The small heat shock protein B8 (HSPB8) efficiently removes aggregating species of dipeptides produced in C9ORF72-related neurodegenerative diseases

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are two neurodegenerative diseases in which similar pathogenic mechanisms are involved. Both diseases associate to the high propensity of specific misfolded proteins, like TDP-43 or FUS, to mislocalize and aggregate. This is partl...

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Veröffentlicht in:	Cell stress & chaperones 2018-01, Vol.23 (1), p.1-12
Hauptverfasser:	Cristofani, Riccardo, Crippa, Valeria, Vezzoli, Giulia, Rusmini, Paola, Galbiati, Mariarita, Cicardi, Maria Elena, Meroni, Marco, Ferrari, Veronica, Tedesco, Barbara, Piccolella, Margherita, Messi, Elio, Carra, Serena, Poletti, Angelo
Format:	Artikel
Sprache:	eng
Schlagworte:	Aberration Agglomeration Amyotrophic lateral sclerosis Animals Autophagy Autophagy - drug effects Biochemistry Biomedical and Life Sciences Biomedicine C9orf72 Protein - metabolism Cancer Research Cell Biology Cell Line, Transformed Dementia disorders Dipeptides - metabolism Frontotemporal dementia Gene Silencing Heat shock proteins HSP20 Heat-Shock Proteins - metabolism Immunology Mice Motor neurone disease Motor neurons Motor Neurons - metabolism Motor Neurons - pathology Neurodegenerative diseases Neurodegenerative Diseases - metabolism Neurodegenerative Diseases - pathology Neurological diseases Neurosciences Original Paper Phagocytosis Proteasome Inhibitors - pharmacology Protein Aggregates Protein folding Quality control Toxicity Transcription Ubiquitin Up-Regulation - drug effects Viability
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