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000000276 0247_ $$2DOI$$a10.1016/j.jmb.2008.05.026
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000000276 084__ $$2WoS$$aBiochemistry & Molecular Biology
000000276 1001_ $$0P:(DE-Juel1)VDB77857$$aHeise, H.$$b0$$uFZJ
000000276 245__ $$aSolid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein
000000276 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2008
000000276 300__ $$a444 - 450
000000276 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000276 440_0 $$03552$$aJournal of Molecular Biology$$v380$$x0022-2836$$y3
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000000276 520__ $$aFibrils from the Parkinson's-disease-related A53T mutant of alpha-synuclein were investigated by solid-state NMR spectroscopy, electron microscopy, and atomic force microscopy. Sequential solid-state NMR resonance assignments were obtained for a large fraction of the fibril core. Experiments conducted above and below the freezing point suggest that the fibrils contain regions with increased mobility and structural elements different from beta-strand character, in addition to the rigid beta-sheet-rich core region. As in earlier studies on wild-type alpha-synuclein, the C-terminus was found to be flexible and unfolded, whereas the main core region was highly rigid and rich in beta-sheets. Compared to fibrils from wild-type alpha-synuclein, the well-ordered beta-sheet region extends to at least L38 and L100. These results demonstrate that a disease-related mutant of alpha-synuclein differs in both aggregation kinetics and fibril structure.
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000000276 650_2 $$2MeSH$$aAmino Acid Sequence
000000276 650_2 $$2MeSH$$aEscherichia coli: genetics
000000276 650_2 $$2MeSH$$aFreezing
000000276 650_2 $$2MeSH$$aHumans
000000276 650_2 $$2MeSH$$aMicroscopy, Atomic Force
000000276 650_2 $$2MeSH$$aMicroscopy, Electron
000000276 650_2 $$2MeSH$$aMolecular Sequence Data
000000276 650_2 $$2MeSH$$aMutation
000000276 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular: methods
000000276 650_2 $$2MeSH$$aParkinson Disease: genetics
000000276 650_2 $$2MeSH$$aParkinson Disease: pathology
000000276 650_2 $$2MeSH$$aProtein Structure, Secondary
000000276 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000000276 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000000276 650_2 $$2MeSH$$aRecombinant Proteins: ultrastructure
000000276 650_2 $$2MeSH$$aalpha-Synuclein: chemistry
000000276 650_2 $$2MeSH$$aalpha-Synuclein: genetics
000000276 650_2 $$2MeSH$$aalpha-Synuclein: metabolism
000000276 650_2 $$2MeSH$$aalpha-Synuclein: ultrastructure
000000276 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000000276 650_7 $$00$$2NLM Chemicals$$aalpha-Synuclein
000000276 650_7 $$2WoSType$$aJ
000000276 65320 $$2Author$$asolid-state NMR
000000276 65320 $$2Author$$aamyloid
000000276 65320 $$2Author$$aParkinson's disease
000000276 65320 $$2Author$$aalpha-synuclein
000000276 65320 $$2Author$$aAFM
000000276 7001_ $$0P:(DE-HGF)0$$aCelej, M.S.$$b1
000000276 7001_ $$0P:(DE-HGF)0$$aBecker, S.$$b2
000000276 7001_ $$0P:(DE-HGF)0$$aRiedel, D.$$b3
000000276 7001_ $$0P:(DE-HGF)0$$aPelah, A.$$b4
000000276 7001_ $$0P:(DE-HGF)0$$aKumar, A.$$b5
000000276 7001_ $$0P:(DE-HGF)0$$aJovin, T.M.$$b6
000000276 7001_ $$0P:(DE-HGF)0$$aBaldus, M.$$b7
000000276 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2008.05.026$$gVol. 380, p. 444 - 450$$p444 - 450$$q380<444 - 450$$tJournal of molecular biology$$v380$$x0022-2836$$y2008
000000276 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2008.05.026
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