Articles with "domain fus" as a keyword



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Sidechain hydrogen bonding interactions within amyloid-like fibrils formed by the low-complexity domain of FUS: Evidence from solid state nuclear magnetic resonance spectroscopy.

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Published in 2020 at "Biochemistry"

DOI: 10.1021/acs.biochem.9b00892

Abstract: In aqueous solutions, the 214-residue low-complexity domain of the FUS protein (FUS-LC) is known to undergo liquid-liquid phase separation and also to self-assemble into amyloid-like fibrils. In previous work based on solid state nuclear magnetic… read more here.

Keywords: amyloid like; domain fus; low complexity; like fibrils ... See more keywords