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42 results on '"Campioni, Silvia"'

4. Regulation of α-synuclein by chaperones in mammalian cells

Author

Burmann, Björn M., Gerez, Juan A., Matečko-Burmann, Irena, Campioni, Silvia, Kumari, Pratibha, Ghosh, Dhiman, Mazur, Adam, Aspholm, Emelie E., Šulskis, Darius, Wawrzyniuk, Magdalena, Bock, Thomas, Schmidt, Alexander, Rüdiger, Stefan G. D., Riek, Roland, and Hiller, Sebastian

Published
2020
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10. In vivo demonstration that α-synuclein oligomers are toxic

Author

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., and Riek, Roland

Published
2011

20. Regulation of α-synuclein by chaperones in mammalian cells

Author

Burmann, Björn M., primary, Gerez, Juan A., additional, Matečko-Burmann, Irena, additional, Campioni, Silvia, additional, Kumari, Pratibha, additional, Ghosh, Dhiman, additional, Mazur, Adam, additional, Aspholm, Emelie E., additional, Šulskis, Darius, additional, Wawrzyniuk, Magdalena, additional, Bock, Thomas, additional, Schmidt, Alexander, additional, Rüdiger, Stefan G. D., additional, Riek, Roland, additional, and Hiller, Sebastian, additional

Published
2019
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23. Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation

Author

Calloni, Giulia, Lendel, Christopher, Campioni, Silvia, Giannini, Silva, Gliozzi, Alessandra, Relini, Annalisa, Vendruscolo, Michele, Dobson, Christopher M., Salvatella, Xavier, and Chiti, Fabrizio

Subjects
Fluorescence -- Evaluation, Nuclear magnetic resonance spectroscopy -- Usage, Protein folding -- Analysis, Circular dichroism -- Usage, Chemistry
Abstract

The highly dynamic conformational state formed by the protein domain HypF-N at low pH, before aggregation, is examined by using fluorescence, circular dichroism and NMR spectroscopies. The studies have shown that strategies solely based on the characterization of the partially unfolded states populated before aggregation are unlikely to provide a detailed description of the mechanism of aggregation.

Published
2008

24. Sequence and structural determinants of amyloid fibril formation

Author

Bemporad, Francesco, Calloni, Giulia, Campioni, Silvia, Plakoutsi, Georgia, Taddie, Niccolo, and Chiti, Fabrizio

Subjects
Glycoproteins -- Structure, Proteins -- Structure, Proteins -- Research, Chemistry, Science and technology
Abstract

The sequence and structural determinants of protein aggregation in amyloid fibril formation and the factors that dominate the aggregation of unfolded peptides and proteins is described. The factors that pertain to the aggregation of partially structured states are reviewed and the ability of the even fully folded proteins states to aggregate into early oligomers in any case with no need to undergo significant conformational changes are presented.

Published
2006

25. Preparation and Characterization of Stable α-Synuclein Lipoprotein Particles

Author

Eichmann, Cédric, primary, Campioni, Silvia, additional, Kowal, Julia, additional, Maslennikov, Innokentiy, additional, Gerez, Juan, additional, Liu, Xiaoxia, additional, Verasdonck, Joeri, additional, Nespovitaya, Nadezhda, additional, Choe, Senyon, additional, Meier, Beat H., additional, Picotti, Paola, additional, Rizo, Josep, additional, Stahlberg, Henning, additional, and Riek, Roland, additional

Published
2016
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39. Preparation and Characterization of Stable -Synuclein Lipoprotein Particles

Author

Eichmann, Cedric, Campioni, Silvia, Kowal, Julia, Maslennikov, Innokentiy, Gerez, Juan, Liu, Xiaoxia, Verasdonck, Joeri, Nespovitaya, Nadezhda, Choe, Senyon, Meier, Beat H., Picotti, Paola, Rizo, Josep, Stahlberg, Henning, and Riek, Roland

Subjects
nervous system, animal diseases, lipids (amino acids, peptides, and proteins), environment and public health, nervous system diseases
Abstract

Multiple neurodegenerative diseases are caused by the aggregation of the human -Synuclein (-Syn) protein. -Syn possesses high structural plasticity and the capability of interacting with membranes. Both features are not only essential for its physiological function but also play a role in the aggregation process. Recently it has been proposed that -Syn is able to form lipid-protein particles reminiscent of high-density lipoproteins. Here, we present a method to obtain a stable and homogeneous population of nanometer-sized particles composed of -Syn and anionic phospholipids. These particles are called -Syn lipoprotein (nano)particles to indicate their relationship to high-density lipoproteins formed by human apolipoproteins in vivo and of in vitro self-assembling phospholipid bilayer nanodiscs. Structural investigations of the -Syn lipoprotein particles by circular dichroism (CD) and magic angle solid-state nuclear magnetic resonance (MAS SS-NMR) spectroscopy establish that -Syn adopts a helical secondary structure within these particles. Based on cryo-electron microscopy (cryo-EM) and dynamic light scattering (DLS) -Syn lipoprotein particles have a defined size with a diameter of approximate to 23 nm. Chemical cross-linking in combination with solution-state NMR and multiangle static light scattering (MALS) of -Syn particles reveal a high-order protein-lipid entity composed of approximate to 8-10 -Syn molecules. The close resemblance in size between cross-linked in vitro-derived -Syn lipoprotein particles and a cross-linked species of endogenous -Syn from SH-SY5Y human neuroblastoma cells indicates a potential functional relevance of -Syn lipoprotein nanoparticles.

40. An Easy Path for Correlative Electron and Super-Resolution Light Microscopy

Author

Pinotsi, Dorothea, Rodighiero, Simona, Campioni, Silvia, and Csucs, Gabor

Subjects
3. Good health
Abstract

A number of new Correlative Light and Electron Microscopy approaches have been developed over the past years, offering the opportunity to combine the specificity and bio-compatibility of light microscopy with the high resolution achieved in electron microscopy. More recently, these approaches have taken one step further and also super-resolution light microscopy was combined with transmission or scanning electron microscopy. This combination usually requires moving the specimen between different imaging systems, an expensive set-up and relatively complicated imaging workflows. Here we present a way to overcome these difficulties by exploiting a commercially available wide-field fluorescence microscope integrated in the specimen chamber of a Scanning Electron Microscope (SEM) to perform correlative LM/EM studies. Super-resolution light microscopy was achieved by using a recently developed algorithm - the Super-Resolution Radial Fluctuations (SRRF) - to improve the resolution of diffraction limited fluorescent images. With this combination of hardware/software it is possible to obtain correlative super-resolution light and scanning electron microscopy images in an easy and fast way. The imaging workflow is described and demonstrated on fluorescently labelled amyloid fibrils, fibrillar protein aggregates linked to the onset of multiple neurodegenerative diseases, revealing information about their polymorphism., Scientific Reports, 9 (1), ISSN:2045-2322

41. Accumulation of oligomer-prone α-synuclein exacerbates synaptic and neuronal degeneration in vivo

Author

Rockenstein, Edward, Nuber, Silke, Overk, Cassia R., Ubhi, Kiren, Mante, Michael, Patrick, Christina, Adame, Anthony, Trejo-Morales, Margarita, Gerez, Juan, Picotti, Paola, Jensen, Poul H., Campioni, Silvia, Riek, Roland, Winkler, Jürgen, Gage, Fred H., Winner, Beate, Masliah, Eliezer, Rockenstein, Edward, Nuber, Silke, Overk, Cassia R., Ubhi, Kiren, Mante, Michael, Patrick, Christina, Adame, Anthony, Trejo-Morales, Margarita, Gerez, Juan, Picotti, Paola, Jensen, Poul H., Campioni, Silvia, Riek, Roland, Winkler, Jürgen, Gage, Fred H., Winner, Beate, and Masliah, Eliezer

Abstract

The toxicity of α-synuclein invivo is not well understood. Rockenstein etal. describe an α-synuclein transgenic model expressing the E57K mutant that forms stable oligomers. They show that oligomers accumulate at synapses and that the mutation interferes with synaptic vesicles and is associated with behavioural deficits and neurodegeneration

42. In vivo demonstration that alpha-synuclein oligomers are toxic.

Author

Winner B, Jappelli R, Maji SK, Desplats PA, 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 FH, and Riek R

Subjects
Animals, Brain metabolism, Lentivirus genetics, Rats, alpha-Synuclein genetics, alpha-Synuclein metabolism, Biopolymers toxicity, alpha-Synuclein toxicity
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.

Published
2011
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