Functional Properties of Phase Separation and Intranuclear Complex of FUS in the Pathogenesis of ALS/FTLD
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Publisher
Springer Nature Singapore
Link
https://link.springer.com/content/pdf/10.1007/978-981-99-4886-4_14
Reference108 articles.
1. An H et al (2019) ALS-linked FUS mutations confer loss and gain of function in the nucleus by promoting excessive formation of dysfunctional paraspeckles. Acta Neuropathol Commun 7:7. https://doi.org/10.1186/s40478-019-0658-x
2. Babinchak WM et al (2020) Small molecules as potent biphasic modulators of protein liquid-liquid phase separation. Nat Commun 11:5574. https://doi.org/10.1038/s41467-020-19211-z
3. Baechtold H et al (1999) Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation. J Biol Chem 274:34337–34342. https://doi.org/10.1074/jbc.274.48.34337
4. Baumer D et al (2010) Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations. Neurology 75:611–618. https://doi.org/10.1212/WNL.0b013e3181ed9cde
5. Becker LA et al (2017) Therapeutic reduction of ataxin-2 extends lifespan and reduces pathology in TDP-43 mice. Nature 544:367–371. https://doi.org/10.1038/nature22038
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