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. 2019 Nov 8;13:1179. doi: 10.3389/fnins.2019.01179

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Copyright © 2019 Allison, Edgar and Reid.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Assessment of interactions between spastin MIT domains and MIM-regions of CHMP1B and IST1 by GST pull-down. Purified proteins consisting of GST alone, GST fused to the wild-type spastin MIT domain, or to spastin MIT domains harboring the sequence changes indicated were used in in vitro GST pull-down experiments vs. myc- and 6His-tagged fragments of CHMP1B (A) or IST1 (B) that incorporate the spastin-binding MIM regions. In each set of experiments, the upper panels show Coomassie-stained gels, while the bottom panel shows corresponding anti-myc immunoblotting.