What does make an amyloid toxic: morphology, structure or interaction with membrane?
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Stem Cell Therapy: A Prospective Treatment for Alzheimer's Diseaseβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHLearning To Fold Proteins Using Energy Landscape Theory.α-Synuclein oligomers induced by docosahexaenoic acid affect membrane integrity.The Position of Aβ22-40 and Aβ1-42 in Anionic Lipid Membranes Containing Cholesterol.Free energy landscapes for initiation and branching of protein aggregation.Atomic force microscopy to study molecular mechanisms of amyloid fibril formation and toxicity in Alzheimer's disease.Distinguishing closely related amyloid precursors using an RNA aptamer.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.A structure-toxicity study of Aß42 reveals a new anti-parallel aggregation pathway.Metal complexes for multimodal imaging of misfolded protein-related diseases.Tip-Enhanced Raman Spectroscopy to Distinguish Toxic Oligomers from Aβ1-42 Fibrils at the Nanometer Scale.The Amyloid Fibril-Forming Properties of the Amphibian Antimicrobial Peptide Uperin 3.5.Alzheimer's peptide amyloid-β, fragment 22-40, perturbs lipid dynamics.No effects without causes: the Iron Dysregulation and Dormant Microbes hypothesis for chronic, inflammatory diseases.
P2860
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P2860
What does make an amyloid toxic: morphology, structure or interaction with membrane?
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article científic
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What does make an amyloid toxic: morphology, structure or interaction with membrane?
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What does make an amyloid toxic: morphology, structure or interaction with membrane?
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What does make an amyloid toxic: morphology, structure or interaction with membrane?
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P1433
P1476
What does make an amyloid toxic: morphology, structure or interaction with membrane?
@en
P2093
Sophie Lecomte
P356
10.1016/J.BIOCHI.2012.07.011
P577
2012-07-20T00:00:00Z