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

Heise, H.; Celej, M. S.; Becker, S.; Riedel, D.; Pelah, A.; Kumar, A.; Jovin, T. M.; Baldus, M.

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

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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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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: https://hdl.handle.net/11858/00-001M-0000-0012-DB5D-D

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