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Your search keyword '"Kaminski Schierle, Gabriele S."' showing total 15 results
Start Over Author "Kaminski Schierle, Gabriele S." Publisher cold spring harbor laboratory
15 results on '"Kaminski Schierle, Gabriele S."'

3. A multiplex platform to identify mechanisms and modulators of proteotoxicity in neurodegeneration

Author

Resnick, Samuel J., primary, Qamar, Seema, additional, Sheng, Jenny, additional, Huang, Lei Haley, additional, Nixon-Abell, Jonathon, additional, Melore, Schuyler, additional, Chung, Chyi Wei, additional, Li, Xuecong, additional, Wang, Jingshu, additional, Zhang, Nancy, additional, Shneider, Neil A., additional, Kaminski, Clemens F., additional, Ruggeri, Francesco Simone, additional, Kaminski Schierle, Gabriele S., additional, George-Hyslop, Peter St, additional, and Chavez, Alejandro, additional

Published
2022
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4. ERnet: a tool for the semantic segmentation and quantitative analysis of endoplasmic reticulum topology for video-rate super-resolution imaging

Author

Lu, Meng, primary, Christensen, Charles N., additional, Weber, Jana M., additional, Konno, Tasuku, additional, Läubli, Nino F., additional, Scherer, Katharina M., additional, Avezov, Edward, additional, Lio, Pietro, additional, Lapkin, Alexei A., additional, Kaminski Schierle, Gabriele S., additional, and Kaminski, Clemens F., additional

Published
2022
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6. A unified in vitro to in vivo fluorescence lifetime screening platform yields amyloid β aggregation inhibitors

Author

Collins, Súil, primary, van Vliet, Liisa, additional, Gielen, Fabrice, additional, Janeček, Matej, additional, Valladolid, Sara Wagner, additional, Poudel, Chetan, additional, Fusco, Giuliana, additional, De Simone, Alfonso, additional, Michel, Claire, additional, Kaminski, Clemens F., additional, Spring, David R, additional, Hollfelder, Florian, additional, and Kaminski Schierle, Gabriele S, additional

Published
2022
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9. The SARS-CoV-2 nucleocapsid protein associates with the replication organelles before viral assembly at the Golgi/ERGIC and lysosome-mediated egress

Author

Scherer, Katharina M., primary, Mascheroni, Luca, additional, Carnell, George W., additional, Wunderlich, Lucia C. S., additional, Makarchuk, Stanislaw, additional, Brockhoff, Marius, additional, Mela, Ioanna, additional, Fernandez-Villegas, Ana, additional, Barysevich, Max, additional, Stewart, Hazel, additional, Sans, Maria Suau, additional, George, Charlotte L., additional, Lamb, Jacob R., additional, Kaminski-Schierle, Gabriele S., additional, Heeney, Jonathan L., additional, and Kaminski, Clemens F., additional

Published
2021
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10. Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies

Author

Hardenberg, Maarten C., primary, Sinnige, Tessa, additional, Casford, Sam, additional, Dada, Samuel, additional, Poudel, Chetan, additional, Robinson, Lizzy, additional, Fuxreiter, Monika, additional, Kaminksi, Clemens, additional, Kaminski Schierle, Gabriele S., additional, Nollen, Ellen A. A., additional, Dobson, Christopher M., additional, and Vendruscolo, Michele, additional

Published
2020
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12. A waveguide imaging platform for live-cell TIRF imaging of neurons over large fields of view

Author

Opstad, Ida S., primary, Ströhl, Florian, additional, Fantham, Marcus, additional, Hockings, Colin, additional, Vanderpoorten, Oliver, additional, van Tartwijk, Francesca W., additional, Lin, Julie Qiaojin, additional, Tinguely, Jean-Claude, additional, Dullo, Firehun T., additional, Kaminski-Schierle, Gabriele S., additional, Ahluwalia, Balpreet S., additional, and Kaminski, Clemens F., additional

Published
2019
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13. Fast fluorescence lifetime imaging reveals the aggregation processes of α-synuclein and polyglutamine in aging Caenorhabditis elegans

Author

Laine, Romain F., primary, Sinnige, Tessa, additional, Ma, Kai Yu, additional, Haack, Amanda J., additional, Poudel, Chetan, additional, Gaida, Peter, additional, Curry, Nathan, additional, Perni, Michele, additional, Nollen, Ellen A.A., additional, Dobson, Christopher M., additional, Vendruscolo, Michele, additional, Kaminski Schierle, Gabriele S., additional, and Kaminski, Clemens F., additional

Published
2018
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14. Label-free characterisation of amyloids and alpha-Synuclein polymorphs by exploiting their intrinsic fluorescence property

Author

Gabriele S. Kaminski Schierle, Edward Ward, Clemens F. Kaminski, Yuqing Feng, Molly Jo Davis, Chyi Wei Chung, Amberley D. Stephens, Chung, Chyi Wei [0000-0003-1780-3486], Stephens, Amberley D [0000-0002-7303-6392], Kaminski, Clemens F [0000-0002-5194-0962], Kaminski Schierle, Gabriele S [0000-0002-1843-2202], and Apollo - University of Cambridge Repository

Subjects
Alpha-synuclein, Amyloid, Chemistry, Amyloidogenic Proteins, Intrinsic fluorescence, Fibril, Fluorescence, Small molecule, In vitro, Analytical Chemistry, chemistry.chemical_compound, alpha-Synuclein, Biophysics, Protein Conformation, beta-Strand, Label free
Abstract

Funder: Infinitus China Ltd., Conventional in vitro aggregation assays often involve tagging with extrinsic fluorophores, which can interfere with aggregation. We propose the use of intrinsic amyloid fluorescence lifetime probed using two-photon excitation and represented by model-free phasor plots as a label-free assay to characterize the amyloid structure. Intrinsic amyloid fluorescence arises from the structured packing of β-sheets in amyloids and is independent of aromatic-based fluorescence. We show that different amyloids [i.e., α-Synuclein (αS), β-Lactoglobulin (βLG), and TasA] and different polymorphic populations of αS (induced by aggregation in salt-free and salt buffers mimicking the intra-/extracellular environments) can be differentiated by their unique fluorescence lifetimes. Moreover, we observe that disaggregation of the preformed fibrils of αS and βLG leads to increased fluorescence lifetimes, distinct from those of their fibrillar counterparts. Our assay presents a medium-throughput method for rapid classification of amyloids and their polymorphs (the latter of which recent studies have shown lead to different disease pathologies) and for testing small-molecule inhibitory compounds.

Published
2021

15. Fast fluorescence lifetime imaging reveals the aggregation processes of α-synuclein and polyglutamine in aging Caenorhabditis elegans

Author

Amanda J. Haack, Peter Gaida, Tessa Sinnige, Michele Vendruscolo, Nathan Curry, Kai Yu Ma, Clemens F. Kaminski, Romain F. Laine, Michele Perni, Christopher M. Dobson, Chetan Poudel, Gabriele S. Kaminski Schierle, Ellen A. A. Nollen, Laine, Romain F [0000-0002-2151-4487], Sinnige, Tessa [0000-0002-9353-126X], Poudel, Chetan [0000-0002-8512-9238], Perni, Michele [0000-0001-7593-8376], Vendruscolo, Michele [0000-0002-3616-1610], Kaminski Schierle, Gabriele S [0000-0002-1843-2202], Kaminski, Clemens F [0000-0002-5194-0962], Apollo - University of Cambridge Repository, and Molecular Neuroscience and Ageing Research (MOLAR)

Subjects
0301 basic medicine, Aging, Amyloid, Fluorescence-lifetime imaging microscopy, Huntingtin, ved/biology.organism_classification_rank.species, PROTEIN, Protein aggregation, 01 natural sciences, Biochemistry, DISEASE, Article, Protein Aggregates, 03 medical and health sciences, HUNTINGTIN, 0302 clinical medicine, In vivo, Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Model organism, 030304 developmental biology, 0303 health sciences, biology, 010405 organic chemistry, ved/biology, Chemistry, Optical Imaging, General Medicine, IN-VITRO, biology.organism_classification, In vitro, 0104 chemical sciences, Cell biology, Functional imaging, 030104 developmental biology, AMYLOID FORMATION, alpha-Synuclein, Molecular Medicine, α synuclein, Peptides, 030217 neurology & neurosurgery
Abstract

The nematode worm Caenorhabditis elegans has emerged as an important model organism to study the molecular mechanisms of protein misfolding diseases associated with amyloid formation because of its small size, ease of genetic manipulation and optical transparency. Obtaining a reliable and quantitative read-out of protein aggregation in this system, however, remains a challenge. To address this problem, we here present a fast time-gated fluorescence lifetime imaging (TG-FLIM) method and show that it provides functional insights into the process of protein aggregation in living animals by enabling the rapid characterisation of different types of aggregates. More specifically, in longitudinal studies of C. elegans models of Parkinson’s and Huntington’s diseases, we observed marked differences in the aggregation kinetics and the nature of the protein inclusions formed by α-synuclein and polyglutamine. In particular, we found that α-synuclein inclusions do not display amyloid-like features until late in the life of the worms, whereas polyglutamine forms amyloid characteristics rapidly in early adulthood. Furthermore, we show that the TG-FLIM method is capable of imaging live and non-anaesthetised worms moving in specially designed agarose micro-chambers. Taken together, our results show that the TG-FLIM method enables high-throughput functional imaging of living C. elegans that can be used to study in vivo mechanisms of aggregation and that has the potential to aid the search for therapeutic modifiers of protein aggregation and toxicity.

Published
2018

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