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Journal Article

Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation

MPS-Authors
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Bertoncini,  C. W.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Rasia,  R. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Bertoncini, C. W., Rasia, R. M., Lamberto, G. R., Binolfi, A., Zweckstetter, M., Griesinger, C., et al. (2007). Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation. Journal of Molecular Biology, 372(3), 708-722. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WK7-4P6VDXJ-2-V&_cdi=6899&_user=38661&_orig=search&_coverDate=09%2F21%2F2007&_sk=996279996&view=c&wchp=dGLzVtz-zSkWz&md5=4e78b1ecb98361349a8ca292b24a8c7d&ie=/sdarticle.pdf.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-DF3B-8
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