Sequence-independent Control of Peptide Conformation in Liposomal Vaccines for Targeting Protein Misfolding Diseases
Open Access
- 1 April 2011
- journal article
- Published by Elsevier BV
- Vol. 286 (16), 13966-13976
- https://doi.org/10.1074/jbc.m110.186338
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Structure–neurotoxicity relationships of amyloid β-protein oligomersProceedings of the National Academy of Sciences, 2009
- Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current statusJournal of Chemical Biology, 2009
- Amino Acid Position-specific Contributions to Amyloid β-Protein OligomerizationJournal of Biological Chemistry, 2009
- Two-state selection of conformation-specific antibodiesProceedings of the National Academy of Sciences, 2009
- Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memoryNature Medicine, 2008
- Structural basis for the binding of the neutralizing antibody, 7D11, to the poxvirus L1 proteinVirology, 2007
- Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic miceProceedings of the National Academy of Sciences, 2007
- Natural oligomers of the amyloid-β protein specifically disrupt cognitive functionNature Neuroscience, 2004
- Folding proteins in fatal waysNature, 2003
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002