αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide
- 1 November 2010
- journal article
- research article
- Published by Elsevier BV in Cell Stress and Chaperones
- Vol. 15 (6), 1013-1026
- https://doi.org/10.1007/s12192-010-0212-z
Abstract
No abstract availableThis publication has 66 references indexed in Scilit:
- Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregationProceedings of the National Academy of Sciences of the United States of America, 2010
- Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicityProceedings of the National Academy of Sciences of the United States of America, 2010
- Amyloid β-Protein Toxicity and the Pathogenesis of Alzheimer DiseasePublished by Elsevier BV ,2009
- Dissociation from the Oligomeric State Is the Rate-limiting Step in Fibril Formation by κ-CaseinPublished by Elsevier BV ,2008
- In Vitro and In Vivo Neurotoxicity of Prion Protein OligomersPLoS Pathogens, 2007
- Mimicking phosphorylation of αB-crystallin affects its chaperone activityBiochemical Journal, 2006
- Amyloid Fibril Formation by Bovine Milk κ-Casein and Its Inhibition by the Molecular Chaperones αS- and β-CaseinBiochemistry, 2005
- Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone ActivityJournal of Molecular Biology, 2004
- Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolutionJournal of Molecular Medicine, 2003
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002