Preprint Review Version 2 Preserved in Portico This version is not peer-reviewed

Structural Variations of Prions and Prion-Like Proteins Associated with Neurodegeneration

Version 1 : Received: 15 August 2023 / Approved: 15 August 2023 / Online: 16 August 2023 (11:37:48 CEST)
Version 2 : Received: 17 December 2023 / Approved: 18 December 2023 / Online: 19 December 2023 (09:42:02 CET)

A peer-reviewed article of this Preprint also exists.

Christensen, C.S.; Wang, S.; Li, W.; Yu, D.; Li, H.J. Structural Variations of Prions and Prion-like Proteins Associated with Neurodegeneration. Current Issues in Molecular Biology 2024, 46, 6423–6439, doi:10.3390/cimb46070384. Christensen, C.S.; Wang, S.; Li, W.; Yu, D.; Li, H.J. Structural Variations of Prions and Prion-like Proteins Associated with Neurodegeneration. Current Issues in Molecular Biology 2024, 46, 6423–6439, doi:10.3390/cimb46070384.

Abstract

Neurodegeneration is becoming one of the leading causes of death worldwide as the population expands and grows older. There is a growing desire to understand the mechanisms behind prion proteins as well as the prion-like proteins that make up neurodegenerative diseases (NDs) including Alzheimer’s Disease (AD). Both amyloid β (Aβ) and hyperphosphorylated tau (p-tau) proteins behave in ways similar to that of the infectious form of the prion protein, PrPSc, such as aggregating, seeding, and replicating under not yet fully understood mechanisms, thus the designation of prion-like. This review aims to highlight the shared mechanisms between prion-like proteins and prion proteins in the structural variations associated with aggregation and disease development. These mechanisms are largely focusing on the dysregulation of protein homeostasis, self-replication, and protein aggregation, and how this knowledge could contribute to diagnoses and treatments for the given NDs.

Keywords

prions; neurodegeneration; Alzheimer’s disease; protein homeostasis; aggregation; prion-like proteins; amyloid beta; hyperphosphorylated tau; self replication

Subject

Biology and Life Sciences, Neuroscience and Neurology

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