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Direct measurement ...
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation
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- Flagmeier, Patrick (author)
- University of Cambridge
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- De, Suman (author)
- University of Cambridge
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- Michaels, Thomas C.T. (author)
- University of Cambridge,Harvard University
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- Yang, Xiaoting (author)
- University of Cambridge
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- Dear, Alexander J. (author)
- University of Cambridge,Harvard University
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- Emanuelsson, Cecilia (author)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Vendruscolo, Michele (author)
- University of Cambridge
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- Linse, Sara (author)
- 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,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
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- Klenerman, David (author)
- University of Cambridge
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- Knowles, Tuomas P.J. (author)
- University of Cambridge
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- Dobson, Christopher M. (author)
- University of Cambridge
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(creator_code:org_t)
- 2020-08-10
- 2020
- English 6 s.
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In: Nature Structural and Molecular Biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 27:10, s. 886-891
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Abstract
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- The formation of amyloid deposits in human tissues is a defining feature of more than 50 medical disorders, including Alzheimer’s disease. Strong genetic and histological evidence links these conditions to the process of protein aggregation, yet it has remained challenging to identify a definitive connection between aggregation and pathogenicity. Using time-resolved fluorescence microscopy of individual synthetic vesicles, we show for the Aβ42 peptide implicated in Alzheimer’s disease that the disruption of lipid bilayers correlates linearly with the time course of the levels of transient oligomers generated through secondary nucleation. These findings indicate a specific role of oligomers generated through the catalytic action of fibrillar species during the protein aggregation process in driving deleterious biological function and establish a direct causative connection between amyloid formation and its pathological effects.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
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- art (subject category)
- ref (subject category)
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- By the author/editor
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Flagmeier, Patri ...
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De, Suman
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Michaels, Thomas ...
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Yang, Xiaoting
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Dear, Alexander ...
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Emanuelsson, Cec ...
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show more...
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Vendruscolo, Mic ...
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Linse, Sara
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Klenerman, David
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Knowles, Tuomas ...
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Dobson, Christop ...
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show less...
- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Cell and Molecul ...
- Articles in the publication
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Nature Structura ...
- By the university
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Lund University