Acceleration of α-synuclein aggregation

Ricardo GasparDepartment of Physical-Chemistry and ;Department of Biochemistry and Structural Biology, Lund University, Sweden, Correspondence[email protected]

Georg MeislDepartment of Chemistry, University of Cambridge, Cambridge, UK,

Alexander K. BuellDepartment of Chemistry, University of Cambridge, Cambridge, UK, ;Institute of Physical Biology, University of Düsseldorf, Düsseldorf, Germany, and

Laurence YoungDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK

Clemens F. KaminskiDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK

Tuomas P. J. KnowlesDepartment of Chemistry, University of Cambridge, Cambridge, UK,

Emma SparrDepartment of Physical-Chemistry and

Sara LinseDepartment of Biochemistry and Structural Biology, Lund University, Sweden,

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References

Buell AK, Galvagnion C, Gaspar R, Sparr E, Vendruscolo M, Knowles TPJ, Linse S, et al. Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation. Proc Natl Acad Sci USA 2014;111:7671–6.
PubMed Web of Science ®Google Scholar
Grey M, Linse S, Nilsson H, Brundin P, Sparr E. Membrane interaction of α-synuclein in different aggregation states. J Parkinsons Dis 2011;1:359–71.
PubMedGoogle Scholar
Gaspar R, Meisl G, Buell AK, Young L, Kaminski CF, Knowles TPJ, et al. Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification. Quart Rev Biophys – Discovery, in press.
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Acceleration of α-synuclein aggregation

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