Tauopathy in Transgenic Mouse Brain

By M. Tolnay. 2011

1,556 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/444e891eae5a7e368d2aec305b6424c2eec448b0

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Citations in the corpus

Distinct tau prion strains propagate in cells and mice and define different tauopathies (2014, background): “In vivo work supports this model (Clavaguera et al., 2009; de Calignon et al., 2012; Iba et al., 2013; Kim et al., 2010; Liu et al., 2012) as has similar work with other intracellular amyloids such as a-synuclein (Desplats et al.”
Brain homogenates from human tauopathies induce tau inclusions in mouse brain (2013, methodology): “Total counts of silver-positive structures at the hippocampal injection site were assessed on selected Gallyas-Braak–stained coronal sections as described (20).”
Biochemistry and cell biology of tau protein in neurofibrillary degeneration. (2012, background): “One hypothesis is that affected neurons release pathological Tau, which is taken up by neighboring cells and thus spreads the pathology in a prion-like fashion (Clavaguera et al. 2009; Frost et al. 2009).”
Alzheimer’s Disease: The Challenge of the Second Century (2011, background): “In the case of tau, injections of brain extracts from genetically modified mice that have tau aggregates into the brains of mice that express wild-type human tau that would otherwise not develop tau aggregates result in assembly of wild-type tau into filaments and spreading of pathology from the sit”
The Many Faces of Tau (2011, background): “2 promoter caused intraneuronal formation of wild-type 4R2N human tau inclusions in the hippocampus that spread along synaptic connections to distant brain regions (Clavaguera et al., 2009).”
Prion-like spreading of pathological α-synuclein in brain (2013, background): “In addition, a growing body of evidence indicates that self-propagating protein aggregates play central roles in many neurodegenerative diseases, including Parkinson’s disease and Alzheimer’s disease (Clavaguera et al., 2009; Mougenot et al., 2012; Luk et al., 2012b; Stohr et al., 2012).”
Aβ Oligomers Cause Localized Ca2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines (2010, background): “, 2007), and indeed the Tau pathology correlates well with clinical symptoms (Braak and Braak, 1991; Clavaguera et al., 2009).”
Prion-like transmission of protein aggregates in neurodegenerative diseases (2010, background): “This is supported by observations that mutant human tau injected into mouse brains induces the aggregation of the endogenous wild-type mouse protein, and that pathology spreads from the injection site to neighbouring brain region”
Alzheimer’s and Parkinson’s diseases: The prion concept in relation to assembled Aβ, tau, and α-synuclein (2015, unknown): “Intracerebral injection of human mutant tau inclusions into the brains of mice transgenic for wild-type human tau induced the formation of inclusions that spread to distant brain regions (79).”
Predicting regional neurodegeneration from the healthy brain functional connectome. (2012, background): “Providing a more parsimonious account, growing evidence suggests that prion-like mechanisms may promote the spread of toxic, misfolded, nonprion protein species between interconnected neurons (Baker et al., 1993, 1994; Brundin et al., 2010; Clavaguera et al., 2009; Frost and Diamond, 2010; Frost et ”