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Título

Editorial: Molecular chaperones and neurodegeneration

AutorRoodveldt, Cintia ; Outeiro, Tiago F.; Braun, Félix
Palabras claveNeuroprotection
Neurodegenerative disease
Protein misfolding
Amyloid protein
Proteostasis
Molecular chaperone
Heat-shock protein
Therapeutics
Fecha de publicación2017
EditorFrontiers Media
CitaciónFrontiers in Neuroscience 11: 565 (2017)
ResumenMolecular chaperones, including heat-shock proteins (HSPs), or stress proteins, are highly conserved proteins that play a critical role in the regulation of cellular protein homeostasis (proteostasis). Proteostasis is essential for the maintenance of the functionality of the proteome and, ultimately, of cells. Disruption of proteostasis leads to the accumulation of aberrantly folded proteins that typically lose their function. The accumulation of misfolded and aggregated proteins, due to genetic mutations, posttranslational modifications, or due to an age-related decline in cellular functions, can be also cytotoxic and has been linked to the pathogenesis of various degenerative diseases including those affecting the nervous system, such as Alzheimer’s (AD), Parkinson’s (PD) and Huntington’s diseases (HD), or amyotrophic lateral sclerosis (ALS).
URIhttp://hdl.handle.net/10261/165528
Identificadoresdoi: 10.3389/fnins.2017.00565
e-issn: 1662-453X
issn: 1662-4548
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