2024-03-28T17:30:30Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1655282020-12-13T09:16:23Zcom_10261_134com_10261_1col_10261_387
Editorial: Molecular chaperones and neurodegeneration
Roodveldt, Cintia
Outeiro, Tiago F.
Braun, Félix
European Commission
Instituto de Salud Carlos III
Ministerio de Economía y Competitividad (España)
Neuroprotection
Neurodegenerative disease
Protein misfolding
Amyloid protein
Proteostasis
Molecular chaperone
Heat-shock protein
Therapeutics
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).
2018-06-01T10:54:03Z
2018-06-01T10:54:03Z
2017
2018-06-01T10:54:03Z
artículo
Frontiers in Neuroscience 11: 565 (2017)
http://hdl.handle.net/10261/165528
10.3389/fnins.2017.00565
http://dx.doi.org/10.13039/501100004587
http://dx.doi.org/10.13039/501100003329
http://dx.doi.org/10.13039/501100000780
29085276
eng
Publisher's version
Sí
http://creativecommons.org/licenses/by/4.0/
openAccess
Frontiers Media