Polymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape
Top Cited Papers
Open Access
- 19 April 2010
- journal article
- review article
- Published by American Chemical Society (ACS) in Chemical Reviews
- Vol. 110 (8) , 4820-4838
- https://doi.org/10.1021/cr900377t
Abstract
No abstract availableThis publication has 295 references indexed in Scilit:
- Misfolded Amyloid Ion Channels Present Mobile β-Sheet Subunits in Contrast to Conventional Ion ChannelsBiophysical Journal, 2009
- Polymorphism of Alzheimer's Aβ17-42 (p3) Oligomers: The Importance of the Turn Location and Its ConformationBiophysical Journal, 2009
- Globular Tetramers of β2-Microglobulin Assemble into Elaborate Amyloid FibrilsJournal of Molecular Biology, 2009
- The Structure of Aβ42 C-Terminal Fragments Probed by a Combined Experimental and Theoretical StudyJournal of Molecular Biology, 2009
- Replica Exchange Simulations of the Thermodynamics of Aβ Fibril GrowthBiophysical Journal, 2009
- Principles of flexible protein–protein dockingProteins-Structure Function and Bioinformatics, 2008
- Structures and Free-Energy Landscapes of the Wild Type and Mutants of the Aβ21–30 Peptide Are Determined by an Interplay between Intrapeptide Electrostatic and Hydrophobic InteractionsJournal of Molecular Biology, 2008
- Conformational Stability of PrP Amyloid Fibrils Controls Their Smallest Possible Fragment SizeJournal of Molecular Biology, 2008
- Fibril Growth Kinetics Reveal a Region of β2-microglobulin Important for Nucleation and Elongation of AggregationJournal of Molecular Biology, 2008
- Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigmBiochimica et Biophysica Acta (BBA) - Biomembranes, 2007