Amyloid-beta binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/beta-catenin signaling.

@article{Magdesian2008AmyloidbetaBT,
  title={Amyloid-beta binds to the extracellular cysteine-rich domain of Frizzled and inhibits Wnt/beta-catenin signaling.},
  author={Margaret Haiganouch Magdesian and Milena Mouta Verdan França Carvalho and Fabio Almeida Mendes and Leonardo Martins Saraiva and Maria Apararecida Juliano and Luiz Juliano and Jos{\'e} Garcia-Abreu and S{\'e}rgio T. Ferreira},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 14},
  pages={
          9359-68
        }
}
The amyloid-beta peptide (Abeta) plays a major role in neuronal dysfunction and neurotoxicity in Alzheimer disease. However, the signal transduction mechanisms involved in Abeta-induced neuronal dysfunction remain to be fully elucidated. A major current unknown is the identity of the protein receptor(s) involved in neuronal Abeta binding. Using phage display of peptide libraries, we have identified a number of peptides that bind Abeta and are homologous to neuronal receptors putatively involved… CONTINUE READING
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