Protein disaggregation in multicellular organisms
Protein aggregates are formed in cells with profoundly perturbed proteostasis, where the generation of misfolded proteins exceeds the cellular refolding and degradative capacity. They are a hallmark of protein conformational disorders and aged and/or environmentally stressed cells. Protein aggregati...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
28 February 2018
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| In: |
Trends in biochemical sciences
Year: 2018, Volume: 43, Issue: 4, Pages: 285-300 |
| ISSN: | 1362-4326 |
| DOI: | 10.1016/j.tibs.2018.02.003 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.tibs.2018.02.003 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0968000418300240 
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| Author Notes: | Nadinath B. Nillegoda, Anne S. Wentink, and Bernd Bukau |
| Summary: | Protein aggregates are formed in cells with profoundly perturbed proteostasis, where the generation of misfolded proteins exceeds the cellular refolding and degradative capacity. They are a hallmark of protein conformational disorders and aged and/or environmentally stressed cells. Protein aggregation is a reversible process in vivo, which counteracts proteotoxicities derived from aggregate persistence, but the chaperone machineries involved in protein disaggregation in Metazoa were uncovered only recently. Here we highlight recent advances in the mechanistic understanding of the major protein disaggregation machinery mediated by the Hsp70 chaperone system and discuss emerging alternative disaggregation activities in multicellular organisms. |
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| Item Description: | Gesehen am 06.03.2020 |
| Physical Description: | Online Resource |
| ISSN: | 1362-4326 |
| DOI: | 10.1016/j.tibs.2018.02.003 |