Effects of β-Amyloid-(25-35) Peptides on Radioligand Binding to Excitatory Amino Acid Receptors and Voltage-Dependent Calcium Channels: Evidence for a Selective Affinity for the Glutamate and Glycine Recognition Sites of the NMDA Receptor

@article{Cowburn1997EffectsO,
  title={Effects of β-Amyloid-(25-35) Peptides on Radioligand Binding to Excitatory Amino Acid Receptors and Voltage-Dependent Calcium Channels: Evidence for a Selective Affinity for the Glutamate and Glycine Recognition Sites of the NMDA Receptor},
  author={Richard F. Cowburn and Birgitta Wiehager and Ewa Trief and Mo Li-Li and Erik Sundstr{\"o}m},
  journal={Neurochemical Research},
  year={1997},
  volume={22},
  pages={1437-1442}
}
The neurotoxic fragment corresponding to residues 25-35 of the β-amyloid (Aβ) peptide [Aβ-(25-35)] has been shown to exert effects on (+)-[3H]5-methyl-10,11-dihydro-5H-dibenzo[a,d]-cyclohepten-5,10-imine maleate ([3H]MK-801) binding to the cation channel of the N-methyl-D-aspartate (NMDA) receptor. In the present study, we investigated whether the amidated and carboxylic acid C-terminated forms of Aβ-(25-35) [Aβ-(25-35-NH2) and Aβ-(25-35-COOH), respectively] exert effects on other excitatory… CONTINUE READING
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