SEARCH

SEARCH BY CITATION

References

  • 1
    Böhlen, P., Stein, S., Dairman, W., & Udenfriend, S. (1973). Fluorometric assay of proteins in the nanogram range. Arch. Biochem. Biophys. 155, 213220.
  • 2
    Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992). Assembly and aggregation properties of synthetic Alzheimer's A4/β amyloid peptide analogs. J. Biol. Chem. 267, 546554.
  • 3
    Burke, M.J. & Rougevie, M.A. (1972). Cross-β protein structures. I. Insulin fibrils. Biochemistry 11, 24352438.
  • 4
    Fraser, P.E., Duffy, L.K., O'Malley, M.B., Nguyen, J., Inouye, H., & Kirschner, D.A. (1991). Morphology and antibody recognition of synthetic β-amyloid peptides. J. Neurosci. Res. 28, 474485.
  • 5
    Glenner, G.G. & Wong, C.W. (1984). Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885890.
  • 6
    Halverson, K., Fraser, P.E., Kirschner, D.A., & Lansbury, P.T., Jr. (1990). Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments. Biochemistry 29, 26392644.
  • 7
    Hilbich, C., Kisters-Woike, B., Reed, J., Masters, C.L., & Beyreuther, K. (1991). Aggregation and secondary structure of synthetic amyloid β/A4 peptides of Alzheimer's disease. J. Mol. Biol. 218, 149163.
  • 8
    Joachim, C.L. & Selkoe, D.J. (1992). The seminal role of β-amyloid in the pathogenesis of Alzheimer disease. Alzheimer Dis. Assoc. Disord. 6, 734.
  • 9
    Kelényi, G. (1967). On the histochemistry of azo group-free thiazole dyes. J. Histochem. Cytochem. 15, 172180.
  • 10
    Kirschner, D.A., Inouye, H., Duffy, L.K., Sinclair, A., Lind, M., & Selkoe, D.J. (1987). Synthetic peptide homologous to β protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. USA 84, 69536957.
  • 11
    Klunk, W.E., Pettegrew, J.W., & Abraham, D.J. (1989). Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37, 12731281.
  • 12
    Lansbury, P.T., Jr. (1992). In pursuit of the molecular structure of amyloid plaque: New technology provides unexpected and critical information. Biochemistry 31, 68656870.
  • 13
    Masters, C.L., Multhaup, G., Simms, G., Pottiglesser, J., Martins, R.N., & Beyreuther, K. (1985). Neuronal origin of a cerebral amyloid. EMBO J. 4, 27572763.
  • 14
    McGeer, P.L., McGeer, E.G., Kawamata, T., Yamada, T., & Akiyama, H. (1991). Reactions of the immune system in chronic degenerative neurological diseases. Can. J. Neurol. Sci. 18, 376379.
  • 15
    Naiki, H., Higuchi, K., Hosokawa, M., & Takeda, T. (1989). Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T. Anal. Biochem. 177, 244249.
  • 16
    Naiki, H., Higuchi, K., Matsushima, K., Shimada, A., Chen, W.-H., Hosokawa, M., & Takeda, T. (1990). Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: Use of the fluorescent indicator thioflavine T. Lab. Invest. 62, 768773.
  • 17
    Naiki, H., Higuchi, K., Nakakuki, K., & Takeda, T. (1991). Kinetic analysis of amyloid fibril polymerization in vitro. Lab. Invest. 65, 104110.
  • 18
    Tomski, S.J. & Murphy, R.M. (1992). Kinetics of aggregation of synthetic β-amyloid peptide. Arch. Biochem. Biophys. 294, 630638.
  • 19
    Vassar, P.S. & Culling, C.F.A. (1959). Fluorescent stains, with special reference to amyloid and connective tissue. Arch. Pathol. 68, 487498.
  • 20
    Venkataraman, K. (1952). In The Chemistry of Synthetic Dyes (Fieser, L.F. & Fieser, M., Eds.), pp. 622624. Academic Press, New York.
  • 21
    Virchow, R. (1855). Zur Cellulose-Fruge. Virchows Arch. 8, 140144.