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Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II
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“Recently, it was shown that before FUS converts into insoluble deposits, it undergoes liquid–liquid phase separation (LLPS)28–30.”
From Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau (2017) · cites this paper as [30]
In the citing paper
“In contrast to K18, domains of proteins, which were previously shown to undergo LLPS (e.g., FUS), are glutamine/asparagine-rich and undergo liquid demixing only at low temperature (below 20 °C)28–30.”
From Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau (2017) · cites this paper as [30]
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Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · cited 7×
“mutations located within the regions coding for FUS LC are linked to ALS (Belzil et al., 2009; Cruts et al., 2012; Ling et al., 2013; Ticozzi et al., 2009), including G156E, which increases FUS aggregation propensity in vitro and in cell culture (Nomura et al.”
InfluentialIdentification and characterization of FUS/TLS as a new target of ATM
Gardiner, M., Toth, R., Vandermoere, F., Morrice, N. A., & Rouse, J. (2008) · Biochemical Journal · doi:10.1042/bj20081135 · Cited by 111
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Valence and patterning of aromatic residues determine the phase behavior of prion-like domains
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Metadata
- Authors
- Burke, K. A., Janke, A. M., Rhine, C. L., & Fawzi, N. L.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2015-10
- Volume
- 60
- Issue
- 2
- Pages
- 231-241
- ISSN
- 1097-2765
- PMC
- PMC4609301
- Cited by
- 1,024
- References
- 4
- Language
- en
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