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Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease.
Neurodegener Dis. 2011;8(6):397-412. doi: 10.1159/000324514. Epub 2011 Mar 16.
Neurodegener Dis. 2011.
PMID: 21411979
Review.
Chaperones and proteases: cellular fold-controlling factors of proteins in neurodegenerative diseases and aging.
Hinault MP, Ben-Zvi A, Goloubinoff P.
Hinault MP, et al.
J Mol Neurosci. 2006;30(3):249-65. doi: 10.1385/JMN:30:3:249.
J Mol Neurosci. 2006.
PMID: 17401151
Review.
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Molecular crime and cellular punishment: active detoxification of misfolded and aggregated proteins in the cell by the chaperone and protease networks.
Hinault MP, Goloubinoff P.
Hinault MP, et al.
Adv Exp Med Biol. 2007;594:47-54. doi: 10.1007/978-0-387-39975-1_5.
Adv Exp Med Biol. 2007.
PMID: 17205674
Review.
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The Mitochondrial Small Heat Shock Protein HSP22 from Pea is a Thermosoluble Chaperone Prone to Co-Precipitate with Unfolding Client Proteins.
Avelange-Macherel MH, Rolland A, Hinault MP, Tolleter D, Macherel D.
Avelange-Macherel MH, et al. Among authors: hinault mp.
Int J Mol Sci. 2019 Dec 21;21(1):97. doi: 10.3390/ijms21010097.
Int J Mol Sci. 2019.
PMID: 31877784
Free PMC article.
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Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones.
Hinault MP, Cuendet AF, Mattoo RU, Mensi M, Dietler G, Lashuel HA, Goloubinoff P.
Hinault MP, et al.
J Biol Chem. 2010 Dec 3;285(49):38173-82. doi: 10.1074/jbc.M110.127753. Epub 2010 Sep 16.
J Biol Chem. 2010.
PMID: 20847048
Free PMC article.
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