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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 ...

  • 2018-06-08
  • New York, NY :Springer New York,2018

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  • LIBRIS-ID:oai:research.chalmers.se:9bad7e98-c2a6-42d2-b6d6-1d9306263000
  • https://research.chalmers.se/publication/503788URI
  • https://doi.org/10.1007/978-1-4939-7816-8_6DOI

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  • Language:English
  • Summary in:English

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  • Subject category:kap swepub-publicationtype
  • Subject category:vet swepub-contenttype

Notes

  • 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)
  • Wittung Stafshede, Pernilla,1968Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)perwit (author)
  • Chalmers tekniska högskola (creator_code:org_t)

Related titles

  • In:Methods in Molecular BiologyNew York, NY : Springer New York1779, s. 73-831940-60291064-3745

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