The C9orf72 repeat expansion disrupts nucleocytoplasmic transport-Reference-Cited by-同舟云学术

The C9orf72 repeat expansion disrupts nucleocytoplasmic transport

Published:2015-08-26 Issue:7567 Volume:525 Page:56-61
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Zhang Ke,Donnelly Christopher J.,Haeusler Aaron R.,Grima Jonathan C.,Machamer James B.,Steinwald Peter,Daley Elizabeth L.,Miller Sean J.,Cunningham Kathleen M.,Vidensky Svetlana,Gupta Saksham,Thomas Michael A.,Hong Ingie,Chiu Shu-Ling,Huganir Richard L.,Ostrow Lyle W.,Matunis Michael J.,Wang Jiou,Sattler Rita,Lloyd Thomas E.,Rothstein Jeffrey D.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature14973.pdf

Reference49 articles.

1. Majounie, E. et al. Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: a cross-sectional study. Lancet Neurol. 11, 323–330 (2012)

2. DeJesus-Hernandez, M. et al. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 72, 245–256 (2011)

3. Renton, A. E. et al. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 72, 257–268 (2011)

4. Ash, P. E. et al. Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS. Neuron 77, 639–646 (2013)

5. Mori, K. et al. The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS. Science 339, 1335–1338 (2013)

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