Skip to main content
The Journal of Biological Chemistry logoLink to The Journal of Biological Chemistry
. 2009 Sep 11;284(37):25459. doi: 10.1074/jbc.A109.010264

TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity.

Brian S Johnson, David Snead, Jonathan J Lee, J Michael McCaffery, James Shorter, Aaron D Gitler
PMCID: PMC2757247

VOLUME 284 (2009) PAGES 20329–20339

On page 20329 in the Abstract, the sentence beginning on line 10 should read as follows: “Here, we report that, in the absence of other components, TDP-43 spontaneously forms aggregates bearing remarkable ultrastructural similarities to TDP-43 deposits in degenerating neurons of ALS and FTLD-U patients.”


Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology

RESOURCES