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

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.

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Bertoncini, C. W.1, Author           
Rasia, R. M.1, Author           
Lamberto, G. R., Author
Binolfi, A., Author
Zweckstetter, M.2, Author           
Griesinger, C.3, Author           
Fernandez, C. O., Author
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
3Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: NMR; amyloid; protein aggregation; unfolded state; polyproline II
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 Dates: 2007-09-21
 Publication Status: Issued
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Title: Journal of Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 372 (3) Sequence Number: - Start / End Page: 708 - 722 Identifier: -