Elena Tantardini

Elena Tantardini
University of Zurich | UZH · Department of quantitative biomedicine

PharmD and PhD student
Investigating molecular pathophysiology ALS and FTD focusing on Fused in Sarcoma protein (FUS) and RNA homeostasis.

About

10
Publications
2,989
Reads
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172
Citations
Introduction
I am PhD student currently working in Polymenidou's laboratory at UZH, Zurich. Our lab is interested in the pathophysiological roles of two RNA-binding proteins, TDP-43 and FUS, which are possibilty involved in the onset of ALS and FTD. Specifically, I am investigating the role of FUS in neuronal RNAs homeostasis and synaptic integrity.
Additional affiliations
January 2019 - present
University of Zurich
Position
  • PhD Student
October 2016 - September 2018
Centre for Genomic Regulation
Position
  • Research Assistant
March 2015 - March 2016
Imperial College London
Position
  • Master's Student
Education
October 2010 - April 2016
University of Pavia
Field of study
  • Pharmacy

Publications

Publications (10)
Preprint
Aggregation of the RNA-binding protein TDP-43 is the main common neuropathological feature of TDP-43 proteinopathies. In physiological conditions, TDP-43 is predominantly nuclear and contained in biomolecular condensates formed via liquid-liquid phase separation (LLPS). However, in disease, TDP-43 is depleted from these compartments and forms cytop...
Article
Full-text available
While the initial pathology of Parkinson's disease and other α-synucleinopathies is often confined to circumscribed brain regions, it can spread and progressively affect adjacent and distant brain locales. This process may be controlled by cellular receptors of α-synuclein fibrils, one of which was proposed to be the LAG3 immune checkpoint molecule...
Article
Full-text available
Mutations disrupting the nuclear localization of the RNA-binding protein FUS characterize a subset of amyotrophic lateral sclerosis patients (ALS-FUS). FUS regulates nuclear RNAs, but its role at the synapse is poorly understood. Using super-resolution imaging we determined that the localization of FUS within synapses occurs predominantly near the...
Preprint
Full-text available
While the initial pathology of Parkinson's disease and other α-synucleinopathies is often confined to circumscribed brain regions, it can spread and progressively affect adjacent and distant brain locales. This process may be controlled by cellular receptors of α-synuclein fibrils, one of which was proposed to be the LAG3 immune checkpoint molecule...
Preprint
Full-text available
While the initial pathology of Parkinson’s disease and other α-synucleinopathies is often confined to circumscribed brain regions, it can spread and progressively affect adjacent and distant brain locales. This process may be controlled by cellular receptors of α-synuclein fibrils, one of which was proposed to be the LAG3 immune checkpoint molecule...
Preprint
Full-text available
FUS is a primarily nuclear RNA-binding protein with important roles in RNA processing and transport. FUS mutations disrupting its nuclear localization characterize a subset of amyotrophic lateral sclerosis (ALS-FUS) patients, through an unidentified pathological mechanism. FUS regulates nuclear RNAs, but its role at the synapse is poorly understood...
Article
Full-text available
FUS is a primarily nuclear RNA-binding protein with important roles in RNA processing and transport. FUS mutations disrupting its nuclear localization characterize a subset of amyotrophic lateral sclerosis (ALS-FUS) patients, through an unidentified pathological mechanism. FUS regulates nuclear RNAs, but its role at the synapse is poorly understood...
Article
Full-text available
In the version of this Article originally published, the affiliations for Roland A. Fleck and José Antonio Del Río were incorrect due to a technical error that resulted in affiliations 8 and 9 being switched. The correct affiliations are: Roland A. Fleck:8Centre for Ultrastructural Imaging, Kings College London, London, UK. José Antonio Del Río:2Ce...
Article
Full-text available
Reactive oxygen species (ROS) contribute to tissue damage and remodelling mediated by the inflammatory response after injury. Here we show that ROS, which promote axonal dieback and degeneration after injury, are also required for axonal regeneration and functional recovery after spinal injury. We find that ROS production in the injured sciatic ner...

Questions

Questions (4)
Question
I aim to culture motoneurons from spinal cord.
what is the best protocol to get healthy motoneuorns? should I culture from embrios or p0/p1 mice are good enough?
what-s the right medium I have to use? does the medium have to contain factors? if yes, which ones and why? thank you!
Question
Hello,
i am culturing adult (p20)DRGs neurons in compartmentalized microfluidich chambers (XONA 450um).
I plate 100k or 150k cells in channel.
after 48 they have completely crossed the barrier and the axons are sprouting in the axonal part.
unfortunately after 10-12 days of culture axons degenerate (they show the dotted pattern).
the medium is the following:
-neurobasal
-p/s
-b27 without vit A 2%
and i add also GDNF, BDNF and CTNF.
thank you in advance!
Question
I want to see by IF APC and I want the antibody to mark the C-terminus since I am planning to see his co-localization with actin and microtubules..
thank you! :-)
Question
Hello everybody,
I have problem with my cell culture of retinal cells.
I take retinas from P9-P12 mice and I dissociated them following the protocol attached.
I have the 7% of alive cells maximum (checked with Trypan Blue).

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Projects

Projects (2)
Archived project
Techniques used: western blot, IP, RT-PCR, Chip, cell culture, DRGs culture, DRGs extraction, sciatic nerves extraction, flow cytometry, immunohystochemistry, immunocytochemistry.
Archived project
I am investigating on the missing link between actin and MT structures when, after axonal injury, a retraction bulb forms. I am currently work on neuroblastoma, PC12 and retinal ganglion cells.