Published in J Biol Chem on May 06, 2004
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Amyloid-like aggregates of the yeast prion protein ure2 enter vertebrate cells by specific endocytotic pathways and induce apoptosis. PLoS One (2010) 0.80
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Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature (2003) 4.98
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Amyloid formation by globular proteins under native conditions. Nat Chem Biol (2009) 3.72
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc Natl Acad Sci U S A (2004) 3.58
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Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature (2004) 2.84
The importance of sequence diversity in the aggregation and evolution of proteins. Nature (2005) 2.70
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Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J Mol Biol (2004) 2.14
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