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In vitro analysis o...
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Horvath, Istvan,1979Chalmers tekniska högskola,Chalmers University of Technology
(author)
In vitro analysis of α-synuclein amyloid formation and cross-reactivity
- Article/chapterEnglish2018
Publisher, publication year, extent ...
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2018-06-08
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New York, NY :Springer New York,2018
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LIBRIS-ID:oai:research.chalmers.se:9bad7e98-c2a6-42d2-b6d6-1d9306263000
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https://research.chalmers.se/publication/503788URI
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https://doi.org/10.1007/978-1-4939-7816-8_6DOI
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Language:English
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Summary in:English
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Subject category:kap swepub-publicationtype
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Subject category:vet swepub-contenttype
Notes
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In vitro time-resolved characterization of protein aggregation into amyloid fibers and the effects of other proteins on the aggregation process are fundamentally important measurements to obtain a better understanding of the mechanisms contributing to neurodegeneration, as well as other diseases involving amyloid formation. Here, we describe how to perform in vitro aggregation experiments with α-synuclein, the amyloidogenic protein involved in Parkinson’s disease, including how to assess the starting material, useful experimental/instrumental conditions, as well as how to set up cross-seeding and co-aggregation experiments. The high variability of data reported for in vitro α-synuclein amyloid formation may in part be explained by experimental differences.
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Rocha, Sandra,1975Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)rochas
(author)
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Wittung Stafshede, Pernilla,1968Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)perwit
(author)
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Chalmers tekniska högskola
(creator_code:org_t)
Related titles
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In:Methods in Molecular BiologyNew York, NY : Springer New York1779, s. 73-831940-60291064-3745
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