Protein Misfolding in Neurodegenerative Diseases: Recent Advances and Therapeutical Implications
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biology".
Deadline for manuscript submissions: closed (15 October 2021) | Viewed by 5194
Special Issue Editor
Interests: neurodegeneration; protein conformational disorders; alpha-synuclein; Parkinson's disease and related synucleinopathies; transthyretin (TTR); TTR-related amyloidosis
Special Issue Information
Dear Colleagues,
A common molecular hallmark feature shared by several clinicopathologically different neurodegenerative diseases is the altered protein homeostasis, leading to protein misfolding and the aggregation of a broad variety of otherwise soluble proteins in the form of insoluble amyloid deposits. Although the precise mechanisms by which protein misfolding and aggregation is involved in neurodegeneration are still unclear, compelling evidence supports a loss of physiological function and/or gain of toxic function upon protein misfolding, leading to the abnormal intra- or extracellular accumulation of amyloid deposits that are resistant to degradation playing a major role in the pathogenesis of protein conformational diseases. Building on these findings, several disease-modifying therapeutical approaches have been proposed, which target the different steps in the synthesis and processing of aggregation-prone proteins, including lowering the concentration of the amyloidogenic protein, stabilization of the protein native state conformation and therefore preventing its aggregation, modulation of the proteome quality control via proteasome and autophagy pathways, and decreasing the vicious cycle of amyloid formation seeding and spreading. The aim of this Special Issue is to summarise the current knowledge on the molecular mechanisms underlying protein misfolding and its relationship with neurotoxicity, and to highlight emerging therapeutic strategies for the prevention or treatment of neurodegenerative disorders associated with protein aggregation.
Dr. Nelson Ferreira
Guest Editor
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