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Article Abstract
CHCHD10 is mutated in rare cases of FTD and ALS and aggregates in mouse models of disease. Here we show that the disordered N-terminal domain of CHCHD10 forms amyloid fibrils and report their cryoEM structure. Disease-associated mutations cannot be accommodated by the WT fibril structure, while sequence differences between CHCHD10 and CHCHD2 are tolerated, explaining the co-aggregation of the two proteins and linking CHCHD10 and CHCHD2 amyloid fibrils to neurodegeneration.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11291021 | PMC |
| http://dx.doi.org/10.1101/2024.07.18.604174 | DOI Listing |
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