Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy
- Autores
- Roberti, Maria Julia; Fölling, Jonas; Celej, Maria Soledad; Bossi, Mariano Luis; Jovin, Thomas M.; Jares, Elizabeth Andrea
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
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
Fil: Fölling, Jonas. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Celej, Maria Soledad. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Bossi, Mariano Luis. Institut Max Planck Fuer Gesellschaft; Alemania
Fil: Jovin, Thomas M.. Institut Max Planck Fuer Gesellschaft; Alemania
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 - Materia
-
Palm
Nanoscopy
Amyloid
Synuclein - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/72394
Ver los metadatos del registro completo
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Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopyRoberti, Maria JuliaFölling, JonasCelej, Maria SoledadBossi, Mariano LuisJovin, Thomas M.Jares, Elizabeth AndreaPalmNanoscopyAmyloidSynucleinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The 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.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; ArgentinaFil: Fölling, Jonas. Institut Max Planck Fuer Gesellschaft; AlemaniaFil: Celej, Maria Soledad. Institut Max Planck Fuer Gesellschaft; AlemaniaFil: Bossi, Mariano Luis. Institut Max Planck Fuer Gesellschaft; AlemaniaFil: Jovin, Thomas M.. Institut Max Planck Fuer Gesellschaft; AlemaniaFil: 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; ArgentinaCell Press2012-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/72394Roberti, 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; 1598-16070006-3495CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349512002925info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2012.03.010info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:08:35Zoai:ri.conicet.gov.ar:11336/72394instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:08:35.49CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy |
title |
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy |
spellingShingle |
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy Roberti, Maria Julia Palm Nanoscopy Amyloid Synuclein |
title_short |
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy |
title_full |
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy |
title_fullStr |
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy |
title_full_unstemmed |
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy |
title_sort |
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy |
dc.creator.none.fl_str_mv |
Roberti, Maria Julia Fölling, Jonas Celej, Maria Soledad Bossi, Mariano Luis Jovin, Thomas M. Jares, Elizabeth Andrea |
author |
Roberti, Maria Julia |
author_facet |
Roberti, Maria Julia Fölling, Jonas Celej, Maria Soledad Bossi, Mariano Luis Jovin, Thomas M. Jares, Elizabeth Andrea |
author_role |
author |
author2 |
Fölling, Jonas Celej, Maria Soledad Bossi, Mariano Luis Jovin, Thomas M. Jares, Elizabeth Andrea |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Palm Nanoscopy Amyloid Synuclein |
topic |
Palm Nanoscopy Amyloid Synuclein |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
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. 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 Fil: Fölling, Jonas. Institut Max Planck Fuer Gesellschaft; Alemania Fil: Celej, Maria Soledad. Institut Max Planck Fuer Gesellschaft; Alemania Fil: Bossi, Mariano Luis. Institut Max Planck Fuer Gesellschaft; Alemania Fil: Jovin, Thomas M.. Institut Max Planck Fuer Gesellschaft; Alemania 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 |
description |
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. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-04 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/72394 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 0006-3495 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/72394 |
identifier_str_mv |
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 0006-3495 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349512002925 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2012.03.010 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Cell Press |
publisher.none.fl_str_mv |
Cell Press |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1842270050816360448 |
score |
13.13397 |