ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import
By D. Dormann, R. Rodde, D. Edbauer, Eva Bentmann, I. Fischer, Alexander Hruscha, M. Than, I. Mackenzie, A. Capell, Bettina Schmid and 2 more. EMBO Journal, 2010
825 citations recorded by the source corpus.
Subfields: Genetics, Molecular Biology, Neurology
View Paper: https://www.semanticscholar.org/paper/cf6401ae06ab9f566ef5b7f8c5be97ddef7f4f4a
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Citations in the corpus
- Stress granules as crucibles of ALS pathogenesis (2013, background): “Most of the bona fide ALS-causing FUS mutations cluster in a small region in the extreme C-terminal domain of FUS, which encodes a PY-NLS motif (Dormann et al., 2010; Zhang et al., 2012).”
- Converging mechanisms in ALS and FTD: Disrupted RNA and protein homeostasis (2013, neutral): “Given that TDP-43 and FUS/TLS inclusion can also be found in glia (Mackenzie et al., 2010a), it is conceivable that glia contribute to disease pathogenesis.”
- Liquid-Liquid Phase Separation in Disease. (2019, background): “First, ALS-causing mutations in RNA-binding proteins, such as FUS, TDP-43, HNRNPA1, HNRNPA2, and TIA1, promote accumulation of the respective protein in membraneless compartments called stress granules (SGs) (24, 43, 45, 88, 99).”
- Distinct stages in stress granule assembly and disassembly (2016, background): “However, pathological mutations in proteins that either increase the formation, or decrease the clearance of stress granules, can lead to abnormal accumulation of aggregates that share components with stress granules (Buchan et al., 2013; Dormann et al., 2010; Izumi et al., 2015; Kim et al., 2013).”