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  Turn plasticity distinguishes different modes of amyloid-beta aggregation.

Rezaei-Ghaleh, N., Amininasab, M., Giller, K., Kumar, S., Stuendl, A., Schneider, A., et al. (2014). Turn plasticity distinguishes different modes of amyloid-beta aggregation. Journal of the American Chemical Society, 136(13), 4913-4919. doi:10.1021/ja411707y.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-7739-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4323-8
Genre: Journal Article

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http://pubs.acs.org/doi/pdf/10.1021/ja411707y (Publisher version)
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 Creators:
Rezaei-Ghaleh, N.1, Author              
Amininasab, M., Author
Giller, K.2, Author              
Kumar, S., Author
Stuendl, A., Author
Schneider, A., Author
Becker, S.2, Author              
Walter, J., Author
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Strcture Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: Pathogenesis of Alzheimer's disease (AD) is associated with aggregation of the amyloid-beta (A beta) peptide into oligomeric and fibrillar assemblies; however, little is known about the molecular basis of aggregation of A beta into distinct assembly states. Here we demonstrate that phosphorylation at serine 26 (S26) impairs A beta fibrillization while stabilizing its monomers and nontoxic soluble assemblies of nonfibrillar morphology. NMR spectroscopy and replica-exchange molecular dynamics indicate that introduction of a phosphate group or phosphomimetic at position 26 diminishes A beta's propensity to form a beta-hairpin, rigidifies the region around the modification site, and interferes with formation of a fibril-specific salt bridge between aspartic acid 23 and lysine 28. The combined data demonstrate that phosphorylation of S26 prevents a distinct conformational rearrangement that is required for progression of A beta aggregation toward fibrils and provide a basis for a possible role of phosphorylation at serine 26 in AD.

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Language(s): eng - English
 Dates: 2014-03-112014-04-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/ja411707y
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 136 (13) Sequence Number: - Start / End Page: 4913 - 4919 Identifier: -