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Bernardino Ghetti

Researcher at Indiana University

Publications -  52
Citations -  5720

Bernardino Ghetti is an academic researcher from Indiana University. The author has contributed to research in topics: Tau protein & Neurodegeneration. The author has an hindex of 27, co-authored 52 publications receiving 3714 citations. Previous affiliations of Bernardino Ghetti include Indiana University – Purdue University Indianapolis & Harvard University.

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Structures of filaments from Pick’s disease reveal a novel tau protein fold

TL;DR: This work determines the structures of tau filaments from patients with Pick’s disease, a neurodegenerative disorder characterized by frontotemporal dementia, and shows how tau can adopt distinct folds in the human brain in different diseases, an essential step for understanding the formation and propagation of molecular conformers.
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Serum neurofilament dynamics predicts neurodegeneration and clinical progression in presymptomatic Alzheimer’s disease

TL;DR: Serum NfL dynamics in serum predict disease progression and brain neurodegeneration at the early presymptomatic stages of familial Alzheimer’s disease, which supports its potential utility as a clinically useful biomarker.
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Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules.

TL;DR: Cryo-electron microscopy structures of tau filaments from the brains of three individuals with chronic traumatic encephalopathy reveal distinct assembled tau conformers, with a novel protofilament fold enclosing hydrophobic molecules, and support the hypothesis that the formation and propagation of distinct conformers ofassembled tau underlie different neurodegenerative diseases.
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Structures of α-synuclein filaments from multiple system atrophy

TL;DR: Cryo-electron microscopy reveals the structures of α-synuclein filaments from the brains of individuals with multiple system atrophy, which has implications for understanding the mechanisms of aggregate propagation and neurodegeneration in the human brain.
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Invited review: Frontotemporal dementia caused by microtubule-associated protein tau gene (MAPT) mutations: a chameleon for neuropathology and neuroimaging.

TL;DR: In this article, three neuropathologic subtypes can be recognized, based on the presence of inclusions made of tau isoforms with three and four repeats, predominantly three repeats and mostly four repeats.