Biblio
Found 14 results
Filters: Keyword is Amyloid [Clear All Filters]
Simulation studies of amyloidogenic polypeptides and their aggregates. Chemical Reviews. 119(12):6956-6993.
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2019. Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria. Nature Chemical Biology. 8(8):701-706.
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2012. Photocontrol of reversible amyloid formation with a minimal-design peptide. The Journal of Physical Chemistry B. 116(30):8961-8973.
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2012. Surfactant effects on amyloid aggregation kinetics. Journal of Molecular Biology. 414(2):303-312.
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2011. Amyloid fibril polymorphism is under kinetic control. Journal of the American Chemical Society. 132(42):14960-14970.
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2010. 9,10-Anthraquinone hinders beta-aggregation: How does a small molecule interfere with Abeta-peptide amyloid fibrillation? Protein Science. 18(4):792-800.
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2009. Amyloid aggregation on lipid bilayers and its impact on membrane permeability. J. Mol. Biol.. 387(2):407-415.
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2009. Computational analysis of the S. cerevisiae proteome reveals the function and cellular localization of the least and most amyloidogenic proteins. Proteins: Structure, Function, and Bioinformatics. 68(1):273-278.
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2007. Pathways and intermediates of amyloid fibril formation. Journal of Molecular Biology. 374(4):917-924.
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2007. Interpreting the aggregation kinetics of amyloid peptides. Journal of Molecular Biology. 360(4):882-892.
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2006. A molecular dynamics approach to the structural characterization of amyloid aggregation. Journal of Molecular Biology. 357(4):1306-1321.
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2006. Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Science. 14(10):2723-2734.
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2005. Replica exchange molecular dynamics simulations of amyloid peptide aggregation. Journal of Chemical Physics. 121(21):10748-10756.
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2004. The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35. Proceedings of the National Academy of Sciences of the United States of America. 100(9):5154-5159.
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