Articles with "complexity domain" as a keyword



Three J-proteins impact Hsp104-mediated variant-specific prion elimination: a new critical role for a low-complexity domain

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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.… read more here.

Keywords: prion; low complexity; variant specific; hsp104 mediated ... See more keywords

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

CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid

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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… read more here.

Keywords: hnrnpa2; low complexity; structure; pathogenic amyloid ... See more keywords

The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils

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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… read more here.

Keywords: different faces; low complexity; complexity domain; liquid droplets ... See more keywords