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Hou L., Shao H.Y., Zhang Y.B., Li H., Menon N.K., Neuhaus E.B., Brewer J.M., Byeon I.J.L., Ray D.G., Vitek M.P., et al. Solution NMR studies of the Aβ(1-40) and Aβ(1-42) peptides establish that the met35 oxidation state affects the mechanism of amyloid formation. J Am Chem Soc 126 (2004) 1992-2005
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Hou, L.1
Shao, H.Y.2
Zhang, Y.B.3
Li, H.4
Menon, N.K.5
Neuhaus, E.B.6
Brewer, J.M.7
Byeon, I.J.L.8
Ray, D.G.9
Vitek, M.P.10
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A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
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Petkova A.T., Ishii Y., Balbach J.J., Antzutkin O.N., Leapman R.D., Delaglio F., and Tycko R. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 99 (2002) 16742-16747
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Petkova, A.T.1
Ishii, Y.2
Balbach, J.J.3
Antzutkin, O.N.4
Leapman, R.D.5
Delaglio, F.6
Tycko, R.7
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46
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Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis
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Williams A.D., Portelius E., Kheterpal I., Guo J.T., Cook K.D., Xu Y., and Wetzel R. Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis. J Mol Biol 335 (2004) 833-842
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Williams, A.D.1
Portelius, E.2
Kheterpal, I.3
Guo, J.T.4
Cook, K.D.5
Xu, Y.6
Wetzel, R.7
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47
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The amyloid stretch hypothesis: recruiting proteins toward the dark side
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The nonamyloidogenic protein α-spectrin Src homology 3 domain was converted into a β-aggregation prone sequence upon insertion of a six-residues amyloidogenic segment which did not perturb the stability of the folded state. Moreover, short stretches close to the inserted segment were also shown to belong to the protease-resistant core of the fibril. These experimental results provide strong evidence that the amyloidogenic part of a polypeptide sequence is located in short segments which can even promote the aggregation of adjacent stretches.
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Esteras-Chopo A., Serrano L., and de la Paz M.L. The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc Natl Acad Sci USA 102 (2005) 16672-16677. The nonamyloidogenic protein α-spectrin Src homology 3 domain was converted into a β-aggregation prone sequence upon insertion of a six-residues amyloidogenic segment which did not perturb the stability of the folded state. Moreover, short stretches close to the inserted segment were also shown to belong to the protease-resistant core of the fibril. These experimental results provide strong evidence that the amyloidogenic part of a polypeptide sequence is located in short segments which can even promote the aggregation of adjacent stretches.
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Proc Natl Acad Sci USA
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Esteras-Chopo, A.1
Serrano, L.2
de la Paz, M.L.3
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Inhibition of amyloid fibril formation and cytotoxicity by hydroxyindole derivatives
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Three inhibitors of aggregation of the Alzheimer's Aβ(1-42) peptide were identified by screening 29 indole derivatives using fluorescence spectroscopy, atomic force microscopy and electron microscopy. Very interestingly, 4-hydroxyindole was shown to be the most effective inhibitor, whereas indole did not inhibit. This indicates that the understanding of the mechanism of inhibition requires investigations at the atomic level of detail.
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Cohen T., Frydman-Marom A., Rechter M., and Gazit E. Inhibition of amyloid fibril formation and cytotoxicity by hydroxyindole derivatives. Biochemistry 45 (2006) 4727-4735. Three inhibitors of aggregation of the Alzheimer's Aβ(1-42) peptide were identified by screening 29 indole derivatives using fluorescence spectroscopy, atomic force microscopy and electron microscopy. Very interestingly, 4-hydroxyindole was shown to be the most effective inhibitor, whereas indole did not inhibit. This indicates that the understanding of the mechanism of inhibition requires investigations at the atomic level of detail.
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(2006)
Biochemistry
, vol.45
, pp. 4727-4735
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Cohen, T.1
Frydman-Marom, A.2
Rechter, M.3
Gazit, E.4
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