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Tsuneya Ikezu

Researcher at Boston University

Publications -  156
Citations -  19547

Tsuneya Ikezu is an academic researcher from Boston University. The author has contributed to research in topics: Microglia & Neurodegeneration. The author has an hindex of 47, co-authored 140 publications receiving 14117 citations. Previous affiliations of Tsuneya Ikezu include Boston University Medical Campus & University of Tokyo.

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Minimal information for studies of extracellular vesicles 2018 (MISEV2018) : a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

Clotilde Théry, +417 more
TL;DR: The MISEV2018 guidelines include tables and outlines of suggested protocols and steps to follow to document specific EV-associated functional activities, and a checklist is provided with summaries of key points.
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The spectrum of disease in chronic traumatic encephalopathy

TL;DR: The frequent association of chronic traumatic encephalopathy with other neurodegenerative disorders suggests that repetitive brain trauma and hyperphosphorylated tau protein deposition promote the accumulation of other abnormally aggregated proteins including TAR DNA-binding protein 43, amyloid beta protein and alpha-synuclein.
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Depletion of microglia and inhibition of exosome synthesis halt tau propagation

TL;DR: It is found that depleting microglia dramatically suppressed the propagation of tau and reduced excitability in the dentate gyrus in this mouse model, and this data suggest that microglian involvement in tau propagation and the exosome secretion pathway may be a therapeutic target.
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Identification of Peptide and Protein Ligands for the Caveolin-scaffolding Domain IMPLICATIONS FOR THE INTERACTION OF CAVEOLIN WITH CAVEOLAE-ASSOCIATED PROTEINS

TL;DR: The Caveolin-scaffolding domain is used as a receptor to select random peptide ligands from phage display libraries and it is found that the scaffolding domains of caveolins 1 and 3 both recognize the same peptide and protein ligands, whereas the corresponding domain within caveolin-2 fails to recognize these ligands under the same conditions.