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Phosphorylation at S87 is enhanced in synucleinopathies, inhibits α-synuclein oligomerization and influences synuclein-membrane interactions.

MPS-Authors
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Kim,  H. Y.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Fernandez,  C. O.
Department of NMR Based Structural 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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Fulltext (public)

587747.pdf
(Publisher version), 3MB

Supplementary Material (public)

587747-Suppl.pdf
(Supplementary material), 2MB

Citation

Paleologou, K. E., Oueslati, A., Shakked, G., Rospigliosi, C. C., Kim, H. Y., Lamberto, G. R., et al. (2010). Phosphorylation at S87 is enhanced in synucleinopathies, inhibits α-synuclein oligomerization and influences synuclein-membrane interactions. Journal of Neuroscience, 30(9), 3184-3198. doi:10.1523/JNEUROSCI.5922-09.2010.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-D601-5
Abstract
Phosphorylation at S87 is enhanced in synucleinopathies, inhibits α-synuclein oligomerization and influences synuclein-membrane interactions