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Harrison Tudor Evans

Researcher at University of Queensland

Publications -  9
Citations -  341

Harrison Tudor Evans is an academic researcher from University of Queensland. The author has contributed to research in topics: Tauopathy & Proteome. The author has an hindex of 6, co-authored 9 publications receiving 198 citations.

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Combined effects of scanning ultrasound and a tau-specific single chain antibody in a tau transgenic mouse model

TL;DR: It is demonstrated that non-invasive scanning ultrasound increases the delivery of tau-specific single-chain antibody fragments across the blood-brain barrier and into neurons of t Tau transgenic mice, reducing anxiety-like behaviour and tau pathology.
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Decreased synthesis of ribosomal proteins in tauopathy revealed by non-canonical amino acid labelling.

TL;DR: These findings present a potential pathomechanism by which pathological tau interferes with cellular functions through the dysregulation of ribosomal protein synthesis.
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Accelerated aging exacerbates a pre-existing pathology in a tau transgenic mouse model

TL;DR: It is concluded that accelerated aging exacerbates pathological tau phosphorylation, leading to changes in normal behaviour, and further suggest that SApT mice may be a useful novel model in which to study the role of a complex geriatric phenotype in tauopathy.
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Cell-specific non-canonical amino acid labelling identifies changes in the de novo proteome during memory formation

TL;DR: A novel mouse strain is generated, which enables cell-type-specific labelling of newly synthesised proteins with non-canonical amino acids (NCAAs) by genetically restricting the expression of the mutant tRNA synthetase, NLL-MetRS, to hippocampal neurons.
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PTEN activation contributes to neuronal and synaptic engulfment by microglia in tauopathy

TL;DR: It is found that pathological Tau promotes early activation of PTEN, which precedes apoptotic caspase-3 cleavage in the rTg4510 mouse model of FTLD-Tau, suggesting that in tauopathy, PTEN has a role in the synaptotoxicity of pathological Tau and promotes microglial removal of affected neuronal structures.