| Year |
Citation |
Score |
| 2013 |
Hou L, Lee HG, Han F, Tedesco JM, Perry G, Smith MA, Zagorski MG. Modification of amyloid-β1-42 fibril structure by methionine-35 oxidation. Journal of Alzheimer's Disease : Jad. 37: 9-18. PMID 23719512 DOI: 10.3233/Jad-122389 |
0.632 |
|
| 2008 |
Zagorski MG, Li L, Hou L, Miller M, Bhaskar K, Anderson V, Mann J, Lamb B. P1-431: Production of micelle-like structures during the early stages of Aβ(1-40) and Aβ(1-42) association Alzheimer's & Dementia. 4: T346-T346. DOI: 10.1016/J.Jalz.2008.05.1013 |
0.643 |
|
| 2006 |
Hou L, Zagorski MG. NMR reveals anomalous copper(II) binding to the amyloid Abeta peptide of Alzheimer's disease. Journal of the American Chemical Society. 128: 9260-1. PMID 16848423 DOI: 10.1021/Ja046032U |
0.682 |
|
| 2004 |
Hou L, Shao H, Zhang Y, Li H, Menon NK, Neuhaus EB, Brewer JM, Byeon IJ, Ray DG, Vitek MP, Iwashita T, Makula RA, Przybyla AB, Zagorski MG. Solution NMR studies of the A beta(1-40) and A beta(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. Journal of the American Chemical Society. 126: 1992-2005. PMID 14971932 DOI: 10.1021/Ja036813F |
0.689 |
|
| 2004 |
Hou L, Zagorski MG. Sorting out the driving forces for parallel and antiparallel alignment in the abeta peptide fibril structure. Biophysical Journal. 86: 1-2. PMID 14695243 DOI: 10.1016/S0006-3495(04)74077-1 |
0.704 |
|
| 2004 |
Zagorski MG, Hou L, Shao H, Zhang Y, Menon N. P1-200 Solution NMR studies of the AB(1-40) and AB(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation Neurobiology of Aging. 25: S153. DOI: 10.1016/S0197-4580(04)80513-X |
0.715 |
|
| 2002 |
Hou L, Kang I, Marchant RE, Zagorski MG. Methionine 35 oxidation reduces fibril assembly of the amyloid abeta-(1-42) peptide of Alzheimer's disease. The Journal of Biological Chemistry. 277: 40173-6. PMID 12198111 DOI: 10.1074/Jbc.C200338200 |
0.733 |
|
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