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Título: | Editorial: Molecular chaperones and neurodegeneration |
Autor: | Roodveldt, Cintia CSIC ORCID; Outeiro, Tiago F.; Braun, Félix | Palabras clave: | Neuroprotection Neurodegenerative diseases Protein misfolding Amyloid protein Proteostasis Molecular chaperone Heat-shock proteins Therapeutics |
Fecha de publicación: | 2017 | Editor: | Frontiers Media | Citación: | Frontiers in Neuroscience 11: 565 (2017) | Resumen: | Molecular 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). | URI: | http://hdl.handle.net/10261/165528 | DOI: | 10.3389/fnins.2017.00565 | Identificadores: | doi: 10.3389/fnins.2017.00565 e-issn: 1662-453X issn: 1662-4548 |
Aparece en las colecciones: | (CABIMER) Artículos |
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