Canine SOD1 harboring E40K or T18S mutations promotes protein aggregation without reducing the global structural stability.

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作者： Shintaro,Kimura ^[1] ; Yuji O,Kamatari ^[2] ; Yukina,Kuwahara ^[3] ; Hideaki,Hara ^[4] ; Osamu,Yamato ^[5] ; Sadatoshi,Maeda ^[1] ; Hiroaki,Kamishina ^[1] ; Ryo,Honda ^[6]

作者单位： The United Graduate School of Veterinary Sciences, Gifu University, Gifu, Japan. ^[1] Life Science Research Center, Gifu University, Gifu, Japan. ^[2] Joint Department of Veterinary Medicine, Faculty of Applied Biological Sciences, Gifu University, Gifu, Japan. ^[3] Molecular Pharmacology, Department of Biofunctional Evaluation, Gifu Pharmaceutical University, Gifu, Japan. ^[4] Laboratory of Veterinary Clinical Pathology, Joint Faculty of Veterinary Medicine, Kagoshima University, Kagoshima, Japan. ^[5] Center for Highly Advanced Integration of Nano and Life Sciences, Gifu University, Gifu, Japan. ^[6] The United Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, Gifu, Japan. ^[7]

关键词 ALS Aggregation Degenerative myelopathy SOD1 E40K mutation SOD1 T18S mutation

DOI 10.7717/peerj.9512

PMID 32742795

发布时间 2020-09-28

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Canine SOD1 harboring E40K or T18S mutations promotes protein aggregation without reducing the global structural stability.

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Canine SOD1 harboring E40K or T18S mutations promotes protein aggregation without reducing the global structural stability.

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