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Uncovering the univ...
Uncovering the universality of self-replication in protein aggregation and its link to disease
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- Meisl, Georg (författare)
- University of Cambridge
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- Xu, Catherine K. (författare)
- University of Cambridge
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- Taylor, Jonathan D. (författare)
- Imperial College London
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- Michaels, Thomas C. T. (författare)
- University of Cambridge
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- Levin, Aviad (författare)
- University of Cambridge
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- Otzen, Daniel (författare)
- Aarhus University
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- Klenerman, David (författare)
- University of Cambridge
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- Matthews, Steve (författare)
- Imperial College London
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- Linse, Sara (författare)
- Lund University,Lunds universitet,NanoLund: Centre for Nanoscience,Annan verksamhet, LTH,Lunds Tekniska Högskola,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,LTH profilområde: Nanovetenskap och halvledarteknologi,LTH profilområden,Other operations, LTH,Faculty of Engineering, LTH,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,LTH Profile Area: Nanoscience and Semiconductor Technology,LTH Profile areas,Faculty of Engineering, LTH
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- Andreasen, Maria (författare)
- University of Cambridge,Aarhus University
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- Knowles, Tuomas P. J. (författare)
- University of Cambridge
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(creator_code:org_t)
- American Association for the Advancement of Science (AAAS), 2022
- 2022
- Engelska 10 s.
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Ingår i: Science Advances. - : American Association for the Advancement of Science (AAAS). - 2375-2548. ; 8:32
- Relaterad länk:
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http://dx.doi.org/10... (free)
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Fibrillar protein aggregates are a hallmark of a range of human disorders, from prion diseases to dementias, but are also encountered in several functional contexts. Yet, the fundamental links between protein assembly mechanisms and their functional or pathological roles have remained elusive. Here, we analyze the aggregation kinetics of a large set of proteins that self-assemble by a nucleated-growth mechanism, from those associated with disease, over those whose aggregates fulfill functional roles in biology, to those that aggregate only under artificial conditions. We find that, essentially, all such systems, regardless of their biological role, are capable of self-replication. However, for aggregates that have evolved to fulfill a structural role, the rate of self-replication is too low to be significant on the biologically relevant time scale. By contrast, all disease-related proteins are able to self-replicate quickly compared to the time scale of the associated disease. Our findings establish the ubiquity of self-replication and point to its potential importance across aggregation-related disorders.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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- ref (ämneskategori)
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Meisl, Georg
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Xu, Catherine K.
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Taylor, Jonathan ...
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Michaels, Thomas ...
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Levin, Aviad
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Otzen, Daniel
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visa fler...
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Klenerman, David
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Matthews, Steve
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Linse, Sara
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Andreasen, Maria
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Knowles, Tuomas ...
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visa färre...
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