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Open Access Green as soon as Postprint is submitted to ZB.
The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS.
Science 339, 1335-1338 (2013)
Expansion of a GGGGCC hexanucleotide repeat upstream of the C9orf72 coding region is the most common cause of familial frontotemporal lobar degeneration and amyotrophic lateral sclerosis (FTLD/ALS), but the pathomechanisms involved are unknown. As in other FTLD/ALS variants, characteristic intracellular inclusions of misfolded proteins define C9orf72 pathology, but the core proteins of the majority of inclusions are still unknown. Here, we found that most of these characteristic inclusions contain poly-(Gly-Ala) and, to a lesser extent, poly-(Gly-Pro) and poly-(Gly-Arg) dipeptide-repeat proteins presumably generated by non-ATG-initiated translation from the expanded GGGGCC repeat in three reading frames. These findings directly link the FTLD/ALS-associated genetic mutation to the predominant pathology in patients with C9orf72 hexanucleotide expansion.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Amyotrophic-lateral-sclerosis ; Frontotemporal Dementia ; Hexanucleotide Repeat ; Expansion ; Identification ; Initiation ; Ftd ; Als
ISSN (print) / ISBN
0036-8075
e-ISSN
1095-9203
Journal
Science
Quellenangaben
Volume: 339,
Issue: 6125,
Pages: 1335-1338
Publisher
American Association for the Advancement of Science (AAAS)
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Molecular Immunology (IMI)