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The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

In vivo demonstration that α-synuclein oligomers are toxic

Winner, Beate, Jappelli, Roberto, Maji, Samir K., Desplats, Paula A., Boyer, Leah, Aigner, Stefan, Hetzer, Claudia, Loher, Thomas, Vilar, Marçal, Campioni, Silvia, Tzitzilonis, Christos, Soragni, Alice, Jessberger, Sebastian, Mira, Helena, Consiglio, Antonella, Pham, Emiley, Masliah, Eliezer, Gage, Fred H., Riek, Roland·2011·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.1100976108
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Abstract

The aggregation of proteins into oligomers and amyloid fibrils is characteristic of several neurodegenerative diseases, including Parkinson disease (PD). In PD, the process of aggregation of α-synuclein (α-syn) from monomers, via oligomeric intermediates, into amyloid fibrils is considered the disease-causative toxic mechanism. We developed α-syn mutants that promote oligomer or fibril formation and tested the toxicity of these mutants by using a rat lentivirus system to investigate loss of dopaminergic neurons in the substantia nigra. The most severe dopaminergic loss in the substantia nigra is observed in animals with the α-syn variants that form oligomers (i.e., E57K and E35K), whereas the α-syn variants that form fibrils very quickly are less toxic. We show that α-syn oligomers are toxic in vivo and that α-syn oligomers might interact with and potentially disrupt membranes.

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Research works printed but not linked: 30

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Metadata

Authors
Winner, B., Jappelli, R., Maji, S. K., Desplats, P. A., Boyer, L., Aigner, S., Hetzer, C., Loher, T., Vilar, M., Campioni, S., Tzitzilonis, C., Soragni, A., Jessberger, S., Mira, H., Consiglio, A., Pham, E., Masliah, E., Gage, F. H., & Riek, R.
Affiliations
  • Salk Institute for Biological Studies, La Jolla, CA 92037;
  • Laboratory of Physical Chemistry, Eidgenössische Technische Hochschule Zurich, 8093 Zurich, Switzerland;
  • Department of Neurosciences and Department of Pathology and
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2011-02-15
Volume
108
Issue
10
Pages
4194-4199
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.1100976108
Cited by
1,463
References
5
Language
en

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