Published in J Mol Biol on October 05, 2001
Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci U S A (2002) 5.46
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A partially folded structure of amyloid-beta(1-40) in an aqueous environment. Biochem Biophys Res Commun (2011) 1.51
Structure of the 21-30 fragment of amyloid beta-protein. Protein Sci (2006) 1.51
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A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides. Protein Eng Des Sel (2009) 1.38
Design of small molecules that target metal-A{beta} species and regulate metal-induced A{beta} aggregation and neurotoxicity. Proc Natl Acad Sci U S A (2010) 1.37
Aqueous urea solution destabilizes Abeta(16-22) oligomers. Proc Natl Acad Sci U S A (2004) 1.34
Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAIL. Biophys J (2003) 1.33
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Hypoxia due to cardiac arrest induces a time-dependent increase in serum amyloid β levels in humans. PLoS One (2011) 1.09
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Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM. Proc Natl Acad Sci U S A (2015) 1.07
Binding of amyloid beta-peptide to ganglioside micelles is dependent on histidine-13. Biochem J (2006) 1.05
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils. J Lipid Res (2011) 1.05
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Formation of amyloid fibrils from fully reduced hen egg white lysozyme. Protein Sci (2004) 1.03
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The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency. Biochim Biophys Acta (2011) 0.95
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Nanoprobing of the effect of Cu(2+) cations on misfolding, interaction and aggregation of amyloid β peptide. J Neuroimmune Pharmacol (2012) 0.89
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