O'Nuallain, B., Freir, D.B., Nicoll, A.J., Risse, E., Ferguson, N., Herron, C.E., Collinge, J. and Walsh, D.M. (2010) Amyloid Beta-Protein Dimers Rapidly Form Stable Synaptotoxicprotofibrils. The Journal of Neuroscience, 30, 14411-14419.
http://dx.doi.org/10.1523/JNEUROSCI.3537-10.2010

has been cited by the following article:

• TITLE: Copper Ions Enhance Signal Intensity of Sandwich ELISA for Amorphous Aggregates of Amyloid-β42

  AUTHORS: Akira Itakura, Yoshio F. Kanematsu, Ryoko Suzuki, Hideki Kohno, Kazuaki Yoshimune

  KEYWORDS: Amyloid-β42, Soluble Aggregates, Antibody, ELISA

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.7 No.9, August 22, 2016

  ABSTRACT: Amyloid-β42 (Aβ42) accumulates within senileplaque, a pathological hall mark of Alzheimer’s disease (AD). Our previous reports showed that the monoclonal antibodies 37-11 and 77-3 react with conformational epitopes on the surface of the soluble aggregates of Aβ42 and that sandwich ELISA using these two monoclonal antibodies yields high reactivity to detect soluble aggregates of Aβ42. Here, the reactivity of the sandwich ELISA was shown to increase in the presence of 50 μM Cu2+. However, the addition of Cu2+ had only a small effect on the reactivity of a direct ELISA using antibody 37-11 or 77-3, suggesting that Cu2+ has a small effect on the number of epitopes on the surface of the aggregates. Atomic force microscopy images showed that larger aggregates were formed in the presence of Cu2+, as shown in the other reports. Cu2+ may gather the aggregates with distinct epitopes recognized by antibodies 37-11 and 77-3, leading to increased signal intensity of the sandwich ELISA.