Biblio
Found 9 results
Filters: Author is Friedman, R. [Clear All Filters]
Wild type and mutants of the HET-s(218-289) prion show different flexibility at fibrillar ends: A simulation study. Proteins: Structure, Function, and Bioinformatics. 82(3):399-404.
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2014. Surfactant effects on amyloid aggregation kinetics. Journal of Molecular Biology. 414(2):303-312.
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2011. Wordom: A user-friendly program for the analysis of molecular structures, trajectories, and free energy surfaces. Journal of Computational Chemistry. 32(6):1183-1194.
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2011. On the orientation of the catalytic dyad in aspartic proteases. Proteins. 78(6):1575-1582.
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2010. Soluble protofibrils as metastable intermediates in simulations of amyloid fibril degradation induced by lipid vesicles. The Journal of Physical Chemistry Letters. 1(2):471-474.
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2010. Amyloid aggregation on lipid bilayers and its impact on membrane permeability. J. Mol. Biol.. 387(2):407-415.
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2009. Discovery of plasmepsin inhibitors by fragment-based docking and consensus scoring. ChemMedChem. 4(8):1317-1326.
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2009. Pepsinogen-like activation intermediate of plasmepsin II revealed by molecular dynamics analysis. Proteins: Structure, Function, and Bioinformatics. 73(4):814-827.
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2008. The protonation state of the catalytic aspartates in plasmepsin II. FEBS Letters. 581(21):4120-4124.
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2007.