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| Home > Publications database > Copper Binding to the N-Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding > print |
| 001 | 202935 | ||
| 005 | 20240625095118.0 | ||
| 024 | 7 | _ | |a 10.1021/jacs.5b01911 |2 doi |
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| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Miotto, Marco C. |b 0 |
| 245 | _ | _ | |a Copper Binding to the N-Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding |
| 260 | _ | _ | |a Washington, DC |b American Chemical Society |c 2015 |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1438324999_32580 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a Growing 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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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Zweckstetter, Markus |b 3 |
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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Selenko, Philipp |b 5 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Griesinger, Christian |b 6 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Binolfi, Andres |b 7 |e Corresponding author |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Fernández, Claudio O. |b 8 |e Corresponding author |
| 773 | _ | _ | |0 PERI:(DE-600)1472210-0 |a 10.1021/jacs.5b01911 |g Vol. 137, no. 20, p. 6444 - 6447 |n 20 |p 6444 - 6447 |t Journal of the American Chemical Society |v 137 |x 1520-5126 |y 2015 |
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