Publikation:

Alpha-Synuclein Disease Mutations Are Structurally Defective and Locally Affect Membrane Binding

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Robotta_2-107onzb7rsmoq4.pdf
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2017

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Martins, Juliana Cristina

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http://nbn-resolving.de/urn:nbn:de:bsz:352-2-107onzb7rsmoq4
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https://doi.org/10.1021/jacs.6b05335
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oops

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Journal of the American Chemical Society : JACS. 2017, 139(12), pp. 4254-4257. ISSN 0002-7863. eISSN 1520-5126. Available under: doi: 10.1021/jacs.6b05335

Zusammenfassung

The intrinsically disordered human protein alpha-Synuclein (αS) has a prominent role in Parkinson's disease (PD) pathology. Several familial variants of αS are correlated with inherited PD. Disease mutations have been shown to have an impact on lipid membrane binding. Here, using electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling, we show that familial PD-associated variants are structurally defective in membrane binding and alter the local binding properties of the protein.

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540 Chemie

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ISO 690ROBOTTA, Marta, Julia CATTANI, Juliana Cristina MARTINS, Vinod SUBRAMANIAM, Malte DRESCHER, 2017. Alpha-Synuclein Disease Mutations Are Structurally Defective and Locally Affect Membrane Binding. In: Journal of the American Chemical Society : JACS. 2017, 139(12), pp. 4254-4257. ISSN 0002-7863. eISSN 1520-5126. Available under: doi: 10.1021/jacs.6b05335
BibTex
@article{Robotta2017-03-29Alpha-39012,
  year={2017},
  doi={10.1021/jacs.6b05335},
  title={Alpha-Synuclein Disease Mutations Are Structurally Defective and Locally Affect Membrane Binding},
  number={12},
  volume={139},
  issn={0002-7863},
  journal={Journal of the American Chemical Society : JACS},
  pages={4254--4257},
  author={Robotta, Marta and Cattani, Julia and Martins, Juliana Cristina and Subramaniam, Vinod and Drescher, Malte}
}
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