An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity-Reference-Cited by-同舟云学术

An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity

Published:2011-06-12 Issue:7 Volume:18 Page:822-830
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Guo Weirui,Chen Yanbo,Zhou Xiaohong,Kar Amar,Ray Payal,Chen Xiaoping,Rao Elizabeth J,Yang Mengxue,Ye Haihong,Zhu Li,Liu Jianghong,Xu Meng,Yang Yanlian,Wang Chen,Zhang David,Bigio Eileen H,Mesulam Marsel,Shen Yan,Xu Qi,Fushimi Kazuo,Wu Jane Y

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2053.pdf

Reference49 articles.

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3. Arai, T. et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 351, 602–611 (2006).

4. Neumann, M. et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130–133 (2006).

5. Kwiatkowski, T.J. Jr. et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323, 1205–1208 (2009).

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