Glenner, G.G. and Wong, C.W. (1984) Alzheimer’s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochemical and Biophysical Research Communications, 120, 885 890.
 Yamaguchi, H., Nakazato, Y., Hirai, S., Shoji, M. and Harigaya, Y. (1989) Electron micrograph of diffuse plaques. Initial stage of senile plaque formation in the Alzheimer brain. The American Journal of Pathology, 135, 593597.
 Hashimoto, M., Rockenstein, E., Crews, L. and Masliah, E. (2003) Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer’s and Parkinson’s diseases. Neuromolecular Medicine, 4, 21 35.
 Bucciantini, M., Calloni, G., Chiti, F., Formigli, L., Nosi, D., Dobson, C.M. and Stefani, M. (2004) Prefibrillar amyloid protein aggregates share common features of cytotoxicity. The Journal of Biological Chemistry, 279, 3137431382.
 Rogers, J., Cooper, N.R., Webster, S., Schultz, J., McGeer, P.L., Styren, S.D., Civin, W.H., Brachova, L., Bradt, B. and Ward, P. (1992) Complement activation by betaamyloid in Alzheimer disease. Proceedings of National Academy of Science of the United States of America, 89, 1001610020.
 Rudyk, H., Vasiljevic, S., Hennion, R.M., Birkett, C.R., Hope, J. and Gilbert, I.H. (2000) Screening Congo red and it is analogues for their ability to prevent the formation of PrPres in scrapieinfected cell. Journal of General Virology, 81, 11551164.
 Klunk, W.E., Pettegrew, J.W. and Abraham, D.J. (1989) Quantitative evaluation of Congo red binding to amyloid like proteins with a ?pleated sheet conformation. Journal of Histochemistry and Cytochemistry, 37, 1273 1281.
 Yokoyama, K., Briglio, N.M., Sri Hartati, D., Tsang, S.M.W., MacCormac, J.E. and Welchons, D.R. (2008) Nanoscale Size Dependence in the Conjugation of Amyloid Beta and Ovalbumin Proteins on the Surface of Gold Colloidal Particles. Nanotechnology, 19, 375101 375108.
 Yokoyama, K., Cho, H., Cullen, S.P., Kowalik, M., Briglio, N.M., Hoops, H.J., Zhao, Z. and Carpenter, M.A. (2009) Microscopic Investigation of Reversible Nanoscale Surface Size Dependent Protein Conjugation. International Journal of Molecular Science, 10, 2348 2366.
 Yokoyama, K., Gaulin, N.B., Cho, H. and Briglio, N.M. (2010) Temperature Dependence of Conjugation of Amyloid Beta Peptide on the Gold Colloidal Nanoparticles”. Journal of Physical Chemistry A, 114, 15211528.
 Harper, J.D. and Lansbury, P.T. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time dependent solubility of amyloid proteins. Annual Reviews of Biochemistry, 66, 385407.
 Harper, J.D., Lieber, C.M. and Lansbury, P.T. (1997) Atomic force microscopic imaging of seeded fibrilformation and fibril branching by the Alzheimer’s disease amyloidb protein. Chemistry and Biology, 4, 951959.
 Gursky, O. and Aleshkov, S. (2000) Temperature ependent betasheet formation in betaamyloid A? (140) peptide in water: uncoupling betastructure folding from aggregation. Biochimica et Biophysica Acta, 1476, 93 102.
 Perczel, A., Park, K. and Fasman, G.D. (1992) Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide. Analytical Biochemistry, 203, 8393.
 Wu, C., Lei, H.X., Wang, Z.X., Zhang, W. and Duan, Y. (2007) Dual binding modes of Congo red to amyloid protofibril surface observed in molecular dynamics simulations. Journal of the American Chemical Society, 129, 12251232.
 Turrell, W.G. and Finch, J.T. (1992) Binding of the dye Congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloidforming peptide sequences. Journal of Molecular Biology, 227, 12051223.
 McLaurin, J., Franklin, T., Zhang, X., Deng, J.P. and Fraser, P.E. (1999) Interactions of Alzheimer amyloid? peptides with glycosaminoglycanseffects on fibril nucleation and growth. European Journal of Biochemistry, 266, 11011110.
 Esler, W.P., Stimson, E.R., Ghilardi, J.R., Lu, Y.A., Felix, A.M., Vinters, H.V., Mantyh, P.W., Lee, J.P. and Maggio, J.E. (1996) Point substitution in the central hydrophobic cluster of a human bamyloid congener disrupts peptide folding and abolishes plaque competence. Biochemistry, 35, 1391413921.