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  Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy.

Roberti, M. J., Fölling, J., Celej, M. S., Bossi, M. L., Jovin, T. M., & Jares-Erijman, E. A. (2012). Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy. Biophysical Journal, 102(7), 1598-1607. doi:10.1016/j.bpj.2012.03.010.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-83AD-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-357F-D
Genre: Journal Article

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 Creators:
Roberti, M. J.1, Author              
Fölling, J.2, Author              
Celej, M. S.1, Author              
Bossi, M. L.2, Author              
Jovin, T. M.1, Author              
Jares-Erijman, E. A., Author
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1Emeritus Group Laboratory of Cellular Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578629              
2Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society, ou_578627              

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 Abstract: The morphological features of α-synuclein (AS) amyloid aggregation in vitro and in cells were elucidated at the nanoscale by far-field subdiffraction fluorescence localization microscopy. Labeling AS with rhodamine spiroamide probes allowed us to image AS fibrillar structures by fluorescence stochastic nanoscopy with an enhanced resolution at least 10-fold higher than that achieved with conventional, diffraction-limited techniques. The implementation of dual-color detection, combined with atomic force microscopy, revealed the propagation of individual fibrils in vitro. In cells, labeled protein appeared as amyloid aggregates of spheroidal morphology and subdiffraction sizes compatible with in vitro supramolecular intermediates perceived independently by atomic force microscopy and cryo-electron tomography. We estimated the number of monomeric protein units present in these minute structures. This approach is ideally suited for the investigation of the molecular mechanisms of amyloid formation both in vitro and in the cellular milieu.

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Language(s): eng - English
 Dates: 2012-04-042012-04-19
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2012.03.010
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 102 (7) Sequence Number: - Start / End Page: 1598 - 1607 Identifier: -