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dc.contributor.author
Roberti, Maria Julia
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Fölling, Jonas
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Celej, Maria Soledad
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Bossi, Mariano Luis
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Jovin, Thomas M.
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Jares, Elizabeth Andrea
dc.date.available
2019-03-25T01:51:24Z
dc.date.issued
2012-04
dc.identifier.citation
Roberti, Maria Julia; Fölling, Jonas; Celej, Maria Soledad; Bossi, Mariano Luis; Jovin, Thomas M.; et al.; Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy; Cell Press; Biophysical Journal; 102; 7; 4-2012; 1598-1607
dc.identifier.issn
0006-3495
dc.identifier.uri
http://hdl.handle.net/11336/72394
dc.description.abstract
The morphological features of alpha-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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Cell Press
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Palm
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Nanoscopy
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Amyloid
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Synuclein
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-01-02T19:09:58Z
dc.journal.volume
102
dc.journal.number
7
dc.journal.pagination
1598-1607
dc.journal.pais
Estados Unidos
dc.journal.ciudad
United States
dc.description.fil
Fil: Roberti, Maria Julia. Max Planck Institute For Biophysical Chemistry (karl Friedrich Bonhoeffer Institute); . Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
dc.description.fil
Fil: Fölling, Jonas. Institut Max Planck Fuer Gesellschaft; Alemania
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Fil: Celej, Maria Soledad. Institut Max Planck Fuer Gesellschaft; Alemania
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Fil: Bossi, Mariano Luis. Institut Max Planck Fuer Gesellschaft; Alemania
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Fil: Jovin, Thomas M.. Institut Max Planck Fuer Gesellschaft; Alemania
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Fil: Jares, Elizabeth Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
dc.journal.title
Biophysical Journal
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349512002925
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bpj.2012.03.010
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