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Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant α-synuclein.

MPS-Authors
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Heise,  H.
Research Group of Solid State NMR Spectroscopy, MPI for biophysical chemistry, Max Planck Society;

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Celej,  M. S.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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

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Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Pelah,  A.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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

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Jovin,  T. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Baldus,  M.
Research Group of Solid State NMR Spectroscopy, MPI for biophysical chemistry, Max Planck Society;

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377535.pdf
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Citation

Heise, H., Celej, M. S., Becker, S., Riedel, D., Pelah, A., Kumar, A., et al. (2008). Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant α-synuclein. Journal of Molecular Biology, 380(3), 444-450. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WK7-4SHVT2K-C-C&_cdi=6899&_user=38661&_orig=browse&_coverDate=07%2F11%2F2008&_sk=996199996&view=c&wchp=dGLbVlW-zSkzV&md5=eba0f7efffc4e784ecbbccb5f69f10d4&ie=/sdarticle.pdf.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-DB5D-D
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