Please use this identifier to cite or link to this item: https://www.um.edu.mt/library/oar/handle/123456789/119066
Title: Editorial : oligomers in amyloid-associated diseases—structural properties and toxicity
Authors: Vassallo, Neville
Ongeri, Sandrine
De Simone, Alfonso
Keywords: Amyloid
Nervous system -- Degeneration
Toxicity testing
Oligomers
Nervous system -- Diseases
Issue Date: 2023
Publisher: Frontiers Research Foundation
Citation: Vassallo, N., Ongeri, S., & De Simone, A. (2023). Editorial : Oligomers in amyloid-associated diseases—structural properties and toxicity. Frontiers in Molecular Biosciences, 10, 1215340.
Abstract: The so-called “amyloid proteinopathies” represent a constellation of human diseases associated with the pathological formation and deposition of aberrant insoluble protein aggregates. They include neurodegenerative conditions such as Alzheimer’s, Parkinson’s and Huntington’s diseases, amyotrophic lateral sclerosis, and prion diseases; but may also involve organs and tissues outside the central nervous system, for instance the pancreas in type-2 diabetes mellitus. Collectively, amyloid-associated disorders affect around 50 million people each year worldwide and no cure is essentially known to stop the underlying molecular mechanisms of their origin. These conditions therefore generate significant burden on individuals, societies and healthcare budgets, and there is a burgeoning need for the rational development of effective therapeutic strategies.
URI: https://www.um.edu.mt/library/oar/handle/123456789/119066
ISSN: 2296889X
Appears in Collections:Scholarly Works - FacM&SPB



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