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Published in 2019 at "Current Genetics"
DOI: 10.1007/s00294-019-01006-5
Abstract: Prions are self-propagating protein isoforms that are typically amyloid. In Saccharomyces cerevisiae , amyloid prion aggregates are fragmented by a trio involving three classes of chaperone proteins: Hsp40s, also known as J-proteins, Hsp70s, and Hsp104.…
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Keywords:
prion;
low complexity;
variant specific;
hsp104 mediated ... See more keywords
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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…
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Keywords:
amyloid like;
domain fus;
low complexity;
like fibrils ... See more keywords
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Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-020-17905-y
Abstract: hnRNPA2 is a human ribonucleoprotein (RNP) involved in RNA metabolism. It forms fibrils both under cellular stress and in mutated form in neurodegenerative conditions. Previous work established that the C-terminal low-complexity domain (LCD) of hnRNPA2…
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Keywords:
hnrnpa2;
low complexity;
structure;
pathogenic amyloid ... See more keywords
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Published in 2021 at "International Journal of Molecular Sciences"
DOI: 10.3390/ijms22158213
Abstract: Transactive response DNA-binding protein 43 (TDP-43) is a nucleic acid-binding protein that is involved in transcription and translation regulation, non-coding RNA processing, and stress granule assembly. Aside from its multiple functions, it is also known…
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Keywords:
different faces;
low complexity;
complexity domain;
liquid droplets ... See more keywords