Arctic mutant Aβ40 aggregates on α7 nicotinic acetylcholine receptors and inhibits their functions
Article first published online: 14 AUG 2014
© 2014 International Society for Neurochemistry
Journal of Neurochemistry
Volume 131, Issue 5, pages 667–674, December 2014
How to Cite
J. Neurochem. (2014) 131, 667–674.
- Issue published online: 19 NOV 2014
- Article first published online: 14 AUG 2014
- Accepted manuscript online: 24 JUL 2014 08:42AM EST
- Manuscript Revised: 18 JUL 2014
- Manuscript Accepted: 18 JUL 2014
- Manuscript Received: 22 APR 2014
- KAKENHI. Grant Number: 21700415
- High-Tech Research Center (TWIns)
- Consolidated Research Institute of Advanced Science and Medical Care (ASMeW)
- Global COE ‘Practical Chemical Wisdom’ projects
- Waseda University
- COI STREAM
- Ministry of Education, Culture, Sports, Science and Technology
Figure S1. Arctic Aβ42 binds to CHRNA7 with a higher affinity than wild-type Aβ42. An in vitro binding experiment using Arctic Aβ42 and wild-type Aβ42 was performed. Arctic Aβ42 bound to GST-CHRNA7 more strongly than wild-type Aβ42 while a band corresponding to a Aβ42 dimer (~8 kDa) was also detected. Aggregates were visible in the input sample used for in vitro binding experiment suggesting the self-accumulation of Arctic Aβ42 and wild-type Aβ42.
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