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Khandogin, J., Brooks, C. L. (2007) Linking folding with aggregation in Alzheimer's beta-amyloid peptides. Proceedings of the National Academy of Sciences, 104 (43) 16880-16885 doi:10.1073/pnas.0703832104

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Reference TypeJournal (article/letter/editorial)
TitleLinking folding with aggregation in Alzheimer's beta-amyloid peptides
JournalProceedings of the National Academy of Sciences
AuthorsKhandogin, J.Author
Brooks, C. L.Author
Year2007 (October 23)Volume104
Issue43
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0703832104Search in ResearchGate
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Mindat Ref. ID1743735Long-form Identifiermindat:1:5:1743735:8
GUID0
Full ReferenceKhandogin, J., Brooks, C. L. (2007) Linking folding with aggregation in Alzheimer's beta-amyloid peptides. Proceedings of the National Academy of Sciences, 104 (43) 16880-16885 doi:10.1073/pnas.0703832104
Plain TextKhandogin, J., Brooks, C. L. (2007) Linking folding with aggregation in Alzheimer's beta-amyloid peptides. Proceedings of the National Academy of Sciences, 104 (43) 16880-16885 doi:10.1073/pnas.0703832104
In(2007, October) Proceedings of the National Academy of Sciences Vol. 104 (43) Proceedings of the National Academy of Sciences

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Khandogin, J., Chen, J., Brooks, C. L. (2006) Exploring atomistic details of pH-dependent peptide folding. Proceedings of the National Academy of Sciences, 103 (49) 18546-18550 doi:10.1073/pnas.0605216103
Flajolet, M., He, G., Heiman, M., Lin, A., Nairn, A. C., Greengard, P. (2007) Regulation of Alzheimer's disease amyloid-beta formation by casein kinase I. Proceedings of the National Academy of Sciences, 104 (10) 4159-4164 doi:10.1073/pnas.0611236104
Rajendran, L., Honsho, M., Zahn, T. R., Keller, P., Geiger, K. D., Verkade, P., Simons, K. (2006) Alzheimer's disease beta-amyloid peptides are released in association with exosomes. Proceedings of the National Academy of Sciences, 103 (30) 11172-11177 doi:10.1073/pnas.0603838103
Grant, M. A., Lazo, N. D., Lomakin, A., Condron, M. M., Arai, H., Yamin, G., Rigby, A. C., Teplow, D. B. (2007) Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleus. Proceedings of the National Academy of Sciences, 104 (42) 16522-16527 doi:10.1073/pnas.0705197104
Im, W., Brooks, C. L. (2005) Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations. Proceedings of the National Academy of Sciences, 102 (19) 6771-6776 doi:10.1073/pnas.0408135102
Gouras, G. K., Xu, H., Gross, R. S., Greenfield, J. P., Hai, B., Wang, R., Greengard, P. (2000) Testosterone reduces neuronal secretion of Alzheimer's beta -amyloid peptides. Proceedings of the National Academy of Sciences, 97 (3) 1202-1205 doi:10.1073/pnas.97.3.1202
Parkin, E. T., Watt, N. T., Hussain, I., Eckman, E. A., Eckman, C. B., Manson, J. C., Baybutt, H. N., Turner, A. J., Hooper, N. M. (2007) Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein. Proceedings of the National Academy of Sciences, 104 (26) 11062-11067 doi:10.1073/pnas.0609621104
Bali, J., Gheinani, A. H., Zurbriggen, S., Rajendran, L. (2012) Role of genes linked to sporadic Alzheimer's disease risk in the production of  -amyloid peptides. Proceedings of the National Academy of Sciences, 109 (38) 15307-15311 doi:10.1073/pnas.1201632109
Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V., Lee, J.-M. (2009) Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proceedings of the National Academy of Sciences, 106 (48) 20324-20329 doi:10.1073/pnas.0911281106
Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M., Mucke, L. (2001)  -Amyloid peptides enhance  -synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease. Proceedings of the National Academy of Sciences, 98 (21) 12245-12250 doi:10.1073/pnas.211412398
Brooks, C. L. (2002) Viewing protein folding from many perspectives. Proceedings of the National Academy of Sciences, 99 (3) 1099-1100 doi:10.1073/pnas.042708199
 
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