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Bri2 BRICHOS client...
Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
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- Chen, Gefei (author)
- Karolinska Institutet,Karolinska Institute, Sweden
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- Abelein, Axel (author)
- Karolinska Institutet,Karolinska Institute, Sweden
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- Nilsson, Harriet E. (author)
- Karolinska Institutet,KTH,Strukturell bioteknik,Karolinska Institute, Sweden; KTH Royal Institute Technology, Sweden
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- Leppert, Axel (author)
- Karolinska Institute, Sweden
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- Andrade-Talavera, Yuniesky (author)
- Karolinska Institutet,Karolinska Institute, Sweden
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- Tambaro, Simone (author)
- Karolinska Institutet,Karolinska Institute, Sweden
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- Hemmingsson, Lovisa (author)
- Linköpings universitet,Institutionen för fysik, kemi och biologi,Tekniska fakulteten,Karolinska Institute, Sweden
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- Roshan, Firoz (author)
- Karolinska Institute, Sweden
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- Landreh, Michael (author)
- Karolinska Institutet,University of Oxford, England; Karolinska Institute, Sweden
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- Biverstal, Henrik (author)
- Karolinska Institutet,Karolinska Institute, Sweden; Latvian Institute Organ Synth, Latvia
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- Koeck, Philip J. B. (author)
- Karolinska Institutet,KTH,Strukturell bioteknik,Karolinska Institute, Sweden; KTH Royal Institute Technology, Sweden
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- Presto, Jenny (author)
- Karolinska Institutet,Karolinska Institute, Sweden
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- Hebert, Hans (author)
- Karolinska Institute, Sweden; KTH Royal Institute Technology, Sweden
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- Fisahn, Andre (author)
- Karolinska Institute, Sweden
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Johansson, Jan (author)
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(creator_code:org_t)
- 2017-12-12
- 2017
- English.
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In: Nature Communications. - : Nature Publishing Group. - 2041-1723. ; 8
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Abstract
Subject headings
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- . Protein misfolding and aggregation is increasingly being recognized as a cause of disease. In Alzheimer's disease the amyloid-beta peptide (A beta) misfolds into neurotoxic oligomers and assembles into amyloid fibrils. The Bri2 protein associated with Familial British and Danish dementias contains a BRICHOS domain, which reduces A beta fibrillization as well as neurotoxicity in vitro and in a Drosophila model, but also rescues proteins from irreversible nonfibrillar aggregation. How these different activities are mediated is not known. Here we show that Bri2 BRICHOS monomers potently prevent neuronal network toxicity of A beta, while dimers strongly suppress A beta fibril formation. The dimers assemble into high-molecular-weight oligomers with an apparent two-fold symmetry, which are efficient inhibitors of non-fibrillar protein aggregation. These results indicate that Bri2 BRICHOS affects qualitatively different aspects of protein misfolding and toxicity via different quaternary structures, suggesting a means to generate molecular chaperone diversity.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Chen, Gefei
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Abelein, Axel
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Nilsson, Harriet ...
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Leppert, Axel
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Andrade-Talavera ...
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Tambaro, Simone
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show more...
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Hemmingsson, Lov ...
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Roshan, Firoz
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Landreh, Michael
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Biverstal, Henri ...
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Koeck, Philip J. ...
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Presto, Jenny
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Hebert, Hans
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Fisahn, Andre
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Johansson, Jan
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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Nature Communica ...
- By the university
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Royal Institute of Technology
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Karolinska Institutet
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Linköping University