Amyloid Toxicity Is Independent of Polypeptide Sequence, Length and Chirality
- 18 January 2008
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 375 (3) , 695-707
- https://doi.org/10.1016/j.jmb.2007.08.012
Abstract
No abstract availableKeywords
Funding Information
- European Commission
- Ministerio de Educación, Cultura y Deporte
This publication has 40 references indexed in Scilit:
- High-resolution Atomic Force Microscopy of Soluble Aβ42 OligomersJournal of Molecular Biology, 2006
- Secondary Structure of α-Synuclein Oligomers: Characterization by Raman and Atomic Force MicroscopyJournal of Molecular Biology, 2006
- Probing the Mechanism of Amyloidogenesis through a Tandem Repeat of the PI3-SH3 Domain Suggests a Generic Model for Protein Aggregation and Fibril FormationJournal of Molecular Biology, 2005
- Seeding-dependent Propagation and Maturation of Amyloid Fibril ConformationJournal of Molecular Biology, 2005
- Multiple Assembly Pathways Underlie Amyloid-β Fibril PolymorphismsJournal of Molecular Biology, 2005
- Natural oligomers of the amyloid-β protein specifically disrupt cognitive functionNature Neuroscience, 2004
- Fibrillogenesis and Cytotoxic Activity of the Amyloid-forming Apomyoglobin Mutant W7FW14FJournal of Biological Chemistry, 2004
- Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolutionJournal of Molecular Medicine, 2003
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of PathogenesisScience, 2003
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002