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000202935 1001_ $$0P:(DE-HGF)0$$aMiotto, Marco C.$$b0
000202935 245__ $$aCopper Binding to the N-Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding
000202935 260__ $$aWashington, DC$$bAmerican Chemical Society$$c2015
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000202935 520__ $$aGrowing evidence supports a link between brain copper homeostasis, the formation of alpha-synuclein (AS)-copper complexes, and the development of Parkinson disease (PD). Recently it was demonstrated that the physiological form of AS is N-terminally acetylated (AcAS). Here we used NMR spectroscopy to structurally characterize the interaction between Cu(I) and AcAS. We found that the formation of an AcAS–Cu(I) complex at the N-terminal region stabilizes local conformations with α-helical secondary structure and restricted motility. Our work provides new evidence into the metallo-biology of PD and opens new lines of research as the formation of AcAS–Cu(I) complex might impact on AcAS membrane binding and aggregation.
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000202935 7001_ $$0P:(DE-HGF)0$$aValiente-Gabioud, Ariel A.$$b1
000202935 7001_ $$0P:(DE-Juel1)145921$$aRossetti, Giulia$$b2$$ufzj
000202935 7001_ $$0P:(DE-HGF)0$$aZweckstetter, Markus$$b3
000202935 7001_ $$0P:(DE-Juel1)145614$$aCarloni, Paolo$$b4$$ufzj
000202935 7001_ $$0P:(DE-HGF)0$$aSelenko, Philipp$$b5
000202935 7001_ $$0P:(DE-HGF)0$$aGriesinger, Christian$$b6
000202935 7001_ $$0P:(DE-HGF)0$$aBinolfi, Andres$$b7$$eCorresponding author
000202935 7001_ $$0P:(DE-HGF)0$$aFernández, Claudio O.$$b8$$eCorresponding author
000202935 773__ $$0PERI:(DE-600)1472210-0$$a10.1021/jacs.5b01911$$gVol. 137, no. 20, p. 6444 - 6447$$n20$$p6444 - 6447$$tJournal of the American Chemical Society$$v137$$x1520-5126$$y2015
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