Magdalini Polymenidou Department of Quantitative Biomedicine, University of Zurich,
1 protocol

Manuela Pérez-Berlanga Department of Quantitative Biomedicine, University of Zurich,
1 protocol

Florent Laferrière
  • Post-Doc, Department of Quantitative Biomedicine, University of Zurich,
Research focus
  • Neurodegenerative Diseases - Synucleinopathies
  • 1 Author merit


PhD, University Paris VII, 2013

Lab information

Erwan Bezard Lab


• Igel-Egalon, A., Laferrière, F., Moudjou, M., Bohl, J., Mezache, M., Knapple, T., Herzog, L., Reine, F., Jas-Duval, C., Doumic, M., Rezaei, H. and Beringue, V. (2019). Early stage prion assembly involves two subpopulations with different quaternary structures and a secondary templating pathway. Commun Biol 2: 363. doi: 10.1038/s42003-019-0608-y.
• Laferrière, F., Maniecka, Z., Perez-Berlanga, M., Hruska-Plochan, M., Gilhespy, L., Hock, E. M., Wagner, U., Afroz, T., Boersema, P. J., Barmettler, G., Foti, S. C., Asi, Y. T., Isaacs, A. M., Al-Amoudi, A., Lewis, A., Stahlberg, H., Ravits, J., De Giorgi, F., Ichas, F., Bezard, E., Picotti, P., Lashley, T. and Polymenidou, M. (2019). TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates. Nat Neurosci 22(1): 65-77. doi: 10.1038/s41593-018-0294-y.
• Jawaid, A., Woldemichael, B. T., Kremer, E. A., Laferrière, F., Gaur, N., Afroz, T., Polymenidou, M. and Mansuy, I. M. (2019). Memory Decline and Its Reversal in Aging and Neurodegeneration Involve miR-183/96/182 Biogenesis. Mol Neurobiol 56(5): 3451-3462. doi: 10.1007/s12035-018-1314-3.
• Hock, E. M., Maniecka, Z., Hruska-Plochan, M., Reber, S., Laferrière, F., Sahadevan, M. K. S., Ederle, H., Gittings, L., Pelkmans, L., Dupuis, L., Lashley, T., Ruepp, M. D., Dormann, D. and Polymenidou, M. (2018). Hypertonic Stress Causes Cytoplasmic Translocation of Neuronal, but Not Astrocytic, FUS due to Impaired Transportin Function. Cell Rep 24(4): 987-1000 e1007. doi: 10.1016/j.celrep.2018.06.094.
• Afroz, T., Hock, E. M., Ernst, P., Foglieni, C., Jambeau, M., Gilhespy, L. A. B., Laferrière, F., Maniecka, Z., Pluckthun, A., Mittl, P., Paganetti, P., Allain, F. H. T. and Polymenidou, M. (2017). Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation. Nat Commun 8(1): 45. doi: 10.1038/s41467-017-00062-0.
• Leske, H., Hornemann, S., Herrmann, U. S., Zhu, C., Dametto, P., Li, B., Laferrière, F., Polymenidou, M., Pelczar, P., Reimann, R. R., Schwarz, P., Rushing, E. J., Wuthrich, K. and Aguzzi, A. (2017). Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein. PLoS One 12(2): e0170503. doi: 10.1371/journal.pone.0170503.
• Laferrière, F. and Polymenidou, M. (2015). Advances and challenges in understanding the multifaceted pathogenesis of amyotrophic lateral sclerosis. Swiss Med Wkly 145: w14054. doi: 10.4414/smw.2015.14054.
• Moudjou, M., Sibille, P., Fichet, G., Reine, F., Chapuis, J., Herzog, L., Jaumain, E., Laferrière, F., Richard, C. A., Laude, H., Andreoletti, O., Rezaei, H. and Beringue, V. (2013). Highly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification. MBio 5(1): e00829-00813. doi: 10.1128/mBio.00829-13.
• Laferrière, F., Tixador, P., Moudjou, M., Chapuis, J., Sibille, P., Herzog, L., Reine, F., Jaumain, E., Laude, H., Rezaei, H. and Béringue, V. (2013). Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics. PLoS Pathog 9(10): e1003702. doi: 10.1371/journal.ppat.1003702.
1 Protocol published
SarkoSpin: A Technique for Biochemical Isolation and Characterization of Pathological TDP-43 Aggregates
Authors:  Manuela Pérez-Berlanga, Florent Laferrière and Magdalini Polymenidou, date: 11/20/2019, view: 515, Q&A: 0
TDP-43 is the main aggregating protein in neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Aggregated TDP-43 is resistant to diverse detergent solubilization, yet physiological ...
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