Posttranslational modification impact on the mechanism by which amyloid-β induces synaptic dysfunction.

  title={Posttranslational modification impact on the mechanism by which amyloid-β induces synaptic dysfunction.},
  author={Katarzyna M. Grochowska and Pingan Yuanxiang and J. Austin Baer and Rajeev Raman and Gemma Brugal and Giriraj Sahu and Michaela Schweizer and Arthur F Bikbaev and Stephan Schilling and Hans-Ulrich Demuth and Michael R Kreutz},
  journal={EMBO reports},
  volume={18 6},
Oligomeric amyloid-β (Aβ) 1-42 disrupts synaptic function at an early stage of Alzheimer's disease (AD). Multiple posttranslational modifications of Aβ have been identified, among which N-terminally truncated forms are the most abundant. It is not clear, however, whether modified species can induce synaptic dysfunction on their own and how altered biochemical properties can contribute to the synaptotoxic mechanisms. Here, we show that a prominent isoform, pyroglutamated Aβ3(pE)-42, induces… CONTINUE READING
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Inhibition of the polyamine system counteracts beta-amyloid EMBO reports Vol 18 | No 6 | 2017 a 2017 The Authors EMBO reports Modification of Ab and synaptic dysfunction

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