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In vitro analysis of α-synuclein amyloid formation and cross-reactivity

Horvath, Istvan, 1979 (author)
Chalmers tekniska högskola,Chalmers University of Technology
Rocha, Sandra, 1975 (author)
Chalmers tekniska högskola,Chalmers University of Technology
Wittung Stafshede, Pernilla, 1968 (author)
Chalmers tekniska högskola,Chalmers University of Technology
 (creator_code:org_t)
2018-06-08
2018
English.
In: Methods in Molecular Biology. - New York, NY : Springer New York. - 1940-6029 .- 1064-3745. ; , s. 73-83
  • Book chapter (other academic/artistic)
Abstract Subject headings
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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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biofysik (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biophysics (hsv//eng)
MEDICIN OCH HÄLSOVETENSKAP  -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)

Keyword

Parkinson’s disease
Fluorescence
Thioflavin T
Electron microscopy
Amylin
Type-2 diabetes
α-Synuclein
Amyloid

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