Publications by authors named "A Calliari"
Genetic variants in TMEM106B, coding for a transmembrane protein of unknown function, have been identified as critical genetic modulators in various neurodegenerative diseases with a strong effect in patients with frontotemporal degeneration. The luminal domain of TMEM106B can form amyloid-like fibrils upon proteolysis. Whether this luminal domain is generated under physiological conditions and which protease(s) are involved in shedding remain unclear.
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- The letter discusses how new types of cryptic proteins produced by TDP-43 dysfunction could indicate TDP-43-related issues in neurodegenerative diseases.
- It highlights the significance of these novel proteins as potential biomarkers for diagnosing or understanding these diseases.
- The findings could lead to improved methods for detecting and studying conditions linked to TDP-43 pathology, such as ALS and frontotemporal dementia.
In frontotemporal dementia and amyotrophic lateral sclerosis, the RNA-binding protein TDP-43 is depleted from the nucleus. TDP-43 loss leads to cryptic exon inclusion but a role in other RNA processing events remains unresolved. Here, we show that loss of TDP-43 causes widespread changes in alternative polyadenylation, impacting expression of disease-relevant genes (e.
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