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Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases

Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, School of Medicine, Via S. Pansini 5, 80131 Naples, Italy
Int. J. Mol. Sci. 2018, 19(10), 3081; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19103081
Received: 4 September 2018 / Revised: 1 October 2018 / Accepted: 5 October 2018 / Published: 9 October 2018
(This article belongs to the Collection Protein Folding)
The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases including Alzheimer’s disease, Parkinson’s disease, and prion diseases. It is believed that misfolded and abnormal β-sheets forms of wild-type proteins are the vectors of these diseases by acting as seeds for the aggregation of endogenous proteins. Cellular prion protein (PrPC) is a glycosyl-phosphatidyl-inositol (GPI) anchored glycoprotein that is able to misfold to a pathogenic isoform PrPSc, the causative agent of prion diseases which present as sporadic, dominantly inherited and transmissible infectious disorders. Increasing evidence highlights the importance of prion-like seeding as a mechanism for pathological spread in Alzheimer’s disease and Tauopathy, as well as other neurodegenerative disorders. Here, we report the latest findings on the mechanisms controlling protein folding, focusing on the ER (Endoplasmic Reticulum) quality control of GPI-anchored proteins and describe the “prion-like” properties of amyloid-β and tau assemblies. Furthermore, we highlight the importance of pathogenic assemblies interaction with protein and lipid membrane components and their implications in both prion and Alzheimer’s diseases View Full-Text
Keywords: Aβ; aggregation; amyloid; APP; misfolding; prion protein; prion-like; PrP; seeds; tau ; aggregation; amyloid; APP; misfolding; prion protein; prion-like; PrP; seeds; tau
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MDPI and ACS Style

Sarnataro, D. Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases. Int. J. Mol. Sci. 2018, 19, 3081. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19103081

AMA Style

Sarnataro D. Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases. International Journal of Molecular Sciences. 2018; 19(10):3081. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19103081

Chicago/Turabian Style

Sarnataro, Daniela. 2018. "Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases" International Journal of Molecular Sciences 19, no. 10: 3081. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms19103081

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